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

 4F2_MOUSE               Reviewed;         526 AA.
P10852; G3UWA6; Q54AH5;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 1.
07-APR-2021, entry version 189.
RecName: Full=4F2 cell-surface antigen heavy chain {ECO:0000303|PubMed:2928113};
Short=4F2hc;
AltName: Full=Solute carrier family 3 member 2;
AltName: CD_antigen=CD98;
Name=Slc3a2; Synonyms=Mdu1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND INDUCTION.
STRAIN=C57BL/6 X DBA/2, and ICR; TISSUE=Macrophage, and Pre-B cell;
PubMed=2928113; DOI=10.1093/nar/17.5.1915;
Parmacek M.S., Karpinski B.A., Gottsdiener K.M., Thompson C.B.,
Leiden J.M.;
"Structure, expression and regulation of the murine 4F2 heavy chain.";
Nucleic Acids Res. 17:1915-1931(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=ICR; TISSUE=Brain;
Kanai Y., Watanabe M., Endou H.;
"Localization of expression of system L neutral amino acid transporter LAT1
in brain.";
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J; TISSUE=Kidney, and Testis;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of the
mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Brain;
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).
[7]
PROTEIN SEQUENCE OF 43-53; 163-171; 456-463 AND 488-496, AND IDENTIFICATION
BY MASS SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[8]
FUNCTION, SUBUNIT, INTERACTION WITH SLC7A5, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION, AND MUTAGENESIS OF CYS-103.
STRAIN=BALB/cJ;
PubMed=9915839; DOI=10.1074/jbc.274.5.3009;
Nakamura E., Sato M., Yang H., Miyagawa F., Harasaki M., Tomita K.,
Matsuoka S., Noma A., Iwai K., Minato N.;
"4F2 (CD98) heavy chain is associated covalently with an amino acid
transporter and controls intracellular trafficking and membrane topology of
4F2 heterodimer.";
J. Biol. Chem. 274:3009-3016(1999).
[9]
SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=10574970; DOI=10.1074/jbc.274.49.34948;
Rossier G., Meier C., Bauch C., Summa V., Sordat B., Verrey F., Kuehn L.C.;
"LAT2, a new basolateral 4F2hc/CD98-associated amino acid transporter of
kidney and intestine.";
J. Biol. Chem. 274:34948-34954(1999).
[10]
FUNCTION, AND SUBUNIT.
PubMed=11011012; DOI=10.1016/s0006-8993(00)02758-x;
Kageyama T., Nakamura M., Matsuo A., Yamasaki Y., Takakura Y., Hashida M.,
Kanai Y., Naito M., Tsuruo T., Minato N., Shimohama S.;
"The 4F2hc/LAT1 complex transports L-DOPA across the blood-brain barrier.";
Brain Res. 879:115-121(2000).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[12]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-166; ASN-259; ASN-385 AND
ASN-399.
TISSUE=Myoblast;
PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.;
"The mouse C2C12 myoblast cell surface N-linked glycoproteome:
identification, glycosite occupancy, and membrane orientation.";
Mol. Cell. Proteomics 8:2555-2569(2009).
[13]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-166; ASN-259; ASN-385 AND
ASN-399.
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).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and expression.";
Cell 143:1174-1189(2010).
[15]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 105-526.
PubMed=30958588; DOI=10.1002/prot.25686;
Deuschle F.C., Schiefner A., Skerra A.;
"Structural differences between the ectodomains of murine and human
CD98hc.";
Proteins 0:0-0(2019).
