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Cationic amino acid transporter 2 (CAT-2) (CAT2) (20.5) (Low affinity cationic amino acid transporter 2) (Solute carrier family 7 member 2) (T-cell early activation protein) (TEA)

 CTR2_MOUSE              Reviewed;         657 AA.
P18581; E9QPL9; Q38RA6; Q3TB99; Q3U3R5;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
03-OCT-2012, sequence version 3.
10-MAY-2017, entry version 155.
RecName: Full=Cationic amino acid transporter 2;
Short=CAT-2;
Short=CAT2;
AltName: Full=20.5;
AltName: Full=Low affinity cationic amino acid transporter 2 {ECO:0000303|PubMed:8385111};
AltName: Full=Solute carrier family 7 member 2;
AltName: Full=T-cell early activation protein {ECO:0000303|PubMed:8195186};
Short=TEA {ECO:0000303|PubMed:8195186};
Name=Slc7a2; Synonyms=Atrc2, Tea;
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 2).
STRAIN=AKR/J; TISSUE=T-cell;
PubMed=1694015; DOI=10.1128/MCB.10.7.3663;
Macleod C.L., Finley K., Kakuda D., Kozak C.A., Wilkinson M.F.;
"Activated T cells express a novel gene on chromosome 8 that is
closely related to the murine ecotropic retroviral receptor.";
Mol. Cell. Biol. 10:3663-3674(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION.
TISSUE=Liver;
PubMed=8385111;
Closs E.I., Albritton L.M., Kim J.W., Cunningham J.M.;
"Identification of a low affinity, high capacity transporter of
cationic amino acids in mouse liver.";
J. Biol. Chem. 268:7538-7544(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
LOCATION, AND ALTERNATIVE SPLICING.
TISSUE=Liver;
PubMed=8195186;
Kavanaugh M.P., Wang H., Zhang Z., Zhang W., Wu Y.N., Dechant E.,
North R.A., Kabat D.;
"Control of cationic amino acid transport and retroviral receptor
functions in a membrane protein family.";
J. Biol. Chem. 269:15445-15450(1994).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
STRAIN=Swiss Webster / NIH;
PubMed=16239143; DOI=10.1016/j.cell.2005.08.033;
Prasanth K.V., Prasanth S.G., Xuan Z., Hearn S., Freier S.M.,
Bennett C.F., Zhang M.Q., Spector D.L.;
"Regulating gene expression through RNA nuclear retention.";
Cell 123:249-263(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J, and NOD;
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).
[6]
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).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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).
[8]
FUNCTION, AND INDUCTION.
PubMed=16670299; DOI=10.4049/jimmunol.176.10.5918;
Yeramian A., Martin L., Serrat N., Arpa L., Soler C., Bertran J.,
McLeod C., Palacin M., Modolell M., Lloberas J., Celada A.;
"Arginine transport via cationic amino acid transporter 2 plays a
critical regulatory role in classical or alternative activation of
macrophages.";
J. Immunol. 176:5918-5924(2006).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-645, 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).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-645, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
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).
-!- FUNCTION: Isoform 1 functions as low-affinity, high capacity
permease involved in the transport of the cationic amino acids
(arginine, lysine and ornithine). Isoform 2 also functions as
permease that mediates the transport of the cationic amino acids
(arginine, lysine and ornithine), but it has much higher affinity
for arginine than isoform 1. May play a role in classical or
alternative activation of macrophages via its role in arginine
transport. {ECO:0000269|PubMed:16670299,
ECO:0000269|PubMed:8195186, ECO:0000269|PubMed:8385111}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8195186,
ECO:0000269|PubMed:8385111}; Multi-pass membrane protein
{ECO:0000269|PubMed:8195186, ECO:0000269|PubMed:8385111}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Alpha;
IsoId=P18581-1; Sequence=Displayed;
Name=2; Synonyms=Beta;
IsoId=P18581-2; Sequence=VSP_000025;
Note=Affinity of isoform 2 for arginine uptake is 70-fold higher
than for isoform 1. {ECO:0000269|PubMed:8195186};
-!- TISSUE SPECIFICITY: Detected in liver (at protein level)
(PubMed:8385111). Highest expression in liver and T-cells. Also
expressed in brain and lung. {ECO:0000269|PubMed:16239143,
ECO:0000269|PubMed:8385111}.
