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UCP5_HUMAN
ID   UCP5_HUMAN              Reviewed;         325 AA.
AC   O95258; D3DTG2; Q0VDH7; Q9HC60; Q9HC61;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 183.
DE   RecName: Full=Brain mitochondrial carrier protein 1;
DE            Short=BMCP-1;
DE   AltName: Full=Mitochondrial uncoupling protein 5;
DE            Short=UCP 5;
DE   AltName: Full=Solute carrier family 25 member 14;
GN   Name=SLC25A14; Synonyms=BMCP1, UCP5; ORFNames=UNQ791/PRO1682;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=9852133; DOI=10.1074/jbc.273.51.34611;
RA   Sanchis D., Fleury C., Chomiki N., Goubern M., Huang Q., Neverova M.,
RA   Gregoire F., Easlick J., Raimbault S., Levi-Meyrueis C., Miroux B.,
RA   Collins S., Seldin M., Richard D., Warden C., Bouillaud F., Ricquier D.;
RT   "BMCP1, a novel mitochondrial carrier with high expression in the central
RT   nervous system of humans and rodents, and respiration uncoupling activity
RT   in recombinant yeast.";
RL   J. Biol. Chem. 273:34611-34615(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RX   PubMed=10928996; DOI=10.1096/fj.99-0834com;
RA   Yu X.X., Mao W., Zhong A., Schow P., Brush J., Sherwood S.W., Adams S.H.,
RA   Pan G.;
RT   "Characterization of novel UCP5/BMCP1 isoforms and differential regulation
RT   of UCP4 and UCP5 expression through dietary or temperature manipulation.";
RL   FASEB J. 14:1611-1618(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA   Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA   Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA   Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA   Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA   Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA   Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA   Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA   Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA   Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA   Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA   Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA   Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA   Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA   Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA   Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA   Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA   Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA   Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA   Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA   Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA   Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA   Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA   Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA   Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA   Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA   Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA   Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA   Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA   Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA   Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA   Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA   d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA   Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA   Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA   Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA   Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA   Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA   Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA   Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
CC   -!- FUNCTION: Participates in the mitochondrial proton leak measured in
CC       brain mitochondria.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=UCP5L;
CC         IsoId=O95258-1; Sequence=Displayed;
CC       Name=2; Synonyms=UCP5S;
CC         IsoId=O95258-2; Sequence=VSP_003272;
CC       Name=3; Synonyms=UCP5SI;
CC         IsoId=O95258-3; Sequence=VSP_003272, VSP_003273;
CC   -!- TISSUE SPECIFICITY: Mainly expressed in brain. Some expression in
CC       testis and pituitary. {ECO:0000269|PubMed:10928996}.
CC   -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC       {ECO:0000305}.
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DR   EMBL; AF078544; AAD04346.1; -; mRNA.
DR   EMBL; AF155809; AAG29582.1; -; mRNA.
DR   EMBL; AF155810; AAG29583.1; -; mRNA.
DR   EMBL; AF155811; AAG29584.1; -; mRNA.
DR   EMBL; AY358099; AAQ88466.1; -; mRNA.
DR   EMBL; AL035423; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471107; EAX11804.1; -; Genomic_DNA.
DR   EMBL; BC119666; AAI19667.1; -; mRNA.
DR   EMBL; BC119667; AAI19668.1; -; mRNA.
DR   CCDS; CCDS14623.1; -. [O95258-1]
DR   CCDS; CCDS14624.1; -. [O95258-2]
DR   CCDS; CCDS76020.1; -. [O95258-3]
DR   RefSeq; NP_001269124.1; NM_001282195.1. [O95258-1]
DR   RefSeq; NP_001269125.1; NM_001282196.1. [O95258-2]
DR   RefSeq; NP_001269126.1; NM_001282197.1. [O95258-3]
DR   RefSeq; NP_001269127.1; NM_001282198.1.
DR   AlphaFoldDB; O95258; -.
DR   BioGRID; 114485; 30.
DR   IntAct; O95258; 7.
DR   STRING; 9606.ENSP00000477981; -.
DR   TCDB; 2.A.29.24.1; the mitochondrial carrier (mc) family.
DR   iPTMnet; O95258; -.
DR   PhosphoSitePlus; O95258; -.
DR   BioMuta; SLC25A14; -.
DR   EPD; O95258; -.
DR   jPOST; O95258; -.
DR   MassIVE; O95258; -.
DR   MaxQB; O95258; -.
DR   PaxDb; O95258; -.
DR   PeptideAtlas; O95258; -.
DR   PRIDE; O95258; -.
DR   ProteomicsDB; 50752; -. [O95258-1]
DR   ProteomicsDB; 50753; -. [O95258-2]
DR   ProteomicsDB; 50754; -. [O95258-3]
DR   Antibodypedia; 16263; 95 antibodies from 26 providers.
DR   DNASU; 9016; -.
DR   Ensembl; ENST00000218197.9; ENSP00000218197.5; ENSG00000102078.16. [O95258-1]
DR   Ensembl; ENST00000339231.3; ENSP00000342797.3; ENSG00000102078.16. [O95258-3]
DR   Ensembl; ENST00000361980.9; ENSP00000354455.5; ENSG00000102078.16. [O95258-2]
DR   Ensembl; ENST00000545805.6; ENSP00000444642.2; ENSG00000102078.16. [O95258-1]
DR   Ensembl; ENST00000612248.4; ENSP00000477981.1; ENSG00000102078.16. [O95258-3]
DR   GeneID; 9016; -.
