CTR2_CHICK
ID CTR2_CHICK Reviewed; 654 AA.
AC B3TP03; B3TP04; B3TP05;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Cationic amino acid transporter 2;
DE Short=CAT-2;
DE Short=CAT2;
DE Short=cCAT-2;
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 Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), IDENTIFICATION OF ISOFORM
RP 3 AS POTENTIAL NMD TARGET, AND TISSUE SPECIFICITY.
RC TISSUE=Pectoralis muscle;
RX PubMed=18495509; DOI=10.1016/j.cbpb.2008.03.018;
RA Humphrey B.D., Kirsch S., Morris D.;
RT "Molecular cloning and characterization of the chicken cationic amino acid
RT transporter-2 gene.";
RL Comp. Biochem. Physiol. 150B:301-311(2008).
CC -!- FUNCTION: Low-affinity, high capacity permease involved in the
CC transport of the cationic amino acids (arginine, lysine and ornithine).
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=3;
CC Name=1; Synonyms=cCAT-2A;
CC IsoId=B3TP03-1; Sequence=Displayed;
CC Name=2; Synonyms=cCAT-2B;
CC IsoId=B3TP03-2; Sequence=VSP_037357;
CC Name=3; Synonyms=cCAT-2C;
CC IsoId=B3TP03-3; Sequence=VSP_037356, VSP_037358;
CC -!- TISSUE SPECIFICITY: Expressed in liver, pectoralis and gastrocnemius.
CC {ECO:0000269|PubMed:18495509}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. Lacks the domain responsible for mediating amino acids
CC transport. {ECO:0000305}.
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; EU360448; ACA61195.1; -; mRNA.
DR EMBL; EU360449; ACA61196.1; -; mRNA.
DR EMBL; EU360450; ACA61197.1; -; mRNA.
DR AlphaFoldDB; B3TP03; -.
DR SMR; B3TP03; -.
DR STRING; 9031.ENSGALP00000041429; -.
DR PaxDb; B3TP03; -.
DR PRIDE; B3TP03; -.
DR VEuPathDB; HostDB:geneid_422730; -.
DR eggNOG; KOG1286; Eukaryota.
DR InParanoid; B3TP03; -.
DR PhylomeDB; B3TP03; -.
DR SABIO-RK; B3TP03; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:AgBase.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:AgBase.
DR GO; GO:0005794; C:Golgi apparatus; IDA:AgBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:AgBase.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0061459; F:L-arginine transmembrane transporter activity; IDA:AgBase.
DR GO; GO:0015189; F:L-lysine transmembrane transporter activity; IDA:AgBase.
DR GO; GO:0000064; F:L-ornithine transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006865; P:amino acid transport; IBA:GO_Central.
DR GO; GO:0097638; P:L-arginine import across plasma membrane; IDA:AgBase.
DR GO; GO:0097639; P:L-lysine import across plasma membrane; IDA:AgBase.
DR GO; GO:1903352; P:L-ornithine transmembrane transport; IBA:GO_Central.
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 Alternative splicing; Amino-acid transport; Cell membrane; Glycoprotein;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..654
FT /note="Cationic amino acid transporter 2"
FT /id="PRO_0000375228"
FT TOPO_DOM 1..37
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..65
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 87..103
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 125..162
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..191
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 213..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..522
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 523..543
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 544..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..654
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 611..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..654
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 233
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 353..358
FT /note="LLGSMF -> YYGISV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:18495509"
FT /id="VSP_037356"
FT VAR_SEQ 357..397
FT /note="MFPLPRIVFAMARDGLLFSFLAKVSKRQAPLLATLTAGVIS -> IFPMPRV
FT IYAMAKDGLLFKCLAQINSKTKTPLVATPSSGAVA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:18495509"
FT /id="VSP_037357"
FT VAR_SEQ 359..654
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:18495509"
FT /id="VSP_037358"
SQ SEQUENCE 654 AA; 71216 MW; AB262A5B8ADC5B27 CRC64;
MLPCGPALTF VRCLVRKKNI KGEGLEDSLC RCLSTLDLIA LGVGSTLGAG VYVLAGEVAK
SDSGPSIVVS FLIAALASVM AGLCYAEFGA RVPKTGSAYL YTYVAVGELW AFITGWNLIL
SYVIGTSSVA RAWSGTFDEL LGKQISHFFK TYFKMNYPGL AEYPDFFAVF LILLLSGLLS
FGVKESAWVN KIFTAINILV LLFVMISGFV KGDVDNWRIS EEYLINLSEI AENFSSYKNV
TSIYGSGGFM PYGFTGTLAG AATCFYAFVG FDCIATTGEE VRNPQKAIPI GIVVSLLVCF
MAYFGVSAAL TLMMPYYLLD EKSPLPVAFA YVGWGPAKYV VAVGSLCALS TSLLGSMFPL
PRIVFAMARD GLLFSFLAKV SKRQAPLLAT LTAGVISAIM AFLFDLKALV DIMSIGTLLA
YSLVATCVLI LRYQPSLTYE QPKYSPEKAT LAASKRESAV SESQINMIQE SHFSLQTLIN
PSSLPTEQTA TTVNCFVGLL AFLVCGLSAL TTYGTHFIAN LEPWSICLLA TLVVSFIVTI
LLIQRQPQNQ QKVAFMVPLL PFLPSLSILV NIYLMVQLSA DTWIRFSIWM ALGFIIYFTY
GIRHSLEGRH SDGDGDSCSE NSGLQEKNPV EEVDEPENAN ESDKFLARER TSEC
