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4F2 cell-surface antigen heavy chain (4F2hc) (4F2 heavy chain antigen) (Lymphocyte activation antigen 4F2 large subunit) (Solute carrier family 3 member 2) (CD antigen CD98)

 4F2_HUMAN               Reviewed;         630 AA.
P08195; Q13543;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
01-SEP-2009, sequence version 3.
10-OCT-2018, entry version 212.
RecName: Full=4F2 cell-surface antigen heavy chain;
Short=4F2hc;
AltName: Full=4F2 heavy chain antigen;
AltName: Full=Lymphocyte activation antigen 4F2 large subunit;
AltName: Full=Solute carrier family 3 member 2;
AltName: CD_antigen=CD98;
Name=SLC3A2; Synonyms=MDU1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=3476959; DOI=10.1073/pnas.84.18.6526;
Quackenbush E., Clabby M., Gottesdiener K.M., Barbosa J., Jones N.H.,
Strominger J.L., Speck S., Leiden J.M.;
"Molecular cloning of complementary DNAs encoding the heavy chain of
the human 4F2 cell-surface antigen: a type II membrane glycoprotein
involved in normal and neoplastic cell growth.";
Proc. Natl. Acad. Sci. U.S.A. 84:6526-6530(1987).
[2]
ERRATUM, AND SEQUENCE REVISION.
Quackenbush E., Clabby M., Gottesdiener K.M., Barbosa J., Jones N.H.,
Strominger J.L., Speck S., Leiden J.M.;
Proc. Natl. Acad. Sci. U.S.A. 84:8618-8618(1987).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=3036867;
Teixeira S., di Grandi S., Kuehn L.C.;
"Primary structure of the human 4F2 antigen heavy chain predicts a
transmembrane protein with a cytoplasmic NH2 terminus.";
J. Biol. Chem. 262:9574-9580(1987).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND
INDUCTION.
TISSUE=Fibroblast;
PubMed=3480538; DOI=10.1073/pnas.84.24.9204;
Lumadue J.A., Glick A.B., Ruddle F.H.;
"Cloning, sequence analysis, and expression of the large subunit of
the human lymphocyte activation antigen 4F2.";
Proc. Natl. Acad. Sci. U.S.A. 84:9204-9208(1987).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 2),
TISSUE SPECIFICITY, AND INDUCTION.
PubMed=3265470; DOI=10.1128/MCB.8.9.3809;
Gottesdiener K.M., Karpinski B.A., Lindsten T., Strominger J.L.,
Jones N.H., Thompson C.B., Leiden J.M.;
"Isolation and structural characterization of the human 4F2 heavy-
chain gene, an inducible gene involved in T-lymphocyte activation.";
Mol. Cell. Biol. 8:3809-3819(1988).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBUNIT, AND TISSUE
SPECIFICITY.
TISSUE=Placenta;
PubMed=11557028; DOI=10.1016/S0005-2736(01)00384-4;
Yanagida O., Kanai Y., Chairoungdua A., Kim D.K., Segawa H., Nii T.,
Cha S.H., Matsuo H., Fukushima J., Fukasawa Y., Tani Y., Taketani Y.,
Uchino H., Kim J.Y., Inatomi J., Okayasu I., Miyamoto K., Takeda E.,
Goya T., Endou H.;
"Human L-type amino acid transporter 1 (LAT1): characterization of
function and expression in tumor cell lines.";
Biochim. Biophys. Acta 1514:291-302(2001).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE
SPLICING (ISOFORM 4).
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=Lung, and Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
PROTEIN SEQUENCE OF 1-17; 146-171; 227-245; 304-313; 440-451; 511-525
AND 593-630, ACETYLATION AT MET-1, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Cervix carcinoma;
Bienvenut W.V., Lao L., Ryan K.L.;
Submitted (OCT-2009) to UniProtKB.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 83-209 (ISOFORM 4).
TISSUE=Lung carcinoma;
Strausberg R.L.;
Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
[11]
PROTEIN SEQUENCE OF 112-122; 148-160; 227-245; 248-255; 288-298;
304-313; 440-451; 511-524 AND 593-625, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=B-cell lymphoma;
Bienvenut W.V.;
Submitted (MAR-2005) to UniProtKB.
[12]
FUNCTION, SUBUNIT, INHIBITION, AND MUTAGENESIS OF CYS-210 AND CYS-431.
PubMed=9829974; DOI=10.1074/jbc.273.49.32437;
Torrents D., Estevez R., Pineda M., Fernandez E., Lloberas J.,
Shi Y.-B., Zorzano A., Palacin M.;
"Identification and characterization of a membrane protein (y+L amino
acid transporter-1) that associates with 4F2hc to encode the amino
acid transport activity y+L. A candidate gene for lysinuric protein
intolerance.";
J. Biol. Chem. 273:32437-32445(1998).
[13]
FUNCTION, AND SUBUNIT.
