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BMCP_DROME
ID   BMCP_DROME              Reviewed;         303 AA.
AC   Q7K566;
DT   18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Mitochondrial uncoupling protein Bmcp {ECO:0000305};
DE   AltName: Full=Brain mitochondrial carrier protein 1 {ECO:0000303|PubMed:15337852};
DE            Short=Bmcp-1 {ECO:0000303|PubMed:15337852};
DE   AltName: Full=Mitochondrial uncoupling protein 5 {ECO:0000305|PubMed:15337852};
GN   Name=Bmcp {ECO:0000312|FlyBase:FBgn0036199};
GN   Synonyms=Ucp5 {ECO:0000303|PubMed:15337852};
GN   ORFNames=CG7314 {ECO:0000312|FlyBase:FBgn0036199};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN   [1] {ECO:0000312|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2] {ECO:0000312|Proteomes:UP000000803}
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3] {ECO:0000312|EMBL:AAK92857.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley {ECO:0000312|EMBL:AAK92857.1};
RC   TISSUE=Head {ECO:0000312|EMBL:AAK92857.1};
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [4] {ECO:0000305}
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=15337852; DOI=10.1023/b:jobb.0000031973.20153.c6;
RA   Fridell Y.W., Sanchez-Blanco A., Silvia B.A., Helfand S.L.;
RT   "Functional characterization of a Drosophila mitochondrial uncoupling
RT   protein.";
RL   J. Bioenerg. Biomembr. 36:219-228(2004).
RN   [5] {ECO:0000305}
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=16387864; DOI=10.1534/genetics.105.053389;
RA   Sanchez-Blanco A., Fridell Y.W., Helfand S.L.;
RT   "Involvement of Drosophila uncoupling protein 5 in metabolism and aging.";
RL   Genetics 172:1699-1710(2006).
CC   -!- FUNCTION: Regulates metabolic homeostasis in response to nutritional
CC       cues and may therefore be involved in adaptation to dietary variations.
CC       May not function in creating mitochondrial proton leaks across the
CC       inner mitochondrial membrane (i.e. mitochondrial uncoupling).
CC       {ECO:0000269|PubMed:16387864}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expression levels are higher in the head than the
CC       body. {ECO:0000269|PubMed:15337852}.
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout development. Expression
CC       levels are very weak, but increase in the adult stages.
CC       {ECO:0000269|PubMed:15337852}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype. Reduced levels of total
CC       sugars (glucose and trehalose) in normal-fed flies and increased
CC       susceptibility to starvation. Life span is increased when fed a low-
CC       calorie diet and flies gain less weight when fed a high-calorie diet.
CC       Females lay a lower proportion of eggs, particularly under a restricted
CC       diet. Glycogen and triacylglyceride (TAG) levels are not affected in
CC       normal-fed flies. However, TAG levels decrease at a faster rate under
CC       starvation conditions. No increase in life span when fed a high-calorie
CC       diet or under starvation conditions. {ECO:0000269|PubMed:16387864}.
CC   -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Functions as a mitochondrial uncoupling protein when expressed
CC       in yeast. {ECO:0000269|PubMed:15337852}.
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DR   EMBL; AE014296; AAF50019.1; -; Genomic_DNA.
DR   EMBL; AE014296; AAN11881.1; -; Genomic_DNA.
DR   EMBL; AY051433; AAK92857.1; -; mRNA.
DR   RefSeq; NP_648501.1; NM_140244.5.
DR   RefSeq; NP_729738.1; NM_168472.2.
DR   AlphaFoldDB; Q7K566; -.
DR   SMR; Q7K566; -.
DR   STRING; 7227.FBpp0075846; -.
DR   PaxDb; Q7K566; -.
DR   PRIDE; Q7K566; -.
DR   DNASU; 39322; -.
DR   EnsemblMetazoa; FBtr0076114; FBpp0075845; FBgn0036199.
DR   EnsemblMetazoa; FBtr0076115; FBpp0075846; FBgn0036199.
DR   GeneID; 39322; -.
DR   KEGG; dme:Dmel_CG7314; -.
DR   UCSC; CG7314-RA; d. melanogaster.
DR   CTD; 39322; -.
DR   FlyBase; FBgn0036199; Bmcp.
DR   VEuPathDB; VectorBase:FBgn0036199; -.
DR   eggNOG; KOG0753; Eukaryota.
DR   GeneTree; ENSGT00940000173356; -.
DR   HOGENOM; CLU_015166_14_2_1; -.
DR   InParanoid; Q7K566; -.
DR   OMA; VWSNIIC; -.
DR   OrthoDB; 1126848at2759; -.
DR   PhylomeDB; Q7K566; -.
DR   Reactome; R-DME-167826; The fatty acid cycling model.
DR   Reactome; R-DME-167827; The proton buffering model.
DR   BioGRID-ORCS; 39322; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 39322; -.
DR   PRO; PR:Q7K566; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0036199; Expressed in cleaving embryo and 27 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
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:0071423; P:malate transmembrane transport; IBA:GO_Central.
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:0019222; P:regulation of metabolic process; IMP:FlyBase.
DR   GO; GO:0007605; P:sensory perception of sound; IMP:FlyBase.
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; IPR002067; Mit_carrier.
DR   InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR   InterPro; IPR023395; Mt_carrier_dom_sf.
DR   Pfam; PF00153; Mito_carr; 3.
DR   PRINTS; PR00926; MITOCARRIER.
DR   SUPFAM; SSF103506; SSF103506; 1.
DR   PROSITE; PS50920; SOLCAR; 3.
PE   2: Evidence at transcript level;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW   Repeat; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..303
FT                   /note="Mitochondrial uncoupling protein Bmcp"
FT                   /id="PRO_0000438778"
FT   TRANSMEM        10..27
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        72..90
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        112..131
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        171..190
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        209..229
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        278..297
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          8..97
FT                   /note="Solcar 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT   REPEAT          111..196
FT                   /note="Solcar 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
FT   REPEAT          203..303
FT                   /note="Solcar 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00282"
SQ   SEQUENCE   303 AA;  33493 MW;  E52A93E2A2E5AC48 CRC64;
     MGEVKDWRPF VYGGVASITA EFGTFPIDTT KTRLQIQGQK IDQSFSQLRY RGMTDAFVKI
     SREEGLRALY SGIWPAVLRQ ATYGTIKFGT YYTLKKLANE RGLLINEDGS ERVWSNILCA
     AAAGAISSAI ANPTDVLKVR MQVHGKGQHK GLLGCFGEIY KYEGVRGLWR GVGPTAQRAV
     VIASVELPVY DFCKLQLMNA FGDHVGNHFI SSFIASLGSA IASTPIDVIR TRLMNQRPVS
     ITMNGVVTAA ATPKLYSGSL DCAVQTIRNE GLPALYKGFI PTWVRMGPWN IIFFITYEQL
     KKY
 
 
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