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Conserved domains on  [gi|1370475556|ref|XP_024307388|]
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reticulocalbin-3 isoform X1 [Homo sapiens]

Protein Classification

CREC-EF hand family protein; EF-hand domain-containing protein( domain architecture ID 11610940)

CREC (Cab45/reticulocalbin/ERC45/calumenin)-EF hand family protein; the family consists of a group of six EF-hand, low-affinity Ca2+-binding proteins, including reticulocalbin (RCN-1), ER Ca2+-binding protein of 55, reticulocalbin-3 (RCN-3), cab45 Ca2+-binding protein, and calumenin (also known as crocalbin or CBP-50)| EF-hand (EFh) domain-containing protein may be involved in binding intracellular calcium and in calcium signal transduction

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
EFh_CREC_RCN3 cd16230
EF-hand, calcium binding motif, found in reticulocalbin-3 (RCN-3); RCN-3, also termed EF-hand ...
44-348 0e+00

EF-hand, calcium binding motif, found in reticulocalbin-3 (RCN-3); RCN-3, also termed EF-hand calcium-binding protein RLP49, is a putative six EF-hand Ca2+-binding protein that contains five RXXR (X is any amino acid) motifs and a C-terminal ER retrieval signal His-Asp-Glu-Leu (HDEL) tetrapeptide. The RXXR motif represents the target sequence of subtilisin-like proprotein convertases (SPCs). RCN-3 is specifically bound to the paired basic amino-acid-cleaving enzyme-4 (PACE4) precursor protein and plays an important role in the biosynthesis of PACE4.


:

Pssm-ID: 320028 [Multi-domain]  Cd Length: 268  Bit Score: 501.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475556  44 PHDDAHGNFQYDHEAFLGREVAKEFDQLTPEESQARLGRIVDRMDRAGDGDGWVSLAELRAWIAHTQQRHIRDSVSAAWD 123
Cdd:cd16230     1 PHDDAHGNFQYDHEAFLGREVAKEFDQLSPEESQARLGRIVDRMDRAGDGDGWVSLAELRAWIAHTQQRHIRDSVSAAWQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475556 124 TYDTDRDGRVGWEELRNATYGHYAPGEEFHDVEDAETYKKMLARDERRFRVADQDGDSMATREELTAFLHPEEFPHMRDI 203
Cdd:cd16230    81 TYDTDRDGRVGWEELRNATYGHYEPGEEFHDVEDAETYKKMLARDERRFRVADQDGDSMATREELTAFLHPEEFPHMRDI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475556 204 VIAlpgakfprepltltpgvqpppgarvigpqpqcpfllqETLEDLDRNKDGYVQVEEYIADLYSAEPGEEEPAWVQTER 283
Cdd:cd16230   161 VVA-------------------------------------ETLEDLDKNKDGYVQVEEYIADLYSGEPGEEEPAWVQTER 203
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370475556 284 QQFRDFRDLNKDGHLDGSEVGHWVLPPAQDQPLVEANHLLHESDTDKDGRLSKAEILGNWNMFVG 348
Cdd:cd16230   204 QQFRQFRDLNKDGRLDGSEVGHWVLPPSQDQPLVEANHLLHESDTDKDGRLSKAEILGNWNMFVG 268
 
Name Accession Description Interval E-value
EFh_CREC_RCN3 cd16230
EF-hand, calcium binding motif, found in reticulocalbin-3 (RCN-3); RCN-3, also termed EF-hand ...
44-348 0e+00

EF-hand, calcium binding motif, found in reticulocalbin-3 (RCN-3); RCN-3, also termed EF-hand calcium-binding protein RLP49, is a putative six EF-hand Ca2+-binding protein that contains five RXXR (X is any amino acid) motifs and a C-terminal ER retrieval signal His-Asp-Glu-Leu (HDEL) tetrapeptide. The RXXR motif represents the target sequence of subtilisin-like proprotein convertases (SPCs). RCN-3 is specifically bound to the paired basic amino-acid-cleaving enzyme-4 (PACE4) precursor protein and plays an important role in the biosynthesis of PACE4.


