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Arginine permease CAN1 (Canavanine resistance protein 1)

 CAN1_YEAST              Reviewed;         590 AA.
P04817; D3DLI7;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 2.
28-MAR-2018, entry version 165.
RecName: Full=Arginine permease CAN1;
AltName: Full=Canavanine resistance protein 1 {ECO:0000303|PubMed:3327612};
Name=CAN1 {ECO:0000303|PubMed:3327612}; OrderedLocusNames=YEL063C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
PubMed=3327612; DOI=10.1007/BF00418125;
Ahmad M., Bussey H.;
"Yeast arginine permease: nucleotide sequence of the CAN1 gene.";
Curr. Genet. 10:587-592(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3900064;
Hoffmann W.;
"Molecular characterization of the CAN1 locus in Saccharomyces
cerevisiae. A transmembrane protein without N-terminal hydrophobic
signal sequence.";
J. Biol. Chem. 260:11831-11837(1985).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169868;
Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G.,
Hunicke-Smith S., Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H.,
Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P.,
Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T.,
Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
Nature 387:78-81(1997).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
FUNCTION.
PubMed=8436127; DOI=10.1111/j.1432-1033.1993.tb17596.x;
Opekarova M., Caspari T., Tanner W.;
"Unidirectional arginine transport in reconstituted plasma-membrane
vesicles from yeast overexpressing CAN1.";
Eur. J. Biochem. 211:683-688(1993).
[6]
FUNCTION.
PubMed=9231419; DOI=10.1111/j.1574-6968.1997.tb10437.x;
Opekarova M., Kubin J.;
"On the unidirectionality of arginine uptake in the yeast
Saccharomyces cerevisiae.";
FEMS Microbiol. Lett. 152:261-267(1997).
[7]
PHOSPHORYLATION.
PubMed=9544242;
DOI=10.1002/(SICI)1097-0061(199802)14:3<215::AID-YEA214>3.0.CO;2-3;
Opekarova M., Caspari T., Pinson B., Brethes D., Tanner W.;
"Post-translational fate of CAN1 permease of Saccharomyces
cerevisiae.";
Yeast 14:215-224(1998).
[8]
FUNCTION.
PubMed=10654085; DOI=10.1007/s002940050506;
Regenberg B., During-Olsen L., Kielland-Brandt M.C., Holmberg S.;
"Substrate specificity and gene expression of the amino-acid permeases
in Saccharomyces cerevisiae.";
Curr. Genet. 36:317-328(1999).
[9]
FUNCTION, AND MUTAGENESIS OF PRO-113; PRO-148; VAL-149; SER-152;
TYR-173; GLY-308; PRO-313; TYR-356; TRP-451 AND PHE-461.
PubMed=11746604; DOI=10.1002/yea.792;
Regenberg B., Kielland-Brandt M.C.;
"Amino acid residues important for substrate specificity of the amino
acid permeases Can1p and Gnp1p in Saccharomyces cerevisiae.";
Yeast 18:1429-1440(2001).
[10]
SUBCELLULAR LOCATION.
PubMed=12100990; DOI=10.1016/S0005-2736(02)00455-8;
Opekarova M., Robl I., Tanner W.;
"Phosphatidyl ethanolamine is essential for targeting the arginine
transporter Can1p to the plasma membrane of yeast.";
Biochim. Biophys. Acta 1564:9-13(2002).
[11]
SUBCELLULAR LOCATION.
PubMed=14551254; DOI=10.1091/mbc.E03-04-0221;
Malinska K., Malinsky J., Opekarova M., Tanner W.;
"Visualization of protein compartmentation within the plasma membrane
of living yeast cells.";
Mol. Biol. Cell 14:4427-4436(2003).
[12]
SUBCELLULAR LOCATION.
PubMed=21223946; DOI=10.1016/j.bbamem.2011.01.002;
Hosiner D., Sponder G., Graschopf A., Reipert S., Schweyen R.J.,
Schueller C., Aleschko M.;
"Pun1p is a metal ion-inducible, calcineurin/Crz1p-regulated plasma
membrane protein required for cell wall integrity.";
Biochim. Biophys. Acta 1808:1108-1119(2011).
[13]
SUBCELLULAR LOCATION, RECYCLING, AND INTERACTION WITH RRT2.
PubMed=21880895; DOI=10.1091/mbc.E11-05-0440;
Shi Y., Stefan C.J., Rue S.M., Teis D., Emr S.D.;
"Two novel WD40 domain-containing proteins, Ere1 and Ere2, function in
the retromer-mediated endosomal recycling pathway.";
Mol. Biol. Cell 22:4093-4107(2011).
[14]
DISRUPTION PHENOTYPE.
