ID   VATC1_RAT               Reviewed;         382 AA.
AC   Q5FVI6;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 103.
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;
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 [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2] {ECO:0007744|PDB:6VQ6, ECO:0007744|PDB:6VQ7, ECO:0007744|PDB:6VQ8, ECO:0007744|PDB:6VQI, ECO:0007744|PDB:6VQJ, ECO:0007744|PDB:6VQK}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.90 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: 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:32165585). 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:32165585). 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:32165585}.
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:32165585). 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:32165585). 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:32165585).
CC       {ECO:0000269|PubMed:32165585}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC       vesicle membrane {ECO:0000269|PubMed:32165585}; Peripheral membrane
CC       protein {ECO:0000305}. Cytoplasmic vesicle, clathrin-coated vesicle
CC       membrane {ECO:0000269|PubMed:32165585}; Peripheral membrane protein
CC       {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in brain (at protein level).
CC       {ECO:0000269|PubMed:32165585}.
CC   -!- SIMILARITY: Belongs to the V-ATPase C subunit family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC089961; AAH89961.1; -; mRNA.
DR   RefSeq; NP_001011992.1; NM_001011992.1.
DR   PDB; 6VQ6; EM; 3.90 A; G=1-382.
DR   PDB; 6VQ7; EM; 4.00 A; G=1-382.
DR   PDB; 6VQ8; EM; 3.90 A; G=1-382.
DR   PDB; 6VQI; EM; 4.30 A; G=1-382.
DR   PDB; 6VQJ; EM; 5.70 A; G=1-382.
DR   PDB; 6VQK; EM; 5.70 A; G=1-382.
DR   PDBsum; 6VQ6; -.
DR   PDBsum; 6VQ7; -.
DR   PDBsum; 6VQ8; -.
DR   PDBsum; 6VQI; -.
DR   PDBsum; 6VQJ; -.
DR   PDBsum; 6VQK; -.
DR   AlphaFoldDB; Q5FVI6; -.
DR   SMR; Q5FVI6; -.
DR   BioGRID; 256396; 1.
DR   IntAct; Q5FVI6; 2.
DR   STRING; 10116.ENSRNOP00000006917; -.
DR   iPTMnet; Q5FVI6; -.
DR   PhosphoSitePlus; Q5FVI6; -.
DR   SwissPalm; Q5FVI6; -.
DR   jPOST; Q5FVI6; -.
DR   PaxDb; Q5FVI6; -.
DR   PRIDE; Q5FVI6; -.
DR   Ensembl; ENSRNOT00000006917; ENSRNOP00000006917; ENSRNOG00000004846.
DR   GeneID; 299971; -.
DR   KEGG; rno:299971; -.
DR   UCSC; RGD:1311082; rat.
DR   CTD; 528; -.
DR   RGD; 1311082; Atp6v1c1.
DR   eggNOG; KOG2909; Eukaryota.
DR   GeneTree; ENSGT00390000004263; -.
DR   HOGENOM; CLU_017554_3_0_1; -.
DR   InParanoid; Q5FVI6; -.
DR   OMA; GEYWLIS; -.
DR   OrthoDB; 1016088at2759; -.
DR   PhylomeDB; Q5FVI6; -.
DR   TreeFam; TF314912; -.
DR   Reactome; R-RNO-1222556; ROS and RNS production in phagocytes.
DR   Reactome; R-RNO-77387; Insulin receptor recycling.
DR   Reactome; R-RNO-917977; Transferrin endocytosis and recycling.
DR   Reactome; R-RNO-9639288; Amino acids regulate mTORC1.
DR   Reactome; R-RNO-983712; Ion channel transport.
DR   PRO; PR:Q5FVI6; -.
DR   Proteomes; UP000002494; Chromosome 7.
DR   Bgee; ENSRNOG00000004846; Expressed in cerebellum and 19 other tissues.
DR   Genevisible; Q5FVI6; RN.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0045177; C:apical part of cell; IDA:RGD.
DR   GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IDA:RGD.
DR   GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; ISS:UniProtKB.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; ISO:RGD.
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; Hydrogen ion transport;
KW   Ion transport; Membrane; Reference proteome; 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_0000307374"
FT   MOD_RES         2
FT                   /note="N-acetylthreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P21283"
SQ   SEQUENCE   382 AA;  43901 MW;  FEFADA5FF3DB65BA CRC64;
     MTEFWLISAP GEKTCQQTWE KLHAATTKNN NLAVSSKFNI PDLKVGTLDV LVGLSDELAK
     LDAFVEGVVK KVAQYMADVL EDSKDKVQEN LLASGVDLVT YITRFQWDMA KYPIKQSLKN
     ISEIIAKGVT QIDNDLKSRA SAYNNLKGNL QNLERKNAGS LLTRSLAEIV KKDDFVLDSE
     YLVTLLVVVP KLNHNDWIKQ YETLAEMVVP RSSNVLSEDQ DSYLCNVTLF KKAVDDFRHK
     ARENKFIVRD FQYNEEEMRA DKEEMNRLST DKKKQFGPLV RWLKVNFSEA FIAWIHIKAL
     RVFVESVLRY GLPVNFQAML LQPNKKSVKK LREVLHELYK HLDSSAAAII DAPMDIPGLN
     LSQQEYYPYV YYKIDCNLLE FK