VAS1_BOVIN
ID VAS1_BOVIN Reviewed; 468 AA.
AC P40682;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=V-type proton ATPase subunit S1;
DE Short=V-ATPase subunit S1;
DE AltName: Full=V-ATPase Ac45 subunit;
DE AltName: Full=V-ATPase S1 accessory protein;
DE AltName: Full=Vacuolar proton pump subunit S1;
DE Flags: Precursor;
GN Name=ATP6AP1; Synonyms=ATP6IP1, ATP6S1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 378-388.
RC TISSUE=Adrenal chromaffin;
RX PubMed=7929063; DOI=10.1016/s0021-9258(19)51053-5;
RA Supek F., Supekova L., Mandiyan S., Pan Y.-C.E., Nelson H., Nelson N.;
RT "A novel accessory subunit for vacuolar H(+)-ATPase from chromaffin
RT granules.";
RL J. Biol. Chem. 269:24102-24106(1994).
RN [2] {ECO:0007744|PDB:6XBW, ECO:0007744|PDB:6XBY}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.37 ANGSTROMS), GLYCOSYLATION AT
RP ASN-271; ASN-294; ASN-301; ASN-348; ASN-355 AND ASN-404, AND DISULFIDE
RP BONDS.
RX PubMed=32764564; DOI=10.1038/s41467-020-17762-9;
RA Wang R., Long T., Hassan A., Wang J., Sun Y., Xie X.S., Li X.;
RT "Cryo-EM structures of intact V-ATPase from bovine brain.";
RL Nat. Commun. 11:3921-3921(2020).
CC -!- FUNCTION: Accessory subunit of the proton-transporting vacuolar (V)-
CC ATPase protein pump, which is required for luminal acidification of
CC secretory vesicles (PubMed:32764564). Guides the V-type ATPase into
CC specialized subcellular compartments, such as neuroendocrine regulated
CC secretory vesicles or the ruffled border of the osteoclast, thereby
CC regulating its activity. Involved in membrane trafficking and Ca(2+)-
CC dependent membrane fusion. May play a role in the assembly of the V-
CC type ATPase complex. In aerobic conditions, involved in intracellular
CC iron homeostasis, thus triggering the activity of Fe(2+) prolyl
CC hydroxylase (PHD) enzymes, and leading to HIF1A hydroxylation and
CC subsequent proteasomal degradation (By similarity). In islets of
CC Langerhans cells, may regulate the acidification of dense-core
CC secretory granules (By similarity). {ECO:0000250|UniProtKB:Q15904,
CC ECO:0000250|UniProtKB:Q9R1Q9, ECO:0000269|PubMed:32764564}.
CC -!- SUBUNIT: Accessory component of the multisubunit proton-transporting
CC vacuolar (V)-ATPase protein pump (PubMed:32764564). Interacts (via N-
CC terminus) with ATP6AP2 (via N-terminus) (PubMed:32764564). Interacts
CC with RNASEK (By similarity). {ECO:0000250|UniProtKB:Q15904,
CC ECO:0000269|PubMed:32764564}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q15904}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q15904}. Endoplasmic reticulum-Golgi
CC intermediate compartment membrane {ECO:0000250|UniProtKB:Q15904}.
CC Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane
CC {ECO:0000250|UniProtKB:O54715}; Single-pass type I membrane protein
CC {ECO:0000305}. Cytoplasmic vesicle, clathrin-coated vesicle membrane
CC {ECO:0000269|PubMed:32764564}; Single-pass type I membrane protein
CC {ECO:0000305}. Note=Not detected in trans-Golgi network.
CC {ECO:0000250|UniProtKB:Q15904}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:32764564}.
CC -!- SIMILARITY: Belongs to the vacuolar ATPase subunit S1 family.
CC {ECO:0000305}.
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DR EMBL; U10039; AAA50752.1; -; mRNA.
DR PIR; A55116; A55116.
DR RefSeq; NP_787000.1; NM_175806.2.
DR PDB; 6XBW; EM; 3.37 A; s=1-468.
DR PDB; 6XBY; EM; 3.79 A; s=1-468.
DR PDB; 7KHR; EM; 3.62 A; s=1-468.
DR PDBsum; 6XBW; -.
DR PDBsum; 6XBY; -.
DR PDBsum; 7KHR; -.
DR AlphaFoldDB; P40682; -.
DR SMR; P40682; -.
DR CORUM; P40682; -.
DR STRING; 9913.ENSBTAP00000016073; -.
DR PaxDb; P40682; -.
DR PeptideAtlas; P40682; -.
DR PRIDE; P40682; -.
DR Ensembl; ENSBTAT00000016073; ENSBTAP00000016073; ENSBTAG00000012117.