PubMed=28228255; DOI=10.1016/j.celrep.2017.01.077;
Beaupere C., Wasko B.M., Lorusso J., Kennedy B.K., Kaeberlein M.,
Labunskyy V.M.;
"CAN1 arginine permease deficiency extends yeast replicative lifespan
via translational activation of stress response genes.";
Cell Rep. 18:1884-1892(2017).
-!- FUNCTION: High-affinity permease for arginine (PubMed:8436127,
PubMed:9231419, PubMed:10654085, PubMed:11746604).
{ECO:0000269|PubMed:10654085, ECO:0000269|PubMed:11746604,
ECO:0000269|PubMed:8436127, ECO:0000269|PubMed:9231419}.
-!- SUBUNIT: Interacts with RRT2 (PubMed:21880895).
{ECO:0000269|PubMed:21880895}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12100990,
ECO:0000269|PubMed:14551254, ECO:0000269|PubMed:21223946,
ECO:0000269|PubMed:21880895}; Multi-pass membrane protein
{ECO:0000269|PubMed:21880895}. Endosome membrane
{ECO:0000269|PubMed:21880895}; Multi-pass membrane protein
{ECO:0000269|PubMed:21880895}. Note=Recycled via the retromer-
mediated pathway (PubMed:21880895). Requires phosphatidyl
ethanolamine (PE) for localization and exclusively associated with
lipid rafts called MCCs (membrane compartment occupied by CAN1)
(PubMed:12100990, PubMed:14551254, PubMed:21223946).
{ECO:0000269|PubMed:12100990, ECO:0000269|PubMed:14551254,
ECO:0000269|PubMed:21223946, ECO:0000269|PubMed:21880895}.
-!- PTM: Phosphorylated probably at multiple sites (PubMed:9544242).
{ECO:0000269|PubMed:9544242}.
-!- DISRUPTION PHENOTYPE: Abolishes canavanine sensitivity
(PubMed:3327612). Extends replicative lifespan and leads to
distinct changes in transcriptional and translational profiles,
including translational activation of the GCN4 transcription
factor (PubMed:28228255). {ECO:0000269|PubMed:28228255,
ECO:0000269|PubMed:3327612}.
-!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
superfamily. YAT (TC 2.A.3.10) family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X03784; CAA27416.1; -; Genomic_DNA.
EMBL; M11724; AAA34467.1; -; Genomic_DNA.
EMBL; U18795; AAB65024.1; -; Genomic_DNA.
EMBL; BK006939; DAA07591.1; -; Genomic_DNA.
PIR; A23922; QRBYPR.
RefSeq; NP_010851.1; NM_001178878.1.
ProteinModelPortal; P04817; -.
BioGrid; 36666; 72.
DIP; DIP-4062N; -.
IntAct; P04817; 45.
MINT; P04817; -.
STRING; 4932.YEL063C; -.
TCDB; 2.A.3.10.4; the amino acid-polyamine-organocation (apc) family.
iPTMnet; P04817; -.
PaxDb; P04817; -.
PRIDE; P04817; -.
EnsemblFungi; YEL063C; YEL063C; YEL063C.
GeneID; 856646; -.
KEGG; sce:YEL063C; -.
EuPathDB; FungiDB:YEL063C; -.
SGD; S000000789; CAN1.
GeneTree; ENSGT00510000049744; -.
HOGENOM; HOG000261850; -.
InParanoid; P04817; -.
KO; K16261; -.
OMA; INFITRY; -.
OrthoDB; EOG092C164R; -.
BioCyc; YEAST:G3O-30178-MONOMER; -.
PRO; PR:P04817; -.
Proteomes; UP000002311; Chromosome V.
GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0045121; C:membrane raft; IDA:SGD.
GO; GO:0005886; C:plasma membrane; IDA:SGD.
GO; GO:0015181; F:arginine transmembrane transporter activity; IMP:SGD.
GO; GO:0015174; F:basic amino acid transmembrane transporter activity; IDA:SGD.
GO; GO:0015809; P:arginine transport; IGI:SGD.
GO; GO:0015802; P:basic amino acid transport; IDA:SGD.
GO; GO:0055085; P:transmembrane transport; IDA:SGD.
InterPro; IPR004841; AA-permease/SLC12A_dom.
InterPro; IPR002293; AA/rel_permease1.
InterPro; IPR004762; Amino_acid_permease_fungi.
InterPro; IPR004840; Amoino_acid_permease_CS.
Pfam; PF00324; AA_permease; 1.
PIRSF; PIRSF006060; AA_transporter; 1.
TIGRFAMs; TIGR00913; 2A0310; 1.