PubMed=9751058; DOI=10.1038/26246;
Mastroberardino L., Spindler B., Pfeiffer R., Skelly P.J., Loffing J.,
Shoemaker C.B., Verrey F.;
"Amino-acid transport by heterodimers of 4F2hc/CD98 and members of a
permease family.";
Nature 395:288-291(1998).
[14]
FUNCTION, AND SUBUNIT.
PubMed=9878049; DOI=10.1093/emboj/18.1.49;
Pfeiffer R., Rossier G., Spindler B., Meier C., Kuehn L.C., Verrey F.;
"Amino acid transport of y+L-type by heterodimers of 4F2hc/CD98 and
members of the glycoprotein-associated amino acid transporter
family.";
EMBO J. 18:49-57(1999).
[15]
FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=10903140; DOI=10.1042/bj3490787;
Broeer A., Wagner C.A., Lang F., Broeer S.;
"The heterodimeric amino acid transporter 4F2hc/y+LAT2 mediates
arginine efflux in exchange with glutamine.";
Biochem. J. 349:787-795(2000).
[16]
FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=11311135;
Broeer A., Friedrich B., Wagner C.A., Fillon S., Ganapathy V.,
Lang F., Broeer S.;
"Association of 4F2hc with light chains LAT1, LAT2 or y+LAT2 requires
different domains.";
Biochem. J. 355:725-731(2001).
[17]
FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=11389679; DOI=10.1042/0264-6021:3560719;
Ritchie J.W.A., Taylor P.M.;
"Role of the System L permease LAT1 in amino acid and iodothyronine
transport in placenta.";
Biochem. J. 356:719-725(2001).
[18]
SUBUNIT, INTERACTION WITH BETA-1 INTEGRINS, AND MUTAGENESIS OF CYS-210
AND CYS-431.
PubMed=11696247; DOI=10.1186/1472-2091-2-10;
Kolesnikova T.V., Mannion B.A., Berditchevski F., Hemler M.E.;
"Beta1 integrins show specific association with CD98 protein in low
density membranes.";
BMC Biochem. 2:10-10(2001).
[19]
FUNCTION, AND SUBUNIT.
PubMed=11564694; DOI=10.1210/endo.142.10.8418;
Friesema E.C.H., Docter R., Moerings E.P.C.M., Verrey F.,
Krenning E.P., Hennemann G., Visser T.J.;
"Thyroid hormone transport by the heterodimeric human system L amino
acid transporter.";
Endocrinology 142:4339-4348(2001).
[20]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
PubMed=11742812;
Okamoto Y., Sakata M., Ogura K., Yamamoto T., Yamaguchi M., Tasaka K.,
Kurachi H., Tsurudome M., Murata Y.;
"Expression and regulation of 4F2hc and hLAT1 in human trophoblasts.";
Am. J. Physiol. 282:C196-C204(2002).
[21]
INTERACTION WITH FAM57A/CT120.
PubMed=12270127; DOI=10.1016/S0006-291X(02)02227-1;
He X.H., Di Y., Li J., Xie Y., Tang Y., Zhang F., Wei L., Zhang Y.,
Qin W.X., Huo K., Li Y., Wan D.F., Gu J.R.;
"Molecular cloning and characterization of CT120, a novel membrane-
associated gene involved in amino acid transport and glutathione
metabolism.";
Biochem. Biophys. Res. Commun. 297:528-536(2002).
[22]
FUNCTION.
PubMed=12117417; DOI=10.1042/BJ20020841;
Simmons-Willis T.A., Koh A.S., Clarkson T.W., Ballatori N.;
"Transport of a neurotoxicant by molecular mimicry: the methylmercury-
L-cysteine complex is a substrate for human L-type large neutral amino
acid transporter (LAT) 1 and LAT2.";
Biochem. J. 367:239-246(2002).
[23]
FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=12225859; DOI=10.1016/S0005-2736(02)00516-3;
Kim D.K., Kanai Y., Choi H.W., Tangtrongsup S., Chairoungdua A.,
Babu E., Tachampa K., Anzai N., Iribe Y., Endou H.;
"Characterization of the system L amino acid transporter in T24 human
bladder carcinoma cells.";
Biochim. Biophys. Acta 1565:112-121(2002).
[24]
MASS SPECTROMETRY.
