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P18581 (CTR2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Low affinity cationic amino acid transporter 2

Short name=CAT-2
Short name=CAT2
Alternative name(s):
20.5
Solute carrier family 7 member 2
T-cell early activation protein
Short name=TEA
Gene names
Name:Slc7a2
Synonyms:Atrc2, Tea
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length657 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Low-affinity, high capacity permease involved in the transport of the cationic amino acids (arginine, lysine and ornithine). Plays a regulatory role in classical or alternative activation of macrophages. Ref.2 Ref.8

Subcellular location

Membrane; Multi-pass membrane protein.

Tissue specificity

Highest expression in liver and T-cells. Also expressed in brain and lung. Ref.4

Induction

By macrophage activation. Ref.8

Sequence similarities

Belongs to the amino acid-polyamine-organocation (APC) superfamily. Cationic amino acid transporter (CAT) (TC 2.A.3.3) family. [View classification]

Ontologies

Keywords
   Biological processAmino-acid transport
Transport
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
   DomainTransmembrane
Transmembrane helix
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processL-alpha-amino acid transmembrane transport

Inferred from direct assay PubMed 15659399. Source: GOC

L-amino acid transport

Inferred from direct assay PubMed 15659399. Source: MGI

arginine transport

Inferred from direct assay Ref.3Ref.2. Source: MGI

lysine transport

Inferred from direct assay Ref.2. Source: MGI

macrophage activation

Inferred from mutant phenotype PubMed 16703566. Source: MGI

nitric oxide biosynthetic process

Inferred from mutant phenotype PubMed 12675924. Source: MGI

nitric oxide production involved in inflammatory response

Inferred from mutant phenotype PubMed 11278602PubMed 17003120. Source: MGI

ornithine transport

Inferred from direct assay Ref.2. Source: MGI

regulation of inflammatory response

Inferred from mutant phenotype PubMed 17003120. Source: MGI

regulation of macrophage activation

Inferred from mutant phenotype Ref.8. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: Ensembl

integral component of membrane

Inferred from direct assay PubMed 8187816. Source: MGI

   Molecular_functionL-amino acid transmembrane transporter activity

Inferred from direct assay PubMed 15659399. Source: MGI

L-lysine transmembrane transporter activity

Inferred from direct assay Ref.2. Source: MGI

L-ornithine transmembrane transporter activity

Inferred from direct assay Ref.2. Source: MGI

arginine transmembrane transporter activity

Inferred from direct assay Ref.3Ref.2. Source: MGI

high affinity arginine transmembrane transporter activity

Inferred from direct assay Ref.3. Source: MGI

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P18581-1)

Also known as: Alpha;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P18581-2)

Also known as: Beta;

The sequence of this isoform differs from the canonical sequence as follows:
     357-397: MFPLPRILFA...AATMTAGVIS → IFPMPRVIYA...IATLSSGAVA
Note: Affinity of isoform 2 for arginine uptake is 70-fold higher than for isoform 1.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 657657Low affinity cationic amino acid transporter 2
PRO_0000054265

Regions

Topological domain1 – 3737Cytoplasmic Potential
Transmembrane38 – 5922Helical; Potential
Topological domain60 – 634Extracellular Potential
Transmembrane64 – 8421Helical; Potential
Topological domain85 – 10420Cytoplasmic Potential
Transmembrane105 – 12521Helical; Potential
Topological domain126 – 16338Extracellular Potential
Transmembrane164 – 18421Helical; Potential
Topological domain185 – 1928Cytoplasmic Potential
Transmembrane193 – 21321Helical; Potential
Topological domain214 – 24835Extracellular Potential
Transmembrane249 – 26921Helical; Potential
Topological domain270 – 28920Cytoplasmic Potential
Transmembrane290 – 30920Helical; Potential
Topological domain310 – 33930Extracellular Potential
Transmembrane340 – 36021Helical; Potential
Topological domain361 – 38525Cytoplasmic Potential
Transmembrane386 – 40621Helical; Potential
Topological domain407 – 4093Extracellular Potential
Transmembrane410 – 43021Helical; Potential
Topological domain431 – 48959Cytoplasmic Potential
Transmembrane490 – 51021Helical; Potential
Topological domain511 – 52313Extracellular Potential
Transmembrane524 – 54825Helical; Potential
Topological domain549 – 5568Cytoplasmic Potential
Transmembrane557 – 57721Helical; Potential
Topological domain578 – 5814Extracellular Potential
Transmembrane582 – 60221Helical; Potential
Topological domain603 – 65755Cytoplasmic Potential

Amino acid modifications

Modified residue6451Phosphoserine Ref.9
Glycosylation1571N-linked (GlcNAc...) Potential
Glycosylation2271N-linked (GlcNAc...) Potential
Glycosylation2391N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence357 – 39741MFPLP…AGVIS → IFPMPRVIYAMAEDGLLFKC LAQINSKTKTPVIATLSSGA VA in isoform 2.
VSP_000025

