NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1833563400|ref|NP_057631|]
View 

45 kDa calcium-binding protein isoform 1 precursor [Homo sapiens]

Protein Classification

CREC-EF hand family protein; EF-hand domain-containing protein( domain architecture ID 11610931)

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
60-297 1.11e-128

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: 368.94  E-value: 1.11e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833563400  60 LEMDGHLNRGFHQEVFLGKDLGGFDEDAEPRRsRRKLMVIFSKVDVNTDRKISAKEMQRWIMEKTAEHFQEAMEESKTHF 139
Cdd:cd16225     1 LERDGHLNKEFHKEVFLGNEKEEFEEDSEPKK-RKKLKEIFKKVDVNTDGFLSAEELEDWIMEKTQEHFQEAVEENEQIF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833563400 140 RAVDPDGDGHVSWDEYKVKFLASKGHSEKEVADAIRLNEELKVDEETQEVLENLKDRWYQADsPPADLLLTEEEFLSFLH 219
Cdd:cd16225    80 KAVDTDKDGNVSWEEYRVHFLLSKGYSEEEAEEKIKNNEELKLDEDDKEVLDRYKDRWSQAD-EPEDGLLDVEEFLSFRH 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1833563400 220 PEHSRGMLRFMVKEIVRDLDQDGDKQLSVPEFISLPVGTVENQQGQDiDDNWVKDRKKEFEELIDSNHDGIVTAEELE 297
Cdd:cd16225   159 PEHSRGMLKNMVKEILHDLDQDGDEKLTLDEFVSLPPGTVEEQQAED-DDEWKKERKKEFEEVIDLNHDGKVTKEELE 235
 
Name Accession Description Interval E-value
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
60-297 1.11e-128

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: 368.94  E-value: 1.11e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833563400  60 LEMDGHLNRGFHQEVFLGKDLGGFDEDAEPRRsRRKLMVIFSKVDVNTDRKISAKEMQRWIMEKTAEHFQEAMEESKTHF 139
Cdd:cd16225     1 LERDGHLNKEFHKEVFLGNEKEEFEEDSEPKK-RKKLKEIFKKVDVNTDGFLSAEELEDWIMEKTQEHFQEAVEENEQIF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833563400 140 RAVDPDGDGHVSWDEYKVKFLASKGHSEKEVADAIRLNEELKVDEETQEVLENLKDRWYQADsPPADLLLTEEEFLSFLH 219
Cdd:cd16225    80 KAVDTDKDGNVSWEEYRVHFLLSKGYSEEEAEEKIKNNEELKLDEDDKEVLDRYKDRWSQAD-EPEDGLLDVEEFLSFRH 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1833563400 220 PEHSRGMLRFMVKEIVRDLDQDGDKQLSVPEFISLPVGTVENQQGQDiDDNWVKDRKKEFEELIDSNHDGIVTAEELE 297
Cdd:cd16225   159 PEHSRGMLKNMVKEILHDLDQDGDEKLTLDEFVSLPPGTVEEQQAED-DDEWKKERKKEFEEVIDLNHDGKVTKEELE 235
EF-hand_7 pfam13499
EF-hand domain pair;
93-156 2.74e-07

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 47.25  E-value: 2.74e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1833563400  93 RRKLMVIFSKVDVNTDRKISAKEMQRwIMEKTAEHFQEAMEESKTHFRAVDPDGDGHVSWDEYK 156
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKK-LLRKLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFL 63
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
83-154 3.02e-07

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 49.02  E-value: 3.02e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1833563400  83 FDEDAEPRRSRRKLMVIFSKVDVNTDRKISAKEMQRWI--MEKTAEHFQEAmeeskthFRAVDPDGDGHVSWDE 154
Cdd:COG5126    58 GMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLtaLGVSEEEADEL-------FARLDTDGDGKISFEE 124
 
Name Accession Description Interval E-value
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
60-297 1.11e-128

