GenomeNet

Database: UniProt
Entry: A0A096N613_PAPAN
LinkDB: A0A096N613_PAPAN
Original site: A0A096N613_PAPAN 
ID   A0A096N613_PAPAN        Unreviewed;       532 AA.
AC   A0A096N613;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 2.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=V-type proton ATPase subunit a {ECO:0000256|RuleBase:RU361189};
GN   Name=TCIRG1 {ECO:0000313|Ensembl:ENSPANP00000007900.2};
OS   Papio anubis (Olive baboon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Papio.
OX   NCBI_TaxID=9555 {ECO:0000313|Ensembl:ENSPANP00000007900.2, ECO:0000313|Proteomes:UP000028761};
RN   [1] {ECO:0000313|Ensembl:ENSPANP00000007900.2, ECO:0000313|Proteomes:UP000028761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Liu Y.L., Abraham K.A., Akbar H.A., Ali S.A., Anosike U.A., Aqrawi P.A.,
RA   Arias F.A., Attaway T.A., Awwad R.A., Babu C.B., Bandaranaike D.B.,
RA   Battles P.B., Bell A.B., Beltran B.B., Berhane-Mersha D.B., Bess C.B.,
RA   Bickham C.B., Bolden T.B., Carter K.C., Chau D.C., Chavez A.C.,
RA   Clerc-Blankenburg K.C., Coyle M.C., Dao M.D., Davila M.L.D.,
RA   Davy-Carroll L.D., Denson S.D., Dinh H.D., Fernandez S.F., Fernando P.F.,
RA   Forbes L.F., Francis C.F., Francisco L.F., Fu Q.F., Garcia-Iii R.G.,
RA   Garrett T.G., Gross S.G., Gubbala S.G., Hirani K.H., Hogues M.H.,
RA   Hollins B.H., Jackson L.J., Javaid M.J., Jhangiani S.J., Johnson A.J.,
RA   Johnson B.J., Jones J.J., Joshi V.J., Kalu J.K., Khan N.K., Korchina V.K.,
RA   Kovar C.K., Lago L.L., Lara F.L., Le T.-K.L., Lee S.L., Legall-Iii F.L.,
RA   Lemon S.L., Liu J.L., Liu Y.-S.L., Liyanage D.L., Lopez J.L.,
RA   Lorensuhewa L.L., Mata R.M., Mathew T.M., Mercado C.M., Mercado I.M.,
RA   Morales K.M., Morgan M.M., Munidasa M.M., Ngo D.N., Nguyen L.N.,
RA   Nguyen T.N., Nguyen N.N., Obregon M.O., Okwuonu G.O., Ongeri F.O.,
RA   Onwere C.O., Osifeso I.O., Parra A.P., Patil S.P., Perez A.P., Perez Y.P.,
RA   Pham C.P., Pu L.-L.P., Puazo M.P., Quiroz J.Q., Rouhana J.R., Ruiz M.R.,
RA   Ruiz S.-J.R., Saada N.S., Santibanez J.S., Scheel M.S., Schneider B.S.,
RA   Simmons D.S., Sisson I.S., Tang L.-Y.T., Thornton R.T., Tisius J.T.,
RA   Toledanes G.T., Trejos Z.T., Usmani K.U., Varghese R.V., Vattathil S.V.,
RA   Vee V.V., Walker D.W., Weissenberger G.W., White C.W., Williams A.W.,
RA   Woodworth J.W., Wright R.W., Zhu Y.Z., Han Y.H., Newsham I.N.,
RA   Nazareth L.N., Worley K.W., Muzny D.M., Rogers J.R., Gibbs R.G.;
RT   "Whole Genome Assembly of Papio anubis.";
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPANP00000007900.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Essential component of the vacuolar proton pump (V-ATPase), a
CC       multimeric enzyme that catalyzes the translocation of protons across
CC       the membranes. Required for assembly and activity of the V-ATPase.
CC       {ECO:0000256|RuleBase:RU361189}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family.
CC       {ECO:0000256|ARBA:ARBA00009904, ECO:0000256|RuleBase:RU361189}.
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DR   AlphaFoldDB; A0A096N613; -.
DR   STRING; 9555.ENSPANP00000007900; -.
DR   Ensembl; ENSPANT00000014897.3; ENSPANP00000007900.2; ENSPANG00000012975.3.
DR   eggNOG; KOG2189; Eukaryota.
DR   GeneTree; ENSGT00950000182881; -.
DR   HOGENOM; CLU_005230_0_0_1; -.
DR   OMA; HYVIHTI; -.
DR   Proteomes; UP000028761; Chromosome 12.
DR   Bgee; ENSPANG00000012975; Expressed in aorta and 61 other cell types or tissues.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR   GO; GO:0005770; C:late endosome; IEA:Ensembl.
DR   GO; GO:0005764; C:lysosome; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0030670; C:phagocytic vesicle membrane; IEA:Ensembl.