-!- FUNCTION: Component of several heterodimeric amino acid transporter
complexes. The precise substrate specificity depends on the other
subunit in the heterodimer (PubMed:9915839). The heterodimer with
SLC3A2 functions as sodium-independent, high-affinity transporter that
mediates uptake of large neutral amino acids such as phenylalanine,
tyrosine, L-DOPA, leucine, histidine, methionine and tryptophan
(PubMed:9915839). The complexes with SLC7A6 and SLC7A7 mediate uptake
of dibasic amino acids. The complexes function as amino acid exchangers
(By similarity). Required for targeting of SLC7A5 and SLC7A8 to the
plasma membrane and for channel activity (PubMed:9915839). Plays a role
in nitric oxide synthesis in human umbilical vein endothelial cells
(HUVECs) via transport of L-arginine (By similarity). The heterodimer
with SLC7A5/LAT1 may play a role in the transport of L-DOPA across the
blood-brain barrier (Probable). May mediate blood-to-retina L-leucine
transport across the inner blood-retinal barrier (By similarity). The
heterodimer with SLC7A5/LAT1 can mediate the transport of thyroid
hormones triiodothyronine (T3) and thyroxine (T4) across the cell
membrane. 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. The heterodimer with SLC7A5 is involved in the uptake of
toxic methylmercury (MeHg) when administered as the L-cysteine or D,L-
homocysteine complexes. Together with ICAM1, regulates the transport
activity SLC7A8 in polarized intestinal cells, by generating and
delivering intracellular signals. When associated with LAPTM4B, the
heterodimer formed by SLC3A2 and SLC7A5 is recruited to lysosomes to
promote leucine uptake into these organelles, and thereby mediates
mTORC1 activation (By similarity). {ECO:0000250|UniProtKB:P08195,
ECO:0000250|UniProtKB:Q794F9, ECO:0000269|PubMed:9915839,
ECO:0000305|PubMed:11011012}.
-!- SUBUNIT: Disulfide-linked heterodimer with a non-glycosylated light
chain (SLC7A5, SLC7A6, SLCA7A7, SLC7A8, SLC7A10 or SLCA7A11)
(PubMed:9915839, PubMed:10574970, PubMed:11011012). Interacts with
TLCD3A/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 (By
similarity). {ECO:0000250, ECO:0000250|UniProtKB:P08195,
ECO:0000269|PubMed:10574970, ECO:0000269|PubMed:11011012,
ECO:0000269|PubMed:9915839}.
-!- SUBCELLULAR LOCATION: Apical cell membrane
{ECO:0000250|UniProtKB:P08195}. Cell membrane
{ECO:0000269|PubMed:10574970, ECO:0000269|PubMed:9915839}; Single-pass
type II membrane protein {ECO:0000250|UniProtKB:P08195}. Cell junction
{ECO:0000269|PubMed:9915839}. Lysosome membrane
{ECO:0000250|UniProtKB:P08195}. Melanosome
{ECO:0000250|UniProtKB:P08195}. Note=Localized at the plasma membrane
when associated with SLC7A5 or SLC7A8. Localized to the apical membrane
of placental syncytiotrophoblastic cells. Recruited to lysosomes by
LAPTM4B (By similarity). Located selectively at cell-cell adhesion
sites (PubMed:9915839). 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,
ECO:0000250|UniProtKB:P08195, ECO:0000269|PubMed:9915839}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P10852-1; Sequence=Displayed;
Name=2;
IsoId=P10852-2; Sequence=VSP_054953;
-!- TISSUE SPECIFICITY: Detected on the surface of embryonic epithelial
cells in the epidermis, thymus, kidney, intestine, brain choroid
plexus, and in retina. Detected in adult and embryonic brain, spleen,
kidney, intestine and liver, and in adult testis (at protein level)
(PubMed:9915839). Observed in all adult tissues tested with strongest
expression in kidney, small intestine, spleen, thymus and liver
(PubMed:9915839). Moderate expression in brain, stomach, heart, testis,
lung, skin, pancreas and skeletal muscle. In brain expressed on
capillary endothelia in cerebral cortex. {ECO:0000269|PubMed:10574970,
ECO:0000269|PubMed:2928113, ECO:0000269|PubMed:9915839}.
-!- DEVELOPMENTAL STAGE: Strong expression in the liver of 14 dpc embryo
and in brain, spleen, liver, kidney and intestine of an 18 dpc embryo.
{ECO:0000269|PubMed:9915839}.
-!- INDUCTION: Expression induced by concanavalin-A stimulation. Induced
during cell activation but is subsequently maintained at constant
levels throughout the cell cycle in exponentially growing cells.
{ECO:0000269|PubMed:2928113, ECO:0000269|PubMed:9915839}.
-!- PTM: Phosphorylation on Ser-300 or Ser-302 and on Ser-420 by ecto-
protein kinases favors heterotypic cell-cell interactions.
{ECO:0000250|UniProtKB:P08195}.
-!- MISCELLANEOUS: Leucine uptake was inhibited by ileum, valine histidine
and phenylalanine as well as by 2-aminobicyclo-(2,2,1)-heptane-2-
carboxylic acid (BCH) (a specific inhibitor of system L transport).
