CAT1_SCHPO
ID CAT1_SCHPO Reviewed; 587 AA.
AC Q9URZ4; Q9URW8;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 3.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Cationic amino acid transporter 1;
GN Name=cat1; ORFNames=SPAC869.11, SPAC922.08c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; SER-30 AND SER-37, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=18219492; DOI=10.1007/s00438-008-0320-y;
RA Aspuria P.J., Tamanoi F.;
RT "The Tsc/Rheb signaling pathway controls basic amino acid uptake via the
RT Cat1 permease in fission yeast.";
RL Mol. Genet. Genomics 279:441-450(2008).
CC -!- FUNCTION: Major permease specifically involved in arginine and lysine
CC uptake. {ECO:0000269|PubMed:18219492}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18219492};
CC Multi-pass membrane protein {ECO:0000269|PubMed:18219492}. Cell tip
CC {ECO:0000269|PubMed:18219492}. Note=enriched toward the growing ends of
CC the cells.
CC -!- DISRUPTION PHENOTYPE: Leads to a dramatic decrease in the uptake of
CC arginine or lysine and resistance to canavanine and thialysine.
CC {ECO:0000269|PubMed:18219492}.
CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC superfamily. {ECO:0000305}.
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DR EMBL; CU329670; CAB63555.3; -; Genomic_DNA.
DR PIR; T39122; T39122.
DR RefSeq; NP_595008.3; NM_001020439.2.
DR AlphaFoldDB; Q9URZ4; -.
DR SMR; Q9URZ4; -.
DR BioGRID; 279988; 36.
DR STRING; 4896.SPAC869.11.1; -.
DR TCDB; 2.A.3.10.21; the amino acid-polyamine-organocation (apc) family.
DR iPTMnet; Q9URZ4; -.
DR MaxQB; Q9URZ4; -.
DR PaxDb; Q9URZ4; -.
DR PRIDE; Q9URZ4; -.
DR EnsemblFungi; SPAC869.11.1; SPAC869.11.1:pep; SPAC869.11.
DR GeneID; 2543573; -.
DR KEGG; spo:SPAC869.11; -.
DR PomBase; SPAC869.11; cat1.
DR VEuPathDB; FungiDB:SPAC869.11; -.
DR eggNOG; KOG1286; Eukaryota.
DR HOGENOM; CLU_007946_12_0_1; -.
DR InParanoid; Q9URZ4; -.
DR OMA; AGGFNTY; -.
DR PRO; PR:Q9URZ4; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0032153; C:cell division site; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0032178; C:medial membrane band; IDA:PomBase.
DR GO; GO:0005886; C:plasma membrane; IDA:PomBase.
DR GO; GO:0031520; C:plasma membrane of cell tip; IDA:PomBase.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0061459; F:L-arginine transmembrane transporter activity; IMP:PomBase.
DR GO; GO:0015189; F:L-lysine transmembrane transporter activity; IMP:PomBase.
DR GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR GO; GO:0097638; P:L-arginine import across plasma membrane; IMP:PomBase.
DR GO; GO:0097639; P:L-lysine import across plasma membrane; IMP:PomBase.
DR InterPro; IPR004841; AA-permease/SLC12A_dom.
DR InterPro; IPR004840; Amoino_acid_permease_CS.
DR Pfam; PF00324; AA_permease; 1.
DR PROSITE; PS00218; AMINO_ACID_PERMEASE_1; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell membrane; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..587
FT /note="Cationic amino acid transporter 1"
FT /id="PRO_0000054179"
FT TOPO_DOM 1..90
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 112..115
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 137..158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..193
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 215..222
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 244..272
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 273..293
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 294..310
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 311..331
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 332..354
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 376..405
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 427..444
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 445..465
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 466..491
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 492..512
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 513..520
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 521..541
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 542..580
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 587 AA; 64479 MW; FBB74D5ADAE52B27 CRC64;
MSHSDFNMEP EYVSFSDKDT KSILNESKSS LKDVKPSLEE KSYITPGLVD DVEPKGKNFV
VRFFDDFKPA KATGEDGTAL KRSLKSRHMQ MISIGGAIGT GLYVGSGSSL ADGGPASVII
NYSLIGIMMF FIVYALGEMA VAYPVAGGFN TYATRFIDPA WGFAVSWNYF INYFVTFPLE
LTTCAITFRY WTDINSAAWI SIFLVVIIIV NLFGVRAYGE VEFILSTVKV VATFGFIILA
IIINCGGVPT DHRGYIGGSI IKHKPFRHGF KGFCSVFTTA AFSFSGTEVI GLAAAEVDNP
QKALPHAVKQ VFWRIAIFYV VSLILIGLLI SPDDPNLMGN GSTSVSPFVL AIKEANIKGL
PSVFNAVIII SVVSVTNSST YTAGRTLHGM ANLKQAPSFF KYTDRLGRPL LAMIVVLLFG
FFAYINEADK NGNDVSDTVF NWLLALSGLS NFFTWGSICL CHIIFRLAFK KQGHSLKELG
FVSPMGIWGS CIGLFFNILC LMAQFYVSLF PIGGKPNAND FFQGYLAAPV TLAFFIGYKI
YDRSHIPSLD KLDITTGLKT YENLDEEEDE PTTASKRIFK KISSVFC
