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CTR2_RAT
ID   CTR2_RAT                Reviewed;         657 AA.
AC   B5D5N9; B5D5P0;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Cationic amino acid transporter 2;
DE            Short=CAT-2;
DE            Short=CAT2;
DE   AltName: Full=Low affinity cationic amino acid transporter 2;
DE   AltName: Full=Solute carrier family 7 member 2;
GN   Name=Slc7a2; Synonyms=Atrc2, Cat2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=Wistar; TISSUE=Aortic smooth muscle;
RA   Cui Z., Kelly J., Brzeski H., Marber M., Pearson J.D., Baydoun A.R.;
RT   "Rattus cationic amino acid transporter-2 (rCAT-2) mRNA.";
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-645, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Functions as permease involved in the transport of the
CC       cationic amino acids (arginine, lysine and ornithine). The affinity for
CC       its substrates differs between isoforms created by alternative
CC       splicing. May play a role in classical or alternative activation of
CC       macrophages via its role in arginine transport.
CC       {ECO:0000250|UniProtKB:P18581}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P18581};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:P18581}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=CAT2A;
CC         IsoId=B5D5N9-1; Sequence=Displayed;
CC       Name=2; Synonyms=CAT2B;
CC         IsoId=B5D5N9-2; Sequence=VSP_037355;
CC   -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC       superfamily. Cationic amino acid transporter (CAT) (TC 2.A.3.3) family.
CC       {ECO:0000305}.
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DR   EMBL; AF245001; AAQ14243.1; -; mRNA.
DR   EMBL; AF245002; AAQ14244.1; -; mRNA.
DR   EMBL; CH473995; EDL78824.1; -; Genomic_DNA.
DR   EMBL; CH473995; EDL78825.1; -; Genomic_DNA.
DR   RefSeq; NP_001128158.1; NM_001134686.2. [B5D5N9-2]
DR   RefSeq; NP_072141.2; NM_022619.3. [B5D5N9-1]
DR   AlphaFoldDB; B5D5N9; -.
DR   SMR; B5D5N9; -.
DR   BioGRID; 249135; 1.
DR   IntAct; B5D5N9; 1.
DR   MINT; B5D5N9; -.
DR   STRING; 10116.ENSRNOP00000055811; -.
DR   GlyGen; B5D5N9; 3 sites.
DR   iPTMnet; B5D5N9; -.
DR   PhosphoSitePlus; B5D5N9; -.
DR   jPOST; B5D5N9; -.
DR   PeptideAtlas; B5D5N9; -.
DR   Ensembl; ENSRNOT00000014809; ENSRNOP00000014809; ENSRNOG00000011016. [B5D5N9-2]
DR   Ensembl; ENSRNOT00000015127; ENSRNOP00000015127; ENSRNOG00000011016. [B5D5N9-1]
DR   GeneID; 64554; -.
DR   KEGG; rno:64554; -.
DR   CTD; 6542; -.
DR   RGD; 68387; Slc7a2.
DR   eggNOG; KOG1286; Eukaryota.
DR   GeneTree; ENSGT00940000160440; -.
DR   HOGENOM; CLU_007946_15_7_1; -.
DR   InParanoid; B5D5N9; -.
DR   OMA; WFAKTHP; -.
DR   OrthoDB; 439017at2759; -.
DR   PhylomeDB; B5D5N9; -.
DR   Reactome; R-RNO-352230; Amino acid transport across the plasma membrane.
DR   PRO; PR:B5D5N9; -.
DR   Proteomes; UP000002494; Chromosome 16.
DR   Proteomes; UP000234681; Chromosome 16.
DR   Bgee; ENSRNOG00000011016; Expressed in liver and 17 other tissues.
DR   GO; GO:0030054; C:cell junction; IEA:Ensembl.
DR   GO; GO:0016021; C:integral component of membrane; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0015171; F:amino acid transmembrane transporter activity; ISO:RGD.
DR   GO; GO:0015179; F:L-amino acid transmembrane transporter activity; ISO:RGD.
DR   GO; GO:0061459; F:L-arginine transmembrane transporter activity; IDA:RGD.
DR   GO; GO:0015189; F:L-lysine transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0000064; F:L-ornithine transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0089718; P:amino acid import across plasma membrane; ISO:RGD.
DR   GO; GO:0006865; P:amino acid transport; IBA:GO_Central.
DR   GO; GO:1902475; P:L-alpha-amino acid transmembrane transport; ISO:RGD.
DR   GO; GO:0015807; P:L-amino acid transport; ISO:RGD.
DR   GO; GO:0097638; P:L-arginine import across plasma membrane; ISO:RGD.
DR   GO; GO:1903826; P:L-arginine transmembrane transport; IDA:RGD.
DR   GO; GO:1903352; P:L-ornithine transmembrane transport; IBA:GO_Central.
DR   GO; GO:0042116; P:macrophage activation; ISO:RGD.
DR   GO; GO:0006809; P:nitric oxide biosynthetic process; ISO:RGD.
DR   GO; GO:0002537; P:nitric oxide production involved in inflammatory response; ISO:RGD.
DR   GO; GO:0050727; P:regulation of inflammatory response; ISO:RGD.
DR   GO; GO:0043030; P:regulation of macrophage activation; ISO:RGD.
DR   InterPro; IPR002293; AA/rel_permease1.
DR   InterPro; IPR004755; Cat_AA_permease.
DR   InterPro; IPR029485; CAT_C.
DR   Pfam; PF13520; AA_permease_2; 1.
DR   Pfam; PF13906; AA_permease_C; 1.
DR   TIGRFAMs; TIGR00906; 2A0303; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Amino-acid transport; Cell membrane; Glycoprotein;
KW   Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..657
FT                   /note="Cationic amino acid transporter 2"
FT                   /id="PRO_0000375227"
FT   TOPO_DOM        1..38
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        39..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        60..66
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        67..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        88..104
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        105..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        126..163
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        164..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        185..192
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        193..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        214..248
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        249..269
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        270..289
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        290..310
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        311..339
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        340..360
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        361..385
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        386..406
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        407..409
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        410..430
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        431..489
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        490..510
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        511..523
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        524..544
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        545..554
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        555..575
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        576..581
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        582..602
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        603..657
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         24
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P52569"
FT   MOD_RES         463
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P52569"
FT   MOD_RES         645
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   CARBOHYD        157
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        227
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        239
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         357..397
FT                   /note="MFPLPRILFAMARDGLLFRFLARVSKRQSPVAATMTAGVIS -> IFPMPRV
FT                   IYAMAEDGLLFKCLAQINSKTKTPIIATLSSGAVA (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_037355"
SQ   SEQUENCE   657 AA;  71694 MW;  313E0A05771931B7 CRC64;
     MIPCRAVLTF TRCLIRRKIV TLDSLEDSKL CRCLTTMDLI 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 YVGWGPAKYV VAAGSLCALS TSLLGSMFPL
     PRILFAMARD GLLFRFLARV SKRQSPVAAT MTAGVISAVM AFLFDLKALV DMMSIGTLMA
     YSLVAACVLI LRYQPGLCYE QPKYTPEKDI LESCTNATSK SESQVTMLQG QGFSLRTLFN
     PSALPTRQSA SLVSFLVGFL AFLIAGLSIL TTYGVQAIAR LEAWSLALLA LFLVLCAAVI
     LTIWRQPQNQ QKVAFMVPFL PFLPAFSILV NIYLMVQLSA DTWVRFSIWM VLGFLIYFAY
     GIRHSLEGNP RDEEEDEDVC PDNVNAAAEE KSAMQANDHH QRNLSLPFIL HEKTSEC
 
 
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