Pssm-ID: 320028 [Multi-domain]  Cd Length: 268  Bit Score: 501.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475556  44 PHDDAHGNFQYDHEAFLGREVAKEFDQLTPEESQARLGRIVDRMDRAGDGDGWVSLAELRAWIAHTQQRHIRDSVSAAWD 123
Cdd:cd16230     1 PHDDAHGNFQYDHEAFLGREVAKEFDQLSPEESQARLGRIVDRMDRAGDGDGWVSLAELRAWIAHTQQRHIRDSVSAAWQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475556 124 TYDTDRDGRVGWEELRNATYGHYAPGEEFHDVEDAETYKKMLARDERRFRVADQDGDSMATREELTAFLHPEEFPHMRDI 203
Cdd:cd16230    81 TYDTDRDGRVGWEELRNATYGHYEPGEEFHDVEDAETYKKMLARDERRFRVADQDGDSMATREELTAFLHPEEFPHMRDI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475556 204 VIAlpgakfprepltltpgvqpppgarvigpqpqcpfllqETLEDLDRNKDGYVQVEEYIADLYSAEPGEEEPAWVQTER 283
Cdd:cd16230   161 VVA-------------------------------------ETLEDLDKNKDGYVQVEEYIADLYSGEPGEEEPAWVQTER 203
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370475556 284 QQFRDFRDLNKDGHLDGSEVGHWVLPPAQDQPLVEANHLLHESDTDKDGRLSKAEILGNWNMFVG 348
Cdd:cd16230   204 QQFRQFRDLNKDGRLDGSEVGHWVLPPSQDQPLVEANHLLHESDTDKDGRLSKAEILGNWNMFVG 268
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
70-198 7.22e-09

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 53.64  E-value: 7.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475556  70 QLTPEESQARLGRIVDRMDRAGD--GDGWVSLAELRAWIAHTQQRHIRDSVSAAWDTYDTDRDGRVGWEELRNATyghya 147
Cdd:COG5126    21 VLERDDFEALFRRLWATLFSEADtdGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLL----- 95
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1370475556 148 pgeEFHDVEDAETykkmlardERRFRVADQDGDSMATREELTAFLHPEEFP 198
Cdd:COG5126    96 ---TALGVSEEEA--------DELFARLDTDGDGKISFEEFVAAVRDYYTP 135
EF-hand_7 pfam13499
EF-hand domain pair;
283-340 8.73e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 40.31  E-value: 8.73e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475556 283 RQQFRDFrDLNKDGHLDGSEVGHWVLPPAQDQPLV--EANHLLHESDTDKDGRLSKAEIL 340
Cdd:pfam13499   5 KEAFKLL-DSDGDGYLDVEELKKLLRKLEEGEPLSdeEVEELFKEFDLDKDGRISFEEFL 63
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
92-192 2.49e-03

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 38.89  E-value: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475556  92 DGDGWVSLAELRAWIAHTQQRHIRDSVSAAWDTYDTDRDGRVGWEELRNATYGHYAPGEEFHDVEDAETykkmlarderR 171
Cdd:NF041410   39 DGDGSVSQDELSSALSSKSDDGSLIDLSELFSDLDSDGDGSLSSDELAAAAPPPPPPPDQAPSTELADD----------L 108
                          90       100
                  ....*....|....*....|.
gi 1370475556 172 FRVADQDGDSMATREELTAFL 192
Cdd:NF041410  109 LSALDTDGDGSISSDELSAGL 129
PTZ00184 PTZ00184
calmodulin; Provisional
47-137 4.61e-03

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 37.05  E-value: 4.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475556  47 DAHGNFQYDHEAFLGREVAKEFDQLTPEESQARLgRIVDRmdragDGDGWVSLAELRAWIAHTQQRHIRDSVSAAWDTYD 126
Cdd:PTZ00184   57 DADGNGTIDFPEFLTLMARKMKDTDSEEEIKEAF-KVFDR-----DGNGFISAAELRHVMTNLGEKLTDEEVDEMIREAD 130
                          90
                  ....*....|.
gi 1370475556 127 TDRDGRVGWEE 137
Cdd:PTZ00184  131 VDGDGQINYEE 141
 
Name Accession Description Interval E-value
EFh_CREC_RCN3 cd16230
EF-hand, calcium binding motif, found in reticulocalbin-3 (RCN-3); RCN-3, also termed EF-hand ...
44-348 0e+00

EF-hand, calcium binding motif, found in reticulocalbin-3 (RCN-3); RCN-3, also termed EF-hand calcium-binding protein RLP49, is a putative six EF-hand Ca2+-binding protein that contains five RXXR (X is any amino acid) motifs and a C-terminal ER retrieval signal His-Asp-Glu-Leu (HDEL) tetrapeptide. The RXXR motif represents the target sequence of subtilisin-like proprotein convertases (SPCs). RCN-3 is specifically bound to the paired basic amino-acid-cleaving enzyme-4 (PACE4) precursor protein and plays an important role in the biosynthesis of PACE4.