Experimental info

Sequence conflict1421L → P in BAE32720. Ref.5
Sequence conflict2421S → R in BAE32720. Ref.5
Sequence conflict2801E → K in BAE42415. Ref.5
Sequence conflict3351S → G in AAA75250. Ref.1
Sequence conflict3351S → G in AAA37372. Ref.2
Sequence conflict3351S → G in AAA37350. Ref.2
Sequence conflict3351S → G in AAA20397. Ref.3
Sequence conflict3351S → G in AAY87029. Ref.4
Sequence conflict3351S → G in BAE42415. Ref.5
Sequence conflict3351S → G in AAI27083. Ref.7
Sequence conflict3421S → A in AAA75250. Ref.1
Sequence conflict3421S → A in AAA37372. Ref.2
Sequence conflict3421S → A in AAA37350. Ref.2
Sequence conflict3421S → A in AAA20397. Ref.3
Sequence conflict3421S → A in AAY87029. Ref.4
Sequence conflict3421S → A in BAE42415. Ref.5
Sequence conflict3421S → A in AAI27083. Ref.7
Sequence conflict3571M → I in AAA75250. Ref.1
Sequence conflict3571M → I in BAE32720. Ref.5
Sequence conflict3571M → I in BAE42415. Ref.5
Sequence conflict3691R → E in AAA75250. Ref.1
Sequence conflict3691R → E in BAE32720. Ref.5
Sequence conflict3691R → E in BAE42415. Ref.5
Sequence conflict4301I → M in AAA37372. Ref.2
Sequence conflict4401D → E in AAA75250. Ref.1
Sequence conflict4401D → E in AAA37372. Ref.2
Sequence conflict4401D → E in AAA37350. Ref.2
Sequence conflict4401D → E in AAA20397. Ref.3
Sequence conflict4401D → E in AAY87029. Ref.4
Sequence conflict4401D → E in BAE42415. Ref.5
Sequence conflict4401D → E in AAI27083. Ref.7
Sequence conflict5371V → A in AAA75250. Ref.1
Sequence conflict5371V → A in AAA37372. Ref.2
Sequence conflict5371V → A in AAA37350. Ref.2
Sequence conflict5371V → A in AAA20397. Ref.3
Sequence conflict5371V → A in AAY87029. Ref.4
Sequence conflict5371V → A in BAE42415. Ref.5
Sequence conflict5371V → A in AAI27083. Ref.7
Sequence conflict6221D → E in AAA75250. Ref.1
Sequence conflict6221D → E in AAA37372. Ref.2
Sequence conflict6221D → E in AAA37350. Ref.2
Sequence conflict6221D → E in AAA20397. Ref.3
Sequence conflict6221D → E in AAY87029. Ref.4
Sequence conflict6221D → E in BAE42415. Ref.5
Sequence conflict6221D → E in AAI27083. Ref.7
Sequence conflict6261A → V in AAA75250. Ref.1
Sequence conflict6261A → V in AAA37372. Ref.2
Sequence conflict6261A → V in AAA37350. Ref.2
Sequence conflict6261A → V in AAA20397. Ref.3
Sequence conflict6261A → V in AAY87029. Ref.4
Sequence conflict6261A → V in BAE42415. Ref.5
Sequence conflict6261A → V in AAI27083. Ref.7
Sequence conflict6331A → V in AAA75250. Ref.1
Sequence conflict6331A → V in AAA37372. Ref.2
Sequence conflict6331A → V in AAA37350. Ref.2
Sequence conflict6331A → V in AAA20397. Ref.3
Sequence conflict6331A → V in AAY87029. Ref.4
Sequence conflict6331A → V in BAE42415. Ref.5
Sequence conflict6331A → V in AAI27083. Ref.7

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Alpha) [UniParc].

Last modified October 3, 2012. Version 3.
Checksum: 140CC99D3AB96082

FASTA65771,856
        10         20         30         40         50         60 
MIPCRAVLTF ARCLIRRKIV TLDSLEDSKL CRCLTTVDLI ALGVGSTLGA GVYVLAGEVA 

        70         80         90        100        110        120 
KADSGPSIVV SFLIAALASV MAGLCYAEFG ARVPKTGSAY LYTYVTVGEL WAFITGWNLI 

       130        140        150        160        170        180 
LSYVIGTSSV ARAWSGTFDE LLNKQIGQFF KTYFKMNYTG LAEYPDFFAV CLVLLLAGLL 

       190        200        210        220        230        240 
SFGVKESAWV NKFFTAINIL VLLFVMVAGF VKGNVANWKI SEEFLKNISA SAREPPSENG 

       250        260        270        280        290        300 
TSIYGAGGFM PYGFTGTLAG AATCFYAFVG FDCIATTGEE VRNPQKAIPI GIVTSLLVCF 

       310        320        330        340        350        360 
MAYFGVSAAL TLMMPYYLLD EKSPLPVAFE YVRWSPAKYV VSAGSLCALS TSLLGSMFPL 

       370        380        390        400        410        420 
PRILFAMARD GLLFRFLARV SKRQSPVAAT MTAGVISAVM AFLFDLKALV DMMSIGTLMA 

       430        440        450        460        470        480 
YSLVAACVLI LRYQPGLCYD QPKYTPEKET LESCTNATLK SESQVTMLQG QGFSLRTLFS 

       490        500        510        520        530        540 
PSALPTRQSA SLVSFLVGFL AFLILGLSIL TTYGVQAIAR LEAWSLALLA LFLVLCVAVI 

       550        560        570        580        590        600 
LTIWRQPQNQ QKVAFMVPFL PFLPAFSILV NIYLMVQLSA DTWIRFSIWM ALGFLIYFAY 

       610        620        630        640        650 
GIRHSLEGNP RDEEDDEDAF SDNINAATEE KSAMQANDHH QRNLSLPFIL HEKTSEC 

« Hide

Isoform 2 (Beta) [UniParc].