PROSITE; PS00218; AMINO_ACID_PERMEASE_1; 1.
1: Evidence at protein level;
Amino-acid transport; Cell membrane; Complete proteome; Endosome;
Membrane; Phosphoprotein; Reference proteome; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 590 Arginine permease CAN1.
/FTId=PRO_0000054148.
TRANSMEM 93 113 Helical. {ECO:0000255}.
TRANSMEM 117 137 Helical. {ECO:0000255}.
TRANSMEM 172 192 Helical. {ECO:0000255}.
TRANSMEM 199 219 Helical. {ECO:0000255}.
TRANSMEM 235 255 Helical. {ECO:0000255}.
TRANSMEM 283 303 Helical. {ECO:0000255}.
TRANSMEM 324 344 Helical. {ECO:0000255}.
TRANSMEM 377 397 Helical. {ECO:0000255}.
TRANSMEM 420 440 Helical. {ECO:0000255}.
TRANSMEM 449 469 Helical. {ECO:0000255}.
TRANSMEM 498 518 Helical. {ECO:0000255}.
TRANSMEM 524 544 Helical. {ECO:0000255}.
MOD_RES 54 54 Phosphoserine.
{ECO:0000250|UniProtKB:P32487}.
MOD_RES 66 66 Phosphoserine.
{ECO:0000250|UniProtKB:P32487}.
MUTAGEN 113 113 P->L: In CAN1-343; confers citrulline
transport activity in GAP1-deleted cells.
{ECO:0000269|PubMed:11746604}.
MUTAGEN 148 148 P->L: In CAN1-337; confers citrulline
transport activity in GAP1-deleted cells
and leads to sensitivity to L-glutamic
acid alpha-hydroxamate, alpha-
aminoisobutyrate, 3-chloro-L-alanine, L-
ethionine, L-allylglycine, and D-
histidine, but not sensitivity to L-
aspartic acid alpha-hydroxamate or p-
fluoro-L-phenylalanine.
{ECO:0000269|PubMed:11746604}.
MUTAGEN 149 149 V->F: In CAN1-315; confers citrulline
transport activity in GAP1-deleted cells.
{ECO:0000269|PubMed:11746604}.
MUTAGEN 152 152 S->F: In CAN1-342; confers citrulline
transport activity in GAP1-deleted cells.
{ECO:0000269|PubMed:11746604}.
MUTAGEN 173 173 Y->D: In CAN1-306; confers citrulline
transport activity in GAP1-deleted cells.
{ECO:0000269|PubMed:11746604}.
MUTAGEN 173 173 Y->H: In CAN1-327; confers citrulline
transport activity in GAP1-deleted cells.
{ECO:0000269|PubMed:11746604}.
MUTAGEN 308 308 G->A: In CAN1-341; confers citrulline
transport activity in GAP1-deleted cells.
{ECO:0000269|PubMed:11746604}.
MUTAGEN 313 313 P->S: In CAN1-329; confers citrulline
transport activity in GAP1-deleted cells
and leads to sensitivity to L-glutamic
acid alpha-hydroxamate, alpha-
aminoisobutyrate, 3-chloro-L-alanine, L-
ethionine, L-allylglycine, and D-
histidine, L-aspartic acid alpha-
hydroxamate and p-fluoro-L-phenylalanine.
{ECO:0000269|PubMed:11746604}.
MUTAGEN 354 355 Missing: In CAN1-318; confers citrulline
transport activity in GAP1-deleted cells.
{ECO:0000269|PubMed:11746604}.
MUTAGEN 356 356 Y->H: In CAN1-340; confers citrulline
transport activity in GAP1-deleted cells.
{ECO:0000269|PubMed:11746604}.
MUTAGEN 356 356 Y->N: In CAN1-339; confers citrulline
transport activity in GAP1-deleted cells.
{ECO:0000269|PubMed:11746604}.
MUTAGEN 451 451 W->C: In CAN1-328; confers citrulline
transport activity in GAP1-deleted cells.
{ECO:0000269|PubMed:11746604}.
MUTAGEN 451 451 W->L: In CAN1-316; confers citrulline
transport activity in GAP1-deleted cells.
{ECO:0000269|PubMed:11746604}.
MUTAGEN 451 451 W->S: In CAN1-335; confers citrulline
transport activity in GAP1-deleted cells.
{ECO:0000269|PubMed:11746604}.
MUTAGEN 461 461 F->S: In CAN1-307; confers citrulline
transport activity in GAP1-deleted cells.
{ECO:0000269|PubMed:11746604}.
CONFLICT 534 534 I -> V (in Ref. 1; CAA27416).
{ECO:0000305}.
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


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