-!- SIMILARITY: Belongs to the SLC3A transporter family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAE36291.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
---------------------------------------------------------------------------
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EMBL; X14309; CAA32490.1; -; mRNA.
EMBL; AB023408; BAA90555.1; -; mRNA.
EMBL; AK161280; BAE36291.1; ALT_INIT; mRNA.
EMBL; AK165417; BAE38172.1; -; mRNA.
EMBL; AC025794; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH466612; EDL33352.1; -; Genomic_DNA.
EMBL; BC065173; AAH65173.1; -; mRNA.
CCDS; CCDS29540.1; -. [P10852-1]
CCDS; CCDS50381.1; -. [P10852-2]
PIR; S03600; S03600.
RefSeq; NP_001154885.1; NM_001161413.1. [P10852-2]
RefSeq; NP_032603.3; NM_008577.4. [P10852-1]
RefSeq; XP_017173567.1; XM_017318078.1. [P10852-1]
PDB; 6I9Q; X-ray; 2.10 A; A=105-526.
PDB; 6SUA; X-ray; 2.75 A; B/D=105-526.
PDBsum; 6I9Q; -.
PDBsum; 6SUA; -.
SMR; P10852; -.
BioGRID; 201377; 9.
IntAct; P10852; 5.
MINT; P10852; -.
STRING; 10090.ENSMUSP00000130194; -.
CAZy; GH13; Glycoside Hydrolase Family 13.
TCDB; 2.A.3.8.5; the amino acid-polyamine-organocation (apc) family.
GlyConnect; 2098; 7 N-Linked glycans (3 sites).
GlyGen; P10852; 8 sites.
iPTMnet; P10852; -.
PhosphoSitePlus; P10852; -.
SwissPalm; P10852; -.
EPD; P10852; -.
jPOST; P10852; -.
MaxQB; P10852; -.
PaxDb; P10852; -.
PeptideAtlas; P10852; -.
PRIDE; P10852; -.
ProteomicsDB; 286031; -. [P10852-1]
ProteomicsDB; 286032; -. [P10852-2]
Antibodypedia; 15042; 1097 antibodies.
Ensembl; ENSMUST00000010239; ENSMUSP00000010239; ENSMUSG00000010095. [P10852-1]
Ensembl; ENSMUST00000170157; ENSMUSP00000130194; ENSMUSG00000010095. [P10852-2]
GeneID; 17254; -.
KEGG; mmu:17254; -.
UCSC; uc008gmi.2; mouse. [P10852-2]
UCSC; uc012bib.1; mouse. [P10852-1]
CTD; 6520; -.
MGI; MGI:96955; Slc3a2.
eggNOG; KOG0471; Eukaryota.
GeneTree; ENSGT00940000156646; -.
HOGENOM; CLU_006462_9_0_1; -.
InParanoid; P10852; -.
OMA; LHFPYVA; -.
OrthoDB; 1384693at2759; -.
PhylomeDB; P10852; -.
TreeFam; TF314498; -.
Reactome; R-MMU-210991; Basigin interactions.
Reactome; R-MMU-352230; Amino acid transport across the plasma membrane.
Reactome; R-MMU-71240; Tryptophan catabolism.
BioGRID-ORCS; 17254; 18 hits in 53 CRISPR screens.
ChiTaRS; Slc3a2; mouse.
PRO; PR:P10852; -.
Proteomes; UP000000589; Chromosome 19.
RNAct; P10852; protein.
Bgee; ENSMUSG00000010095; Expressed in placenta labyrinth and 336 other tissues.
ExpressionAtlas; P10852; baseline and differential.
Genevisible; P10852; MM.
GO; GO:1990184; C:amino acid transport complex; ISO:MGI.
GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
GO; GO:0044225; C:apical pole of neuron; IDA:MGI.
GO; GO:0009925; C:basal plasma membrane; ISO:MGI.
GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
GO; GO:0009986; C:cell surface; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0043025; C:neuronal cell body; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0045202; C:synapse; IDA:SynGO.
GO; GO:0015173; F:aromatic amino acid transmembrane transporter activity; ISO:MGI.
GO; GO:0003824; F:catalytic activity; IEA:InterPro.