Checksum: 4DF5DF9EE57BB7EA
Show »

FASTA65871,786

References

« Hide 'large scale' references
[1]"Activated T cells express a novel gene on chromosome 8 that is closely related to the murine ecotropic retroviral receptor."
Macleod C.L., Finley K., Kakuda D., Kozak C.A., Wilkinson M.F.
Mol. Cell. Biol. 10:3663-3674(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Strain: AKR/J.
Tissue: T-cell.
[2]"Identification of a low affinity, high capacity transporter of cationic amino acids in mouse liver."
Closs E.I., Albritton L.M., Kim J.W., Cunningham J.M.
J. Biol. Chem. 268:7538-7544(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
Tissue: Liver.
[3]"Control of cationic amino acid transport and retroviral receptor functions in a membrane protein family."
Kavanaugh M.P., Wang H., Zhang Z., Zhang W., Wu Y.N., Dechant E., North R.A., Kabat D.
J. Biol. Chem. 269:15445-15450(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Liver.
[4]"Regulating gene expression through RNA nuclear retention."
Prasanth K.V., Prasanth S.G., Xuan Z., Hearn S., Freier S.M., Bennett C.F., Zhang M.Q., Spector D.L.
Cell 123:249-263(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
Strain: Swiss Webster / NIH.
[5]"The transcriptional landscape of the mammalian genome."
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. expand/collapse author list , 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.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: C57BL/6J and NOD.
[6]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
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. expand/collapse author list , 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.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[8]"Arginine transport via cationic amino acid transporter 2 plays a critical regulatory role in classical or alternative activation of macrophages."
Yeramian A., Martin L., Serrat N., Arpa L., Soler C., Bertran J., McLeod C., Palacin M., Modolell M., Lloberas J., Celada A.
J. Immunol. 176:5918-5924(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION.
[9]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-645, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M62838 mRNA. Translation: AAA75250.1.
L03290 mRNA. Translation: AAA37372.1.
L11600 mRNA. Translation: AAA37350.1.
L29006 mRNA. Translation: AAA20397.1.
DQ086834 mRNA. Translation: AAY87029.1.
AK154621 mRNA. Translation: BAE32720.1.
AK171369 mRNA. Translation: BAE42415.1.
AC116511 Genomic DNA. No translation available.
BC127082 mRNA. Translation: AAI27083.1.
PIRA54011.
RefSeqNP_001038205.1. NM_001044740.2.
NP_031540.2. NM_007514.3.
XP_006509316.1. XM_006509253.1.
UniGeneMm.4676.

3D structure databases

ProteinModelPortalP18581.
SMRP18581. Positions 45-431.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

TCDB2.A.3.3.2. the amino acid-polyamine-organocation (apc) family.

PTM databases

PhosphoSiteP18581.

Proteomic databases

PaxDbP18581.
PRIDEP18581.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000057784; ENSMUSP00000058866; ENSMUSG00000031596. [P18581-1]
ENSMUST00000098816; ENSMUSP00000096414; ENSMUSG00000031596. [P18581-2]
ENSMUST00000117077; ENSMUSP00000113729; ENSMUSG00000031596. [P18581-2]
GeneID11988.
KEGGmmu:11988.

Organism-specific databases

CTD6542.
MGIMGI:99828. Slc7a2.

Phylogenomic databases

eggNOGCOG0531.
GeneTreeENSGT00700000104437.
HOGENOMHOG000250623.
HOVERGENHBG000280.
InParanoidQ38RA6.
KOK13864.
OrthoDBEOG72C501.
TreeFamTF315212.

Gene expression databases

ArrayExpressP18581.
GenevestigatorP18581.

Family and domain databases

InterProIPR002293. AA/rel_permease1.
IPR004755. Cat_AA_permease.
[Graphical view]
PANTHERPTHR11785. PTHR11785. 1 hit.
PfamPF13520. AA_permease_2. 1 hit.
[Graphical view]
PIRSFPIRSF006060. AA_transporter. 1 hit.
TIGRFAMsTIGR00906. 2A0303. 1 hit.
ProtoNetSearch...

Other

ChiTaRSSLC7A2. mouse.
NextBio280145.
PROP18581.
SOURCESearch...

Entry information

Entry nameCTR2_MOUSE
AccessionPrimary (citable) accession number: P18581
Secondary accession number(s): E9QPL9 expand/collapse secondary AC list , Q38RA6, Q3TB99, Q3U3R5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: October 3, 2012
Last modified: April 16, 2014
This is version 130 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot