ID CAN1_YEAST Reviewed; 590 AA. AC P04817; D3DLI7; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 2. DT 02-SEP-2026, entry version 200. DE RecName: Full=Arginine permease CAN1; DE AltName: Full=Canavanine resistance protein 1 {ECO:0000303|PubMed:3327612}; GN Name=CAN1 {ECO:0000303|PubMed:3327612}; OrderedLocusNames=YEL063C; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE. RX PubMed=3327612; DOI=10.1007/bf00418125; RA Ahmad M., Bussey H.; RT "Yeast arginine permease: nucleotide sequence of the CAN1 gene."; RL Curr. Genet. 10:587-592(1986). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3900064; DOI=10.1016/s0021-9258(17)39106-8; RA Hoffmann W.; RT "Molecular characterization of the CAN1 locus in Saccharomyces cerevisiae. RT A transmembrane protein without N-terminal hydrophobic signal sequence."; RL J. Biol. Chem. 260:11831-11837(1985). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169868; DOI=10.1038/387s078; RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., RA Botstein D., Davis R.W.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V."; RL Nature 387:78-81(1997). RN [4] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [5] RP FUNCTION. RX PubMed=8436127; DOI=10.1111/j.1432-1033.1993.tb17596.x; RA Opekarova M., Caspari T., Tanner W.; RT "Unidirectional arginine transport in reconstituted plasma-membrane RT vesicles from yeast overexpressing CAN1."; RL Eur. J. Biochem. 211:683-688(1993). RN [6] RP FUNCTION. RX PubMed=9231419; DOI=10.1111/j.1574-6968.1997.tb10437.x; RA Opekarova M., Kubin J.; RT "On the unidirectionality of arginine uptake in the yeast Saccharomyces RT cerevisiae."; RL FEMS Microbiol. Lett. 152:261-267(1997). RN [7] RP PHOSPHORYLATION. RX PubMed=9544242; RX DOI=10.1002/(sici)1097-0061(199802)14:3<215::aid-yea214>3.0.co;2-3; RA Opekarova M., Caspari T., Pinson B., Brethes D., Tanner W.; RT "Post-translational fate of CAN1 permease of Saccharomyces cerevisiae."; RL Yeast 14:215-224(1998). RN [8] RP FUNCTION. RX PubMed=10654085; DOI=10.1007/s002940050506; RA Regenberg B., During-Olsen L., Kielland-Brandt M.C., Holmberg S.; RT "Substrate specificity and gene expression of the amino-acid permeases in RT Saccharomyces cerevisiae."; RL Curr. Genet. 36:317-328(1999). RN [9] RP FUNCTION, AND MUTAGENESIS OF PRO-113; PRO-148; VAL-149; SER-152; TYR-173; RP GLY-308; PRO-313; TYR-356; TRP-451 AND PHE-461. RX PubMed=11746604; DOI=10.1002/yea.792; RA Regenberg B., Kielland-Brandt M.C.; RT "Amino acid residues important for substrate specificity of the amino acid RT permeases Can1p and Gnp1p in Saccharomyces cerevisiae."; RL Yeast 18:1429-1440(2001). RN [10] RP SUBCELLULAR LOCATION. RX PubMed=12100990; DOI=10.1016/s0005-2736(02)00455-8; RA Opekarova M., Robl I., Tanner W.; RT "Phosphatidyl ethanolamine is essential for targeting the arginine RT transporter Can1p to the plasma membrane of yeast."; RL Biochim. Biophys. Acta 1564:9-13(2002). RN [11] RP SUBCELLULAR LOCATION. RX PubMed=14551254; DOI=10.1091/mbc.e03-04-0221; RA Malinska K., Malinsky J., Opekarova M., Tanner W.; RT "Visualization of protein compartmentation within the plasma membrane of RT living yeast cells."; RL Mol. Biol. Cell 14:4427-4436(2003). RN [12] RP SUBCELLULAR LOCATION. RX PubMed=21223946; DOI=10.1016/j.bbamem.2011.01.002; RA Hosiner