CAN1_YEAST
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 03-AUG-2022, entry version 186.
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;
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).
CC -!- FUNCTION: High-affinity permease for arginine (PubMed:8436127,
CC PubMed:9231419, PubMed:10654085, PubMed:11746604).
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}; Multi-pass membrane protein
CC {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: Abolishes canavanine sensitivity
CC (PubMed:3327612). 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}.
CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC superfamily. YAT (TC 2.A.3.10) family. {ECO:0000305}.
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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; 74.
DR DIP; DIP-4062N; -.
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; P04817; -.
DR PRIDE; P04817; -.
DR EnsemblFungi; YEL063C_mRNA; YEL063C; YEL063C.
DR GeneID; 856646; -.
DR KEGG; sce:YEL063C; -.
DR SGD; S000000789; CAN1.
DR VEuPathDB; FungiDB:YEL063C; -.
DR eggNOG; KOG1286; Eukaryota.
DR GeneTree; ENSGT00940000176760; -.
DR HOGENOM; CLU_007946_12_1_1; -.
DR InParanoid; P04817; -.
DR OMA; LMIPGIQ; -.
DR BioCyc; YEAST:G3O-30178-MON; -.
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; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of 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 InterPro; IPR004841; AA-permease/SLC12A_dom.
DR InterPro; IPR004762; Amino_acid_permease_fungi.
DR InterPro; IPR004840; Amoino_acid_permease_CS.
DR Pfam; PF00324; AA_permease; 1.
DR TIGRFAMs; TIGR00913; 2A0310; 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 D-
FT histidine, but not sensitivity to L-aspartic acid alpha-
FT 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 D-
FT histidine, L-aspartic acid alpha-hydroxamate and p-fluoro-
FT 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