GO; GO:0003725; F:double-stranded RNA binding; ISO:MGI.
GO; GO:0015180; F:L-alanine transmembrane transporter activity; ISO:MGI.
GO; GO:0015190; F:L-leucine transmembrane transporter activity; ISO:MGI.
GO; GO:0015175; F:neutral amino acid transmembrane transporter activity; ISS:UniProtKB.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
GO; GO:1904273; P:L-alanine import across plasma membrane; ISO:MGI.
GO; GO:1903801; P:L-leucine import across plasma membrane; ISS:UniProtKB.
GO; GO:0098713; P:leucine import across plasma membrane; ISO:MGI.
GO; GO:0015804; P:neutral amino acid transport; ISO:MGI.
GO; GO:0015823; P:phenylalanine transport; ISO:MGI.
GO; GO:0043330; P:response to exogenous dsRNA; ISO: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; IPR042280; SLC3A2.
InterPro; IPR031984; SLC3A2_N.
PANTHER; PTHR46673; PTHR46673; 1.
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; Alternative splicing; Amino-acid transport; Cell junction;
Cell membrane; Direct protein sequencing; Disulfide bond; Glycoprotein;
Isopeptide bond; Lysosome; Membrane; Phosphoprotein; Reference proteome;
Signal-anchor; Transmembrane; Transmembrane helix; Transport;
Ubl conjugation.
CHAIN 1..526
/note="4F2 cell-surface antigen heavy chain"
/id="PRO_0000064384"
TOPO_DOM 1..75
/note="Cytoplasmic"
/evidence="ECO:0000255"
TRANSMEM 76..99
/note="Helical; Signal-anchor for type II membrane protein"
TOPO_DOM 100..526
/note="Extracellular"
/evidence="ECO:0000255"
MOD_RES 2
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P08195"
MOD_RES 5
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:Q794F9"
MOD_RES 58
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:19144319,
ECO:0007744|PubMed:21183079"
MOD_RES 300
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P08195"
MOD_RES 302
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P08195"
MOD_RES 420
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P08195"
CARBOHYD 166
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:19349973,
ECO:0000269|PubMed:19656770"
CARBOHYD 259
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:19349973,
ECO:0000269|PubMed:19656770"
CARBOHYD 263
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 301
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 318
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 385
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:19349973,
ECO:0000269|PubMed:19656770"
CARBOHYD 399
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:19349973,
ECO:0000269|PubMed:19656770"
CARBOHYD 509
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
DISULFID 103
/note="Interchain (with C-164 in SLC7A5)"
/evidence="ECO:0000250|UniProtKB:P08195,
ECO:0000305|PubMed:9915839"
CROSSLNK 42
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000250|UniProtKB:P08195"
CROSSLNK 59
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000250|UniProtKB:P08195"
VAR_SEQ 1
/note="M -> MDPEPTEHSTDGVSVPRQPPSAQTGLDVQVVSAAGDSGTM (in
isoform 2)"
/evidence="ECO:0000303|PubMed:16141072"
/id="VSP_054953"
MUTAGEN 103
/note="C->S: Loss of interchain disulfide bond. No effect
on guidance of SLC7A5 to the plasma membrane."
/evidence="ECO:0000269|PubMed:9915839"
HELIX 111..114
/evidence="ECO:0007744|PDB:6I9Q"
STRAND 117..121
/evidence="ECO:0007744|PDB:6I9Q"
HELIX 123..127
/evidence="ECO:0007744|PDB:6I9Q"
STRAND 129..131
/evidence="ECO:0007744|PDB:6I9Q"
HELIX 133..138
/evidence="ECO:0007744|PDB:6I9Q"
HELIX 141..146
/evidence="ECO:0007744|PDB:6I9Q"
STRAND 150..154
/evidence="ECO:0007744|PDB:6I9Q"
STRAND 158..160
/evidence="ECO:0007744|PDB:6I9Q"
HELIX 165..167
/evidence="ECO:0007744|PDB:6I9Q"
STRAND 168..173
/evidence="ECO:0007744|PDB:6I9Q"
TURN 175..177
/evidence="ECO:0007744|PDB:6I9Q"
HELIX 180..192
/evidence="ECO:0007744|PDB:6I9Q"
STRAND 196..200
/evidence="ECO:0007744|PDB:6I9Q"
TURN 203..206
/evidence="ECO:0007744|PDB:6I9Q"
STRAND 207..209
/evidence="ECO:0007744|PDB:6I9Q"
HELIX 214..216
/evidence="ECO:0007744|PDB:6I9Q"
HELIX 217..233
/evidence="ECO:0007744|PDB:6I9Q"
STRAND 238..241
/evidence="ECO:0007744|PDB:6I9Q"
HELIX 244..246
/evidence="ECO:0007744|PDB:6I9Q"
HELIX 250..264
/evidence="ECO:0007744|PDB:6I9Q"
STRAND 269..273
/evidence="ECO:0007744|PDB:6I9Q"
HELIX 279..287
/evidence="ECO:0007744|PDB:6I9Q"
STRAND 289..291
/evidence="ECO:0007744|PDB:6I9Q"
STRAND 293..295
/evidence="ECO:0007744|PDB:6I9Q"
HELIX 298..300
/evidence="ECO:0007744|PDB:6I9Q"
HELIX 306..319
/evidence="ECO:0007744|PDB:6I9Q"
TURN 320..322
/evidence="ECO:0007744|PDB:6I9Q"
STRAND 331..333
/evidence="ECO:0007744|PDB:6I9Q"
HELIX 335..338
/evidence="ECO:0007744|PDB:6I9Q"
HELIX 341..343
/evidence="ECO:0007744|PDB:6I9Q"
HELIX 344..353
/evidence="ECO:0007744|PDB:6I9Q"
STRAND 354..361
/evidence="ECO:0007744|PDB:6I9Q"
TURN 362..367
/evidence="ECO:0007744|PDB:6I9Q"
STRAND 384..386
/evidence="ECO:0007744|PDB:6I9Q"
HELIX 388..390
/evidence="ECO:0007744|PDB:6I9Q"
STRAND 392..394
/evidence="ECO:0007744|PDB:6I9Q"
HELIX 398..400
/evidence="ECO:0007744|PDB:6I9Q"
HELIX 402..406
/evidence="ECO:0007744|PDB:6I9Q"
HELIX 412..425
/evidence="ECO:0007744|PDB:6I9Q"
HELIX 427..431
/evidence="ECO:0007744|PDB:6I9Q"
STRAND 433..436
/evidence="ECO:0007744|PDB:6I9Q"
STRAND 443..449
/evidence="ECO:0007744|PDB:6I9Q"
STRAND 455..461
/evidence="ECO:0007744|PDB:6I9Q"
STRAND 463..465
/evidence="ECO:0007744|PDB:6I9Q"
STRAND 484..492
/evidence="ECO:0007744|PDB:6I9Q"
HELIX 494..500
/evidence="ECO:0007744|PDB:6I9Q"
STRAND 504..507
/evidence="ECO:0007744|PDB:6I9Q"
STRAND 517..522
/evidence="ECO:0007744|PDB:6I9Q"
SEQUENCE 526 AA; 58337 MW; AE6261F11C7D9468 CRC64;
MSQDTEVDMK DVELNELEPE KQPMNAADGA AAGEKNGLVK IKVAEDETEA GVKFTGLSKE
ELLKVAGSPG WVRTRWALLL LFWLGWLGML AGAVVIIVRA PRCRELPVQR WWHKGALYRI
GDLQAFVGRD AGGIAGLKSH LEYLSTLKVK GLVLGPIHKN QKDEINETDL KQINPTLGSQ
EDFKDLLQSA KKKSIHIILD LTPNYQGQNA WFLPAQADIV ATKMKEALSS WLQDGVDGFQ
FRDVGKLMNA PLYLAEWQNI TKNLSEDRLL IAGTESSDLQ QIVNILESTS DLLLTSSYLS
NSTFTGERTE SLVTRFLNAT GSQWCSWSVS QAGLLADFIP DHLLRLYQLL LFTLPGTPVF
SYGDELGLQG ALPGQPAKAP LMPWNESSIF HIPRPVSLNM TVKGQNEDPG SLLTQFRRLS
DLRGKERSLL HGDFHALSSS PDLFSYIRHW DQNERYLVVL NFRDSGRSAR LGASNLPAGI
SLPASAKLLL STDSARQSRE EDTSLKLENL SLNPYEGLLL QFPFVA


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