D., Sponder G., Graschopf A., Reipert S., Schweyen R.J., RA Schueller C., Aleschko M.; RT "Pun1p is a metal ion-inducible, calcineurin/Crz1p-regulated plasma RT membrane protein required for cell wall integrity."; RL Biochim. Biophys. Acta 1808:1108-1119(2011). RN [13] RP SUBCELLULAR LOCATION, RECYCLING, AND INTERACTION WITH RRT2. RX PubMed=21880895; DOI=10.1091/mbc.e11-05-0440; RA Shi Y., Stefan C.J., Rue S.M., Teis D., Emr S.D.; RT "Two novel WD40 domain-containing proteins, Ere1 and Ere2, function in the RT retromer-mediated endosomal recycling pathway."; RL Mol. Biol. Cell 22:4093-4107(2011). RN [14] RP DISRUPTION PHENOTYPE. RX PubMed=28228255; DOI=10.1016/j.celrep.2017.01.077; RA Beaupere C., Wasko B.M., Lorusso J., Kennedy B.K., Kaeberlein M., RA Labunskyy V.M.; RT "CAN1 arginine permease deficiency extends yeast replicative lifespan via RT translational activation of stress response genes."; RL Cell Rep. 18:1884-1892(2017). RN [15] RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE. RX PubMed=37005249; DOI=10.2323/jgam.2023.03.003; RA Nishimura A., Tanahashi R., Nakagami K., Morioka Y., Takagi H.; RT "Identification of an arginine transporter in Candida glabrata."; RL J. Gen. Appl. Microbiol. 68:2023.03.003-2023.03.003(2023). CC -!- FUNCTION: High-affinity permease for arginine. CC {ECO:0000269|PubMed:10654085, ECO:0000269|PubMed:11746604, CC ECO:0000269|PubMed:8436127, ECO:0000269|PubMed:9231419}. CC -!- SUBUNIT: Interacts with RRT2 (PubMed:21880895). CC {ECO:0000269|PubMed:21880895}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12100990, CC ECO:0000269|PubMed:14551254, ECO:0000269|PubMed:21223946, CC ECO:0000269|PubMed:21880895, ECO:0000269|PubMed:37005249}; Multi-pass CC membrane protein {ECO:0000269|PubMed:21880895}. Endosome membrane CC {ECO:0000269|PubMed:21880895}; Multi-pass membrane protein CC {ECO:0000269|PubMed:21880895}. Note=Recycled via the retromer-mediated CC pathway (PubMed:21880895). Requires phosphatidyl ethanolamine (PE) for CC localization and exclusively associated with lipid rafts called MCCs CC (membrane compartment occupied by CAN1) (PubMed:12100990, CC PubMed:14551254, PubMed:21223946). {ECO:0000269|PubMed:12100990, CC ECO:0000269|PubMed:14551254, ECO:0000269|PubMed:21223946, CC ECO:0000269|PubMed:21880895}. CC -!- PTM: Phosphorylated probably at multiple sites (PubMed:9544242). CC {ECO:0000269|PubMed:9544242}. CC -!- DISRUPTION PHENOTYPE: Resistance to canavanine (PubMed:3327612, CC PubMed:37005249). Extends replicative lifespan and leads to distinct CC changes in transcriptional and translational profiles, including CC translational activation of the GCN4 transcription factor CC (PubMed:28228255). {ECO:0000269|PubMed:28228255, CC ECO:0000269|PubMed:3327612, ECO:0000269|PubMed:37005249}. CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC) CC superfamily. YAT (TC 2.A.3.10) family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X03784; CAA27416.1; -; Genomic_DNA. DR EMBL; M11724; AAA34467.1; -; Genomic_DNA. DR EMBL; U18795; AAB65024.1; -; Genomic_DNA. DR EMBL; BK006939; DAA07591.1; -; Genomic_DNA. DR PIR; A23922; QRBYPR. DR RefSeq; NP_010851.1; NM_001178878.1. DR AlphaFoldDB; P04817; -. DR SMR; P04817; -. DR BioGRID; 36666; 80. DR DIP; DIP-4062N; -. DR FunCoup; P04817; 196. DR IntAct; P04817; 