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: 368.94  E-value: 1.11e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833563400  60 LEMDGHLNRGFHQEVFLGKDLGGFDEDAEPRRsRRKLMVIFSKVDVNTDRKISAKEMQRWIMEKTAEHFQEAMEESKTHF 139
Cdd:cd16225     1 LERDGHLNKEFHKEVFLGNEKEEFEEDSEPKK-RKKLKEIFKKVDVNTDGFLSAEELEDWIMEKTQEHFQEAVEENEQIF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833563400 140 RAVDPDGDGHVSWDEYKVKFLASKGHSEKEVADAIRLNEELKVDEETQEVLENLKDRWYQADsPPADLLLTEEEFLSFLH 219
Cdd:cd16225    80 KAVDTDKDGNVSWEEYRVHFLLSKGYSEEEAEEKIKNNEELKLDEDDKEVLDRYKDRWSQAD-EPEDGLLDVEEFLSFRH 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1833563400 220 PEHSRGMLRFMVKEIVRDLDQDGDKQLSVPEFISLPVGTVENQQGQDiDDNWVKDRKKEFEELIDSNHDGIVTAEELE 297
Cdd:cd16225   159 PEHSRGMLKNMVKEILHDLDQDGDEKLTLDEFVSLPPGTVEEQQAED-DDEWKKERKKEFEEVIDLNHDGKVTKEELE 235
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
60-297 4.24e-105

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: 308.99  E-value: 4.24e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833563400  60 LEMDGHLNRGFHQEVFLGKDLGGFDEDAEPRRSRRKLMVIFSKVDVNTDRKISAKEMQRWIMEKTAEHfqeAMEESKTHF 139
Cdd:cd15899     1 HEMDGHLNSDYDHEAFLGKEEAEEFDQLTPEESKRRLGVIVSKMDVDKDGFISAKELHSWILESFKRH---AMEESKEQF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833563400 140 RAVDPDGDGHVSWDEYKVKFLASKGHSEKEVADAIrlneelKVDEETQEVLENLKDRWYQADsPPADLLLTEEEFLSFLH 219
Cdd:cd15899    78 RAVDPDEDGHVSWDEYKNDTYGSVGDDEENVADNI------KEDEEYKKLLLKDKKRFEAAD-QDGDLILTLEEFLAFLH 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1833563400 220 PEHSRGMLRFMVKEIVRDLDQDGDKQLSVPEFISLPVGTVENQQGQdiddNWVKDRKKEFEELIDSNHDGIVTAEELE 297
Cdd:cd15899   151 PEESPYMLDFVIKETLEDLDKNGDGFISLEEFISDPYSADENEEEP----EWVKVEKERFVELRDKDKDGKLDGEELL 224
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
63-296 2.34e-38

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: 137.33  E-value: 2.34e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833563400  63 DGHLNRGFHQEVFLGKDLGG-FDEdAEPRRSRRKLMVIFSKVDVNTDRKISAKEMQRWImEKTAEHFQeaMEESKTHFRA 141
Cdd:cd16226     4 DGEHNPEYDHEAFLGKEEAKeFDQ-LTPEESKERLGIIVDKIDKNGDGFVTEEELKDWI-KYVQKKYI--REDVDRQWKE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833563400 142 VDPDGDGHVSWDEYKVkflASKGHSEKEvadairlNEELKVDEETQEVLENLKDRWYQADSPpADLLLTEEEFLSFLHPE 221
Cdd:cd16226    80 YDPNKDGKLSWEEYKK---ATYGFLDDE-------EEDDDLHESYKKMIRRDERRWKAADQD-GDGKLTKEEFTAFLHPE 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1833563400 222 HSRGMLRFMVKEIVRDLDQDGDKQLSVPEFIslpvGTVENQQGQDIDDNWVKDRKKEFEELIDSNHDGIVTAEEL 296
Cdd:cd16226   149 EFPHMRDIVVQETLEDIDKNKDGFISLEEYI----GDMYRDDDEEEDPDWVKSEREQFKEFRDKNKDGKMDREEV 219
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
63-295 1.08e-26