TISSUE=Mammary cancer;
PubMed=11840567;
DOI=10.1002/1615-9861(200202)2:2<212::AID-PROT212>3.0.CO;2-H;
Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A.,
Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J.,
Zvelebil M.J.;
"Cluster analysis of an extensive human breast cancer cell line
protein expression map database.";
Proteomics 2:212-223(2002).
[25]
FUNCTION, SUBUNIT, AND TISSUE SPECIFICITY.
PubMed=14603368; DOI=10.1113/eph8802647;
Arancibia-Garavilla Y., Toledo F., Casanello P., Sobrevia L.;
"Nitric oxide synthesis requires activity of the cationic and neutral
amino acid transport system y+L in human umbilical vein endothelium.";
Exp. Physiol. 88:699-710(2003).
[26]
FUNCTION, SUBUNIT, INTERACTION WITH ICAM1, SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
PubMed=12716892; DOI=10.1074/jbc.M302777200;
Liu X., Charrier L., Gewirtz A., Sitaraman S., Merlin D.;
"CD98 and intracellular adhesion molecule I regulate the activity of
amino acid transporter LAT-2 in polarized intestinal epithelia.";
J. Biol. Chem. 278:23672-23677(2003).
[27]
GLYCOSYLATION AT ASN-365; ASN-381 AND ASN-424.
PubMed=12754519; DOI=10.1038/nbt827;
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
"Identification and quantification of N-linked glycoproteins using
hydrazide chemistry, stable isotope labeling and mass spectrometry.";
Nat. Biotechnol. 21:660-666(2003).
[28]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=15980244; DOI=10.1167/iovs.04-1175;
Tomi M., Mori M., Tachikawa M., Katayama K., Terasaki T., Hosoya K.;
"L-type amino acid transporter 1-mediated L-leucine transport at the
inner blood-retinal barrier.";
Invest. Ophthalmol. Vis. Sci. 46:2522-2530(2005).
[29]
FUNCTION, AND SUBUNIT.
PubMed=15769744; DOI=10.1074/jbc.M413164200;
Li S., Whorton A.R.;
"Identification of stereoselective transporters for S-nitroso-L-
cysteine: role of LAT1 and LAT2 in biological activity of S-
nitrosothiols.";
J. Biol. Chem. 280:20102-20110(2005).
[30]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-381 AND ASN-424.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[31]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[32]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=16496379; DOI=10.1002/ijc.21866;
Nawashiro H., Otani N., Shinomiya N., Fukui S., Ooigawa H., Shima K.,
Matsuo H., Kanai Y., Endou H.;
"L-type amino acid transporter 1 as a potential molecular target in
human astrocytic tumors.";
Int. J. Cancer 119:484-492(2006).
[33]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Melanoma;
PubMed=17081065; DOI=10.1021/pr060363j;
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
Hunt D.F.;
"Proteomic and bioinformatic characterization of the biogenesis and
function of melanosomes.";
J. Proteome Res. 5:3135-3144(2006).
[34]
PHOSPHORYLATION AT SER-406; SER-408; SER-410; SER-527 AND SER-531.
PubMed=19065266; DOI=10.1371/journal.pone.0003895;
Nguyen H.T.T., Dalmasso G., Yan Y., Obertone T.S., Sitaraman S.V.,
Merlin D.;
"Ecto-phosphorylation of CD98 regulates cell-cell interactions.";
PLoS ONE 3:E3895-E3895(2008).
[35]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 (ISOFORM 2), CLEAVAGE OF
INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 2), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[36]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-365; ASN-381 AND ASN-506.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[37]
GLYCOSYLATION AT ASN-424.
PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200;
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F.,
Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
"A strategy for precise and large scale identification of core
fucosylated glycoproteins.";
Mol. Cell. Proteomics 8:913-923(2009).
[38]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-365; ASN-381; ASN-424 AND
ASN-506.
TISSUE=Leukemic T-cell;
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[39]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[40]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[41]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 (ISOFORM 2),
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 (ISOFORM 2), CLEAVAGE
OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 2), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[42]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 (ISOFORM 2), CLEAVAGE OF
INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 2), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[43]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[44]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103; SER-134 AND
SER-165, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[45]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[46]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-166, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[47]
INTERACTION WITH LAPTM4B, AND FUNCTION.
PubMed=25998567; DOI=10.1038/ncomms8250;
Milkereit R., Persaud A., Vanoaica L., Guetg A., Verrey F., Rotin D.;
"LAPTM4b recruits the LAT1-4F2hc Leu transporter to lysosomes and
promotes mTORC1 activation.";
Nat. Commun. 6:7250-7250(2015).
[48]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[49]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 212-630, SUBUNIT, MUTAGENESIS
OF CYS-210, SUBCELLULAR LOCATION, AND DISULFIDE BOND.
