ALP1_YEAST
ID ALP1_YEAST Reviewed; 573 AA.
AC P38971; D6W0S4;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Basic amino-acid permease;
GN Name=ALP1; OrderedLocusNames=YNL270C; ORFNames=N0660;
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].
RC STRAIN=ATCC 28383 / FL100 / VTT C-80102;
RX PubMed=7941748; DOI=10.1002/yea.320100509;
RA Sychrova H., Chevallier M.R.;
RT "APL1, a yeast gene encoding a putative permease for basic amino acids.";
RL Yeast 10:653-657(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8740425;
RX DOI=10.1002/(sici)1097-0061(199604)12:5<505::aid-yea932>3.0.co;2-f;
RA Sen-Gupta M., Lyck R., Fleig U., Niedenthal R.K., Hegemann J.H.;
RT "The sequence of a 24,152 bp segment from the left arm of chromosome XIV
RT from Saccharomyces cerevisiae between the BNI1 and the POL2 genes.";
RL Yeast 12:505-514(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(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).
RN [6]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
CC -!- FUNCTION: High-affinity permease for basic amino acids.
CC {ECO:0000269|PubMed:10654085}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
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; X74069; CAA52199.1; -; Genomic_DNA.
DR EMBL; X92494; CAA63228.1; -; Genomic_DNA.
DR EMBL; Z71546; CAA96177.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10290.1; -; Genomic_DNA.
DR PIR; S60912; S60912.
DR RefSeq; NP_014129.1; NM_001183108.1.
DR AlphaFoldDB; P38971; -.
DR SMR; P38971; -.
DR BioGRID; 35570; 67.
DR IntAct; P38971; 1.
DR STRING; 4932.YNL270C; -.
DR TCDB; 2.A.3.10.11; the amino acid-polyamine-organocation (apc) family.
DR PaxDb; P38971; -.
DR PRIDE; P38971; -.
DR TopDownProteomics; P38971; -.
DR EnsemblFungi; YNL270C_mRNA; YNL270C; YNL270C.
DR GeneID; 855451; -.
DR KEGG; sce:YNL270C; -.
DR SGD; S000005214; ALP1.
DR VEuPathDB; FungiDB:YNL270C; -.
DR eggNOG; KOG1286; Eukaryota.
DR GeneTree; ENSGT00940000176760; -.
DR HOGENOM; CLU_007946_12_1_1; -.
DR InParanoid; P38971; -.
DR OMA; RTVIFFI; -.
DR BioCyc; YEAST:G3O-33264-MON; -.
DR PRO; PR:P38971; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P38971; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
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:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR GO; GO:0015802; P:basic amino acid 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; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..573
FT /note="Basic amino-acid permease"
FT /id="PRO_0000054145"
FT TOPO_DOM 1..73
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 94..95
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..153
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..179
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 201..209
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..265
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 287..306
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 328..359
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 360..380
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 381..403
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 404..424
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 425..431
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 432..452
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 453..477
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 478..498
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 499..510
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 511..531
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 532..573
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 40..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 51
FT /note="D -> DD (in Ref. 1; CAA52199)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="V -> A (in Ref. 1; CAA52199)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="D -> N (in Ref. 1; CAA52199)"
FT /evidence="ECO:0000305"
FT CONFLICT 517
FT /note="I -> V (in Ref. 1; CAA52199)"
FT /evidence="ECO:0000305"
FT CONFLICT 548
FT /note="R -> H (in Ref. 1; CAA52199)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 573 AA; 64014 MW; 359DFE1466C348A1 CRC64;
MDETVNIQMS KEGQYEINSS SIIKEEEFVD EQYSGENVTK AITTERKVED DAAKETESSP
QERREVKRKL KQRHIGMIAL GGTIGTGLII GIGPPLAHAG PVGALISYLF MGTVIYSVTQ
SLGEMVTFIP VTSSFSVFAQ RFLSPALGAT NGYMYWLSWC FTFALELSVL GKVIQYWTEA
VPLAAWIVIF WCLLTSMNMF PVKYYGEFEF CIASIKVIAL LGFIIFSFCV VCGAGQSDGP
IGFRYWRNPG AWGPGIISSD KNEGRFLGWV SSLINAAFTY QGTELVGITA GEAANPRKAL
PRAIKKVVVR ILVFYILSLF FIGLLVPYND PKLDSDGIFV SSSPFMISIE NSGTKVLPDI
FNAVVLITIL SAGNSNVYIG SRVLYSLSKN SLAPRFLSNV TRGGVPYFSV LSTSVFGFLA
FLEVSAGSGK AFNWLLNITG VAGFFAWLLI SFSHIRFMQA IRKRGISRDD LPYKAQMMPF
LAYYASFFIA LIVLIQGFTA FAPTFQPIDF VAAYISIFLF LAIWLSFQVW FKCRLLWKLQ
DIDIDSDRRQ IEELVWIEPE CKTRWQRVWD VLS
