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SO2B1_MOUSE
ID   SO2B1_MOUSE             Reviewed;         683 AA.
AC   Q8BXB6; Q8BLV8;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Solute carrier organic anion transporter family member 2B1;
DE   AltName: Full=Solute carrier family 21 member 9;
GN   Name=Slco2b1; Synonyms=Oatp2b1, Slc21a9;
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 [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Aorta, and Head;
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   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17208939; DOI=10.1074/mcp.m600218-mcp200;
RA   Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT   "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT   MS/MS/MS.";
RL   Mol. Cell. Proteomics 6:669-676(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT   chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Mediates the Na(+)-independent transport of organic anions
CC       such as taurocholate, the prostaglandins PGD2, PGE1, PGE2, leukotriene
CC       C4, thromboxane B2 and iloprost. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the organo anion transporter (TC 2.A.60) family.
CC       {ECO:0000305}.
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DR   EMBL; AK041144; BAC30838.1; -; mRNA.
DR   EMBL; AK048120; BAC33248.1; -; mRNA.
DR   CCDS; CCDS21485.1; -.
DR   RefSeq; NP_001239459.1; NM_001252530.1.
DR   RefSeq; NP_001239460.1; NM_001252531.1.
DR   RefSeq; NP_780525.1; NM_175316.3.
DR   RefSeq; XP_011239942.1; XM_011241640.2.
DR   RefSeq; XP_011239943.1; XM_011241641.2.
DR   AlphaFoldDB; Q8BXB6; -.
DR   SMR; Q8BXB6; -.
DR   STRING; 10090.ENSMUSP00000032985; -.
DR   GlyGen; Q8BXB6; 4 sites.
DR   iPTMnet; Q8BXB6; -.
DR   PhosphoSitePlus; Q8BXB6; -.
DR   jPOST; Q8BXB6; -.
DR   MaxQB; Q8BXB6; -.
DR   PaxDb; Q8BXB6; -.
DR   PRIDE; Q8BXB6; -.
DR   ProteomicsDB; 261105; -.
DR   Antibodypedia; 17309; 109 antibodies from 18 providers.
DR   DNASU; 101488; -.
DR   Ensembl; ENSMUST00000032985; ENSMUSP00000032985; ENSMUSG00000030737.
DR   Ensembl; ENSMUST00000107086; ENSMUSP00000102701; ENSMUSG00000030737.
DR   GeneID; 101488; -.
DR   KEGG; mmu:101488; -.
DR   UCSC; uc009ilw.2; mouse.
DR   CTD; 11309; -.
DR   MGI; MGI:1351872; Slco2b1.
DR   VEuPathDB; HostDB:ENSMUSG00000030737; -.
DR   eggNOG; KOG3626; Eukaryota.
DR   GeneTree; ENSGT01050000244906; -.
DR   HOGENOM; CLU_008954_4_1_1; -.
DR   InParanoid; Q8BXB6; -.
DR   OMA; FMLGSAM; -.
DR   OrthoDB; 1029129at2759; -.
DR   TreeFam; TF317540; -.
DR   Reactome; R-MMU-189483; Heme degradation.
DR   Reactome; R-MMU-879518; Transport of organic anions.
DR   Reactome; R-MMU-9749641; Aspirin ADME.
DR   Reactome; R-MMU-9754706; Atorvastatin ADME.
DR   BioGRID-ORCS; 101488; 4 hits in 72 CRISPR screens.
DR   ChiTaRS; Slco2b1; mouse.
DR   PRO; PR:Q8BXB6; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q8BXB6; protein.
DR   Bgee; ENSMUSG00000030737; Expressed in brain blood vessel and 187 other tissues.
DR   ExpressionAtlas; Q8BXB6; baseline and differential.
DR   Genevisible; Q8BXB6; MM.
