VATC1_BOVIN
ID VATC1_BOVIN Reviewed; 382 AA.
AC P21282; Q0VCX0;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=V-type proton ATPase subunit C 1;
DE Short=V-ATPase subunit C 1;
DE AltName: Full=Vacuolar proton pump subunit C 1;
GN Name=ATP6V1C1; Synonyms=ATP6C, VATC;
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 PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Chromaffin cell;
RX PubMed=2147024; DOI=10.1016/s0021-9258(17)30516-1;
RA Nelson H., Mandiyan S., Noumi T., Moriyama Y., Miedel M.C., Nelson N.;
RT "Molecular cloning of cDNA encoding the C subunit of H(+)-ATPase from
RT bovine chromaffin granules.";
RL J. Biol. Chem. 265:20390-20393(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal muscle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0007744|PDB:6XBW, ECO:0007744|PDB:6XBY}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.37 ANGSTROMS) IN COMPLEX WITH ADP,
RP FUNCTION, IDENTIFICATION IN THE V-ATPASE COMPLEX, SUBCELLULAR LOCATION,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
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: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase),
CC a multisubunit enzyme composed of a peripheral complex (V1) that
CC hydrolyzes ATP and a membrane integral complex (V0) that translocates
CC protons (PubMed:32764564). V-ATPase is responsible for acidifying and
CC maintaining the pH of intracellular compartments and in some cell
CC types, is targeted to the plasma membrane, where it is responsible for
CC acidifying the extracellular environment (PubMed:32764564). Subunit C
CC is necessary for the assembly of the catalytic sector of the enzyme and
CC is likely to have a specific function in its catalytic activity (By
CC similarity). {ECO:0000250|UniProtKB:P31412,
CC ECO:0000269|PubMed:32764564}.
CC -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme made up of two
CC complexes: the ATP-hydrolytic V1 complex and the proton translocation
CC V0 complex (PubMed:32764564). The V1 complex consists of three
CC catalytic AB heterodimers that form a heterohexamer, three peripheral
CC stalks each consisting of EG heterodimers, one central rotor including
CC subunits D and F, and the regulatory subunits C and H
CC (PubMed:32764564). The proton translocation complex V0 consists of the
CC proton transport subunit a, a ring of proteolipid subunits c9c'',
CC rotary subunit d, subunits e and f, and the accessory subunits
CC ATP6AP1/Ac45 and ATP6AP2/PRR (PubMed:32764564).
CC {ECO:0000269|PubMed:32764564}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000250|UniProtKB:Q5FVI6}; Peripheral membrane
CC protein {ECO:0000305}. Cytoplasmic vesicle, clathrin-coated vesicle
CC membrane {ECO:0000269|PubMed:32764564}; Peripheral membrane protein
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in brain (at protein level).
CC {ECO:0000269|PubMed:32764564}.
CC -!- SIMILARITY: Belongs to the V-ATPase C subunit family. {ECO:0000305}.
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DR EMBL; J05681; AAA30803.1; -; mRNA.
DR EMBL; BC119957; AAI19958.1; -; mRNA.
DR PIR; A23671; A23671.
DR RefSeq; NP_788849.1; NM_176676.1.
DR PDB; 6XBW; EM; 3.37 A; G=1-382.
DR PDB; 6XBY; EM; 3.79 A; G=1-382.
DR PDB; 7KHR; EM; 3.62 A; G=1-382.
DR PDBsum; 6XBW; -.
DR PDBsum; 6XBY; -.
DR PDBsum; 7KHR; -.
DR AlphaFoldDB; P21282; -.
DR SMR; P21282; -.
DR CORUM; P21282; -.
DR STRING; 9913.ENSBTAP00000017968; -.
DR PaxDb; P21282; -.
DR PRIDE; P21282; -.
DR Ensembl; ENSBTAT00000017968; ENSBTAP00000017968; ENSBTAG00000013513.
DR GeneID; 338089; -.
DR KEGG; bta:338089; -.
DR CTD; 528; -.
DR VEuPathDB; HostDB:ENSBTAG00000013513; -.
DR VGNC; VGNC:26319; ATP6V1C1.
DR eggNOG; KOG2909; Eukaryota.
DR GeneTree; ENSGT00390000004263; -.
DR HOGENOM; CLU_017554_3_0_1; -.
DR InParanoid; P21282; -.
DR OMA; GEYWLIS; -.
DR OrthoDB; 1016088at2759; -.
DR TreeFam; TF314912; -.
DR Reactome; R-BTA-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-BTA-9639288; Amino acids regulate mTORC1.
DR Proteomes; UP000009136; Chromosome 14.
DR Bgee; ENSBTAG00000013513; Expressed in occipital lobe and 103 other tissues.
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:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; IDA:UniProtKB.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IBA:GO_Central.
DR GO; GO:0045851; P:pH reduction; IC:UniProtKB.
DR GO; GO:1902600; P:proton transmembrane transport; IC:UniProtKB.
DR CDD; cd14785; V-ATPase_C; 1.
DR InterPro; IPR004907; ATPase_V1-cplx_csu.
DR InterPro; IPR036132; Vac_ATP_synth_c_sf.
DR PANTHER; PTHR10137; PTHR10137; 1.
DR Pfam; PF03223; V-ATPase_C; 1.
DR SUPFAM; SSF118203; SSF118203; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasmic vesicle; Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW Synapse; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P21283"
FT CHAIN 2..382
FT /note="V-type proton ATPase subunit C 1"
FT /id="PRO_0000209347"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000250|UniProtKB:P21283"
FT TURN 19..22
FT /evidence="ECO:0007829|PDB:6XBW"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:6XBW"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 49..71
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 97..101
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 113..119
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 120..156
FT /evidence="ECO:0007829|PDB:6XBW"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:6XBW"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 180..191
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 194..198
FT /evidence="ECO:0007829|PDB:6XBW"
FT TURN 199..202
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 203..207
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 220..230
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 234..243
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 255..303
FT /evidence="ECO:0007829|PDB:6XBW"
FT TURN 306..308
FT /evidence="ECO:0007829|PDB:6XBW"
FT HELIX 328..340
FT /evidence="ECO:0007829|PDB:6XBW"
FT STRAND 368..371
FT /evidence="ECO:0007829|PDB:6XBW"
SQ SEQUENCE 382 AA; 43986 MW; 122FECB9F8A8AC9C CRC64;
MTEFWLISAP GEKTCQQTWE KLHAATTKNN NLAVSSKFNI PDLKVGTLDV LVGLSDELAK
LDAFVEGVVK KVAQYMADVL EDSKDKVQEN LLANGVDLVT YITRFQWDMA KYPIKQSLKN
ISEIIAKGVT QIDNDLKSRA SAYNNLKGNL QNLERKNAGS LLTRSLAEIV KKDDFVLDSE
YLVTLLVVVP KLNHNDWIKQ YETLAEMVVP RSSNVLSEDQ DSYLCNVTLF RKAVDDFRHK
ARENKFIVRD FQYNEEEMKA DKEEMNRLST DKKKQFGPLV RWLKVNFSEA FIAWIHVKAL
RVFVESVLRY GLPVNFQAML LQPNKKTMKK LREVLYELYK HLDSSAAAII DAPMDIPGLN
LSQQEYYPYV YYKIDCNLLE FK