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: 106.25  E-value: 1.08e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833563400  63 DGHLNRGFHQEVFLG--KDLGGFDEdAEPRRSRRKLMVIFSKVDVNTDRKISAKEMQRWIMEKtaehFQE-AMEESKTHF 139
Cdd:cd16227     4 DGEHNPEFDHEAVLGsrKEAEEFDE-LPPEEAKRRLAVLAKKMDLNDDGFIDRKELKAWILRS----FKMlDEEEANERF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833563400 140 RAVDPDGDGHVSWDEYKVKflaSKGHSEKEVADAIrlneeLKVDEETQEVLENLKDRWYQADSPpADLLLTEEEFLSFLH 219
Cdd:cd16227    79 EEADEDGDGKVTWEEYLAD---SFGYDDEDNEEMI-----KDSTEDDLKLLEDDKEMFEAADLN-KDGKLDKTEFSAFQH 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1833563400 220 PEHSRGMLRFMVKEIVRDLDQDGDKQLSVPEFISlpvgtvenQQGQDIDDNWVKDRKKEFEELIDSNHDGIVTAEE 295
Cdd:cd16227   150 PEEYPHMHPVLIEQTLRDKDKDNDGFISFQEFLG--------DRAGHEDKEWLLVEKDRFDEDYDKDGDGKLDGEE 217
EFh_CREC_RCN2 cd16224
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2); RCN2, also termed ...
62-296 1.39e-24

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: 100.58  E-value: 1.39e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833563400  62 MDGHLNRGFHQEVFLG--KDLGGFdEDAEPRRSRRKLMVIFSKVDVNTDRKISAKEMQRWImEKTAEHFqeAMEESKTHF 139
Cdd:cd16224     3 PNGEHNAEYDKEAFLGgeEDADEF-AKLSPEEQQKRLKSIIKKIDTDSDGFLTEEELSSWI-QQSFRHY--ALEDAKQQF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833563400 140 RAVDPDGDGHVSWDEYKVkflaskgHSEKEVADairLNEELKVDEETQEVLENL----KDRWYQA--DSPPAdllLTEEE 213
Cdd:cd16224    79 PEYDKDGDGAVTWDEYNM-------QMYDRVID---YDEDTVLDDEEEESFRQLhlkdKKRFDKAntDGGPG---LNLTE 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833563400 214 FLSFLHPEHSRGMLRFMVKEIVRDLDQDGDKQLSVPEFIslpvGTVENQQGQDIDDNWVKDRKKEFEELIDSNHDGIVTA 293
Cdd:cd16224   146 FIAFEHPEEVDYMTEFVIQEALEEHDKDGDGFISLEEFL----GDYRKDPTANEDPEWIIVEKDRFVNDYDKDNDGKLDP 221

                  ...
gi 1833563400 294 EEL 296
Cdd:cd16224   222 QEL 224
EFh_CREC_Calumenin cd16228
EF-hand, calcium binding motif, found in calumenin; Calumenin, also termed crocalbin, or IEF ...
63-295 1.39e-23

