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ORCT_DROME
ID   ORCT_DROME              Reviewed;         548 AA.
AC   Q9VCA2; O01383; O01384;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 154.
DE   RecName: Full=Organic cation transporter protein;
GN   Name=Orct; ORFNames=CG6331;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Larva;
RX   PubMed=9409773; DOI=10.1016/s0378-1119(97)00429-0;
RA   Taylor C.A.M., Stanley K., Shirras A.D.;
RT   "The Orct gene of Drosophila melanogaster codes for a putative organic
RT   cation transporter with six or 12 transmembrane domains.";
RL   Gene 201:69-74(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
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   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Head;
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   [5]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-97, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-linked
RT   cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
CC   -!- FUNCTION: Probably transports organic cations. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in embryos and adults at low level.
CC       Expressed at higher level in third instar larvae.
CC   -!- SIMILARITY: Belongs to the major facilitator (TC 2.A.1) superfamily.
CC       Organic cation transporter (TC 2.A.1.19) family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA73030.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA.; Evidence={ECO:0000305};
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DR   EMBL; Y12399; CAA73030.1; ALT_SEQ; mRNA.
DR   EMBL; Y12400; CAA73031.1; -; mRNA.
DR   EMBL; AE014297; AAF56271.1; -; Genomic_DNA.
DR   EMBL; AY058437; AAL13666.1; -; mRNA.
DR   RefSeq; NP_001262908.1; NM_001275979.1.
DR   RefSeq; NP_524479.1; NM_079755.2.
DR   AlphaFoldDB; Q9VCA2; -.
DR   SMR; Q9VCA2; -.
DR   BioGRID; 67819; 1.
DR   IntAct; Q9VCA2; 1.
DR   STRING; 7227.FBpp0083983; -.
DR   TCDB; 2.A.1.19.36; the major facilitator superfamily (mfs).
DR   GlyGen; Q9VCA2; 4 sites.
DR   iPTMnet; Q9VCA2; -.
DR   PaxDb; Q9VCA2; -.
DR   PRIDE; Q9VCA2; -.
DR   DNASU; 42891; -.
DR   EnsemblMetazoa; FBtr0084599; FBpp0083983; FBgn0019952.
DR   EnsemblMetazoa; FBtr0334870; FBpp0306893; FBgn0019952.
DR   GeneID; 42891; -.
DR   KEGG; dme:Dmel_CG6331; -.
DR   CTD; 42891; -.
DR   FlyBase; FBgn0019952; Orct.
DR   VEuPathDB; VectorBase:FBgn0019952; -.
DR   eggNOG; KOG0255; Eukaryota.
DR   GeneTree; ENSGT00940000167832; -.
DR   HOGENOM; CLU_001265_33_4_1; -.
DR   InParanoid; Q9VCA2; -.
DR   OMA; VQMFFSV; -.
DR   OrthoDB; 704438at2759; -.
DR   PhylomeDB; Q9VCA2; -.
DR   Reactome; R-DME-112311; Neurotransmitter clearance.
DR   Reactome; R-DME-181430; Norepinephrine Neurotransmitter Release Cycle.
DR   Reactome; R-DME-197264; Nicotinamide salvaging.
DR   Reactome; R-DME-200425; Carnitine metabolism.
DR   Reactome; R-DME-2161517; Abacavir transmembrane transport.
DR   Reactome; R-DME-442660; Na+/Cl- dependent neurotransmitter transporters.
DR   Reactome; R-DME-549127; Organic cation transport.
DR   Reactome; R-DME-561048; Organic anion transport.
DR   Reactome; R-DME-9749641; Aspirin ADME.
DR   BioGRID-ORCS; 42891; 0 hits in 3 CRISPR screens.
DR   ChiTaRS; Orct; fly.
DR   GenomeRNAi; 42891; -.
DR   PRO; PR:Q9VCA2; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0019952; Expressed in saliva-secreting gland and 34 other tissues.
DR   ExpressionAtlas; Q9VCA2; baseline and differential.
DR   Genevisible; Q9VCA2; DM.
DR   GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0006915; P:apoptotic process; TAS:UniProtKB.
DR   GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.1250.20; -; 1.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR005828; MFS_sugar_transport-like.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   Pfam; PF00083; Sugar_tr; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Ion transport; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..548
FT                   /note="Organic cation transporter protein"
FT                   /id="PRO_0000220514"
FT   TOPO_DOM        1..22
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        23..43
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        44..127
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        128..148
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        149..158
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        159..179
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        180..189
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        190..210
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        211..219
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        220..240
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        241..244
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        245..265
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        266..337
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        338..358
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        359..366
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        367..387
FT                   /note="Helical; Name=8"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        388..395
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        396..416
FT                   /note="Helical; Name=9"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        417..419
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        420..440
FT                   /note="Helical; Name=10"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        441..453
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        454..474
FT                   /note="Helical; Name=11"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        475..482
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        483..503
FT                   /note="Helical; Name=12"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        504..548
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          512..548
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        533..548
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        55
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        67
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        89
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        97
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973"
FT   CONFLICT        375
FT                   /note="A -> P (in Ref. 1; CAA73031)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        385
FT                   /note="L -> F (in Ref. 1; CAA73031)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        501
FT                   /note="L -> R (in Ref. 1; CAA73031)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   548 AA;  61003 MW;  08D7F97599B477AF CRC64;
     MGYDDVITHL GEFGPYQKRI YYLLCLPAIV CAFHKLAGVF LLAKPDFRCA LPYENGSIYE
     LSPHLWNLSY PENERCSYYD VDYTEEYLNG SIPRSSNETK TCSSYVYDRS KYLNSAVTEW
     NLVCSRSLLS ATSDSLFMLG VLLGSLIFGQ MSDKLGRKPT FFASLVLQLI FGVLAAVAPE
     YFSYTISRMI VGATTSGVFL VAYVIALEMV GSSYRLFAGV AMQMFFSVGF MLTAGFAYFI
     HDWRWLQIAI TLPGLLFLCY YWIIPESARW LLMKGRKDEA FVIIEKAAKE NKVEVPNEIY
     EQLVDEVAEK KKQDEMAASQ PAATVFDLLR YPNLRRKTLL IFFDWFVNSG VYYGLSWNTN
     NLGGNQLVNF MISGAVEIPG YTLLLFTLNR WGRRSILCGT MMVAGISLLA TIFVPSDMNW
     LIVACAMIGK LAITSSYGTI YIFSAEQFPT VVRNVGLGAS SMVARVGGIL APYLKLLGEI
     WRPLPLIICG ALSLTAGLLS LLLPETLNKP MPETIEDGEN FGKKPAPQET AEEGGTQELS
     GMLNGKSG
 
 
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