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V-type proton ATPase 116 kDa subunit a isoform 3 (V-ATPase 116 kDa isoform a3) (Osteoclastic proton pump 116 kDa subunit) (OC-116 kDa) (OC116) (T-cell immune regulator 1) (T-cell immune response cDNA7 protein) (TIRC7) (Vacuolar proton translocating ATPase 116 kDa subunit a isoform 3)

 VPP3_HUMAN              Reviewed;         830 AA.
Q13488; O75877; Q8WVC5;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
10-FEB-2009, sequence version 3.
27-SEP-2017, entry version 171.
RecName: Full=V-type proton ATPase 116 kDa subunit a isoform 3;
Short=V-ATPase 116 kDa isoform a3;
AltName: Full=Osteoclastic proton pump 116 kDa subunit;
Short=OC-116 kDa;
Short=OC116;
AltName: Full=T-cell immune regulator 1;
AltName: Full=T-cell immune response cDNA7 protein;
Short=TIRC7;
AltName: Full=Vacuolar proton translocating ATPase 116 kDa subunit a isoform 3;
Name=TCIRG1; Synonyms=ATP6N1C, ATP6V0A3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
TISSUE=Osteoclastoma;
PubMed=8579597; DOI=10.1006/bbrc.1996.0145;
Li Y.P., Chen W., Stashenko P.;
"Molecular cloning and characterization of a putative novel human
osteoclast-specific 116-kDa vacuolar proton pump subunit.";
Biochem. Biophys. Res. Commun. 218:813-821(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
Utku N., Heinemann T., Bulwin C.-G., Beinke S., Beato F., Randall J.,
Busconi L., Delphire E., Robertson E.R., Kojima R., Volk H.D.,
Milford E.L., Gullans S.R.;
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM SHORT).
PubMed=10329006; DOI=10.1006/geno.1999.5751;
Heinemann T., Bulwin G.C., Randall J., Schnieders B., Sandhoff K.,
Volk H.D., Milford E., Gullans S.R., Utku N.;
"Genomic organization of the gene coding for TIRC7, a novel membrane
protein essential for T cell activation.";
Genomics 57:398-406(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
TISSUE=Lung, and Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
VARIANTS OPTB1 ARG-405 AND LEU-444.
PubMed=11532986; DOI=10.1093/hmg/10.17.1767;
Sobacchi C., Frattini A., Orchard P., Porras O., Tezcan I.,
Andolina M., Babul-Hirji R., Baric I., Canham N., Chitayat D.,
Dupuis-Girod S., Ellis I., Etzioni A., Fasth A., Fisher A.,
Gerritsen B., Gulino V., Horwitz E., Klamroth V., Lanino E.,
Mirolo M., Musio A., Matthijs G., Nonomaya S., Notarangelo L.D.,
Ochs H.D., Superti-Furga A., Valiaho J., van Hove J.L.K., Vihinen M.,
Vujic D., Vezzoni P., Villa A.;
"The mutational spectrum of human malignant autosomal recessive
osteopetrosis.";
Hum. Mol. Genet. 10:1767-1773(2001).
[7]
VARIANT OPTB1 ARG-405.
PubMed=12552563; DOI=10.1002/humu.10165;
Scimeca J.-C., Quincey D., Parrinello H., Romatet D., Grosgeorge J.,
Gaudray P., Philip N., Fischer A., Carle G.F.;
"Novel mutations in the TCIRG1 gene encoding the a3 subunit of the
vacuolar proton pump in patients affected by infantile malignant
osteopetrosis.";
Hum. Mutat. 21:151-157(2003).
[8]
VARIANTS OPTB1 PRO-141; ARG-405; ASN-462 DEL; ASN-517 AND ARG-775.
PubMed=15300850; DOI=10.1002/humu.20076;
Susani L., Pangrazio A., Sobacchi C., Taranta A., Mortier G.,
Savarirayan R., Villa A., Orchard P., Vezzoni P., Albertini A.,
Frattini A., Pagani F.;
"TCIRG1-dependent recessive osteopetrosis: mutation analysis,
functional identification of the splicing defects, and in vitro rescue
by U1 snRNA.";
Hum. Mutat. 24:225-235(2004).