Pssm-ID: 320028 [Multi-domain]  Cd Length: 268  Bit Score: 501.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475556  44 PHDDAHGNFQYDHEAFLGREVAKEFDQLTPEESQARLGRIVDRMDRAGDGDGWVSLAELRAWIAHTQQRHIRDSVSAAWD 123
Cdd:cd16230     1 PHDDAHGNFQYDHEAFLGREVAKEFDQLSPEESQARLGRIVDRMDRAGDGDGWVSLAELRAWIAHTQQRHIRDSVSAAWQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475556 124 TYDTDRDGRVGWEELRNATYGHYAPGEEFHDVEDAETYKKMLARDERRFRVADQDGDSMATREELTAFLHPEEFPHMRDI 203
Cdd:cd16230    81 TYDTDRDGRVGWEELRNATYGHYEPGEEFHDVEDAETYKKMLARDERRFRVADQDGDSMATREELTAFLHPEEFPHMRDI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475556 204 VIAlpgakfprepltltpgvqpppgarvigpqpqcpfllqETLEDLDRNKDGYVQVEEYIADLYSAEPGEEEPAWVQTER 283
Cdd:cd16230   161 VVA-------------------------------------ETLEDLDKNKDGYVQVEEYIADLYSGEPGEEEPAWVQTER 203
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370475556 284 QQFRDFRDLNKDGHLDGSEVGHWVLPPAQDQPLVEANHLLHESDTDKDGRLSKAEILGNWNMFVG 348
Cdd:cd16230   204 QQFRQFRDLNKDGRLDGSEVGHWVLPPSQDQPLVEANHLLHESDTDKDGRLSKAEILGNWNMFVG 268
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
44-348 3.36e-140

EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 (RCN-3), and similar proteins; The family corresponds to a group of six EF-hand Ca2+-binding proteins, including calumenin (also known as crocalbin or CBP-50), reticulocalbin-1 (RCN-1), reticulocalbin-3 (RCN-3), and similar proteins. Calumenin is an endo/sarcoplasmic reticulum (ER/SR) resident low-affinity Ca2+-binding protein that contains six EF-hand domains and a C-terminal SR retention signal His-Asp-Glu-Phe (HDEF) tetrapeptide. It functions as a novel regulator of SERCA2, and its expressional changes are tightly coupled with Ca2+-cycling of cardiomyocytes. It is also broadly involved in haemostasis and in the pathophysiology of thrombosis. Moreover, the extracellular calumenin acts as a suppressor of cell migration and tumor metastasis. RCN-1 is an endoplasmic reticulum resident Ca2+-binding protein with a carboxyl-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide signal. It acts as a potential negative regulator of B-RAF activation and can negatively modulate cardiomyocyte hypertrophy by inhibition of the mitogen-activated protein kinase signalling cascade. It also plays a key role in the development of doxorubicin-associated resistance. RCN-3 is a putative six EF-hand Ca2+-binding protein that contains five RXXR (X is any amino acid) motifs and a C-terminal ER retrieval signal HDEL tetrapeptide. The RXXR motif represents the target sequence of subtilisin-like proprotein convertases (SPCs). RCN-3 is specifically bound to the paired basic amino-acid-cleaving enzyme-4 (PACE4) precursor protein and plays an important role in the biosynthesis of PACE4.


Pssm-ID: 320024 [Multi-domain]  Cd Length: 264  Bit Score: 398.50  E-value: 3.36e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475556  44 PHDDAHGNFQYDHEAFLGREVAKEFDQLTPEESQARLGRIVDRMDraGDGDGWVSLAELRAWIAHTQQRHIRDSVSAAWD 123
Cdd:cd16226     1 HDDDGEHNPEYDHEAFLGKEEAKEFDQLTPEESKERLGIIVDKID--KNGDGFVTEEELKDWIKYVQKKYIREDVDRQWK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475556 124 TYDTDRDGRVGWEELRNATYGHYAPGEEFHDveDAETYKKMLARDERRFRVADQDGDSMATREELTAFLHPEEFPHMRDI 203
Cdd:cd16226    79 EYDPNKDGKLSWEEYKKATYGFLDDEEEDDD--LHESYKKMIRRDERRWKAADQDGDGKLTKEEFTAFLHPEEFPHMRDI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475556 204 VIalpgakfprepltltpgvqpppgarvigpqpqcpfllQETLEDLDRNKDGYVQVEEYIADLYSAEPGEEEPAWVQTER 283
Cdd:cd16226   157 VV-------------------------------------QETLEDIDKNKDGFISLEEYIGDMYRDDDEEEDPDWVKSER 199
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370475556 284 QQFRDFRDLNKDGHLDGSEVGHWVLPPAQDQPLVEANHLLHESDTDKDGRLSKAEILGNWNMFVG 348
Cdd:cd16226   200 EQFKEFRDKNKDGKMDREEVKDWILPEDYDHAEAEAKHLIYEADDDKDGKLTKEEILDKYDLFVG 264
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
44-347 8.87e-136

EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin/ERC45/calumenin)-EF hand family contains a group of six EF-hand, low-affinity Ca2+-binding proteins, including reticulocalbin (RCN-1), ER Ca2+-binding protein of 55 kDa (ERC-55, also known as TCBP-49 or E6BP), reticulocalbin-3 (RCN-3), Ca2+-binding protein of 45 kDa (Cab45 and its splice variant Cab45b), and calumenin ( also known as crocalbin or CBP-50). The proteins are not only localized in various parts of the secretory pathway, but also found in the cytosolic compartment and at the cell surface. They interact with different ligands or proteins and have been implicated in the secretory process, chaperone activity, signal transduction as well as in a large variety of disease processes.


Pssm-ID: 320021 [Multi-domain]  Cd Length: 267  Bit Score: 387.57  E-value: 8.87e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475556  44 PHDDAHGNFQYDHEAFLGREVAKEFDQLTPEESQARLGRIVDRMDraGDGDGWVSLAELRAWIAHTQQRHIRDSVSAAWD 123
Cdd:cd15899     1 HEMDGHLNSDYDHEAFLGKEEAEEFDQLTPEESKRRLGVIVSKMD--VDKDGFISAKELHSWILESFKRHAMEESKEQFR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475556 124 TYDTDRDGRVGWEELRNATYGHYAPGEEFHDV--EDAETYKKMLARDERRFRVADQDGDSMATREELTAFLHPEEFPHMR 201
Cdd:cd15899    79 AVDPDEDGHVSWDEYKNDTYGSVGDDEENVADniKEDEEYKKLLLKDKKRFEAADQDGDLILTLEEFLAFLHPEESPYML 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475556 202 DIVIalpgakfprepltltpgvqpppgarvigpqpqcpfllQETLEDLDRNKDGYVQVEEYIADLYSAEPGEEEPAWVQT 281
Cdd:cd15899   159 DFVI-------------------------------------KETLEDLDKNGDGFISLEEFISDPYSADENEEEPEWVKV 201
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370475556 282 ERQQFRDFRDLNKDGHLDGSEVGHWVLPPAQDQPLVEANHLLHESDTDKDGRLSKAEILGNWNMFV 347
Cdd:cd15899   202 EKERFVELRDKDKDGKLDGEELLSWVDPSNQEIALEEAKHLIAESDENKDGKLSPEEILDNHELFV 267
EFh_CREC_RCN1 cd16229
EF-hand, calcium binding motif, found in reticulocalbin-1 (RCN-1); RCN-1 is an endoplasmic ...
43-348 1.04e-120

EF-hand, calcium binding motif, found in reticulocalbin-1 (RCN-1); RCN-1 is an endoplasmic reticulum resident low-affinity Ca2+-binding protein with six EF-hand motifs and a carboxyl-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide signal. It is expressed at the cell surface. RCN-1 acts as a potential negative regulator of B-RAF activation and can negatively modulate cardiomyocyte hypertrophy by inhibition of the mitogen-activated protein kinase signaling cascade. It also plays a key role in the development of doxorubicin-associated resistance.