45. DR MINT; P04817; -. DR STRING; 4932.YEL063C; -. DR TCDB; 2.A.3.10.4; the amino acid-polyamine-organocation (apc) family. DR iPTMnet; P04817; -. DR PaxDb; 4932-YEL063C; -. DR PeptideAtlas; P04817; -. DR EnsemblFungi; YEL063C_mRNA; YEL063C; YEL063C. DR GeneID; 856646; -. DR KEGG; sce:YEL063C; -. DR AGR; SGD:S000000789; -. DR SGD; S000000789; CAN1. DR VEuPathDB; FungiDB:YEL063C; -. DR eggNOG; KOG1286; Eukaryota. DR HOGENOM; CLU_007946_12_1_1; -. DR InParanoid; P04817; -. DR OMA; MFAYLAV; -. DR OrthoDB; 3900342at2759; -. DR BioCyc; YEAST:G3O-30178-MONOMER; -. DR BioGRID-ORCS; 856646; 5 hits in 10 CRISPR screens. DR PRO; PR:P04817; -. DR Proteomes; UP000002311; Chromosome V. DR RNAct; P04817; protein. DR GO; GO:0032126; C:eisosome; IDA:SGD. DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD. DR GO; GO:0010008; C:endosome membrane; EXP:UniProtKB. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0005739; C:mitochondrion; HDA:SGD. DR GO; GO:0005886; C:plasma membrane; IDA:SGD. DR GO; GO:0015171; F:amino acid transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0015174; F:basic amino acid transmembrane transporter activity; IDA:SGD. DR GO; GO:0061459; F:L-arginine transmembrane transporter activity; IMP:SGD. DR GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central. DR GO; GO:0015802; P:basic amino acid transport; IDA:SGD. DR GO; GO:1903826; P:L-arginine transmembrane transport; IGI:SGD. DR GO; GO:0055085; P:transmembrane transport; IDA:SGD. DR FunFam; 1.20.1740.10:FF:000006; General amino acid permease; 1. DR Gene3D; 1.20.1740.10; Amino acid/polyamine transporter I; 1. DR InterPro; IPR004841; AA-permease/SLC12A_dom. DR InterPro; IPR004840; Amino_acid_permease_CS. DR InterPro; IPR004762; Amino_acid_permease_fungi. DR InterPro; IPR050524; APC_YAT. DR NCBIfam; TIGR00913; 2A0310; 1. DR PANTHER; PTHR43341; AMINO ACID PERMEASE; 1. DR PANTHER; PTHR43341:SF4; ARGININE PERMEASE CAN1-RELATED; 1. 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; Endosome; Membrane; Phosphoprotein; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..590 FT /note="Arginine permease CAN1" FT /id="PRO_0000054148" FT TRANSMEM 93..113 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 117..137 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 172..192 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 199..219 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 235..255 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 283..303 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 324..344 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 377..397 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 420..440 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 449..469 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 498..518 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 524..544 FT /note="Helical" FT /evidence="ECO:0000255" FT MOD_RES 54 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P32487" FT MOD_RES 66 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P32487" FT MUTAGEN 113 FT /note="P->L: In CAN1-343; confers citrulline transport FT activity in GAP1-deleted cells." FT /evidence="ECO:0000269|PubMed:11746604" FT MUTAGEN 148 FT /note="P->L: In CAN1-337; confers citrulline transport FT activity in GAP1-deleted