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: 97.70  E-value: 1.39e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833563400  63 DGHLNRGFHQEVFLGKDLGGFDEDAEPRRSRRKLMVIFSKVDVNTDRKISAKEMQRWIMEKTAEHFQEAMEEsktHFRAV 142
Cdd:cd16228     4 DDAQNFDYDHDAFLGAEEAKTFDQLTPEESKERLGKIVGKIDEDKDGFVTEDELKAWIKFAQKRWIYEDVER---QWKGH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833563400 143 DPDGDGHVSWDEYKVkflASKGH--SEKEVADAIRLNEELKVDEEtqevlenlkdRWYQADSPpADLLLTEEEFLSFLHP 220
Cdd:cd16228    81 DLNEDGLVSWEEYKN---ATYGYilDDPDPDDGFNYKQMMVRDER----------RFKMADKD-GDLRATKEEFTAFLHP 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1833563400 221 EHSRGMLRFMVKEIVRDLDQDGDKQLSVPEFIslpvGTVENQQGQDIDDNWVKDRKKEFEELIDSNHDGIVTAEE 295
Cdd:cd16228   147 EEYDYMKDIVVLETMEDIDKNGDGFIDLEEYI----GDMYSQDGDADEPEWVKTEREQFTEFRDKNKDGKMDKEE 217
EFh_CREC_RCN3 cd16230
EF-hand, calcium binding motif, found in reticulocalbin-3 (RCN-3); RCN-3, also termed EF-hand ...
63-306 1.23e-20

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: 89.65  E-value: 1.23e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833563400  63 DGHLNRGFHQEVFLGKDLGGFDEDAEPRRSRRKLMVIFSKVDV--NTDRKISAKEMQRWIMEKTAEHFQEAMEESkthFR 140
Cdd:cd16230     4 DAHGNFQYDHEAFLGREVAKEFDQLSPEESQARLGRIVDRMDRagDGDGWVSLAELRAWIAHTQQRHIRDSVSAA---WQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833563400 141 AVDPDGDGHVSWDEYKVkflASKGHSEKevadairlNEELK--VDEETQEVLENLKDRWYQADSPPADLLLTEEEFLSFL 218
Cdd:cd16230    81 TYDTDRDGRVGWEELRN---ATYGHYEP--------GEEFHdvEDAETYKKMLARDERRFRVADQDGDSMATREELTAFL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833563400 219 HPEHSRGMLRFMVKEIVRDLDQDGDKQLSVPEFIS-LPVGTVENQQGQdiddnWVKDRKKEFEELIDSNHDGIVTAEELE 297
Cdd:cd16230   150 HPEEFPHMRDIVVAETLEDLDKNKDGYVQVEEYIAdLYSGEPGEEEPA-----WVQTERQQFRQFRDLNKDGRLDGSEVG 224
                         250
                  ....*....|.
gi 1833563400 298 N--VPTLPLQP 306
Cdd:cd16230   225 HwvLPPSQDQP 235
EFh_CREC_RCN1 cd16229
EF-hand, calcium binding motif, found in reticulocalbin-1 (RCN-1); RCN-1 is an endoplasmic ...
70-296 3.41e-19

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: 85.70  E-value: 3.41e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833563400  70 FHQEVFLGKDLGGFDEDAEPRRSRRKLMVIFSKVDVNTDRKISAKEMQRWIMEKTAEHFQEAMEESkthFRAVDPDGDGH 149
Cdd:cd16229    11 YDHEAFLGKEEAKTFDQLTPEESKERLGKIVDRIDDDKDGFVTTEELKAWIKRVQKRYIYENVAKV---WKDYDLNKDNK 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833563400 150 VSWDEYKVkflASKGHSEKEVADAIRLNEELKVdeetQEVLENLKDRWYQADSPpADLLLTEEEFLSFLHPEHSRGMLRF 229
Cdd:cd16229    88 ISWEEYKQ---ATYGYYLGNPEEFQDATDQFSF----KKMLPRDERRFKAADLD-GDLAATREEFTAFLHPEEFEHMKDI 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1833563400 230 MVKEIVRDLDQDGDKQLSVPEFISLPVGTVENQQGQDiddnWVKDRKKEFEELIDSNHDGIVTAEEL 296
Cdd:cd16229   160 VVLETLEDIDKNGDGFVDEDEYIADMFSHEEGGPEPD----WVKTEREQFSDFRDLNKDGKMDKEEI 222
EF-hand_7 pfam13499
EF-hand domain pair;
93-156 2.74e-07