Pssm-ID: 320027 [Multi-domain]  Cd Length: 267  Bit Score: 349.56  E-value: 1.04e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475556  43 APHDDAHgNFQYDHEAFLGREVAKEFDQLTPEESQARLGRIVDRMDraGDGDGWVSLAELRAWIAHTQQRHIRDSVSAAW 122
Cdd:cd16229     1 QLHEDNQ-SFQYDHEAFLGKEEAKTFDQLTPEESKERLGKIVDRID--DDKDGFVTTEELKAWIKRVQKRYIYENVAKVW 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475556 123 DTYDTDRDGRVGWEELRNATYGHY-APGEEFHDVEDAETYKKMLARDERRFRVADQDGDSMATREELTAFLHPEEFPHMR 201
Cdd:cd16229    78 KDYDLNKDNKISWEEYKQATYGYYlGNPEEFQDATDQFSFKKMLPRDERRFKAADLDGDLAATREEFTAFLHPEEFEHMK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475556 202 DIVIAlpgakfprepltltpgvqpppgarvigpqpqcpfllqETLEDLDRNKDGYVQVEEYIADLYSAEPGEEEPAWVQT 281
Cdd:cd16229   158 DIVVL-------------------------------------ETLEDIDKNGDGFVDEDEYIADMFSHEEGGPEPDWVKT 200
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370475556 282 ERQQFRDFRDLNKDGHLDGSEVGHWVLPPAQDQPLVEANHLLHESDTDKDGRLSKAEILGNWNMFVG 348
Cdd:cd16229   201 EREQFSDFRDLNKDGKMDKEEIRHWILPQDYDHAQAEARHLVYESDKDKDQKLTKEEILDNWNMFVG 267
EFh_CREC_Calumenin cd16228
EF-hand, calcium binding motif, found in calumenin; Calumenin, also termed crocalbin, or IEF ...
45-348 2.29e-102

EF-hand, calcium binding motif, found in calumenin; Calumenin, also termed crocalbin, or IEF SSP 9302, is an endo/sarcoplasmic reticulum (ER/SR) resident low-affinity Ca2+-binding protein that contains six EF-hand domains and a C-terminal SR retention signal His-Asp-Glu-Phe (HDEF) tetrapeptide. It is highly expressed in various brain regions. Thus it plays an important role in migration and differentiation of neurons, and/or in Ca2+ signaling between glial cells and neurons. Calumenin is involved in Ca2+ homeostasis through interacting with ryanodine receptor RyR2 and SERCA2. It acts as a novel regulator of SERCA2, and its expressional changes are tightly coupled with Ca2+-cycling of cardiomyocytes. Calumenin also forms a Ca2+-dependent complex with thrombospondin-1, which is broadly involved in haemostasis and thrombosis. Moreover, calumenin is a molecular chaperone that endogenously regulates the vitamin K-dependent gamma-carboxylation of several proteins, including blood coagulation factors (such as FII, FVII, FIX, FX, and proteins C, S and Z), cell survival factors (Gas6) and bone metabolism proteins (such as matrix Gla protein or MGP, osteocalcin and periostin), through targeting the gamma-glutamyl carboxylase. It also functions as a charged F508del-cystic fibrosis transmembrane regulator (CFTR) folding modulator, as well as a G551D-CFTR associated protein. Furthermore, the extracellular calumenin acts as a suppressor of cell migration and tumor metastasis. It binds to and stabilizes fibulin-1, and further inactivates extracellular signal-regulated kinases 1 and 2 (ERK1/2) signaling.


Pssm-ID: 320026 [Multi-domain]  Cd Length: 263  Bit Score: 302.63  E-value: 2.29e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475556  45 HDDAHgNFQYDHEAFLGREVAKEFDQLTPEESQARLGRIVDRMDraGDGDGWVSLAELRAWIAHTQQRHIRDSVSAAWDT 124
Cdd:cd16228     3 HDDAQ-NFDYDHDAFLGAEEAKTFDQLTPEESKERLGKIVGKID--EDKDGFVTEDELKAWIKFAQKRWIYEDVERQWKG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475556 125 YDTDRDGRVGWEELRNATYGHYApgeEFHDVEDAETYKKMLARDERRFRVADQDGDSMATREELTAFLHPEEFPHMRDIV 204
Cdd:cd16228    80 HDLNEDGLVSWEEYKNATYGYIL---DDPDPDDGFNYKQMMVRDERRFKMADKDGDLRATKEEFTAFLHPEEYDYMKDIV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475556 205 IalpgakfprepltltpgvqpppgarvigpqpqcpfllQETLEDLDRNKDGYVQVEEYIADLYSAEPGEEEPAWVQTERQ 284
Cdd:cd16228   157 V-------------------------------------LETMEDIDKNGDGFIDLEEYIGDMYSQDGDADEPEWVKTERE 199
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370475556 285 QFRDFRDLNKDGHLDGSEVGHWVLPPAQDQPLVEANHLLHESDTDKDGRLSKAEILGNWNMFVG 348
Cdd:cd16228   200 QFTEFRDKNKDGKMDKEETKDWILPSDYDHAEAEARHLVYESDQNKDGKLTKEEIVDKYDLFVG 263
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
45-348 3.62e-63

EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This family corresponds to a group of uncharacterized RCN2-like proteins, which are mainly found in protostomes. Although their biological function remains unclear, they show high sequence similarity with RCN2 (also known as E6BP or TCBP-49), which is an endoplasmic reticulum resident low-affinity Ca2+-binding protein that has been implicated in immunity, redox homeostasis, cell cycle regulation and coagulation. Members in this family contain six copies of the EF-hand Ca2+-binding motif, but may lack a C-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide that is required for retention of RCN2 in the endoplasmic reticulum (ER).


