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Conserved domains on  [gi|1907094045|ref|XP_036013981|]
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V-type proton ATPase subunit S1-like protein isoform X3 [Mus musculus]

Protein Classification

V-type proton ATPase subunit S1( domain architecture ID 10530743)

V-type proton ATPase subunit S1 is an accessory subunit of the proton-transporting vacuolar (V)-ATPase protein pump, which is required for luminal acidification of secretory vesicles

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VAS1_LD pfam05827
V-type proton ATPase subunit S1, luminal domain; This entry represents the luminal domain (LD) ...
 20-121 1.03e-20

V-type proton ATPase subunit S1, luminal domain; This entry represents the luminal domain (LD) found in eukaryotic V-type proton ATPase subunit S1 involved in V-ATPase V0 assembly, including Ac45 subunit (ATP6AP1). This domain folds as a globular beta-prism structure which is structurally similar to LAMP1-3, thus, the LD domain of Ac45 is an evolutionarily conserved member of the LAMP family. Ac45 is an ER membrane protein that guides the V-type ATPase into specialized subcellular compartments and is critical for Vo complex assembly as it connects to multiple Vo subunits and phospholipids in the c-ring. Missense mutations in the X-linked ATP6AP1 gene cause immunodeficiency in males that leads to recurrent bacterial infection, hepatopathy, cognitive impairment, and abnormal protein glycosylation.


:

Pssm-ID: 461752  Cd Length: 144  Bit Score: 84.07  E-value: 1.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094045  20 RLSLKFGDDEDPKdIDIRFTLTN-YNKLASQSWFSLHRVEIIFNNSVqATFNAT-GIYALSTYSYRCQRVSSLRrndaLL 97
Cdd:pfam05827  47 DLVLTYNNLNHNS-KLIKFLLSRhFYPVSARGYFTLDNVEIDYNGKA-ATFNSSrDISAPAGFSYHCSSVSFFS----DA 120

                          90       100
                  ....*....|....*....|....
gi 1907094045  98 LLSSSDDVTSLWEVTFIDFQIQGF 121
Cdd:pfam05827 121 LLVPNSPNNSKWRLTFDDFQIQPF 144
Ac45-VOA1_TM pfam20520
V0 complex accessory subunit Ac45/VOA1 transmembrane domain; This entry represents the ...
 138-173 2.54e-07

V0 complex accessory subunit Ac45/VOA1 transmembrane domain; This entry represents the transmembrane domain from ER/Golgi membrane proteins including V0 complex accessory subunit Ac45 (ATP6AP1, also known as V-type proton ATPase subunit S1) from animals and the yeast homolog V0 assembly protein 1 (VOA1) which are essential for V0 ATPase assembly, stability and function. In humans, mutations of ATP6AP1 cause immunodeficiency with hypogammaglobulinemia, hepatopathy and neurocognitive abnormalities. This entry also includes ER membrane BIG1 proteins from yeast, involved in cell wall biogenesis.


:

Pssm-ID: 466669  Cd Length: 39  Bit Score: 45.44  E-value: 2.54e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1907094045 138 FSPAILIGLAMSLILLLVLAYALHMLIYLRYLDRHY 173
Cdd:pfam20520   3 FTPGIWMGLLVSLILLLILYVGLSMLSSLQTYDRFD 38
 
Name Accession Description Interval E-value
VAS1_LD pfam05827
V-type proton ATPase subunit S1, luminal domain; This entry represents the luminal domain (LD) ...
 20-121 1.03e-20

V-type proton ATPase subunit S1, luminal domain; This entry represents the luminal domain (LD) found in eukaryotic V-type proton ATPase subunit S1 involved in V-ATPase V0 assembly, including Ac45 subunit (ATP6AP1). This domain folds as a globular beta-prism structure which is structurally similar to LAMP1-3, thus, the LD domain of Ac45 is an evolutionarily conserved member of the LAMP family. Ac45 is an ER membrane protein that guides the V-type ATPase into specialized subcellular compartments and is critical for Vo complex assembly as it connects to multiple Vo subunits and phospholipids in the c-ring. Missense mutations in the X-linked ATP6AP1 gene cause immunodeficiency in males that leads to recurrent bacterial infection, hepatopathy, cognitive impairment, and abnormal protein glycosylation.


