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VATL_MOUSE
ID   VATL_MOUSE              Reviewed;         155 AA.
AC   P63082; P23967; Q3TD69;
DT   13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=V-type proton ATPase 16 kDa proteolipid subunit c {ECO:0000305};
DE            Short=V-ATPase 16 kDa proteolipid subunit c {ECO:0000305};
DE   AltName: Full=PL16;
DE   AltName: Full=Vacuolar proton pump 16 kDa proteolipid subunit c {ECO:0000305};
GN   Name=Atp6v0c; Synonyms=Atp6c, Atp6l, Atpl, Mvp;
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].
RC   TISSUE=Brain;
RX   PubMed=1828149; DOI=10.1016/0006-291x(91)90391-j;
RA   Hanada H., Hasebe M., Moriyama Y., Maeda M., Futai M.;
RT   "Molecular cloning of cDNA encoding the 16 KDa subunit of vacuolar H(+)-
RT   ATPase from mouse cerebellum.";
RL   Biochem. Biophys. Res. Commun. 176:1062-1067(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8741845; DOI=10.1091/mbc.7.1.129;
RA   Laitala T., Howell M.L., Dean G.E., Vaananen H.K.;
RT   "Resorption-cycle-dependent polarization of mRNAs for different subunits of
RT   V-ATPase in bone-resorbing osteoclasts.";
RL   Mol. Biol. Cell 7:129-142(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11595166; DOI=10.1016/s0378-1119(01)00590-x;
RA   Hayami K., Noumi T., Inoue H., Sun-Wada G.H., Yoshimizu T., Kanazawa H.;
RT   "The murine genome contains one functional gene and two pseudogenes coding
RT   for the 16 kDa proteolipid subunit of vacuolar H+-ATPase.";
RL   Gene 273:199-206(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BALB/cJ;
RX   PubMed=11441017; DOI=10.1074/jbc.m104682200;
RA   Nishi T., Kawasaki-Nishi S., Forgac M.;
RT   "Expression and localization of the mouse homolog of the yeast V-ATPase 21-
RT   kDa subunit c' (Vma16p).";
RL   J. Biol. Chem. 276:34122-34130(2001).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Kidney;
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   [6]
RP   INTERACTION WITH ATP6V0A4.
RC   STRAIN=NOD; TISSUE=Kidney;
RX   PubMed=11495928; DOI=10.1074/jbc.m107267200;
RA   Smith A.N., Finberg K.E., Wagner C.A., Lifton R.P., Devonald M.A., Su Y.,
RA   Karet F.E.;
RT   "Molecular cloning and characterization of Atp6n1b: a novel fourth murine
RT   vacuolar H+-ATPase a-subunit gene.";
RL   J. Biol. Chem. 276:42382-42388(2001).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Heart, Kidney, Liver, and Lung;
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: Proton-conducting pore forming of the V0 complex of
CC       vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a
CC       peripheral complex (V1) that hydrolyzes ATP and a membrane integral
CC       complex (V0) that translocates protons (By similarity). V-ATPase is
CC       responsible for acidifying and maintaining the pH of intracellular
CC       compartments and in some cell types, is targeted to the plasma
CC       membrane, where it is responsible for acidifying the extracellular
CC       environment (By similarity). {ECO:0000250|UniProtKB:P23956,
CC       ECO:0000250|UniProtKB:P27449}.
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). Interacts with the V0 complex V-ATPase subunit a4 ATP6V0A4
CC       (PubMed:11495928). Interacts with LASS2 (By similarity). Interacts with
CC       RNF182; this interaction leads to ubiquitination and degradation via
CC       the proteasome pathway (By similarity). {ECO:0000250|UniProtKB:P27449,
CC       ECO:0000269|PubMed:11495928}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle
CC       membrane {ECO:0000250|UniProtKB:P63081}; Multi-pass membrane protein
CC       {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle
CC       membrane {ECO:0000250|UniProtKB:P63081}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- PTM: Ubiquitinated by RNF182, leading to its degradation via the
CC       ubiquitin-proteasome pathway. {ECO:0000250|UniProtKB:P27449}.
CC   -!- SIMILARITY: Belongs to the V-ATPase proteolipid subunit family.
CC       {ECO:0000305}.
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DR   EMBL; M64298; AAA39775.1; -; mRNA.
DR   EMBL; U13842; AAC52413.1; -; Genomic_DNA.
DR   EMBL; AB059662; BAB64538.1; -; Genomic_DNA.
DR   EMBL; AF356008; AAL02098.1; -; Genomic_DNA.
DR   EMBL; AK002570; BAB22195.1; -; mRNA.
DR   EMBL; AK002871; BAB22419.1; -; mRNA.
