VATC1_MOUSE
ID VATC1_MOUSE Reviewed; 382 AA.
AC Q9Z1G3; Q91Z42;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 4.
DT 03-AUG-2022, entry version 168.
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, Atp6c1, Vatc;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=12527205; DOI=10.1016/s0378-1119(02)01099-5;
RA Sun-Wada G.-H., Yoshimizu T., Imai-Senga Y., Wada Y., Futai M.;
RT "Diversity of mouse proton-translocating ATPase: presence of multiple
RT isoforms of the C, d and G subunits.";
RL Gene 302:147-153(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Howell M.L., Dean G.E.;
RT "cDNA sequences for mouse vacuolar ATPase subunits.";
RL Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Pancreas;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [5]
RP PROTEIN SEQUENCE OF 38-111; 120-137; 148-155; 200-231; 275-281; 310-326 AND
RP 374-382, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By similarity). 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 (By similarity). Subunit C is
CC necessary for the assembly of the catalytic sector of the enzyme and is
CC likely to have a specific function in its catalytic activity (By
CC similarity). {ECO:0000250|UniProtKB:P21282,
CC ECO:0000250|UniProtKB:P21283, ECO:0000250|UniProtKB:P31412}.
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 (By similarity). The V1 complex consists of three catalytic
CC AB heterodimers that form a heterohexamer, three peripheral stalks each
CC consisting of EG heterodimers, one central rotor including subunits D
CC and F, and the regulatory subunits C and H (By similarity). The proton
CC translocation complex V0 consists of the proton transport subunit a, a
CC ring of proteolipid subunits c9c'', rotary subunit d, subunits e and f,
CC and the accessory subunits ATP6AP1/Ac45 and ATP6AP2/PRR (By
CC similarity). {ECO:0000250|UniProtKB:P21283}.
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:0000250|UniProtKB:Q5FVI6}; Peripheral membrane protein
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Abundant in brain, liver, kidney and
CC testis. {ECO:0000269|PubMed:12527205}.
CC -!- SIMILARITY: Belongs to the V-ATPase C subunit family. {ECO:0000305}.
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DR EMBL; AB088407; BAC57953.1; -; mRNA.
DR EMBL; U13839; AAC83084.1; -; mRNA.
DR EMBL; AK075779; BAC35953.1; -; mRNA.
DR EMBL; AK151237; BAE30229.1; -; mRNA.
DR EMBL; BC010217; AAH10217.1; -; mRNA.
DR CCDS; CCDS27439.1; -.
DR RefSeq; NP_079770.2; NM_025494.3.
DR AlphaFoldDB; Q9Z1G3; -.
DR SMR; Q9Z1G3; -.
DR BioGRID; 211393; 20.
DR IntAct; Q9Z1G3; 5.
DR MINT; Q9Z1G3; -.
DR STRING; 10090.ENSMUSP00000022904; -.
DR TCDB; 3.A.2.2.6; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR iPTMnet; Q9Z1G3; -.
DR PhosphoSitePlus; Q9Z1G3; -.
DR SwissPalm; Q9Z1G3; -.
DR EPD; Q9Z1G3; -.
DR jPOST; Q9Z1G3; -.
DR MaxQB; Q9Z1G3; -.
DR PaxDb; Q9Z1G3; -.
DR PeptideAtlas; Q9Z1G3; -.
DR PRIDE; Q9Z1G3; -.
DR ProteomicsDB; 297958; -.
DR Antibodypedia; 4022; 124 antibodies from 24 providers.
DR DNASU; 66335; -.
DR Ensembl; ENSMUST00000022904; ENSMUSP00000022904; ENSMUSG00000022295.
DR GeneID; 66335; -.
DR KEGG; mmu:66335; -.
DR UCSC; uc007vnv.2; mouse.
DR CTD; 528; -.
DR MGI; MGI:1913585; Atp6v1c1.
DR VEuPathDB; HostDB:ENSMUSG00000022295; -.
DR eggNOG; KOG2909; Eukaryota.
DR GeneTree; ENSGT00390000004263; -.
DR HOGENOM; CLU_017554_3_0_1; -.
DR InParanoid; Q9Z1G3; -.
DR OMA; GEYWLIS; -.
DR OrthoDB; 1016088at2759; -.
DR PhylomeDB; Q9Z1G3; -.
DR TreeFam; TF314912; -.
DR Reactome; R-MMU-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-MMU-77387; Insulin receptor recycling.
DR Reactome; R-MMU-917977; Transferrin endocytosis and recycling.
DR Reactome; R-MMU-9639288; Amino acids regulate mTORC1.
DR Reactome; R-MMU-983712; Ion channel transport.
DR BioGRID-ORCS; 66335; 23 hits in 74 CRISPR screens.
DR ChiTaRS; Atp6v1c1; mouse.
DR PRO; PR:Q9Z1G3; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9Z1G3; protein.
DR Bgee; ENSMUSG00000022295; Expressed in Ammon's horn and 88 other tissues.
DR ExpressionAtlas; Q9Z1G3; baseline and differential.
DR Genevisible; Q9Z1G3; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0045177; C:apical part of cell; ISO:MGI.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA: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; ISS:UniProtKB.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IDA:MGI.
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 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_0000209349"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000250|UniProtKB:P21283"
FT CONFLICT 267
FT /note="R -> E (in Ref. 2; AAC83084)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 382 AA; 43888 MW; 6D1851D8C81DF98F CRC64;
MTEFWLISAP GEKTCQQTWE KLHAATTKNN NLAVSSKFNI PDLKVGTLDV LVGLSDELAK
LDAFVEGVVK KVAQYMADVL EDSKDKVQEN LLASGVDLVT YITRFQWDMA KYPIKQSLKN
ISEIIAKGVT QIDNDLKSRA SAYNNLKGNL QNLERKNAGS LLTRSLAEIV KKDDFVLDSE
YLVTLLVVVP KLNHNDWIKQ YETLAEMVVP RSSNVLSEDQ DSYLCNVTLF RKAVDDFRHK
ARENKFIVRD FQYNEEEMKA DKEEMTRLST DKKKQFGPLV RWLKVNFSEA FIAWIHIKAL
RVFVESVLRY GLPVNFQAML LQPNKKSVKK LREVLHELYK HLDSSAAAII DAPMDIPGLN
LSQQEYYPYV YYKIDCNLLE FK