-!- INDUCTION: By macrophage activation.
{ECO:0000269|PubMed:16670299}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:8385111}.
-!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
superfamily. Cationic amino acid transporter (CAT) (TC 2.A.3.3)
family. {ECO:0000305}.
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EMBL; M62838; AAA75250.1; -; mRNA.
EMBL; L03290; AAA37372.1; -; mRNA.
EMBL; L11600; AAA37350.1; -; mRNA.
EMBL; L29006; AAA20397.1; -; mRNA.
EMBL; DQ086834; AAY87029.1; -; mRNA.
EMBL; AK154621; BAE32720.1; -; mRNA.
EMBL; AK171369; BAE42415.1; -; mRNA.
EMBL; AC116511; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC127082; AAI27083.1; -; mRNA.
CCDS; CCDS22258.1; -. [P18581-1]
CCDS; CCDS40327.1; -. [P18581-2]
PIR; A54011; A54011.
RefSeq; NP_001038205.1; NM_001044740.2. [P18581-2]
RefSeq; NP_031540.2; NM_007514.3. [P18581-1]
RefSeq; XP_006509316.1; XM_006509253.3. [P18581-2]
UniGene; Mm.4676; -.
ProteinModelPortal; P18581; -.
STRING; 10090.ENSMUSP00000096414; -.
TCDB; 2.A.3.3.2; the amino acid-polyamine-organocation (apc) family.
iPTMnet; P18581; -.
PhosphoSitePlus; P18581; -.
MaxQB; P18581; -.
PaxDb; P18581; -.
PRIDE; P18581; -.
Ensembl; ENSMUST00000057784; ENSMUSP00000058866; ENSMUSG00000031596. [P18581-1]
Ensembl; ENSMUST00000098816; ENSMUSP00000096414; ENSMUSG00000031596. [P18581-2]
Ensembl; ENSMUST00000117077; ENSMUSP00000113729; ENSMUSG00000031596. [P18581-2]
GeneID; 11988; -.
KEGG; mmu:11988; -.
UCSC; uc009lnf.1; mouse. [P18581-1]
UCSC; uc009lng.1; mouse. [P18581-2]
CTD; 6542; -.
MGI; MGI:99828; Slc7a2.
eggNOG; KOG1286; Eukaryota.
eggNOG; COG0531; LUCA.
GeneTree; ENSGT00760000119151; -.
HOGENOM; HOG000250623; -.
HOVERGEN; HBG000280; -.
InParanoid; P18581; -.
KO; K13864; -.
TreeFam; TF315212; -.
Reactome; R-MMU-352230; Amino acid transport across the plasma membrane.
ChiTaRS; Slc7a2; mouse.
PRO; PR:P18581; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000031596; -.
ExpressionAtlas; P18581; baseline and differential.
Genevisible; P18581; MM.
GO; GO:0030054; C:cell junction; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; IDA:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0015181; F:arginine transmembrane transporter activity; IMP:MGI.
GO; GO:0005289; F:high-affinity arginine transmembrane transporter activity; IDA:MGI.
GO; GO:0097627; F:high-affinity L-ornithine transmembrane transporter activity; IDA:MGI.
GO; GO:0005292; F:high-affinity lysine transmembrane transporter activity; IDA:MGI.
GO; GO:0061459; F:L-arginine transmembrane transporter activity; IMP:MGI.
GO; GO:0015189; F:L-lysine transmembrane transporter activity; IDA:MGI.
GO; GO:0000064; F:L-ornithine transmembrane transporter activity; IDA:MGI.
GO; GO:0097626; F:low-affinity L-arginine transmembrane transporter activity; IDA:MGI.
GO; GO:0097638; P:L-arginine import across plasma membrane; IDA:MGI.
GO; GO:1902023; P:L-arginine transport; IMP:MGI.
GO; GO:0097639; P:L-lysine import across plasma membrane; IDA:MGI.
GO; GO:0097640; P:L-ornithine import across plasma membrane; IDA:MGI.
GO; GO:1903352; P:L-ornithine transmembrane transport; IDA:MGI.
GO; GO:0042116; P:macrophage activation; IMP:MGI.
GO; GO:0006809; P:nitric oxide biosynthetic process; IMP:MGI.
GO; GO:0002537; P:nitric oxide production involved in inflammatory response; IMP:MGI.
GO; GO:0050727; P:regulation of inflammatory response; IMP:MGI.
GO; GO:0043030; P:regulation of macrophage activation; IMP:UniProtKB.
InterPro; IPR002293; AA/rel_permease1.
InterPro; IPR004755; Cat_AA_permease.
InterPro; IPR029485; CAT_C.
Pfam; PF13520; AA_permease_2; 1.
Pfam; PF13906; AA_permease_C; 1.
TIGRFAMs; TIGR00906; 2A0303; 1.
1: Evidence at protein level;
Alternative splicing; Amino-acid transport; Cell membrane;
Complete proteome; Glycoprotein; Membrane; Phosphoprotein;
Reference proteome; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 657 Cationic amino acid transporter 2.
/FTId=PRO_0000054265.
TOPO_DOM 1 37 Cytoplasmic. {ECO:0000255}.
TRANSMEM 38 59 Helical. {ECO:0000255}.
TOPO_DOM 60 63 Extracellular. {ECO:0000255}.
TRANSMEM 64 84 Helical. {ECO:0000255}.
TOPO_DOM 85 104 Cytoplasmic. {ECO:0000255}.
TRANSMEM 105 125 Helical. {ECO:0000255}.
TOPO_DOM 126 163 Extracellular. {ECO:0000255}.
TRANSMEM 164 184 Helical. {ECO:0000255}.
TOPO_DOM 185 192 Cytoplasmic. {ECO:0000255}.
TRANSMEM 193 213 Helical. {ECO:0000255}.
TOPO_DOM 214 248 Extracellular. {ECO:0000255}.
TRANSMEM 249 269 Helical. {ECO:0000255}.
TOPO_DOM 270 289 Cytoplasmic. {ECO:0000255}.
TRANSMEM 290 309 Helical. {ECO:0000255}.
TOPO_DOM 310 339 Extracellular. {ECO:0000255}.
TRANSMEM 340 360 Helical. {ECO:0000255}.
TOPO_DOM 361 385 Cytoplasmic. {ECO:0000255}.
TRANSMEM 386 406 Helical. {ECO:0000255}.
TOPO_DOM 407 409 Extracellular. {ECO:0000255}.
TRANSMEM 410 430 Helical. {ECO:0000255}.
TOPO_DOM 431 489 Cytoplasmic. {ECO:0000255}.
TRANSMEM 490 510 Helical. {ECO:0000255}.
TOPO_DOM 511 523 Extracellular. {ECO:0000255}.
TRANSMEM 524 548 Helical. {ECO:0000255}.
TOPO_DOM 549 556 Cytoplasmic. {ECO:0000255}.
TRANSMEM 557 577 Helical. {ECO:0000255}.
TOPO_DOM 578 581 Extracellular. {ECO:0000255}.
TRANSMEM 582 602 Helical. {ECO:0000255}.
TOPO_DOM 603 657 Cytoplasmic. {ECO:0000255}.
MOD_RES 24 24 Phosphoserine.
{ECO:0000250|UniProtKB:P52569}.
MOD_RES 463 463 Phosphoserine.
{ECO:0000250|UniProtKB:P52569}.
MOD_RES 645 645 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
CARBOHYD 157 157 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 227 227 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 239 239 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 357 397 MFPLPRILFAMARDGLLFRFLARVSKRQSPVAATMTAGVIS
-> IFPMPRVIYAMAEDGLLFKCLAQINSKTKTPVIATLSS
GAVA (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072,
ECO:0000303|PubMed:16239143,
ECO:0000303|PubMed:1694015}.
/FTId=VSP_000025.
CONFLICT 142 142 L -> P (in Ref. 5; BAE32720).
{ECO:0000305}.
CONFLICT 242 242 S -> R (in Ref. 5; BAE32720).
{ECO:0000305}.
CONFLICT 280 280 E -> K (in Ref. 5; BAE42415).
{ECO:0000305}.