DR   GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR   GO; GO:0030667; C:secretory granule membrane; IEA:Ensembl.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0006915; P:apoptotic process; IEA:Ensembl.
DR   GO; GO:0000045; P:autophagosome assembly; IEA:Ensembl.
DR   GO; GO:0030183; P:B cell differentiation; IEA:Ensembl.
DR   GO; GO:0045453; P:bone resorption; IEA:Ensembl.
DR   GO; GO:0071345; P:cellular response to cytokine stimulus; IEA:Ensembl.
DR   GO; GO:0097188; P:dentin mineralization; IEA:Ensembl.
DR   GO; GO:0070166; P:enamel mineralization; IEA:Ensembl.
DR   GO; GO:0030010; P:establishment of cell polarity; IEA:Ensembl.
DR   GO; GO:0051650; P:establishment of vesicle localization; IEA:Ensembl.
DR   GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR   GO; GO:0061484; P:hematopoietic stem cell homeostasis; IEA:Ensembl.
DR   GO; GO:0016064; P:immunoglobulin mediated immune response; IEA:Ensembl.
DR   GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR   GO; GO:0006874; P:intracellular calcium ion homeostasis; IEA:Ensembl.
DR   GO; GO:0035709; P:memory T cell activation; IEA:Ensembl.
DR   GO; GO:0021554; P:optic nerve development; IEA:Ensembl.
DR   GO; GO:0001503; P:ossification; IEA:Ensembl.
DR   GO; GO:0030316; P:osteoclast differentiation; IEA:Ensembl.
DR   GO; GO:0002158; P:osteoclast proliferation; IEA:Ensembl.
DR   GO; GO:0045851; P:pH reduction; IEA:Ensembl.
DR   GO; GO:0090383; P:phagosome acidification; IEA:Ensembl.
DR   GO; GO:0007039; P:protein catabolic process in the vacuole; IEA:Ensembl.
DR   GO; GO:0033365; P:protein localization to organelle; IEA:Ensembl.
DR   GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0050796; P:regulation of insulin secretion; IEA:Ensembl.
DR   GO; GO:0045667; P:regulation of osteoblast differentiation; IEA:Ensembl.
DR   GO; GO:0010155; P:regulation of proton transport; IEA:Ensembl.
DR   GO; GO:0010272; P:response to silver ion; IEA:Ensembl.
DR   GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
DR   GO; GO:0031529; P:ruffle organization; IEA:Ensembl.
DR   GO; GO:0030217; P:T cell differentiation; IEA:Ensembl.
DR   GO; GO:0043029; P:T cell homeostasis; IEA:Ensembl.
DR   GO; GO:0035711; P:T-helper 1 cell activation; IEA:Ensembl.
DR   GO; GO:0044691; P:tooth eruption; IEA:Ensembl.
DR   InterPro; IPR002490; V-ATPase_116kDa_su.
DR   PANTHER; PTHR11629:SF21; V-TYPE PROTON ATPASE 116 KDA SUBUNIT A 3; 1.
DR   PANTHER; PTHR11629; VACUOLAR PROTON ATPASES; 1.
DR   Pfam; PF01496; V_ATPase_I; 1.
PE   3: Inferred from homology;
KW   Hydrogen ion transport {ECO:0000256|RuleBase:RU361189};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW   ECO:0000256|RuleBase:RU361189};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361189};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028761};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU361189};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU361189};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU361189}.
FT   TRANSMEM        100..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        145..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        241..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        272..292
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        299..318
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        338..358
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   TRANSMEM        468..493
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361189"
FT   REGION          383..403
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   532 AA;  58831 MW;  49C5D39246F586D7 CRC64;
     MKAVYLALNQ CSVSTTHKCL IAEAWCSVRD LPALQEALRD SSTEEGVSAV AHRIPCRDMP
     PTLIRTNRFT ASFQGIVDAY GVGRYQEVNP APYTIITFPF LFAVMFGDVG HGLLMFLFAL
     AMVLAENRPA VKAAQNEIWQ TFFRGRYLLL LMGLFSIYTG FIYNECFSRA TSIFPSGWSV
     AAMANQSGWS DAFLAQHAML TLDPNVTGVF LGPYPFGIDP VWSLAANHLS FLNSFKMKMS
     VILGVVHMAF GVVLGIFNHV HFGQRHRLLL ETLPELTFLL GLFGYLVFLV IYKWLCVSAA
     SAASAPSILI HFINMFLFSH SPTNRPLYPR QEVVQATLVV LALAMVPILL LGTPLHLLRR
     HRPHLRRRPT GRQEEDKAGL LDLPDASVNG WSSDEEKAGG LDDEEEAELV PSEVLMHQAI
     HTIEFCLGCV SNTASYLRLW ALSLAHAQLS EVLWAMVMSI GLGLGREVGV AAVVLVPIFA
     AFAVMTVAIL LVMEGLSAFL HALRLHWVEF QNKFYSGTGY KLSPFAFAAT DD
//
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