Pssm-ID: 320025 [Multi-domain]  Cd Length: 263  Bit Score: 202.55  E-value: 3.62e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475556  45 HDDAHGNFQYDHEAFLG-REVAKEFDQLTPEESQARLGRIVDRMDRagDGDGWVSLAELRAWIAHTQQRHIRDSVSAAWD 123
Cdd:cd16227     2 AKDGEHNPEFDHEAVLGsRKEAEEFDELPPEEAKRRLAVLAKKMDL--NDDGFIDRKELKAWILRSFKMLDEEEANERFE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475556 124 TYDTDRDGRVGWEELRNATYGHYAPGEEFHDVEDAETYKKMLARDERRFRVADQDGDSMATREELTAFLHPEEFPHMRdi 203
Cdd:cd16227    80 EADEDGDGKVTWEEYLADSFGYDDEDNEEMIKDSTEDDLKLLEDDKEMFEAADLNKDGKLDKTEFSAFQHPEEYPHMH-- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475556 204 vialpgakfprepltltpgvqpppgarvigpqpqcPFLLQETLEDLDRNKDGYVQVEEYIADLYSAEPGEeepaWVQTER 283
Cdd:cd16227   158 -----------------------------------PVLIEQTLRDKDKDNDGFISFQEFLGDRAGHEDKE----WLLVEK 198
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370475556 284 QQFRDFRDLNKDGHLDGSEVGHWVLPPAQDQPLVEANHLLHESDTDKDGRLSKAEILGNWNMFVG 348
Cdd:cd16227   199 DRFDEDYDKDGDGKLDGEEILSWLVPDNEEIAEEEVDHLFASADDDHDDRLSFDEILDHHEIFVG 263
EFh_CREC_RCN2 cd16224
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2); RCN2, also termed ...
45-346 1.97e-55

EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2); RCN2, also termed calcium-binding protein ERC-55, or E6-binding protein (E6BP), or TCBP-49, is an endoplasmic reticulum resident low-affinity Ca2+-binding protein that has been implicated in immunity, redox homeostasis, cell cycle regulation and coagulation. It is associated with tumorigenesis, in particular with transformation of cells of the cervix induced by human papillomavirus (HPV), through binding to human papillomavirus (HPV) E6 oncogenic protein. It specifically interacts with vitamin D receptor among nuclear receptors. RCN2 contains an N-terminal signal sequence followed by six copies of the EF-hand Ca2+-binding motif, and a C-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide that is required for retention of RCN2 in the endoplasmic reticulum (ER).


Pssm-ID: 320022 [Multi-domain]  Cd Length: 268  Bit Score: 182.63  E-value: 1.97e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475556  45 HDDAHgNFQYDHEAFLGREV-AKEFDQLTPEESQARLGRIVDRMDRagDGDGWVSLAELRAWIAHTQQRHIRDSVSAAWD 123
Cdd:cd16224     3 PNGEH-NAEYDKEAFLGGEEdADEFAKLSPEEQQKRLKSIIKKIDT--DSDGFLTEEELSSWIQQSFRHYALEDAKQQFP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475556 124 TYDTDRDGRVGWEELRNATYGHYAPGEEFHDVEDAE--TYKKMLARDERRFRVADQDGDSMATREELTAFLHPEEFPHMR 201
Cdd:cd16224    80 EYDKDGDGAVTWDEYNMQMYDRVIDYDEDTVLDDEEeeSFRQLHLKDKKRFDKANTDGGPGLNLTEFIAFEHPEEVDYMT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475556 202 DIVIalpgakfprepltltpgvqpppgarvigpqpqcpfllQETLEDLDRNKDGYVQVEEYIADLYSAEPGEEEPAWVQT 281
Cdd:cd16224   160 EFVI-------------------------------------QEALEEHDKDGDGFISLEEFLGDYRKDPTANEDPEWIIV 202
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370475556 282 ERQQFRDFRDLNKDGHLDGSEVGHWVLPPAQDQPLVEANHLLHESDTDKDGRLSKAEILGNWNMF 346
Cdd:cd16224   203 EKDRFVNDYDKDNDGKLDPQELLPWVVPNNYGIAQEEALHLIDEMDLNGDGRLSEEEILENQDLF 267
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
47-346 1.59e-34

EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also termed stromal cell-derived factor 4 (SDF-4), is a soluble, lumenal Golgi resident low-affinity Ca2+-binding protein that contains six copies of the EF-hand Ca2+-binding motif. It is required for secretory pathway calcium ATPase1 (SPCA1)-dependent Ca2+ import into the trans-Golgi network (TGN) and plays an essential role in Ca2+-dependent secretory cargo sorting at the TGN.


Pssm-ID: 320023 [Multi-domain]  Cd Length: 278  Bit Score: 128.19  E-value: 1.59e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475556  47 DAHGNFQYDHEAFLGREVaKEFDQLTPEESQARLGRIVDRMDRagDGDGWVSLAELRAWIAHTQQRHIRDSVSAA---WD 123
Cdd:cd16225     4 DGHLNKEFHKEVFLGNEK-EEFEEDSEPKKRKKLKEIFKKVDV--NTDGFLSAEELEDWIMEKTQEHFQEAVEENeqiFK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475556 124 TYDTDRDGRVGWEELR---------NATYGHYAPGEEFHDVEDAETyKKMLARDERRFRVADQDGDSMATREELTAFLHP 194
Cdd:cd16225    81 AVDTDKDGNVSWEEYRvhfllskgySEEEAEEKIKNNEELKLDEDD-KEVLDRYKDRWSQADEPEDGLLDVEEFLSFRHP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475556 195 EefpHMRDIVIalpgakfprepltltpgvqpppgarvigpqpqcpFLLQETLEDLDRNKDGYVQVEEYIADLYSAEPGEE 274
Cdd:cd16225   160 E---HSRGMLK----------------------------------NMVKEILHDLDQDGDEKLTLDEFVSLPPGTVEEQQ 202
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370475556 275 EPA---WVQTERQQFRDFRDLNKDGHLDGSEVGHWVLPPAQDQPLVEANHLLHESDTDKDGRLSKAEILGNWNMF 346
Cdd:cd16225   203 AEDddeWKKERKKEFEEVIDLNHDGKVTKEELEEYMDPRNERHALNEAKQLIAVADENKDGKLSLEEILKNSDLF 277
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
70-198 7.22e-09

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 53.64  E-value: 7.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475556  70 QLTPEESQARLGRIVDRMDRAGD--GDGWVSLAELRAWIAHTQQRHIRDSVSAAWDTYDTDRDGRVGWEELRNATyghya 147
Cdd:COG5126    21 VLERDDFEALFRRLWATLFSEADtdGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLL----- 95
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1370475556 148 pgeEFHDVEDAETykkmlardERRFRVADQDGDSMATREELTAFLHPEEFP 198
Cdd:COG5126    96 ---TALGVSEEEA--------DELFARLDTDGDGKISFEEFVAAVRDYYTP 135
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
63-148 8.90e-07

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 47.86  E-value: 8.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475556  63 EVAKEFDQLTPEESQARLGRIVDRMDRagDGDGWVSLAELRAWIahTQQRHIRDSVSAAWDTYDTDRDGRVGWEELRNAT 142
Cdd:COG5126    54 EFVAGMESLFEATVEPFARAAFDLLDT--DGDGKISADEFRRLL--TALGVSEEEADELFARLDTDGDGKISFEEFVAAV 129

                  ....*.
gi 1370475556 143 YGHYAP 148
Cdd:COG5126   130 RDYYTP 135
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
74-192 1.30e-06

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 47.48  E-value: 1.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475556  74 EESQARLGRIVDRMDRagDGDGWVSLAELRAWIAHTQQrhirdsvsAAWDTYDTDRDGRVGWEELRnatyghyapgeEFH 153
Cdd:COG5126     1 DLQRRKLDRRFDLLDA--DGDGVLERDDFEALFRRLWA--------TLFSEADTDGDGRISREEFV-----------AGM 59
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1370475556 154 DVEDAETYKKMLardERRFRVADQDGDSMATREELTAFL 192
Cdd:COG5126    60 ESLFEATVEPFA---RAAFDLLDTDGDGKISADEFRRLL 95
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
239-340 8.23e-05