-!- FUNCTION: Part of the proton channel of V-ATPases (By similarity).
Seems to be directly involved in T-cell activation. {ECO:0000250}.
-!- SUBUNIT: The V-ATPase is a heteromultimeric enzyme composed of at
least thirteen different subunits. It has a membrane peripheral V1
sector for ATP hydrolysis and an integral V0 for proton
translocation. The V1 sector comprises subunits A-H, whereas V0
includes subunits a, d, c, c', and c''.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
protein {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Long;
IsoId=Q13488-1; Sequence=Displayed;
Name=Short;
IsoId=Q13488-2; Sequence=VSP_000345;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Isoform long is highly expressed in
osteoclastomas. Isoform short is highly expressed in thymus.
-!- DISEASE: Osteopetrosis, autosomal recessive 1 (OPTB1)
[MIM:259700]: A rare genetic disease characterized by abnormally
dense bone, due to defective resorption of immature bone.
Osteopetrosis occurs in two forms: a severe autosomal recessive
form occurring in utero, infancy, or childhood, and a benign
autosomal dominant form occurring in adolescence or adulthood.
Recessive osteopetrosis commonly manifests in early infancy with
macrocephaly, feeding difficulties, evolving blindness and
deafness, bone marrow failure, severe anemia, and
hepatosplenomegaly. Deafness and blindness are generally thought
to represent effects of pressure on nerves.
{ECO:0000269|PubMed:11532986, ECO:0000269|PubMed:12552563,
ECO:0000269|PubMed:15300850}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=TCIRG1base; Note=TCIRG1 mutation db;
URL="http://structure.bmc.lu.se/idbase/TCIRG1base/";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; U45285; AAA97878.1; -; mRNA.
EMBL; AF025374; AAC35742.1; -; mRNA.
EMBL; AF033033; AAD31081.2; -; Genomic_DNA.
EMBL; CH471076; EAW74691.1; -; Genomic_DNA.
EMBL; BC018133; AAH18133.1; -; mRNA.
EMBL; BC032465; AAH32465.1; -; mRNA.
CCDS; CCDS53670.1; -. [Q13488-2]
CCDS; CCDS8177.1; -. [Q13488-1]
RefSeq; NP_006010.2; NM_006019.3. [Q13488-1]
RefSeq; NP_006044.1; NM_006053.3. [Q13488-2]
RefSeq; XP_005273766.1; XM_005273709.3. [Q13488-1]
RefSeq; XP_011543028.1; XM_011544726.2. [Q13488-1]
UniGene; Hs.495985; -.
UniGene; Hs.716672; -.
ProteinModelPortal; Q13488; -.
BioGrid; 115597; 21.
IntAct; Q13488; 8.
STRING; 9606.ENSP00000265686; -.
iPTMnet; Q13488; -.
PhosphoSitePlus; Q13488; -.
BioMuta; TCIRG1; -.
DMDM; 223634720; -.
EPD; Q13488; -.
MaxQB; Q13488; -.
PaxDb; Q13488; -.
PeptideAtlas; Q13488; -.
PRIDE; Q13488; -.
DNASU; 10312; -.
Ensembl; ENST00000265686; ENSP00000265686; ENSG00000110719. [Q13488-1]
Ensembl; ENST00000532635; ENSP00000434407; ENSG00000110719. [Q13488-2]
GeneID; 10312; -.
KEGG; hsa:10312; -.
UCSC; uc001one.4; human. [Q13488-1]
CTD; 10312; -.
DisGeNET; 10312; -.
EuPathDB; HostDB:ENSG00000110719.9; -.
GeneCards; TCIRG1; -.
HGNC; HGNC:11647; TCIRG1.
HPA; HPA038742; -.
MalaCards; TCIRG1; -.
MIM; 259700; phenotype.
MIM; 604592; gene.
neXtProt; NX_Q13488; -.