CONFLICT 335 335 S -> G (in Ref. 1; AAA75250, 2; AAA37372/
AAA37350, 3; AAA20397, 4; AAY87029, 5;
BAE42415 and 7; AAI27083). {ECO:0000305}.
CONFLICT 342 342 S -> A (in Ref. 1; AAA75250, 2; AAA37372/
AAA37350, 3; AAA20397, 4; AAY87029, 5;
BAE42415 and 7; AAI27083). {ECO:0000305}.
CONFLICT 357 357 M -> I (in Ref. 1; AAA75250 and 5;
BAE32720/BAE42415). {ECO:0000305}.
CONFLICT 369 369 R -> E (in Ref. 1; AAA75250 and 5;
BAE32720/BAE42415). {ECO:0000305}.
CONFLICT 430 430 I -> M (in Ref. 2; AAA37372).
{ECO:0000305}.
CONFLICT 440 440 D -> E (in Ref. 1; AAA75250, 2; AAA37372/
AAA37350, 3; AAA20397, 4; AAY87029, 5;
BAE42415 and 7; AAI27083). {ECO:0000305}.
CONFLICT 537 537 V -> A (in Ref. 1; AAA75250, 2; AAA37372/
AAA37350, 3; AAA20397, 4; AAY87029, 5;
BAE42415 and 7; AAI27083). {ECO:0000305}.
CONFLICT 622 622 D -> E (in Ref. 1; AAA75250, 2; AAA37372/
AAA37350, 3; AAA20397, 4; AAY87029, 5;
BAE42415 and 7; AAI27083). {ECO:0000305}.
CONFLICT 626 626 A -> V (in Ref. 1; AAA75250, 2; AAA37372/
AAA37350, 3; AAA20397, 4; AAY87029, 5;
BAE42415 and 7; AAI27083). {ECO:0000305}.
CONFLICT 633 633 A -> V (in Ref. 1; AAA75250, 2; AAA37372/
AAA37350, 3; AAA20397, 4; AAY87029, 5;
BAE42415 and 7; AAI27083). {ECO:0000305}.
SEQUENCE 657 AA; 71856 MW; 140CC99D3AB96082 CRC64;
MIPCRAVLTF ARCLIRRKIV TLDSLEDSKL CRCLTTVDLI ALGVGSTLGA GVYVLAGEVA
KADSGPSIVV SFLIAALASV MAGLCYAEFG ARVPKTGSAY LYTYVTVGEL WAFITGWNLI
LSYVIGTSSV ARAWSGTFDE LLNKQIGQFF KTYFKMNYTG LAEYPDFFAV CLVLLLAGLL
SFGVKESAWV NKFFTAINIL VLLFVMVAGF VKGNVANWKI SEEFLKNISA SAREPPSENG
TSIYGAGGFM PYGFTGTLAG AATCFYAFVG FDCIATTGEE VRNPQKAIPI GIVTSLLVCF
MAYFGVSAAL TLMMPYYLLD EKSPLPVAFE YVRWSPAKYV VSAGSLCALS TSLLGSMFPL
PRILFAMARD GLLFRFLARV SKRQSPVAAT MTAGVISAVM AFLFDLKALV DMMSIGTLMA
YSLVAACVLI LRYQPGLCYD QPKYTPEKET LESCTNATLK SESQVTMLQG QGFSLRTLFS
PSALPTRQSA SLVSFLVGFL AFLILGLSIL TTYGVQAIAR LEAWSLALLA LFLVLCVAVI
LTIWRQPQNQ QKVAFMVPFL PFLPAFSILV NIYLMVQLSA DTWIRFSIWM ALGFLIYFAY
GIRHSLEGNP RDEEDDEDAF SDNINAATEE KSAMQANDHH QRNLSLPFIL HEKTSEC


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Y105451 Solute Carrier Family 7 (Cationic Amino Acid Transporter, Y+ System), Member 5 (Slc7a5), Human Antibody 50ug
EIAAB37161 Bos taurus,Bovine,Probable cationic amino acid transporter,SLC7A14,Solute carrier family 7 member 14
GS-2062a solute carrier family 7 (cationic amino acid transporter, y+ system), member 5 primary antibody, Host: Rabbit 200ul


 

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