cells and leads to sensitivity to FT L-glutamic acid alpha-hydroxamate, alpha-aminoisobutyrate, FT 3-chloro-L-alanine, L-ethionine, L-allylglycine, and FT D-histidine, but not sensitivity to L-aspartic acid FT alpha-hydroxamate or p-fluoro-L-phenylalanine." FT /evidence="ECO:0000269|PubMed:11746604" FT MUTAGEN 149 FT /note="V->F: In CAN1-315; confers citrulline transport FT activity in GAP1-deleted cells." FT /evidence="ECO:0000269|PubMed:11746604" FT MUTAGEN 152 FT /note="S->F: In CAN1-342; confers citrulline transport FT activity in GAP1-deleted cells." FT /evidence="ECO:0000269|PubMed:11746604" FT MUTAGEN 173 FT /note="Y->D: In CAN1-306; confers citrulline transport FT activity in GAP1-deleted cells." FT /evidence="ECO:0000269|PubMed:11746604" FT MUTAGEN 173 FT /note="Y->H: In CAN1-327; confers citrulline transport FT activity in GAP1-deleted cells." FT /evidence="ECO:0000269|PubMed:11746604" FT MUTAGEN 308 FT /note="G->A: In CAN1-341; confers citrulline transport FT activity in GAP1-deleted cells." FT /evidence="ECO:0000269|PubMed:11746604" FT MUTAGEN 313 FT /note="P->S: In CAN1-329; confers citrulline transport FT activity in GAP1-deleted cells and leads to sensitivity to FT L-glutamic acid alpha-hydroxamate, alpha-aminoisobutyrate, FT 3-chloro-L-alanine, L-ethionine, L-allylglycine, and FT D-histidine, L-aspartic acid alpha-hydroxamate and FT p-fluoro-L-phenylalanine." FT /evidence="ECO:0000269|PubMed:11746604" FT MUTAGEN 354..355 FT /note="Missing: In CAN1-318; confers citrulline transport FT activity in GAP1-deleted cells." FT /evidence="ECO:0000269|PubMed:11746604" FT MUTAGEN 356 FT /note="Y->H: In CAN1-340; confers citrulline transport FT activity in GAP1-deleted cells." FT /evidence="ECO:0000269|PubMed:11746604" FT MUTAGEN 356 FT /note="Y->N: In CAN1-339; confers citrulline transport FT activity in GAP1-deleted cells." FT /evidence="ECO:0000269|PubMed:11746604" FT MUTAGEN 451 FT /note="W->C: In CAN1-328; confers citrulline transport FT activity in GAP1-deleted cells." FT /evidence="ECO:0000269|PubMed:11746604" FT MUTAGEN 451 FT /note="W->L: In CAN1-316; confers citrulline transport FT activity in GAP1-deleted cells." FT /evidence="ECO:0000269|PubMed:11746604" FT MUTAGEN 451 FT /note="W->S: In CAN1-335; confers citrulline transport FT activity in GAP1-deleted cells." FT /evidence="ECO:0000269|PubMed:11746604" FT MUTAGEN 461 FT /note="F->S: In CAN1-307; confers citrulline transport FT activity in GAP1-deleted cells." FT /evidence="ECO:0000269|PubMed:11746604" FT CONFLICT 534 FT /note="I -> V (in Ref. 1; CAA27416)" FT /evidence="ECO:0000305" SQ SEQUENCE 590 AA; 65785 MW; 4E5A21C77145330D CRC64; MTNSKEDADI EEKHMYNEPV TTLFHDVEAS QTHHRRGSIP LKDEKSKELY PLRSFPTRVN GEDTFSMEDG IGDEDEGEVQ NAEVKRELKQ RHIGMIALGG TIGTGLFIGL STPLTNAGPV GALISYLFMG SLAYSVTQSL GEMATFIPVT SSFTVFSQRF LSPAFGAANG YMYWFSWAIT FALELSVVGQ VIQFWTYKVP LAAWISIFWV IITIMNLFPV KYYGEFEFWV ASIKVLAIIG FLIYCFCMVC GAGVTGPVGF RYWRNPGAWG PGIISKDKNE GRFLGWVSSL INAAFTFQGT ELVGITAGEA ANPRKSVPRA IKKVVFRILT FYIGSLLFIG LLVPYNDPKL TQSTSYVSTS PFIIAIENSG TKVLPHIFNA VILTTIISAA NSNIYVGSRI LFGLSKNKLA PKFLSRTTKG GVPYIAVFVT AAFGALAYME TSTGGDKVFE WLLNITGVAG FFAWLFISIS HIRFMQALKY RGISRDELPF KAKLMPGLAY YAATFMTIII IIQGFTAFAP KFNGVSFAAA YISIFLFLAV WILFQCIFRC RFIWKIGDVD IDSDRRDIEA IVWEDHEPKT FWDKFWNVVA //