DR   EMBL; AK170346; BAE41735.1; -; mRNA.
DR   CCDS; CCDS28476.1; -.
DR   PIR; JN0063; JN0063.
DR   RefSeq; NP_033859.1; NM_009729.3.
DR   AlphaFoldDB; P63082; -.
DR   SMR; P63082; -.
DR   BioGRID; 198274; 4.
DR   IntAct; P63082; 3.
DR   MINT; P63082; -.
DR   STRING; 10090.ENSMUSP00000024932; -.
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; P63082; -.
DR   PhosphoSitePlus; P63082; -.
DR   jPOST; P63082; -.
DR   MaxQB; P63082; -.
DR   PaxDb; P63082; -.
DR   PRIDE; P63082; -.
DR   ProteomicsDB; 297875; -.
DR   TopDownProteomics; P63082; -.
DR   Antibodypedia; 23806; 83 antibodies from 18 providers.
DR   DNASU; 11984; -.
DR   Ensembl; ENSMUST00000024932; ENSMUSP00000024932; ENSMUSG00000024121.
DR   Ensembl; ENSMUST00000098862; ENSMUSP00000111059; ENSMUSG00000024121.
DR   GeneID; 11984; -.
DR   KEGG; mmu:11984; -.
DR   UCSC; uc008aup.2; mouse.
DR   CTD; 527; -.
DR   MGI; MGI:88116; Atp6v0c.
DR   VEuPathDB; HostDB:ENSMUSG00000024121; -.
DR   eggNOG; KOG0232; Eukaryota.
DR   GeneTree; ENSGT00550000074873; -.
DR   InParanoid; P63082; -.
DR   OMA; NFIQLGA; -.
DR   OrthoDB; 1534092at2759; -.
DR   PhylomeDB; P63082; -.
DR   TreeFam; TF300025; -.
DR   Reactome; R-MMU-1222556; ROS and RNS production in phagocytes.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
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; 11984; 26 hits in 74 CRISPR screens.
DR   ChiTaRS; Atp6v0c; mouse.
DR   PRO; PR:P63082; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; P63082; protein.
DR   Bgee; ENSMUSG00000024121; Expressed in Ammon's horn and 125 other tissues.
DR   ExpressionAtlas; P63082; baseline and differential.
DR   Genevisible; P63082; MM.
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:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0005764; C:lysosome; ISO:MGI.
DR   GO; GO:0016020; C:membrane; ISO:MGI.
DR   GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; TAS:MGI.
DR   GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; ISS:UniProtKB.
DR   GO; GO:0008553; F:P-type proton-exporting transporter activity; ISA:MGI.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR   GO; GO:0007042; P:lysosomal lumen acidification; TAS:MGI.
DR   GO; GO:1904093; P:negative regulation of autophagic cell death; ISO:MGI.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR   GO; GO:0030177; P:positive regulation of Wnt signaling pathway; ISO:MGI.
DR   GO; GO:0007035; P:vacuolar acidification; TAS:MGI.
DR   Gene3D; 1.20.120.610; -; 1.
DR   InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
DR   InterPro; IPR000245; ATPase_proteolipid_csu.
DR   InterPro; IPR011555; ATPase_proteolipid_su_C_euk.
DR   InterPro; IPR035921; F/V-ATP_Csub_sf.
DR   Pfam; PF00137; ATP-synt_C; 2.
DR   PRINTS; PR00122; VACATPASE.
DR   SUPFAM; SSF81333; SSF81333; 2.
DR   TIGRFAMs; TIGR01100; V_ATP_synt_C; 1.
PE   1: Evidence at protein level;
KW   Cytoplasmic vesicle; Hydrogen ion transport; Ion transport; Membrane;
KW   Reference proteome; Synapse; Transmembrane; Transmembrane helix; Transport;
KW   Ubl conjugation.
FT   CHAIN           1..155
FT                   /note="V-type proton ATPase 16 kDa proteolipid subunit c"
FT                   /id="PRO_0000071744"
FT   TOPO_DOM        1..10
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        11..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        34..55
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        56..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        77..92
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        93..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        115..131
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        132..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        153..155
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   SITE            139
FT                   /note="Essential for proton translocation"
FT                   /evidence="ECO:0000250|UniProtKB:P63081"
SQ   SEQUENCE   155 AA;  15808 MW;  880C280C5AEB0C5C CRC64;
     MADIKNNPEY SSFFGVMGAS SAMVFSAMGA AYGTAKSGTG IAAMSVMRPE LIMKSIIPVV
     MAGIIAIYGL VVAVLIANSL TDGITLYRSF LQLGAGLSVG LSGLAAGFAI GIVGDAGVRG
     TAQQPRLFVG MILILIFAEV LGLYGLIVAL ILSTK
 
 
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