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TSCOT_MOUSE
ID   TSCOT_MOUSE             Reviewed;         479 AA.
AC   Q8CA03; A2ANT4; Q9D3J2; Q9JLQ3;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 2.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Thymic stromal cotransporter protein;
DE   AltName: Full=Solute carrier family 46 member 2;
GN   Name=Slc46a2; Synonyms=Tscot;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], GLYCOSYLATION, TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RC   TISSUE=Thymus;
RX   PubMed=10706709; DOI=10.4049/jimmunol.164.6.3185;
RA   Kim M.G., Flomerfelt F.A., Lee K.-N., Chen C., Schwartz R.H.;
RT   "A putative 12 transmembrane domain cotransporter expressed in thymic
RT   cortical epithelial cells.";
RL   J. Immunol. 164:3185-3192(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC   STRAIN=129;
RX   PubMed=10978518; DOI=10.1016/s0167-4781(00)00177-9;
RA   Chen C., Kim M.G., Lyu M.S., Kozak C.A., Schwartz R.H., Flomerfelt F.A.;
RT   "Characterization of the mouse gene, human promoter and human cDNA of TSCOT
RT   reveals strong interspecies homology.";
RL   Biochim. Biophys. Acta 1493:159-169(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- FUNCTION: May act as a transporter. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed on cortical epithelial cells in the
CC       thymus. Mainly expressed in the thymic cortex and is highly enriched in
CC       SCID thymus. Also expressed in lymph nodes, heart, fetal liver, brain,
CC       spleen, intestine and kidney, but not in adult liver, skin, skeletal
CC       muscle and lung. {ECO:0000269|PubMed:10706709,
CC       ECO:0000269|PubMed:10978518}.
CC   -!- DEVELOPMENTAL STAGE: Highly expressed during fetal thymus development
CC       and decreases after day 16. {ECO:0000269|PubMed:10706709}.
CC   -!- PTM: Glycosylated. {ECO:0000269|PubMed:10706709}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. SLC46A
CC       family. {ECO:0000305}.
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DR   EMBL; AF148145; AAF73110.1; -; mRNA.
DR   EMBL; AF242559; AAK28344.1; -; Genomic_DNA.
DR   EMBL; AK017363; BAB30710.1; -; mRNA.
DR   EMBL; AK040063; BAC30504.1; -; mRNA.
DR   EMBL; AL831738; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS18227.1; -.
DR   RefSeq; NP_066395.3; NM_021053.4.
DR   AlphaFoldDB; Q8CA03; -.
DR   SMR; Q8CA03; -.
DR   STRING; 10090.ENSMUSP00000030081; -.
DR   GlyGen; Q8CA03; 2 sites.
DR   PhosphoSitePlus; Q8CA03; -.
DR   PaxDb; Q8CA03; -.
DR   PRIDE; Q8CA03; -.
DR   ProteomicsDB; 298141; -.
DR   Antibodypedia; 29714; 59 antibodies from 18 providers.
DR   DNASU; 30936; -.
DR   Ensembl; ENSMUST00000030081; ENSMUSP00000030081; ENSMUSG00000028386.
DR   GeneID; 30936; -.
DR   KEGG; mmu:30936; -.
DR   UCSC; uc008taf.2; mouse.
DR   CTD; 57864; -.
DR   MGI; MGI:1353616; Slc46a2.
DR   VEuPathDB; HostDB:ENSMUSG00000028386; -.
DR   eggNOG; KOG2816; Eukaryota.
DR   GeneTree; ENSGT00950000183096; -.
DR   HOGENOM; CLU_028365_3_0_1; -.
DR   InParanoid; Q8CA03; -.
DR   OMA; AYWSGVM; -.
DR   OrthoDB; 763423at2759; -.
DR   PhylomeDB; Q8CA03; -.
DR   TreeFam; TF315701; -.
DR   BioGRID-ORCS; 30936; 1 hit in 71 CRISPR screens.
DR   PRO; PR:Q8CA03; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q8CA03; protein.
DR   Bgee; ENSMUSG00000028386; Expressed in tail skin and 26 other tissues.
DR   Genevisible; Q8CA03; MM.
DR   GO; GO:0009986; C:cell surface; IDA:MGI.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0070233; P:negative regulation of T cell apoptotic process; IGI:MGI.
DR   GO; GO:0070430; P:positive regulation of nucleotide-binding oligomerization domain containing 1 signaling pathway; ISO:MGI.
DR   GO; GO:0045580; P:regulation of T cell differentiation; IGI:MGI.
DR   GO; GO:0043029; P:T cell homeostasis; IGI:MGI.
DR   GO; GO:0048538; P:thymus development; IGI:MGI.
DR   GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR   Gene3D; 1.20.1250.20; -; 1.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   InterPro; IPR001958; Tet-R_TetA/multi-R_MdtG.
DR   Pfam; PF07690; MFS_1; 1.
DR   PRINTS; PR01035; TCRTETA.
DR   SUPFAM; SSF103473; SSF103473; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..479
FT                   /note="Thymic stromal cotransporter protein"
FT                   /id="PRO_0000065660"
FT   TOPO_DOM        1..23
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        24..44
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        45..80
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        81..101
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        102..110
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        111..131
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        132..140
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        141..161
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        162..174
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        175..195
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        196..207
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        208..228
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        229..281
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        282..302
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        303..321
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        322..342
FT                   /note="Helical; Name=8"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        343..348
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        349..369
FT                   /note="Helical; Name=9"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        370..371
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        372..392
FT                   /note="Helical; Name=10"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        393..407
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        408..428
FT                   /note="Helical; Name=11"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        429..441
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        442..462
FT                   /note="Helical; Name=12"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        463..479
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          255..277
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        257..276
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        57
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        61
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        94
FT                   /note="S -> T (in Ref. 3; BAB30710)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        274
FT                   /note="G -> R (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        465
FT                   /note="V -> I (in Ref. 3; BAC30504)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   479 AA;  52083 MW;  EC8BEF1E446A5CFB CRC64;
     MGPGGTCPWS SRLSGFRVRT WIEPVVASTQ VAGSLYDAGL LLVVKESFKS EAGGSSNYSA
     NQSLVEYQED QQQKAISNFN IIYNLVLGLT PLLSAYGLGW LSDRYHRKIS ICTAMLGFLL
     SRIGLLLKVM LDWPVEVMYG AAALNGLCGS FSAYWSGVMA LGSLGCSEGR RSVRLILIDL
     VLGLAGFSGS MASGHLFKQI VGHSAQGLLL TACSVGCAAF ALFYSLFVLK VPESKPNKVH
     PTVDTVSGMM GTYRTLDPDQ QDKQNVPRNP RTPGKGKSSQ REVVALLFVG AIIYDLAAVG
     TVDVMALFVL KEPLHWNQVQ LGYGMASGYI IFITSFLGVL VFSRCFRDTT MIIIGMLSFG
     SGALLLAFVK ETYMFYIARA IMLFALIPIT TIRSAMSKLI KDSSYGKIFV ILQLCLTLTG
     VVTSTIYNKI YQLTLDKFIG TCFVLSSFLS FLAIVPIGVV AYKQVPRSQQ GECAEKQRS
 
 
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