DR   GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR   GO; GO:0009925; C:basal plasma membrane; ISO:MGI.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0015125; F:bile acid transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0008514; F:organic anion transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0015347; F:sodium-independent organic anion transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0015721; P:bile acid and bile salt transport; ISO:MGI.
DR   GO; GO:0015711; P:organic anion transport; ISO:MGI.
DR   GO; GO:0071718; P:sodium-independent icosanoid transport; ISO:MGI.
DR   GO; GO:0043252; P:sodium-independent organic anion transport; IBA:GO_Central.
DR   GO; GO:0055085; P:transmembrane transport; ISO:MGI.
DR   Gene3D; 1.20.1250.20; -; 1.
DR   InterPro; IPR002350; Kazal_dom.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   InterPro; IPR004156; OATP.
DR   PANTHER; PTHR11388; PTHR11388; 1.
DR   Pfam; PF03137; OATP; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   TIGRFAMs; TIGR00805; oat; 1.
DR   PROSITE; PS51465; KAZAL_2; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Disulfide bond; Glycoprotein; Ion transport; Membrane;
KW   Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..683
FT                   /note="Solute carrier organic anion transporter family
FT                   member 2B1"
FT                   /id="PRO_0000191062"
FT   TOPO_DOM        1..41
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        42..61
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        62..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..107
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        108..132
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        133..177
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        178..207
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        208..226
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        227..247
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        248..265
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        266..290
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        291..355
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        356..377
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        378..397
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        398..421
FT                   /note="Helical; Name=8"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        422..425
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        426..449
FT                   /note="Helical; Name=9"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        450..553
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        554..576
FT                   /note="Helical; Name=10"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        577..585
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        586..611
FT                   /note="Helical; Name=11"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        612..644
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        645..662
FT                   /note="Helical; Name=12"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        663..683
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          472..532
FT                   /note="Kazal-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..25
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         21
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17208939,
FT                   ECO:0007744|PubMed:18630941"
FT   MOD_RES         312
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O94956"
FT   MOD_RES         315
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JHI3"
FT   CARBOHYD        143
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        166
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        527
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        534
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        478..509
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        484..505
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        493..530
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
SQ   SEQUENCE   683 AA;  74531 MW;  20D977BA1482688A CRC64;
     MPDRSTKTTM GTEDMHERKV SVEPQDSHQD AQPRGMFHNI KFFVLCHSLL QLTQLMISGY
     LKSSISTVEK RFGLSSQISG LLAAFNEVGN VSLILFVSYF GSRVHRPRMI GYGALLVATA
     GLLMALPHFI SEPYRYDHSS SDNRSLDFEA SLCLPTTMAP ASALSNGSCS SHTETKHLTM
     VGIMFAAQTL LGIGGVPIQP FGISYIDDFA HHSNSPLYIG ILFGITTMGP GLAYGLGSLM
     LRLYVDIDRM PEGGINLTPK DPRWVGAWWL GFLISSGLVV LASSPYFFFP REMPKEKHEF
     HFRRKVLASA ASTASKGEDL SSQHEPLKKQ AGLAQIAPDL TLVQFVKVFP RVLLRNLRHP
     IFLLVVLSQV CTSSMVAGMA TFLPKFLERQ FSITASFANM LLGCLTIPLV IVGIMMGGVL
     VKRLHLSPVQ CSALCLLGSL LCLLFSVPLF FIGCSTHQIA GITQDLGAQP GPSLFPGCSE
     PCSCQSDDFN PVCDTSAYVE YTTPCHAGCT GRVVQEALGK SQVFYTNCSC VAGNGTVPAG
     SCESACSRLV LPFIVLFSLG AGLASITHTP SFMLILRGVK KEDKTLAVGM QFMLLRVLAW
     MPSPVIHGSA IDTTCVHWAL TCGRRAVCRY YDHDLLRNRF IGLQFFFKSG SLVCFTLVLA
     ILRQQSREAS TRTTVKSSEL QQL
 
 
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