Pssm-ID: 461752  Cd Length: 144  Bit Score: 84.07  E-value: 1.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094045  20 RLSLKFGDDEDPKdIDIRFTLTN-YNKLASQSWFSLHRVEIIFNNSVqATFNAT-GIYALSTYSYRCQRVSSLRrndaLL 97
Cdd:pfam05827  47 DLVLTYNNLNHNS-KLIKFLLSRhFYPVSARGYFTLDNVEIDYNGKA-ATFNSSrDISAPAGFSYHCSSVSFFS----DA 120

                          90       100
                  ....*....|....*....|....
gi 1907094045  98 LLSSSDDVTSLWEVTFIDFQIQGF 121
Cdd:pfam05827 121 LLVPNSPNNSKWRLTFDDFQIQPF 144
Ac45-VOA1_TM pfam20520
V0 complex accessory subunit Ac45/VOA1 transmembrane domain; This entry represents the ...
 138-173 2.54e-07

V0 complex accessory subunit Ac45/VOA1 transmembrane domain; This entry represents the transmembrane domain from ER/Golgi membrane proteins including V0 complex accessory subunit Ac45 (ATP6AP1, also known as V-type proton ATPase subunit S1) from animals and the yeast homolog V0 assembly protein 1 (VOA1) which are essential for V0 ATPase assembly, stability and function. In humans, mutations of ATP6AP1 cause immunodeficiency with hypogammaglobulinemia, hepatopathy and neurocognitive abnormalities. This entry also includes ER membrane BIG1 proteins from yeast, involved in cell wall biogenesis.


Pssm-ID: 466669  Cd Length: 39  Bit Score: 45.44  E-value: 2.54e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1907094045 138 FSPAILIGLAMSLILLLVLAYALHMLIYLRYLDRHY 173
Cdd:pfam20520   3 FTPGIWMGLLVSLILLLILYVGLSMLSSLQTYDRFD 38
 
Name Accession Description Interval E-value
VAS1_LD pfam05827
V-type proton ATPase subunit S1, luminal domain; This entry represents the luminal domain (LD) ...
 20-121 1.03e-20

V-type proton ATPase subunit S1, luminal domain; This entry represents the luminal domain (LD) found in eukaryotic V-type proton ATPase subunit S1 involved in V-ATPase V0 assembly, including Ac45 subunit (ATP6AP1). This domain folds as a globular beta-prism structure which is structurally similar to LAMP1-3, thus, the LD domain of Ac45 is an evolutionarily conserved member of the LAMP family. Ac45 is an ER membrane protein that guides the V-type ATPase into specialized subcellular compartments and is critical for Vo complex assembly as it connects to multiple Vo subunits and phospholipids in the c-ring. Missense mutations in the X-linked ATP6AP1 gene cause immunodeficiency in males that leads to recurrent bacterial infection, hepatopathy, cognitive impairment, and abnormal protein glycosylation.


Pssm-ID: 461752  Cd Length: 144  Bit Score: 84.07  E-value: 1.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907094045  20 RLSLKFGDDEDPKdIDIRFTLTN-YNKLASQSWFSLHRVEIIFNNSVqATFNAT-GIYALSTYSYRCQRVSSLRrndaLL 97
Cdd:pfam05827  47 DLVLTYNNLNHNS-KLIKFLLSRhFYPVSARGYFTLDNVEIDYNGKA-ATFNSSrDISAPAGFSYHCSSVSFFS----DA 120

                          90       100
                  ....*....|....*....|....
gi 1907094045  98 LLSSSDDVTSLWEVTFIDFQIQGF 121
Cdd:pfam05827 121 LLVPNSPNNSKWRLTFDDFQIQPF 144
Ac45-VOA1_TM pfam20520
V0 complex accessory subunit Ac45/VOA1 transmembrane domain; This entry represents the ...
 138-173 2.54e-07

V0 complex accessory subunit Ac45/VOA1 transmembrane domain; This entry represents the transmembrane domain from ER/Golgi membrane proteins including V0 complex accessory subunit Ac45 (ATP6AP1, also known as V-type proton ATPase subunit S1) from animals and the yeast homolog V0 assembly protein 1 (VOA1) which are essential for V0 ATPase assembly, stability and function. In humans, mutations of ATP6AP1 cause immunodeficiency with hypogammaglobulinemia, hepatopathy and neurocognitive abnormalities. This entry also includes ER membrane BIG1 proteins from yeast, involved in cell wall biogenesis.


Pssm-ID: 466669  Cd Length: 39  Bit Score: 45.44  E-value: 2.54e-07
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1907094045 138 FSPAILIGLAMSLILLLVLAYALHMLIYLRYLDRHY 173
Cdd:pfam20520   3 FTPGIWMGLLVSLILLLILYVGLSMLSSLQTYDRFD 38
 
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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