DR   KEGG; hsa:9016; -.
DR   MANE-Select; ENST00000545805.6; ENSP00000444642.2; NM_001282195.2; NP_001269124.1.
DR   UCSC; uc004evp.3; human. [O95258-1]
DR   CTD; 9016; -.
DR   DisGeNET; 9016; -.
DR   GeneCards; SLC25A14; -.
DR   HGNC; HGNC:10984; SLC25A14.
DR   HPA; ENSG00000102078; Low tissue specificity.
DR   MIM; 300242; gene.
DR   neXtProt; NX_O95258; -.
DR   OpenTargets; ENSG00000102078; -.
DR   PharmGKB; PA35860; -.
DR   VEuPathDB; HostDB:ENSG00000102078; -.
DR   eggNOG; KOG0753; Eukaryota.
DR   GeneTree; ENSGT00940000159471; -.
DR   InParanoid; O95258; -.
DR   OMA; VWSNIIC; -.
DR   PhylomeDB; O95258; -.
DR   TreeFam; TF323211; -.
DR   PathwayCommons; O95258; -.
DR   Reactome; R-HSA-167826; The fatty acid cycling model.
DR   Reactome; R-HSA-167827; The proton buffering model.
DR   SignaLink; O95258; -.
DR   BioGRID-ORCS; 9016; 7 hits in 700 CRISPR screens.
DR   ChiTaRS; SLC25A14; human.
DR   GeneWiki; SLC25A14; -.
DR   GenomeRNAi; 9016; -.
DR   Pharos; O95258; Tbio.
DR   PRO; PR:O95258; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   RNAct; O95258; protein.
DR   Bgee; ENSG00000102078; Expressed in secondary oocyte and 191 other tissues.
DR   ExpressionAtlas; O95258; baseline and differential.
DR   Genevisible; O95258; HS.
DR   GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR   GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR   GO; GO:0005739; C:mitochondrion; TAS:ProtInc.
DR   GO; GO:0015297; F:antiporter activity; IBA:GO_Central.
DR   GO; GO:0015140; F:malate transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0015131; F:oxaloacetate transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0015141; F:succinate transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0015116; F:sulfate transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0015117; F:thiosulfate transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0009060; P:aerobic respiration; TAS:ProtInc.
DR   GO; GO:0071423; P:malate transmembrane transport; IBA:GO_Central.
DR   GO; GO:0006839; P:mitochondrial transport; IEA:InterPro.
DR   GO; GO:0015729; P:oxaloacetate transport; IBA:GO_Central.
DR   GO; GO:0035435; P:phosphate ion transmembrane transport; IBA:GO_Central.
DR   GO; GO:0071422; P:succinate transmembrane transport; IBA:GO_Central.
DR   GO; GO:0008272; P:sulfate transport; IBA:GO_Central.
DR   GO; GO:0015709; P:thiosulfate transport; IBA:GO_Central.
DR   Gene3D; 1.50.40.10; -; 1.
DR   InterPro; IPR002030; Mit_uncoupling_UCP-like.
DR   InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR   InterPro; IPR023395; Mt_carrier_dom_sf.
DR   InterPro; IPR032933; SLC25A14.
DR   PANTHER; PTHR45618:SF20; PTHR45618:SF20; 1.
DR   Pfam; PF00153; Mito_carr; 3.
DR   PRINTS; PR00784; MTUNCOUPLING.
DR   SUPFAM; SSF103506; SSF103506; 1.
DR   PROSITE; PS50920; SOLCAR; 3.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Reference proteome; Repeat; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..325
FT                   /note="Brain mitochondrial carrier protein 1"
FT                   /id="PRO_0000090677"
FT   TRANSMEM        38..54
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        112..128
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        141..161
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        199..215
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        240..256
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        298..315
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          42..131
FT                   /note="Solcar 1"
FT   REPEAT          139..224
FT                   /note="Solcar 2"
FT   REPEAT          233..323
FT                   /note="Solcar 3"
FT   VAR_SEQ         23..25
FT                   /note="Missing (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_003272"
FT   VAR_SEQ         198
FT                   /note="R -> RCLCSKAVTGCVLWLMPVIPALWEANAGGSLE (in isoform
FT                   3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_003273"
FT   VARIANT         55
FT                   /note="E -> A (in dbSNP:rs2143598)"
FT                   /id="VAR_050138"
SQ   SEQUENCE   325 AA;  36202 MW;  0447E8E3B5374982 CRC64;
     MGIFPGIILI FLRVKFATAA VIVSGHQKST TVSHEMSGLN WKPFVYGGLA SIVAEFGTFP
     VDLTKTRLQV QGQSIDARFK EIKYRGMFHA LFRICKEEGV LALYSGIAPA LLRQASYGTI
     KIGIYQSLKR LFVERLEDET LLINMICGVV SGVISSTIAN PTDVLKIRMQ AQGSLFQGSM
     IGSFIDIYQQ EGTRGLWRGV VPTAQRAAIV VGVELPVYDI TKKHLILSGM MGDTILTHFV
     SSFTCGLAGA LASNPVDVVR TRMMNQRAIV GHVDLYKGTV DGILKMWKHE GFFALYKGFW
     PNWLRLGPWN IIFFITYEQL KRLQI
 
 
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