VAS1_RAT
ID VAS1_RAT Reviewed; 463 AA.
AC O54715;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=V-type proton ATPase subunit S1;
DE Short=V-ATPase subunit S1;
DE AltName: Full=C7-1 protein;
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=10686355; DOI=10.1016/s0169-328x(99)00325-3;
RA Hung H., Tsai M.J., Wu H.C., Lee E.H.Y.;
RT "Age-dependent increase in C7-1 gene expression in rat frontal cortex.";
RL Brain Res. Mol. Brain Res. 75:330-336(2000).
RN [2] {ECO:0007744|PDB:6VQ6, ECO:0007744|PDB:6VQ7, ECO:0007744|PDB:6VQ8, ECO:0007744|PDB:6VQC, ECO:0007744|PDB:6VQG, ECO:0007744|PDB:6VQH}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS), FUNCTION, IDENTIFICATION
RP IN THE V-ATPASE COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND TISSUE SPECIFICITY.
RX PubMed=32165585; DOI=10.1126/science.aaz2924;
RA Abbas Y.M., Wu D., Bueler S.A., Robinson C.V., Rubinstein J.L.;
RT "Structure of V-ATPase from the mammalian brain.";
RL Science 367:1240-1246(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:32165585). 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:32165585}.
CC -!- SUBUNIT: Accessory component of the multisubunit proton-transporting
CC vacuolar (V)-ATPase protein pump (PubMed:32165585). Interacts (via N-
CC terminus) with ATP6AP2 (via N-terminus) (PubMed:32165585). Interacts
CC with RNASEK (By similarity). {ECO:0000250|UniProtKB:Q15904,
CC ECO:0000269|PubMed:32165585}.
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:0000269|PubMed:32165585}; Single-pass type I membrane protein
CC {ECO:0000305}. Cytoplasmic vesicle, clathrin-coated vesicle membrane
CC {ECO:0000269|PubMed:32165585}; Single-pass type I membrane protein
CC {ECO:0000305}. Note=Not detected in trans-Golgi network.
CC {ECO:0000250|UniProtKB:Q15904}.
CC -!- TISSUE SPECIFICITY: Expressed in brain (at protein level).
CC {ECO:0000269|PubMed:32165585}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q15904}.
CC -!- SIMILARITY: Belongs to the vacuolar ATPase subunit S1 family.
CC {ECO:0000305}.
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DR EMBL; AF035387; AAB88008.1; -; mRNA.
DR RefSeq; NP_113973.1; NM_031785.1.
DR PDB; 6VQ6; EM; 3.90 A; c=1-463.
DR PDB; 6VQ7; EM; 4.00 A; c=1-463.
DR PDB; 6VQ8; EM; 3.90 A; c=1-463.
DR PDB; 6VQC; EM; 3.80 A; c=1-463.
DR PDB; 6VQG; EM; 4.20 A; c=1-463.
DR PDB; 6VQH; EM; 4.40 A; c=1-463.
DR PDBsum; 6VQ6; -.
DR PDBsum; 6VQ7; -.
DR PDBsum; 6VQ8; -.
DR PDBsum; 6VQC; -.
DR PDBsum; 6VQG; -.
DR PDBsum; 6VQH; -.
DR AlphaFoldDB; O54715; -.
DR SMR; O54715; -.
DR BioGRID; 249780; 1.
DR IntAct; O54715; 3.
DR MINT; O54715; -.
DR STRING; 10116.ENSRNOP00000053134; -.
DR GlyGen; O54715; 8 sites.
DR iPTMnet; O54715; -.
DR PhosphoSitePlus; O54715; -.
DR PaxDb; O54715; -.
DR PRIDE; O54715; -.
DR GeneID; 83615; -.
DR KEGG; rno:83615; -.
DR CTD; 537; -.
DR RGD; 620423; Atp6ap1.
DR eggNOG; KOG3868; Eukaryota.
DR InParanoid; O54715; -.
DR OrthoDB; 1111170at2759; -.
DR PhylomeDB; O54715; -.
DR Reactome; R-RNO-77387; Insulin receptor recycling.
DR Reactome; R-RNO-8980692; RHOA GTPase cycle.
DR Reactome; R-RNO-917977; Transferrin endocytosis and recycling.
DR Reactome; R-RNO-983712; Ion channel transport.
DR PRO; PR:O54715; -.
DR Proteomes; UP000002494; Unplaced.
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:0016020; C:membrane; ISO:RGD.
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; ISS:UniProtKB.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0008219; P:cell death; IMP:RGD.
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; ISS:UniProtKB.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0036035; P:osteoclast development; ISS:CAFA.
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; Endoplasmic reticulum; Glycoprotein;
KW Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW Signal; Synapse; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..463
FT /note="V-type proton ATPase subunit S1"
FT /id="PRO_0000002545"
FT PROPEP 33..225
FT /evidence="ECO:0000250|UniProtKB:Q9R1Q9"
FT /id="PRO_0000454043"
FT TOPO_DOM 33..412
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 413..433
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 434..463
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT SITE 225..226
FT /note="Cleavage; by furin"
FT /evidence="ECO:0000250|UniProtKB:Q9R1Q9"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 399
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 463 AA; 51123 MW; 6086B8C368A81CC9 CRC64;
MMAATVVSRI RTGTRWAPVL WLLLSLVAVA AAVAAEQQVP LVLWSSDRDL WAPVADTHEG
HITSDMQLST YLDPALELGP RNVLLFLQDK LSIEDFTAYG GVFGNKQDSA FSNLENALDL
APSSLVLPAV DWYAISTLTT YLQEKLGASP LHVDLATLKE LKLNASLPAL LLIRLPYTAS
SGLMAPREVL TGNDEVIGQV LSTLESEDVP YTAALTAVRP SRVARDVAMV AGGLGRQLLQ
TQVASPAIHP PVSYNDTAPR ILFWAQNFSV AYKDEWKDLT SLTFGVENLN LTGSFWNDSF
AMLSLTYEPL FGATVTFKFI LASRFYPVSA RYWFTMERLE IHSNGSVAHF NVSQVTGPSI
YSFHCEYVSS LSKKGSLLVT NVPSLWQMTL HNFQIQAFNV TGEQFSYASD CAGFFSPGIW
MGLLTTLFML FIFTYGLHMI LSLKTMDRFD DRKGPTITLT QIV
