CTR2_PIG
ID CTR2_PIG Reviewed; 657 AA.
AC A8I499; A1YRJ0;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 25-MAY-2022, entry version 68.
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;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zhi A.M., Feng D.Y., Huang Z.Y., Zou S.G., Zuo J.J.;
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 13-657.
RA Zhang Y., Zhou X.Y., Feng D.Y.;
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Functions as permease involved in the transport of the
CC cationic amino acids (arginine, lysine and ornithine). May play a role
CC in classical or alternative activation of macrophages via its role in
CC arginine transport. {ECO:0000250|UniProtKB:P18581}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P18581};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P18581}.
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; EU155140; ABV80234.1; -; mRNA.
DR EMBL; EF125869; ABL75272.1; -; mRNA.
DR RefSeq; NP_001103890.1; NM_001110420.1.
DR AlphaFoldDB; A8I499; -.
DR SMR; A8I499; -.
DR STRING; 9823.ENSSSCP00000007445; -.
DR PaxDb; A8I499; -.
DR PRIDE; A8I499; -.
DR GeneID; 100037298; -.
DR KEGG; ssc:100037298; -.
DR CTD; 6542; -.
DR eggNOG; KOG1286; Eukaryota.
DR InParanoid; A8I499; -.
DR OrthoDB; 439017at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Amino-acid transport; Cell membrane; Glycoprotein; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..657
FT /note="Cationic amino acid transporter 2"
FT /id="PRO_0000375226"
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:0000250|UniProtKB:P52569"
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 CONFLICT 19
FT /note="V -> I (in Ref. 2; ABL75272)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 657 AA; 71458 MW; A5237542F832D6EE CRC64;
MIPCRATLSF ARCLIRRKVV TLDSLEDSKL CRCLSTMDLI ALGVGSTLGA GVYVLAGEVA
KADSGPSIVV SFLIAALASV MAGLCYAEFG ARVPKTGSAY LYTYVTVGEL WAFITGWNLI
LSYVIGTSSV ARAWSGTLDE LLNKQIGQFF RTYFKMNYTG LAEYPDFSAV CLILLLAGLL
SFGVKESAWV NKVFTAVNIL VLLFVMVAGF VKGNVANRKI SEEFLKNISA SAREPPSENG
TSIYGAGGFM PYGFTGTLAG AATCFYAFVG FDCIATTGEE VRNPQKAIPI GIVTSLLVCF
MAYFGVSAAL TLMMPYYVLD EKSPLPVAFE YVGWGPAKYV VAAGSLCALS TSLLGSMFPL
PRILFAMARD GLLFRFLARV SKRQSPVAAT LTAGVISAVM AFLFDLKALV DMMSIGTLLA
YSLVAACVLI LRYQPGLSYE QPKYCPEKEA LGSCASAASK SKSQVTVLPE WGFSLRAFFS
PSLLPTKQSA SLVSFLVGFL AFLILGLSIL TTYGVHAIAR LEAWSLALLV LFLVLCVAVV
LTIWRQPQNQ QKVAFMVPFL PFLPAFSILV NIYLMVQLSA DTWIRFSIWM ALGFLIYFAY
GIRHSLEGNS RDEDEDEDTH SNNVHTAAEE KSAIQANDHH QRHLSLPFIF HEKTSEC