OpenTargets; ENSG00000110719; -.
Orphanet; 486; Autosomal dominant severe congenital neutropenia.
Orphanet; 667; Autosomal recessive malignant osteopetrosis.
PharmGKB; PA36399; -.
eggNOG; KOG2189; Eukaryota.
eggNOG; COG1269; LUCA.
GeneTree; ENSGT00390000004941; -.
HOGENOM; HOG000037059; -.
HOVERGEN; HBG014606; -.
InParanoid; Q13488; -.
KO; K02154; -.
OMA; WRACRGF; -.
OrthoDB; EOG091G031W; -.
PhylomeDB; Q13488; -.
TreeFam; TF300346; -.
BioCyc; MetaCyc:ENSG00000110719-MONOMER; -.
Reactome; R-HSA-1222556; ROS, RNS production in phagocytes.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-77387; Insulin receptor recycling.
Reactome; R-HSA-917977; Transferrin endocytosis and recycling.
Reactome; R-HSA-983712; Ion channel transport.
ChiTaRS; TCIRG1; human.
GeneWiki; TCIRG1; -.
GenomeRNAi; 10312; -.
PRO; PR:Q13488; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000110719; -.
CleanEx; HS_TCIRG1; -.
ExpressionAtlas; Q13488; baseline and differential.
Genevisible; Q13488; HS.
GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
GO; GO:0010008; C:endosome membrane; TAS:Reactome.
GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IBA:GO_Central.
GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
GO; GO:0051117; F:ATPase binding; IBA:GO_Central.
GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IBA:GO_Central.
GO; GO:0005215; F:transporter activity; TAS:ProtInc.
GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
GO; GO:0015986; P:ATP synthesis coupled proton transport; IBA:GO_Central.
GO; GO:0006968; P:cellular defense response; TAS:ProtInc.
GO; GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome.
GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
GO; GO:0016236; P:macroautophagy; ISS:ParkinsonsUK-UCL.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0090383; P:phagosome acidification; TAS:Reactome.
GO; GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc.
GO; GO:0007039; P:protein catabolic process in the vacuole; ISS:ParkinsonsUK-UCL.
GO; GO:0015992; P:proton transport; TAS:ProtInc.
GO; GO:0033572; P:transferrin transport; TAS:Reactome.
GO; GO:0007035; P:vacuolar acidification; IBA:GO_Central.
GO; GO:0070072; P:vacuolar proton-transporting V-type ATPase complex assembly; IBA:GO_Central.
InterPro; IPR002490; V-ATPase_116kDa_su.
InterPro; IPR026028; V-type_ATPase_116kDa_su_euka.
PANTHER; PTHR11629; PTHR11629; 1.
Pfam; PF01496; V_ATPase_I; 1.
PIRSF; PIRSF001293; ATP6V0A1; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Disease mutation;
Hydrogen ion transport; Ion transport; Membrane; Osteopetrosis;
Reference proteome; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 830 V-type proton ATPase 116 kDa subunit a
isoform 3.
/FTId=PRO_0000119218.
TOPO_DOM 1 385 Cytoplasmic. {ECO:0000255}.
TRANSMEM 386 404 Helical. {ECO:0000255}.
TOPO_DOM 405 406 Vacuolar. {ECO:0000255}.
TRANSMEM 407 423 Helical. {ECO:0000255}.
TOPO_DOM 424 438 Cytoplasmic. {ECO:0000255}.
TRANSMEM 439 468 Helical. {ECO:0000255}.
TOPO_DOM 469 532 Vacuolar. {ECO:0000255}.
TRANSMEM 533 552 Helical. {ECO:0000255}.
TOPO_DOM 553 570 Cytoplasmic. {ECO:0000255}.
TRANSMEM 571 591 Helical. {ECO:0000255}.
TOPO_DOM 592 635 Vacuolar. {ECO:0000255}.
TRANSMEM 636 655 Helical. {ECO:0000255}.
TOPO_DOM 656 720 Cytoplasmic. {ECO:0000255}.
TRANSMEM 721 745 Helical. {ECO:0000255}.
TOPO_DOM 746 766 Vacuolar. {ECO:0000255}.
TRANSMEM 767 807 Helical. {ECO:0000255}.
TOPO_DOM 808 830 Cytoplasmic. {ECO:0000255}.
VAR_SEQ 1 216 Missing (in isoform Short).
{ECO:0000303|Ref.2}.
/FTId=VSP_000345.
VARIANT 56 56 R -> W (in dbSNP:rs36027301).
/FTId=VAR_054340.
VARIANT 141 141 A -> P (in OPTB1).
{ECO:0000269|PubMed:15300850}.
/FTId=VAR_020988.
VARIANT 161 161 P -> L (in dbSNP:rs34227834).
/FTId=VAR_054341.
VARIANT 405 405 G -> R (in OPTB1; dbSNP:rs137853150).
{ECO:0000269|PubMed:11532986,
ECO:0000269|PubMed:12552563,
ECO:0000269|PubMed:15300850}.
/FTId=VAR_019569.
VARIANT 444 444 R -> L (in OPTB1; dbSNP:rs137853151).
{ECO:0000269|PubMed:11532986}.
/FTId=VAR_019570.
VARIANT 462 462 Missing (in OPTB1).
{ECO:0000269|PubMed:15300850}.
/FTId=VAR_020989.
VARIANT 517 517 D -> N (in OPTB1; dbSNP:rs369264588).
{ECO:0000269|PubMed:15300850}.
/FTId=VAR_020990.
VARIANT 775 775 P -> R (in OPTB1).
{ECO:0000269|PubMed:15300850}.
/FTId=VAR_020991.
CONFLICT 377 377 A -> R (in Ref. 1; AAA97878).
{ECO:0000305}.
CONFLICT 603 603 Missing (in Ref. 1; AAA97878).
{ECO:0000305}.
SEQUENCE 830 AA; 92968 MW; 50751B41B171D9D2 CRC64;
MGSMFRSEEV ALVQLFLPTA AAYTCVSRLG ELGLVEFRDL NASVSAFQRR FVVDVRRCEE
LEKTFTFLQE EVRRAGLVLP PPKGRLPAPP PRDLLRIQEE TERLAQELRD VRGNQQALRA
QLHQLQLHAA VLRQGHEPQL AAAHTDGASE RTPLLQAPGG PHQDLRVNFV AGAVEPHKAP
ALERLLWRAC RGFLIASFRE LEQPLEHPVT GEPATWMTFL ISYWGEQIGQ KIRKITDCFH
CHVFPFLQQE EARLGALQQL QQQSQELQEV LGETERFLSQ VLGRVLQLLP PGQVQVHKMK
AVYLALNQCS VSTTHKCLIA EAWCSVRDLP ALQEALRDSS MEEGVSAVAH RIPCRDMPPT
LIRTNRFTAS FQGIVDAYGV GRYQEVNPAP YTIITFPFLF AVMFGDVGHG LLMFLFALAM
VLAENRPAVK AAQNEIWQTF FRGRYLLLLM GLFSIYTGFI YNECFSRATS IFPSGWSVAA
MANQSGWSDA FLAQHTMLTL DPNVTGVFLG PYPFGIDPIW SLAANHLSFL NSFKMKMSVI
LGVVHMAFGV VLGVFNHVHF GQRHRLLLET LPELTFLLGL FGYLVFLVIY KWLCVWAARA
ASAPSILIHF INMFLFSHSP SNRLLYPRQE VVQATLVVLA LAMVPILLLG TPLHLLHRHR
RRLRRRPADR QEENKAGLLD LPDASVNGWS SDEEKAGGLD DEEEAELVPS EVLMHQAIHT
IEFCLGCVSN TASYLRLWAL SLAHAQLSEV LWAMVMRIGL GLGREVGVAA VVLVPIFAAF
AVMTVAILLV MEGLSAFLHA LRLHWVEFQN KFYSGTGYKL SPFTFAATDD


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