PUT4_YEAST
ID PUT4_YEAST Reviewed; 627 AA.
AC P15380; D6W343;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Proline-specific permease;
GN Name=PUT4; OrderedLocusNames=YOR348C; ORFNames=O6345;
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].
RX PubMed=2687114; DOI=10.1016/0378-1119(89)90413-7;
RA Vandenbol M., Jauniaux J.-C., Grenson M.;
RT "Nucleotide sequence of the Saccharomyces cerevisiae PUT4 proline-permease-
RT encoding gene: similarities between CAN1, HIP1 and PUT4 permeases.";
RL Gene 83:153-159(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 90843 / S288c / FY73;
RX PubMed=8948102;
RX DOI=10.1002/(sici)1097-0061(199611)12:14<1475::aid-yea32>3.0.co;2-v;
RA Purnelle B., Goffeau A.;
RT "Nucleotide sequence analysis of a 40 kb segment on the right arm of yeast
RT chromosome XV reveals 18 open reading frames including a new pyruvate
RT kinase and three homologues to chromosome I genes.";
RL Yeast 12:1475-1481(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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=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).
CC -!- FUNCTION: Required for high-affinity proline transport. May be
CC responsible for proline recognition and probably also for proline
CC translocation across the plasma membrane. Also functions as non-
CC specific GABA permease. Can also transport alanine and glycine.
CC {ECO:0000269|PubMed:10654085}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- INDUCTION: Requires the presence of GABA.
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; M30583; AAA34925.1; -; Genomic_DNA.
DR EMBL; X95720; CAA65035.1; -; Genomic_DNA.
DR EMBL; Z75256; CAA99676.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11109.1; -; Genomic_DNA.
DR PIR; S67257; S67257.
DR RefSeq; NP_014993.1; NM_001183768.1.
DR AlphaFoldDB; P15380; -.
DR SMR; P15380; -.
DR BioGRID; 34733; 82.
DR DIP; DIP-1541N; -.
DR IntAct; P15380; 6.
DR MINT; P15380; -.
DR STRING; 4932.YOR348C; -.
DR TCDB; 2.A.3.10.3; the amino acid-polyamine-organocation (apc) family.
DR iPTMnet; P15380; -.
DR PaxDb; P15380; -.
DR PRIDE; P15380; -.
DR EnsemblFungi; YOR348C_mRNA; YOR348C; YOR348C.
DR GeneID; 854530; -.
DR KEGG; sce:YOR348C; -.
DR SGD; S000005875; PUT4.
DR VEuPathDB; FungiDB:YOR348C; -.
DR eggNOG; KOG1286; Eukaryota.
DR HOGENOM; CLU_007946_12_1_1; -.
DR InParanoid; P15380; -.
DR OMA; MFAYLAV; -.
DR BioCyc; YEAST:G3O-33820-MON; -.
DR PRO; PR:P15380; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P15380; protein.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
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:0015193; F:L-proline transmembrane transporter activity; IMP:SGD.
DR GO; GO:0015175; F:neutral amino acid transmembrane transporter activity; IDA:SGD.
DR GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR GO; GO:0015812; P:gamma-aminobutyric acid transport; IDA:SGD.
DR GO; GO:0015804; P:neutral amino acid transport; IDA:SGD.
DR GO; GO:0015824; P:proline 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 2: Evidence at transcript level;
KW Amino-acid transport; Glycoprotein; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..627
FT /note="Proline-specific permease"
FT /id="PRO_0000054158"
FT TRANSMEM 115..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..370
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 408..427
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 455..473
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 483..503
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 522..542
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 558..578
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 19..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..68
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 38
FT /note="D -> N (in Ref. 1; AAA34925)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 627 AA; 68788 MW; BC76CBA24BB417BD CRC64;
MVNILPFHKN NRHSAGVVTC ADDVSGDGSG GDTKKEEDVV QVTESPSSGS RNNHRSDNEK
DDAIRMEKIS KNQSASSNGT IREDLIMDVD LEKSPSVDGD SEPHKLKQGL QSRHVQLIAL
GGAIGTGLLV GTSSTLHTCG PAGLFISYII ISAVIYPIMC ALGEMVCFLP GDGSDSAGST
ANLVTRYVDP SLGFATGWNY FYCYVILVAA ECTAASGVVE YWTTAVPKGV WITIFLCVVV
ILNFSAVKVY GESEFWFASI KILCIVGLII LSFILFWGGG PNHDRLGFRY WQHPGAFAHH
LTGGSLGNFT DIYTGIIKGA FAFILGPELV CMTSAECADQ RRNIAKASRR FVWRLIFFYV
LGTLAISVIV PYNDPTLVNA LAQGKPGAGS SPFVIGIQNA GIKVLPHIIN GCILTSAWSA
ANAFMFASTR SLLTMAQTGQ APKCLGRINK WGVPYVAVGV SFLCSCLAYL NVSSSTADVF
NWFSNISTIS GFLGWMCGCI AYLRFRKAIF YNGLYDRLPF KTWGQPYTVW FSLIVIGIIT
ITNGYAIFIP KYWRVADFIA AYITLPIFLV LWFGHKLYTR TWRQWWLPVS EIDVTTGLVE
IEEKSREIEE MRLPPTGFKD KFLDALL