PubMed=17724034; DOI=10.1074/jbc.M704524200;
Fort J., de la Ballina L.R., Burghardt H.E., Ferrer-Costa C.,
Turnay J., Ferrer-Orta C., Uson I., Zorzano A., Fernandez-Recio J.,
Orozco M., Lizarbe M.A., Fita I., Palacin M.;
"The structure of human 4F2hc ectodomain provides a model for
homodimerization and electrostatic interaction with plasma membrane.";
J. Biol. Chem. 282:31444-31452(2007).
-!- FUNCTION: Required for the function of light chain amino-acid
transporters. Involved in sodium-independent, high-affinity
transport of large neutral amino acids such as phenylalanine,
tyrosine, leucine, arginine and tryptophan. Involved in guiding
and targeting of LAT1 and LAT2 to the plasma membrane. When
associated with SLC7A6 or SLC7A7 acts as an arginine/glutamine
exchanger, following an antiport mechanism for amino acid
transport, influencing arginine release in exchange for
extracellular amino acids. Plays a role in nitric oxide synthesis
in human umbilical vein endothelial cells (HUVECs) via transport
of L-arginine. Required for normal and neoplastic cell growth.
When associated with SLC7A5/LAT1, is also involved in the
transport of L-DOPA across the blood-brain barrier, and that of
thyroid hormones triiodothyronine (T3) and thyroxine (T4) across
the cell membrane in tissues such as placenta. Involved in the
uptake of methylmercury (MeHg) when administered as the L-cysteine
or D,L-homocysteine complexes, and hence plays a role in metal ion
homeostasis and toxicity. When associated with SLC7A5 or SLC7A8,
involved in the cellular activity of small molecular weight
nitrosothiols, via the stereoselective transport of L-
nitrosocysteine (L-CNSO) across the transmembrane. Together with
ICAM1, regulates the transport activity LAT2 in polarized
intestinal cells, by generating and delivering intracellular
signals. When associated with SLC7A5, plays an important role in
transporting L-leucine from the circulating blood to the retina
across the inner blood-retinal barrier. When associated with
LAPTM4B, recruits SLC3A2 and SLC7A5 to lysosomes to promote
leucine uptake into these organelles and is required for mTORC1
activation (PubMed:25998567). {ECO:0000269|PubMed:10903140,
ECO:0000269|PubMed:11311135, ECO:0000269|PubMed:11389679,
ECO:0000269|PubMed:11557028, ECO:0000269|PubMed:11564694,
ECO:0000269|PubMed:11742812, ECO:0000269|PubMed:12117417,
ECO:0000269|PubMed:12225859, ECO:0000269|PubMed:12716892,
ECO:0000269|PubMed:14603368, ECO:0000269|PubMed:15769744,
ECO:0000269|PubMed:15980244, ECO:0000269|PubMed:25998567,
ECO:0000269|PubMed:9751058, ECO:0000269|PubMed:9829974,
ECO:0000269|PubMed:9878049}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=295 uM for glutamine (in the presence of NaCl)
{ECO:0000269|PubMed:10903140};
KM=236 uM for leucine (in the presence of NaCl)
{ECO:0000269|PubMed:10903140};
KM=120 uM for arginine (in the presence of NaCl)
{ECO:0000269|PubMed:10903140};
KM=138 uM for arginine (in the absence of NaCl)
{ECO:0000269|PubMed:10903140};
-!- SUBUNIT: Disulfide-linked heterodimer of a glycosylated heavy
chain and a non-glycosylated light chain (SLC7A5, SLC7A6, SLCA7A7,
SLC7A8, SLC7A10 or SLCA7A11). Colocalizes with cadherins (By
similarity). Interacts with FAM57A/CT120 and ICAM1. Constitutively
and specifically associates with beta-1 integrins (alpha-2/beta-1,
alpha-3/beta-1, alpha-5/beta-1 and alpha-6/beta-1), but minimally
with alpha-4/beta-1. Interacts with LAPTM4B; recruits SLC3A2 and
SLC7A5 to lysosomes to promote leucine uptake into these
organelles and is required for mTORC1 activation
(PubMed:25998567). {ECO:0000250, ECO:0000269|PubMed:11311135,
ECO:0000269|PubMed:11389679, ECO:0000269|PubMed:11557028,
ECO:0000269|PubMed:11564694, ECO:0000269|PubMed:11696247,
ECO:0000269|PubMed:12225859, ECO:0000269|PubMed:12270127,
ECO:0000269|PubMed:12716892, ECO:0000269|PubMed:14603368,
ECO:0000269|PubMed:15769744, ECO:0000269|PubMed:17724034,
ECO:0000269|PubMed:25998567, ECO:0000269|PubMed:9751058,
ECO:0000269|PubMed:9829974, ECO:0000269|PubMed:9878049}.
