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S7A13_MOUSE
ID   S7A13_MOUSE             Reviewed;         478 AA.
AC   Q91WN3;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Solute carrier family 7 member 13;
DE   AltName: Full=Sodium-independent aspartate/glutamate transporter 1;
DE   AltName: Full=X-amino acid transporter 2;
GN   Name=Slc7a13; Synonyms=Agt1, Xat2;
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], AND TISSUE SPECIFICITY.
RC   STRAIN=BALB/cJ; TISSUE=Kidney;
RX   PubMed=11943479; DOI=10.1016/s0378-1119(02)00435-3;
RA   Blondeau J.-P.;
RT   "Homologues of amino acid permeases: cloning and tissue expression of XAT1
RT   and XAT2.";
RL   Gene 286:241-248(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC   STRAIN=ICR; TISSUE=Kidney;
RX   PubMed=11907033; DOI=10.1074/jbc.m200019200;
RA   Matsuo H., Kanai Y., Kim J.Y., Chairoungdua A., Kim D.K., Inatomi J.,
RA   Shigeta Y., Ishimine H., Chaekuntode S., Tachampa K., Choi H.W., Babu E.,
RA   Fukuda J., Endou H.;
RT   "Identification of a novel Na+-independent acidic amino acid transporter
RT   with structural similarity to the member of a heterodimeric amino acid
RT   transporter family associated with unknown heavy chains.";
RL   J. Biol. Chem. 277:21017-21026(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Spleen;
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).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney;
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).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney;
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 transport L-aspartate and L-glutamate in a
CC       sodium-independent manner. {ECO:0000269|PubMed:11907033}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in the kidney.
CC       {ECO:0000269|PubMed:11907033, ECO:0000269|PubMed:11943479}.
CC   -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC       superfamily. {ECO:0000305}.
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DR   EMBL; AJ417662; CAD10394.1; -; mRNA.
DR   EMBL; AB072352; BAC00494.1; -; mRNA.
DR   EMBL; AK143768; BAE25532.1; -; mRNA.
DR   EMBL; BX470225; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC014684; AAH14684.1; -; mRNA.
DR   CCDS; CCDS17993.1; -.
DR   RefSeq; NP_083022.1; NM_028746.3.
DR   AlphaFoldDB; Q91WN3; -.
DR   SMR; Q91WN3; -.
DR   STRING; 10090.ENSMUSP00000036228; -.
DR   TCDB; 2.A.3.8.8; the amino acid-polyamine-organocation (apc) family.
DR   PhosphoSitePlus; Q91WN3; -.
DR   jPOST; Q91WN3; -.
DR   PaxDb; Q91WN3; -.
DR   PRIDE; Q91WN3; -.
DR   ProteomicsDB; 256911; -.
DR   Antibodypedia; 54555; 5 antibodies from 4 providers.
DR   DNASU; 74087; -.
DR   Ensembl; ENSMUST00000035890; ENSMUSP00000036228; ENSMUSG00000041052.
DR   GeneID; 74087; -.
DR   KEGG; mmu:74087; -.
DR   UCSC; uc008scf.2; mouse.
DR   CTD; 157724; -.
DR   MGI; MGI:1921337; Slc7a13.
DR   VEuPathDB; HostDB:ENSMUSG00000041052; -.
DR   eggNOG; KOG1287; Eukaryota.
DR   GeneTree; ENSGT00940000162798; -.
DR   HOGENOM; CLU_007946_3_0_1; -.
DR   InParanoid; Q91WN3; -.
DR   OMA; SPNVHYV; -.
DR   OrthoDB; 621852at2759; -.
DR   PhylomeDB; Q91WN3; -.
DR   TreeFam; TF313355; -.
DR   BioGRID-ORCS; 74087; 4 hits in 72 CRISPR screens.
DR   PRO; PR:Q91WN3; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q91WN3; protein.
DR   Bgee; ENSMUSG00000041052; Expressed in right kidney and 30 other tissues.
DR   Genevisible; Q91WN3; MM.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0046982; F:protein heterodimerization activity; IPI:MGI.
DR   GO; GO:0015810; P:aspartate transmembrane transport; IDA:MGI.
DR   GO; GO:0015811; P:L-cystine transport; IDA:MGI.
DR   GO; GO:0015813; P:L-glutamate transmembrane transport; IDA:MGI.
DR   InterPro; IPR002293; AA/rel_permease1.
DR   Pfam; PF13520; AA_permease_2; 1.
PE   1: Evidence at protein level;
KW   Amino-acid transport; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..478
FT                   /note="Solute carrier family 7 member 13"
FT                   /id="PRO_0000330726"
FT   TOPO_DOM        1..14
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        15..35
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        36..47
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        48..68
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        69..89
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        90..110
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        111..129
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        130..150
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        151..163
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        164..184
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        185..208
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        209..229
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        230..242
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        243..263
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        264..288
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        289..309
FT                   /note="Helical; Name=8"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        310..338
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        339..359
FT                   /note="Helical; Name=9"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        360
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        361..381
FT                   /note="Helical; Name=10"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        382..395
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        396..416
FT                   /note="Helical; Name=11"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        417..423
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        424..444
FT                   /note="Helical; Name=12"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        445..478
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   478 AA;  53233 MW;  AF9B82699ED66AB8 CRC64;
     MAMDSKKEIR LKRELGYFWG TNFLIINIIG AGIFVSPKGV LQHSSMNVGV SLCVWAVCAV
     LTLTSALCSA EIGITFPYSG AHYYFLKRCF GPLVAFLRLW TSLFLGPGLI ASQALLLAEY
     GVQPFYPSCS APILPRKCLA LAMLWIVGIL NSRGVKELSW LQTVSSVLKV GILGVISLSG
     LFLLVRGKKE NVQRLQNAFD AEFPEVSQLI EAIFQGYFAF SGGGCFTCIA GELKKPSKTI
     PRCIFTGLPL VTVVYLLANI SYLTVLTPQE MLSSDAVALT WTDRVIPQFT WTVPFAISAS
     LFINLVINVL ETSRVLYIAS ENGQLPLLFC ALNVHSSPFI AVLLIISMAS ILIVLTNLID
     LINYLYFVVS IWTALSIIGI LKLRYQEPNL HRPYKVFLPF TFIALGITLS LVLIPLVKSP
     KLHYIYVFLF LLSGLVFYVP LIHFKVKFVW FQKLTCYLQL LFNICIPDVS DDHIHEES
 
 
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