DR GeneID; 327687; -.
DR KEGG; bta:327687; -.
DR CTD; 537; -.
DR VEuPathDB; HostDB:ENSBTAG00000012117; -.
DR VGNC; VGNC:26306; ATP6AP1.
DR eggNOG; KOG3868; Eukaryota.
DR GeneTree; ENSGT00940000156650; -.
DR HOGENOM; CLU_039408_1_0_1; -.
DR InParanoid; P40682; -.
DR OMA; WFTMEHL; -.
DR OrthoDB; 1111170at2759; -.
DR TreeFam; TF325819; -.
DR Proteomes; UP000009136; Chromosome X.
DR Bgee; ENSBTAG00000012117; Expressed in spermatocyte and 103 other tissues.
DR ExpressionAtlas; P40682; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0033176; C:proton-transporting V-type ATPase complex; IBA:GO_Central.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031267; F:small GTPase binding; IEA:Ensembl.
DR GO; GO:0006879; P:cellular iron ion homeostasis; ISS:UniProtKB.
DR GO; GO:0036295; P:cellular response to increased oxygen levels; ISS:UniProtKB.
DR GO; GO:0099638; P:endosome to plasma membrane protein transport; IEA:Ensembl.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0036035; P:osteoclast development; IEA:Ensembl.
DR GO; GO:0030641; P:regulation of cellular pH; IBA:GO_Central.
DR InterPro; IPR008388; Ac45_acc_su.
DR PANTHER; PTHR12471; PTHR12471; 1.
DR Pfam; PF05827; ATP-synt_S1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasmic vesicle; Direct protein sequencing;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW Signal; Synapse; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..468
FT /note="V-type proton ATPase subunit S1"
FT /id="PRO_0000002542"
FT PROPEP 36..228
FT /evidence="ECO:0000250|UniProtKB:Q9R1Q9"
FT /id="PRO_0000454040"
FT TOPO_DOM 36..417
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 439..468
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT SITE 228..229
FT /note="Cleavage; by furin"
FT /evidence="ECO:0000250|UniProtKB:Q9R1Q9"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:32764564,
FT ECO:0007744|PDB:6XBW, ECO:0007744|PDB:6XBY"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:32764564,
FT ECO:0007744|PDB:6XBW, ECO:0007744|PDB:6XBY"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:32764564,
FT ECO:0007744|PDB:6XBW, ECO:0007744|PDB:6XBY"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:32764564,
FT ECO:0007744|PDB:6XBW, ECO:0007744|PDB:6XBY"
FT CARBOHYD 355
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:32764564,
FT ECO:0007744|PDB:6XBW, ECO:0007744|PDB:6XBY"
FT CARBOHYD 404
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:32764564,
FT ECO:0007744|PDB:6XBW, ECO:0007744|PDB:6XBY"
FT DISULFID 369..416
FT /evidence="ECO:0000269|PubMed:32764564,
FT ECO:0007744|PDB:6XBW, ECO:0007744|PDB:6XBY"
FT STRAND 259..264
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 272..276
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 279..282
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 285..289
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 302..310
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 312..317
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 320..330
FT /evidence="ECO:0007829|PDB:6XBW"
FT TURN 331..334
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 335..346
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 365..370
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 377..379
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 381..388
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 390..401
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 412..416
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 422..445
FT /evidence="ECO:0007829|PDB:6XBW"
SQ SEQUENCE 468 AA; 51781 MW; BF2C42D56ABB1B6D CRC64;
MMAATAAAQV RAGTRWAPAL CRMPWLPLML VAAAAATSEQ QVPLVLWSSD RGLWAPAADT
HEGHITSDMQ LSTYLDPALE LGPRNVLLFL QDKLSIEDFT AYGGVFGNKQ DSAFSNLENA
LDLAPSSLVL PAVDWYAIST LTTYLQEKLG ASPLHVDLAT LQELKLNASI PALLLIRLPY
TASSGLMAPK EVLMGNDEVI GQVLSTLKSE DIPYTAALTA VRPSRVARDV AMVTGGLGRQ
LLQRTVVPPT MNVPVSYNDS YDTRILFWAQ NFSVAYGEHW EDLTSRTFGV QDLNLTGSFW
NDTVARLVLT YDSLFGTMVT FKFILANSYY SVSARHWFTL ENLEIHSNGS VAYFNASQVT
GPSIYSFHCE HVSSENEDGN LLVPDTQPSL WQMTFRDFQI QAFNVTDKKF SYASDCAGFF
SPGIWMGLLT SLFMLFIFTY GLHMILSLKT MDRFDDHKGP TITLTQIV