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 42.09  E-value: 8.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475556 239 PFLLQETLEDLDRNKDGYVQVEEYIADLYSAEPGEEEPawvqTERQQFRDFrDLNKDGHLDGSEVGHWVlpPAQDQPLVE 318
Cdd:COG5126    32 RRLWATLFSEADTDGDGRISREEFVAGMESLFEATVEP----FARAAFDLL-DTDGDGKISADEFRRLL--TALGVSEEE 104
                          90       100
                  ....*....|....*....|..
gi 1370475556 319 ANHLLHESDTDKDGRLSKAEIL 340
Cdd:COG5126   105 ADELFARLDTDGDGKISFEEFV 126
EF-hand_7 pfam13499
EF-hand domain pair;
283-340 8.73e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 40.31  E-value: 8.73e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475556 283 RQQFRDFrDLNKDGHLDGSEVGHWVLPPAQDQPLV--EANHLLHESDTDKDGRLSKAEIL 340
Cdd:pfam13499   5 KEAFKLL-DSDGDGYLDVEELKKLLRKLEEGEPLSdeEVEELFKEFDLDKDGRISFEEFL 63
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
283-340 3.48e-04

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 38.30  E-value: 3.48e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370475556 283 RQQFRDFrDLNKDGHLDGSEVGHWVLPPAQDQPLVEANHLLHESDTDKDGRLSKAEIL 340
Cdd:cd00051     3 REAFRLF-DKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFL 59
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
242-302 1.07e-03

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 37.14  E-value: 1.07e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370475556 242 LQETLEDLDRNKDGYVQVEEYIADLYSAEPGEEEPAWvqteRQQFRDFrDLNKDGHLDGSE 302
Cdd:cd00051     2 LREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEI----DEMIREV-DKDGDGKIDFEE 57
EF-hand_7 pfam13499
EF-hand domain pair;
79-143 1.34e-03

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 36.85  E-value: 1.34e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370475556  79 RLGRIVDRMDRagDGDGWVSLAELRAWIAHTQQRH--IRDSVSAAWDTYDTDRDGRVGWEELRNATY 143
Cdd:pfam13499   3 KLKEAFKLLDS--DGDGYLDVEELKKLLRKLEEGEplSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
92-192 2.49e-03

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 38.89  E-value: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475556  92 DGDGWVSLAELRAWIAHTQQRHIRDSVSAAWDTYDTDRDGRVGWEELRNATYGHYAPGEEFHDVEDAETykkmlarderR 171
Cdd:NF041410   39 DGDGSVSQDELSSALSSKSDDGSLIDLSELFSDLDSDGDGSLSSDELAAAAPPPPPPPDQAPSTELADD----------L 108
                          90       100
                  ....*....|....*....|.
gi 1370475556 172 FRVADQDGDSMATREELTAFL 192
Cdd:NF041410  109 LSALDTDGDGSISSDELSAGL 129
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
284-338 3.05e-03

Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.


Pssm-ID: 238009 [Multi-domain]  Cd Length: 67  Bit Score: 35.66  E-value: 3.05e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370475556 284 QQFRDFrDLNKDGHLDGSEV----GHWVLPPaqdqplVEANHLLHESDTDKDGRLSKAE 338
Cdd:cd00052     3 QIFRSL-DPDGDGLISGDEArpflGKSGLPR------SVLAQIWDLADTDKDGKLDKEE 54
PTZ00184 PTZ00184
calmodulin; Provisional
47-137 4.61e-03

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 37.05  E-value: 4.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370475556  47 DAHGNFQYDHEAFLGREVAKEFDQLTPEESQARLgRIVDRmdragDGDGWVSLAELRAWIAHTQQRHIRDSVSAAWDTYD 126
Cdd:PTZ00184   57 DADGNGTIDFPEFLTLMARKMKDTDSEEEIKEAF-KVFDR-----DGNGFISAAELRHVMTNLGEKLTDEEVDEMIREAD 130
                          90
                  ....*....|.
gi 1370475556 127 TDRDGRVGWEE 137
Cdd:PTZ00184  131 VDGDGQINYEE 141
EF-hand_7 pfam13499
EF-hand domain pair;
121-192 5.54e-03

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 34.92  E-value: 5.54e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370475556 121 AWDTYDTDRDGRVGWEELRNAtYGHYAPGEEFHDVEDAETYKKMlarderrfrvaDQDGDSMATREELTAFL 192
Cdd:pfam13499   7 AFKLLDSDGDGYLDVEELKKL-LRKLEEGEPLSDEEVEELFKEF-----------DLDKDGRISFEEFLELY 66
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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