-!- INTERACTION:
O52302:sepZ (xeno); NbExp=5; IntAct=EBI-702356, EBI-14022357;
-!- SUBCELLULAR LOCATION: Apical cell membrane; Single-pass type II
membrane protein. Melanosome. Note=Identified by mass spectrometry
in melanosome fractions from stage I to stage IV. Localized to the
plasma membrane when associated with SLC7A5 or SLC7A8. Localized
to the placental apical membrane. Located selectively at cell-cell
adhesion sites (By similarity). Colocalized with SLC7A8/LAT2 at
the basolateral membrane of kidney proximal tubules and small
intestine epithelia. Expressed in both luminal and abluminal
membranes of brain capillary endothelial cells (By similarity).
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=P08195-1; Sequence=Displayed;
Name=2;
IsoId=P08195-2; Sequence=VSP_037907;
Note=Initiator Met-1 is removed. Contains a N-acetylserine at
position 2. Contains a phosphoserine at position 2.
{ECO:0000244|PubMed:19413330, ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:22223895};
Name=3;
IsoId=P08195-3; Sequence=VSP_037908;
Name=4;
IsoId=P08195-4; Sequence=VSP_037909;
-!- TISSUE SPECIFICITY: Expressed ubiquitously in all tissues tested
with highest levels detected in kidney, placenta and testis and
weakest level in thymus. During gestation, expression in the
placenta was significantly stronger at full-term than at the mid-
trimester stage. Expressed in HUVECS and at low levels in resting
peripheral blood T-lymphocytes and quiescent fibroblasts. Also
expressed in fetal liver and in the astrocytic process of primary
astrocytic gliomas. Expressed in retinal endothelial cells and in
the intestinal epithelial cell line C2BBe1.
{ECO:0000269|PubMed:11389679, ECO:0000269|PubMed:11557028,
ECO:0000269|PubMed:11742812, ECO:0000269|PubMed:12716892,
ECO:0000269|PubMed:14603368, ECO:0000269|PubMed:15980244,
ECO:0000269|PubMed:16496379, ECO:0000269|PubMed:3265470,
ECO:0000269|PubMed:3480538}.
-!- INDUCTION: Expression is induced in resting peripheral blood T-
lymphocytes following PHA stimulation. Expression increases at the
time of maximal DNA synthesis, in fibroblasts stimulated to
divide. Expression and the uptake of leucine is stimulated in
mononuclear, cytotrophoblast-like choriocarcinoma cells by
combined treatment with PMA and calcium ionophore.
{ECO:0000269|PubMed:11742812, ECO:0000269|PubMed:3265470,
ECO:0000269|PubMed:3480538}.
-!- PTM: Phosphorylation on Ser-406; Ser-408 or Ser-410 and on Ser-527
or Ser-531 by ecto-protein kinases favors heterotypic cell-cell
interactions. {ECO:0000269|PubMed:19065266}.
-!- MASS SPECTROMETRY: Mass=57944.93; Method=MALDI; Range=1-529;
Evidence={ECO:0000269|PubMed:11840567};
-!- MISCELLANEOUS: Arginine uptake is inhibited by increasing
concentrations of leucine in the presence of Na(+).
-!- SIMILARITY: Belongs to the SLC3A transporter family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; J02939; AAA52497.1; -; mRNA.
EMBL; J02769; AAA51540.1; -; mRNA.
EMBL; J03569; AAA35536.1; -; mRNA.
EMBL; M21904; AAA35489.1; -; Genomic_DNA.
EMBL; M21898; AAA35489.1; JOINED; Genomic_DNA.
EMBL; M21899; AAA35489.1; JOINED; Genomic_DNA.
EMBL; M21900; AAA35489.1; JOINED; Genomic_DNA.
EMBL; M21901; AAA35489.1; JOINED; Genomic_DNA.
EMBL; M21902; AAA35489.1; JOINED; Genomic_DNA.
EMBL; M21903; AAA35489.1; JOINED; Genomic_DNA.
EMBL; AB018010; BAA84649.1; -; mRNA.
EMBL; AP001160; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC001061; AAH01061.2; -; mRNA.
EMBL; BC003000; AAH03000.2; -; mRNA.
EMBL; BE794697; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS31589.1; -. [P08195-3]
CCDS; CCDS31590.1; -. [P08195-2]
CCDS; CCDS8039.2; -. [P08195-1]
PIR; A28455; SAHU4F.
RefSeq; NP_001012680.1; NM_001012662.2.