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 47.25  E-value: 2.74e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1833563400  93 RRKLMVIFSKVDVNTDRKISAKEMQRwIMEKTAEHFQEAMEESKTHFRAVDPDGDGHVSWDEYK 156
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKK-LLRKLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFL 63
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
83-154 3.02e-07

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 49.02  E-value: 3.02e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1833563400  83 FDEDAEPRRSRRKLMVIFSKVDVNTDRKISAKEMQRWI--MEKTAEHFQEAmeeskthFRAVDPDGDGHVSWDE 154
Cdd:COG5126    58 GMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLtaLGVSEEEADEL-------FARLDTDGDGKISFEE 124
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
95-154 1.38e-06

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: 45.23  E-value: 1.38e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833563400  95 KLMVIFSKVDVNTDRKISAKEMQRwIMEKTAEHFQEamEESKTHFRAVDPDGDGHVSWDE 154
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKA-ALKSLGEGLSE--EEIDEMIREVDKDGDGKIDFEE 57
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
93-254 5.48e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 45.55  E-value: 5.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833563400  93 RRKLMVIFSKVDVNTDRKISAKEMQRwimektaehfqEAMEESKTHFRAVDPDGDGHVSWDEYKvkflaskghsekevad 172
Cdd:COG5126     4 RRKLDRRFDLLDADGDGVLERDDFEA-----------LFRRLWATLFSEADTDGDGRISREEFV---------------- 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833563400 173 AIRLNEELKVDEETQEVLENLKDRwyqaDSppaDLLLTEEEFLSFLHpehSRGMLRFMVKEIVRDLDQDGDKQLSVPEFI 252
Cdd:COG5126    57 AGMESLFEATVEPFARAAFDLLDT----DG---DGKISADEFRRLLT---ALGVSEEEADELFARLDTDGDGKISFEEFV 126

                  ..
gi 1833563400 253 SL 254
Cdd:COG5126   127 AA 128
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
139-296 2.55e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 43.63  E-value: 2.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833563400 139 FRAVDPDGDGHVSWDEYKVKFLAskghsekevadairlneelkvdeetqevlenLKDRWYQADSPPADLLLTEEEFLSFL 218
Cdd:COG5126    11 FDLLDADGDGVLERDDFEALFRR-------------------------------LWATLFSEADTDGDGRISREEFVAGM 59
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1833563400 219 HPEHSRGMLRFmVKEIVRDLDQDGDKQLSVPEFISLpvgtvenQQGQDIDDnwvkDRKKEFEELIDSNHDGIVTAEEL 296
Cdd:COG5126    60 ESLFEATVEPF-ARAAFDLLDTDGDGKISADEFRRL-------LTALGVSE----EEADELFARLDTDGDGKISFEEF 125
EF-hand_7 pfam13499
EF-hand domain pair;
191-254 2.23e-03

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 36.08  E-value: 2.23e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1833563400 191 ENLKDRWYQADSPpADLLLTEEEFLSFLHP-EHSRGMLRFMVKEIVRDLDQDGDKQLSVPEFISL 254
Cdd:pfam13499   2 EKLKEAFKLLDSD-GDGYLDVEELKKLLRKlEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLEL 65
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
191-297 2.66e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 37.46  E-value: 2.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833563400 191 ENLKDRWYQADSPpADLLLTEEEFLSflhpehsrgMLRFMVKEIVRDLDQDGDKQLSVPEFISLPVGTVENQQGQDIDdn 270
Cdd:COG5126     5 RKLDRRFDLLDAD-GDGVLERDDFEA---------LFRRLWATLFSEADTDGDGRISREEFVAGMESLFEATVEPFAR-- 72
                          90       100
                  ....*....|....*....|....*..
gi 1833563400 271 wvkdrkKEFeELIDSNHDGIVTAEELE 297
Cdd:COG5126    73 ------AAF-DLLDTDGDGKISADEFR 92
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH