ID   S47A1_MOUSE             Reviewed;         567 AA.
AC   Q8K0H1; Q5SS45; Q9CQ64;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 2.
DT   24-JAN-2024, entry version 141.
DE   RecName: Full=Multidrug and toxin extrusion protein 1;
DE            Short=MATE-1;
DE            Short=mMATE-1;
DE   AltName: Full=Solute carrier family 47 member 1;
GN   Name=Slc47a1; Synonyms=Mate1;
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] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Liver, and Tongue;
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   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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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   [4]
RP   TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=16330770; DOI=10.1073/pnas.0506483102;
RA   Otsuka M., Matsumoto T., Morimoto R., Arioka S., Omote H., Moriyama Y.;
RT   "A human transporter protein that mediates the final excretion step for
RT   toxic organic cations.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:17923-17928(2005).
RN   [5]
RP   SUBCELLULAR LOCATION, FUNCTION, TRANSPORTER ACTIVITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND TISSUE SPECIFICITY.
RX   PubMed=16641166; DOI=10.1152/ajpcell.00090.2006;
RA   Hiasa M., Matsumoto T., Komatsu T., Moriyama Y.;
RT   "Wide variety of locations for rodent MATE1, a transporter protein that
RT   mediates the final excretion step for toxic organic cations.";
RL   Am. J. Physiol. 291:C678-C686(2006).
RN   [6]
RP   DISRUPTION PHENOTYPE, FUNCTION, AND TRANSPORTER ACTIVITY.
RX   PubMed=19332510; DOI=10.1124/mol.109.056242;
RA   Tsuda M., Terada T., Mizuno T., Katsura T., Shimakura J., Inui K.;
RT   "Targeted disruption of the multidrug and toxin extrusion 1 (mate1) gene in
RT   mice reduces renal secretion of metformin.";
RL   Mol. Pharmacol. 75:1280-1286(2009).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND IDENTIFICATION BY
RP   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).
RN   [8]
RP   TISSUE SPECIFICITY.
RX   PubMed=24961373; DOI=10.1073/pnas.1314939111;
RA   Chen L., Shu Y., Liang X., Chen E.C., Yee S.W., Zur A.A., Li S., Xu L.,
RA   Keshari K.R., Lin M.J., Chien H.C., Zhang Y., Morrissey K.M., Liu J.,
RA   Ostrem J., Younger N.S., Kurhanewicz J., Shokat K.M., Ashrafi K.,
RA   Giacomini K.M.;
RT   "OCT1 is a high-capacity thiamine transporter that regulates hepatic
RT   steatosis and is a target of metformin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:9983-9988(2014).
CC   -!- FUNCTION: Multidrug efflux pump that functions as a H(+)/organic cation
CC       antiporter (PubMed:16641166, PubMed:19332510). Plays a physiological
CC       role in the excretion of cationic compounds including endogenous
CC       metabolites, drugs, toxins through the kidney and liver, into urine and
CC       bile respectively (By similarity). Mediates the efflux of endogenous
CC       compounds such as creatinine, vitamin B1/thiamine, agmatine and
CC       estrone-3-sulfate (By similarity). May also contribute to regulate the
CC       transport of cationic compounds in testis across the blood-testis-
CC       barrier (By similarity). {ECO:0000250|UniProtKB:Q96FL8,
CC       ECO:0000269|PubMed:16641166, ECO:0000269|PubMed:19332510}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+)(in) + thiamine(out) = H(+)(out) + thiamine(in);
CC         Xref=Rhea:RHEA:71271, ChEBI:CHEBI:15378, ChEBI:CHEBI:18385;
CC         Evidence={ECO:0000250|UniProtKB:Q96FL8};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=estrone 3-sulfate(in) + H(+)(out) = estrone 3-sulfate(out) +
CC         H(+)(in); Xref=Rhea:RHEA:72139, ChEBI:CHEBI:15378, ChEBI:CHEBI:60050;
CC         Evidence={ECO:0000250|UniProtKB:Q96FL8};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=creatinine(in) + H(+)(out) = creatinine(out) + H(+)(in);
CC         Xref=Rhea:RHEA:72183, ChEBI:CHEBI:15378, ChEBI:CHEBI:16737;
CC         Evidence={ECO:0000250|UniProtKB:Q96FL8};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=agmatine(in) + H(+)(out) = agmatine(out) + H(+)(in);
CC         Xref=Rhea:RHEA:72127, ChEBI:CHEBI:15378, ChEBI:CHEBI:58145;
CC         Evidence={ECO:0000250|UniProtKB:Q96FL8};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72128;
CC         Evidence={ECO:0000250|UniProtKB:Q96FL8};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:72129;
CC         Evidence={ECO:0000250|UniProtKB:Q96FL8};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.41 mM for TEA {ECO:0000269|PubMed:16641166};
CC         Vmax=0.6 nmol/min/mg enzyme toward TEA {ECO:0000269|PubMed:16641166};
CC       pH dependence:
CC         Optimum pH is 8.0-8.5. Active from pH 6 to 8.5.
CC         {ECO:0000269|PubMed:16641166};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16330770};
CC       Multi-pass membrane protein {ECO:0000255}. Apical cell membrane
CC       {ECO:0000269|PubMed:16330770, ECO:0000269|PubMed:16641166}; Multi-pass
CC       membrane protein {ECO:0000255}. Note=Localizes to the plasma membrane;
CC       at the brush border membranes of the proximal tubules (kidney) and at
CC       the bile caniculi (liver). {ECO:0000250|UniProtKB:Q96FL8}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8K0H1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8K0H1-2; Sequence=VSP_029906, VSP_029907;
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in kidney and liver
CC       (PubMed:24961373). Also expressed in various cells, including brain
CC       glia-like cells and capillaries, pancreatic duct cells, urinary bladder
CC       epithelium, adrenal gland cortex, heart, stomach, small intestine,
CC       thyroid gland, testes, alpha cells of the islets of Langerhans, Leydig
CC       cells, and vitamin A-storing Ito cells. Expressed in heart, stomach,
CC       small intestine, bladder, thyroid gland, adrenal gland and testes (at
CC       protein level). {ECO:0000269|PubMed:16330770,
CC       ECO:0000269|PubMed:16641166, ECO:0000269|PubMed:24961373}.
CC   -!- DISRUPTION PHENOTYPE: Deficient mice are viable and fertile without any
CC       overt phenotypical or histological alterations. However, mice exhibit
CC       increased blood urea nitrogen, increased circulating creatinine, and
CC       abnormal metformin pharmacokinetics, including increased plasma and
CC       tissue metformin concentration with decreased kidney and liver
CC       metformin clearance. {ECO:0000269|PubMed:19332510}.
CC   -!- MISCELLANEOUS: Mediates the efflux of cationic compounds such as the
CC       model cations, tetraethylammonium (TEA), the neurotoxin 1-methyl-4-
CC       phenylpyridinium (MPP), the platinum-based drugs cisplatin and
CC       oxaliplatin, the drugs procainamide, acyclovir and topotecan, or weak
CC       bases that are positively charged at physiological pH, such as
CC       cimetidine or the antidiabetic drug metformin.
CC       {ECO:0000250|UniProtKB:Q96FL8}.
CC   -!- SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE)
CC       (TC 2.A.66.1) family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BC031436; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AK004994; BAB23729.1; -; mRNA.
DR   EMBL; AK009038; BAB26040.1; -; mRNA.
DR   EMBL; AL669884; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC031436; -; NOT_ANNOTATED_CDS; mRNA.
DR   CCDS; CCDS24811.2; -. [Q8K0H1-1]
DR   RefSeq; NP_080459.2; NM_026183.5. [Q8K0H1-1]
DR   RefSeq; XP_011247491.1; XM_011249189.2. [Q8K0H1-2]
DR   AlphaFoldDB; Q8K0H1; -.
DR   SMR; Q8K0H1; -.
DR   STRING; 10090.ENSMUSP00000010267; -.
DR   BindingDB; Q8K0H1; -.
DR   ChEMBL; CHEMBL3091264; -.
DR   DrugCentral; Q8K0H1; -.
DR   TCDB; 2.A.66.1.18; the multidrug/oligosaccharidyl-lipid/polysaccharide (mop) flippase superfamily.
DR   iPTMnet; Q8K0H1; -.
DR   PhosphoSitePlus; Q8K0H1; -.
DR   SwissPalm; Q8K0H1; -.
DR   jPOST; Q8K0H1; -.
DR   MaxQB; Q8K0H1; -.
DR   PaxDb; 10090-ENSMUSP00000010267; -.
DR   PeptideAtlas; Q8K0H1; -.
DR   ProteomicsDB; 260794; -. [Q8K0H1-1]
DR   ProteomicsDB; 260795; -. [Q8K0H1-2]
DR   Antibodypedia; 13691; 169 antibodies from 30 providers.
DR   Ensembl; ENSMUST00000010267.10; ENSMUSP00000010267.4; ENSMUSG00000010122.15. [Q8K0H1-1]
DR   GeneID; 67473; -.
DR   KEGG; mmu:67473; -.
DR   UCSC; uc007jhh.2; mouse. [Q8K0H1-2]
DR   UCSC; uc007jhi.2; mouse. [Q8K0H1-1]
DR   AGR; MGI:1914723; -.
DR   CTD; 55244; -.
DR   MGI; MGI:1914723; Slc47a1.
DR   VEuPathDB; HostDB:ENSMUSG00000010122; -.
DR   eggNOG; KOG1347; Eukaryota.
DR   GeneTree; ENSGT00940000161644; -.
DR   HOGENOM; CLU_012893_1_3_1; -.
DR   InParanoid; Q8K0H1; -.
DR   OMA; WFFVWKL; -.
DR   OrthoDB; 10858at2759; -.
DR   PhylomeDB; Q8K0H1; -.
DR   TreeFam; TF324441; -.
DR   Reactome; R-MMU-425366; Transport of bile salts and organic acids, metal ions and amine compounds.
DR   BioGRID-ORCS; 67473; 1 hit in 78 CRISPR screens.
DR   PRO; PR:Q8K0H1; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q8K0H1; Protein.
DR   Bgee; ENSMUSG00000010122; Expressed in renal cortex tubule and 137 other cell types or tissues.
DR   ExpressionAtlas; Q8K0H1; baseline and differential.
DR   GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR   GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0031982; C:vesicle; ISO:MGI.
DR   GO; GO:0042887; F:amide transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0015297; F:antiporter activity; IDA:UniProtKB.
DR   GO; GO:0015179; F:L-amino acid transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0061459; F:L-arginine transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0015101; F:organic cation transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0140968; F:polyspecific organic cation:proton antiporter activity; IDA:UniProtKB.
DR   GO; GO:0015489; F:putrescine transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0015234; F:thiamine transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0042910; F:xenobiotic transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0097638; P:L-arginine import across plasma membrane; IEA:Ensembl.
DR   GO; GO:0098655; P:monoatomic cation transmembrane transport; IDA:UniProtKB.
DR   GO; GO:0006812; P:monoatomic cation transport; ISO:MGI.
DR   GO; GO:0015695; P:organic cation transport; ISO:MGI.
DR   GO; GO:0015847; P:putrescine transport; ISS:UniProtKB.
DR   GO; GO:0055085; P:transmembrane transport; ISO:MGI.
DR   GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; IEA:Ensembl.
DR   GO; GO:0006855; P:xenobiotic transmembrane transport; IDA:UniProtKB.
DR   CDD; cd13132; MATE_eukaryotic; 1.
DR   InterPro; IPR045069; MATE_euk.
DR   InterPro; IPR002528; MATE_fam.
DR   NCBIfam; TIGR00797; matE; 1.
DR   PANTHER; PTHR11206:SF73; MULTIDRUG AND TOXIN EXTRUSION PROTEIN 1; 1.
DR   PANTHER; PTHR11206; MULTIDRUG RESISTANCE PROTEIN; 1.
DR   Pfam; PF01554; MatE; 2.
DR   Genevisible; Q8K0H1; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Antiport; Cell membrane; Membrane;
KW   Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..567
FT                   /note="Multidrug and toxin extrusion protein 1"
FT                   /id="PRO_0000312846"
FT   TOPO_DOM        1..37
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        38..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        59..72
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        73..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        94..120
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        121..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        142..152
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        153..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        174..187
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        188..208
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        209..216
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        217..237
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        238..257
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        258..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        278..295
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        296..316
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        317..336
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        337..357
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        358..370
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        371..391
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        392..408
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        409..429
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        430..437
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        438..458
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        459..543
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        544..564
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        565..567
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96FL8"
FT   MOD_RES         18
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   VAR_SEQ         1..142
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_029906"
FT   VAR_SEQ         143..181
FT                   /note="LFRQDPDVSRLTQTYVMIFIPALPAAFLYTLQVKYLLNQ -> MSDTSPQAG
FT                   VLSRARLLQLRRHSSQRPERSGLAGLLERV (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_029907"
SQ   SEQUENCE   567 AA;  61642 MW;  EDAF1D3DB3BBD8F5 CRC64;
     MERTEESAPG PGGADAASER RGLRCLLLPG FLEELRALLV LAGPAFLAQL MMFLISFISS
     VFCGHLGKLE LDAVTLAIAV INVTGISVGH GLSSACDTLI SQTYGSQNLK HVGVILQRGT
     LILLLCCFPC WALFINTEQI LLLFRQDPDV SRLTQTYVMI FIPALPAAFL YTLQVKYLLN
     QGIVLPQIMT GIAANLVNAL ANYVFLYHLH LGVMGSALAN TISQFALAIF LFLYILWRRL
     HQATWGGWSW ECLQDWASFL RLAIPSMLML CIEWWAYEVG SFLSGILGMV ELGAQSITYE
     LAIIVYMIPS GFSVAANVRV GNALGAGNID QAKKSSAISL IVTELFAVTF CVLLLGCKDL
     VGYIFTTDRD IVALVAQVIP IYAVSHLFEG LACTCGGILR GTGNQKVGAI VNAIGYYVIG
     LPIGIALMFA AKLGVIGLWS GIIICTTCQT TCFLAFIARL NWKRACQQAQ VHANLKVNVA
     LNSAVSHEPA HPVCPESHGE IMMTDLEKKD ETQLDQPMNQ QQALPIRPKD SNKLSGKQLA
     LRRGLLLLGV VLVLVGGILV RVYIRIE
//