RefSeq; NP_001012682.1; NM_001012664.2. [P08195-3]
RefSeq; NP_001013269.1; NM_001013251.2. [P08195-2]
RefSeq; NP_002385.3; NM_002394.5. [P08195-1]
UniGene; Hs.502769; -.
PDB; 2DH2; X-ray; 2.10 A; A=212-630.
PDB; 2DH3; X-ray; 2.80 A; A/B=212-630.
PDBsum; 2DH2; -.
PDBsum; 2DH3; -.
ProteinModelPortal; P08195; -.
SMR; P08195; -.
BioGrid; 112411; 87.
CORUM; P08195; -.
IntAct; P08195; 53.
MINT; P08195; -.
STRING; 9606.ENSP00000367123; -.
GuidetoPHARMACOLOGY; 890; -.
CAZy; GH13; Glycoside Hydrolase Family 13.
TCDB; 8.A.9.2.2; the rbat transport accessory protein (rbat) family.
GlyConnect; 984; -.
iPTMnet; P08195; -.
PhosphoSitePlus; P08195; -.
SwissPalm; P08195; -.
BioMuta; SLC3A2; -.
DMDM; 257051063; -.
EPD; P08195; -.
MaxQB; P08195; -.
PaxDb; P08195; -.
PeptideAtlas; P08195; -.
PRIDE; P08195; -.
ProteomicsDB; 52082; -.
ProteomicsDB; 52083; -. [P08195-2]
ProteomicsDB; 52084; -. [P08195-3]
ProteomicsDB; 52085; -. [P08195-4]
DNASU; 6520; -.
Ensembl; ENST00000338663; ENSP00000340815; ENSG00000168003. [P08195-2]
Ensembl; ENST00000377889; ENSP00000367121; ENSG00000168003. [P08195-3]
Ensembl; ENST00000377890; ENSP00000367122; ENSG00000168003. [P08195-1]
GeneID; 6520; -.
KEGG; hsa:6520; -.
UCSC; uc001nwd.4; human. [P08195-1]
CTD; 6520; -.
DisGeNET; 6520; -.
EuPathDB; HostDB:ENSG00000168003.16; -.
GeneCards; SLC3A2; -.
HGNC; HGNC:11026; SLC3A2.
HPA; CAB010455; -.
HPA; HPA017980; -.
MIM; 158070; gene.
neXtProt; NX_P08195; -.
OpenTargets; ENSG00000168003; -.
PharmGKB; PA35894; -.
eggNOG; KOG0471; Eukaryota.
eggNOG; COG0366; LUCA.
GeneTree; ENSGT00900000140965; -.
HOGENOM; HOG000233529; -.
HOVERGEN; HBG000023; -.
InParanoid; P08195; -.
KO; K06519; -.
PhylomeDB; P08195; -.
BioCyc; MetaCyc:ENSG00000168003-MONOMER; -.
Reactome; R-HSA-210991; Basigin interactions.
Reactome; R-HSA-352230; Amino acid transport across the plasma membrane.
Reactome; R-HSA-71240; Tryptophan catabolism.
SABIO-RK; P08195; -.
ChiTaRS; SLC3A2; human.
EvolutionaryTrace; P08195; -.
GeneWiki; SLC3A2; -.
GenomeRNAi; 6520; -.
PRO; PR:P08195; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000168003; Expressed in 227 organ(s), highest expression level in right ovary.
CleanEx; HS_SLC3A2; -.
ExpressionAtlas; P08195; baseline and differential.
Genevisible; P08195; HS.
GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
GO; GO:0005432; F:calcium:sodium antiporter activity; TAS:UniProtKB.
GO; GO:0003824; F:catalytic activity; IEA:InterPro.
GO; GO:0003725; F:double-stranded RNA binding; IDA:MGI.
GO; GO:0015175; F:neutral amino acid transmembrane transporter activity; ISS:UniProtKB.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0006865; P:amino acid transport; TAS:UniProtKB.
GO; GO:0006816; P:calcium ion transport; NAS:UniProtKB.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
GO; GO:1903801; P:L-leucine import across plasma membrane; ISS:UniProtKB.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0043330; P:response to exogenous dsRNA; IMP:MGI.
GO; GO:0015827; P:tryptophan transport; ISS:UniProtKB.
Gene3D; 2.60.40.1180; -; 1.
InterPro; IPR006047; Glyco_hydro_13_cat_dom.
InterPro; IPR013780; Glyco_hydro_b.
InterPro; IPR017853; Glycoside_hydrolase_SF.
InterPro; IPR031984; SLC3A2_N.
Pfam; PF00128; Alpha-amylase; 1.
Pfam; PF16028; SLC3A2_N; 1.
SMART; SM00642; Aamy; 1.
SUPFAM; SSF51445; SSF51445; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Amino-acid transport;
Cell membrane; Complete proteome; Direct protein sequencing;
Disulfide bond; Glycoprotein; Isopeptide bond; Membrane;
Phosphoprotein; Reference proteome; Signal-anchor; Transmembrane;
Transmembrane helix; Transport; Ubl conjugation.
CHAIN 1 630 4F2 cell-surface antigen heavy chain.
/FTId=PRO_0000064383.
TOPO_DOM 102 184 Cytoplasmic. {ECO:0000255}.
TRANSMEM 185 205 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 206 630 Extracellular. {ECO:0000255}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.9}.
MOD_RES 103 103 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 106 106 Phosphothreonine.
{ECO:0000250|UniProtKB:Q794F9}.
MOD_RES 134 134 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 165 165 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 406 406 Phosphoserine.
{ECO:0000305|PubMed:19065266}.
MOD_RES 408 408 Phosphoserine.
{ECO:0000305|PubMed:19065266}.
MOD_RES 410 410 Phosphoserine.
{ECO:0000305|PubMed:19065266}.
MOD_RES 527 527 Phosphoserine.
{ECO:0000305|PubMed:19065266}.
MOD_RES 531 531 Phosphoserine.
{ECO:0000305|PubMed:19065266}.
CARBOHYD 365 365 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19349973}.
CARBOHYD 381 381 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19349973}.
CARBOHYD 424 424 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19139490,
ECO:0000269|PubMed:19349973}.
CARBOHYD 506 506 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19349973}.
DISULFID 210 210 Interchain (with light chain).
{ECO:0000269|PubMed:17724034}.
CROSSLNK 147 147 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
CROSSLNK 166 166 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25114211}.
VAR_SEQ 1 101 Missing (in isoform 2).
{ECO:0000303|PubMed:11557028,
ECO:0000303|PubMed:3036867,
ECO:0000303|PubMed:3476959,
ECO:0000303|PubMed:3480538}.
/FTId=VSP_037907.
VAR_SEQ 38 99 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_037908.
VAR_SEQ 98 98 V -> VTETGFHHVSQADIEFLTSIDPTASASGSAGI (in
isoform 4). {ECO:0000303|Ref.10}.
/FTId=VSP_037909.
MUTAGEN 210 210 C->S: Abolishes dimerization, leucine
uptake and interaction with beta-1
integrins. {ECO:0000269|PubMed:11696247,
ECO:0000269|PubMed:17724034,
ECO:0000269|PubMed:9829974}.
MUTAGEN 431 431 C->S: No effect on dimerization, leucine
uptake or interaction with beta-1
integrins. {ECO:0000269|PubMed:11696247,
ECO:0000269|PubMed:9829974}.
CONFLICT 137 137 G -> E (in Ref. 4; AAA35536).
{ECO:0000305}.
CONFLICT 158 158 A -> P (in Ref. 3; AAA51540).
{ECO:0000305}.
CONFLICT 223 223 A -> P (in Ref. 4; AAA35536).
{ECO:0000305}.
CONFLICT 315 315 E -> D (in Ref. 4; AAA35536).
{ECO:0000305}.
CONFLICT 320 320 S -> F (in Ref. 5; AAA35489).
{ECO:0000305}.
CONFLICT 372 372 E -> G (in Ref. 4; AAA35536).
{ECO:0000305}.
CONFLICT 412 413 GE -> PQ (in Ref. 4; AAA35536).
{ECO:0000305}.
CONFLICT 465 465 V -> L (in Ref. 4; AAA35536).
{ECO:0000305}.
CONFLICT 481 481 G -> P (in Ref. 4; AAA35536).
{ECO:0000305}.
CONFLICT 549 549 G -> E (in Ref. 5; AAA35489).
{ECO:0000305}.
CONFLICT 609 609 L -> P (in Ref. 4; AAA35536).
{ECO:0000305}.
CONFLICT 612 612 E -> G (in Ref. 4; AAA35536).
{ECO:0000305}.
HELIX 218 220 {ECO:0000244|PDB:2DH2}.
STRAND 224 227 {ECO:0000244|PDB:2DH2}.
HELIX 230 234 {ECO:0000244|PDB:2DH2}.
HELIX 241 245 {ECO:0000244|PDB:2DH2}.
HELIX 248 253 {ECO:0000244|PDB:2DH2}.
STRAND 257 261 {ECO:0000244|PDB:2DH2}.
STRAND 265 267 {ECO:0000244|PDB:2DH2}.
STRAND 275 280 {ECO:0000244|PDB:2DH2}.
HELIX 282 284 {ECO:0000244|PDB:2DH2}.
HELIX 287 299 {ECO:0000244|PDB:2DH2}.
STRAND 303 307 {ECO:0000244|PDB:2DH2}.
TURN 310 313 {ECO:0000244|PDB:2DH2}.
STRAND 314 316 {ECO:0000244|PDB:2DH2}.
STRAND 319 321 {ECO:0000244|PDB:2DH3}.
HELIX 323 340 {ECO:0000244|PDB:2DH2}.
STRAND 344 347 {ECO:0000244|PDB:2DH2}.
HELIX 350 352 {ECO:0000244|PDB:2DH2}.
HELIX 356 370 {ECO:0000244|PDB:2DH2}.
STRAND 375 379 {ECO:0000244|PDB:2DH2}.
HELIX 385 391 {ECO:0000244|PDB:2DH2}.
TURN 392 394 {ECO:0000244|PDB:2DH2}.
STRAND 399 401 {ECO:0000244|PDB:2DH2}.
TURN 404 407 {ECO:0000244|PDB:2DH2}.
HELIX 412 426 {ECO:0000244|PDB:2DH2}.
STRAND 437 439 {ECO:0000244|PDB:2DH3}.
HELIX 441 443 {ECO:0000244|PDB:2DH2}.
HELIX 447 449 {ECO:0000244|PDB:2DH2}.
HELIX 450 457 {ECO:0000244|PDB:2DH2}.
STRAND 460 467 {ECO:0000244|PDB:2DH2}.
HELIX 470 472 {ECO:0000244|PDB:2DH2}.
HELIX 476 478 {ECO:0000244|PDB:2DH2}.
STRAND 479 481 {ECO:0000244|PDB:2DH2}.
STRAND 484 486 {ECO:0000244|PDB:2DH2}.
HELIX 493 495 {ECO:0000244|PDB:2DH3}.
HELIX 500 502 {ECO:0000244|PDB:2DH3}.
HELIX 505 507 {ECO:0000244|PDB:2DH2}.
HELIX 509 513 {ECO:0000244|PDB:2DH2}.
HELIX 519 532 {ECO:0000244|PDB:2DH2}.
HELIX 534 538 {ECO:0000244|PDB:2DH2}.
STRAND 540 545 {ECO:0000244|PDB:2DH2}.
STRAND 550 556 {ECO:0000244|PDB:2DH2}.
STRAND 562 568 {ECO:0000244|PDB:2DH2}.
STRAND 570 572 {ECO:0000244|PDB:2DH2}.
STRAND 581 583 {ECO:0000244|PDB:2DH2}.
HELIX 585 587 {ECO:0000244|PDB:2DH2}.
STRAND 591 603 {ECO:0000244|PDB:2DH2}.
STRAND 607 610 {ECO:0000244|PDB:2DH2}.
HELIX 611 613 {ECO:0000244|PDB:2DH2}.
STRAND 621 626 {ECO:0000244|PDB:2DH2}.
SEQUENCE 630 AA; 67994 MW; AE427F8204CC10B0 CRC64;
MELQPPEASI AVVSIPRQLP GSHSEAGVQG LSAGDDSELG SHCVAQTGLE LLASGDPLPS
ASQNAEMIET GSDCVTQAGL QLLASSDPPA LASKNAEVTG TMSQDTEVDM KEVELNELEP
EKQPMNAASG AAMSLAGAEK NGLVKIKVAE DEAEAAAAAK FTGLSKEELL KVAGSPGWVR
TRWALLLLFW LGWLGMLAGA VVIIVRAPRC RELPAQKWWH TGALYRIGDL QAFQGHGAGN
LAGLKGRLDY LSSLKVKGLV LGPIHKNQKD DVAQTDLLQI DPNFGSKEDF DSLLQSAKKK
SIRVILDLTP NYRGENSWFS TQVDTVATKV KDALEFWLQA GVDGFQVRDI ENLKDASSFL
AEWQNITKGF SEDRLLIAGT NSSDLQQILS LLESNKDLLL TSSYLSDSGS TGEHTKSLVT
QYLNATGNRW CSWSLSQARL LTSFLPAQLL RLYQLMLFTL PGTPVFSYGD EIGLDAAALP
GQPMEAPVML WDESSFPDIP GAVSANMTVK GQSEDPGSLL SLFRRLSDQR SKERSLLHGD
FHAFSAGPGL FSYIRHWDQN ERFLVVLNFG DVGLSAGLQA SDLPASASLP AKADLLLSTQ
PGREEGSPLE LERLKLEPHE GLLLRFPYAA


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Genprice Inc, Invoices and accounting
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