AAP1_SCHPO
ID AAP1_SCHPO Reviewed; 594 AA.
AC Q92367; Q9P7A9; Q9UTT7;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 25-MAY-2022, entry version 149.
DE RecName: Full=Amino-acid permease 1;
GN Name=aap1; ORFNames=SPBC1652.02, SPBC16A3.20c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Okazaki K., Okayama H.;
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 473-557.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC superfamily. {ECO:0000305}.
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DR EMBL; D87954; BAA13506.1; -; Genomic_DNA.
DR EMBL; CU329671; CAB86887.1; -; Genomic_DNA.
DR EMBL; AB028013; BAA87317.1; -; Genomic_DNA.
DR PIR; T43246; T43246.
DR RefSeq; NP_596769.2; NM_001023790.3.
DR AlphaFoldDB; Q92367; -.
DR SMR; Q92367; -.
DR BioGRID; 276698; 1.
DR STRING; 4896.SPBC1652.02.1; -.
DR iPTMnet; Q92367; -.
DR MaxQB; Q92367; -.
DR PaxDb; Q92367; -.
DR EnsemblFungi; SPBC1652.02.1; SPBC1652.02.1:pep; SPBC1652.02.
DR GeneID; 2540163; -.
DR KEGG; spo:SPBC1652.02; -.
DR PomBase; SPBC1652.02; -.
DR VEuPathDB; FungiDB:SPBC1652.02; -.
DR eggNOG; KOG1286; Eukaryota.
DR HOGENOM; CLU_007946_12_0_1; -.
DR InParanoid; Q92367; -.
DR OMA; QGWAPRF; -.
DR PhylomeDB; Q92367; -.
DR PRO; PR:Q92367; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0000324; C:fungal-type vacuole; IDA:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; EXP:PomBase.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; ISM:PomBase.
DR GO; GO:0140135; F:mechanosensitive cation channel activity; EXP:PomBase.
DR GO; GO:0003333; P:amino acid transmembrane transport; ISM:PomBase.
DR InterPro; IPR004841; AA-permease/SLC12A_dom.
DR InterPro; IPR004840; Amoino_acid_permease_CS.
DR Pfam; PF00324; AA_permease; 1.
DR PROSITE; PS00218; AMINO_ACID_PERMEASE_1; 1.
PE 3: Inferred from homology;
KW Amino-acid transport; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..594
FT /note="Amino-acid permease 1"
FT /id="PRO_0000054166"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 323..343
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 390..410
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 416..436
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 468..488
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 498..518
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 550..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..584
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 594 AA; 65278 MW; 0072DD039BEFB901 CRC64;
MTSFTESKKL DEIESPVPEI IVPSTTNGNG TIESYKEKSV GTSFLDFFRS YKLRPDNEFA
EVHNSEDFLK PRHLQMIAIG SCIGTGLFVS TGKSLKNAGP GSLMINFIIL SAMILALILS
LGEMCCFLPN QSSITMYTGR LLNNNIGFAQ SWLYFWIWLT VLPSEISAAC EVVDFWTTQH
LNPAIWVTIF LAYVVLVNAF GARSYGECEF VSSFLKVVIV IIFFFVAIII NCGAAPKGGY
IGAHYWHHPG SFRNGFKGFC SVFISSAYSL SGTENIGTAA GNTSNPQRAI PSAVKKVFYR
MGFFYIITIF LITLVVPYDN PDLGNVSPFI IAIKNGGIHV LPHITNAVIL VSVLSVGNAA
VFAASRNAMA LVKQGWAPRF LGRVDQKGRP VISYLCSLAM ACIAYVNAAP DGSVVFDWLM
SVSGGGAFVI WGLSFIDHIR LRYAMKAQKI PDTVLPYKFP GSVYLSYYGV LINFLALCAL
VYISIFPVTH EKPSAYGFFV SFLGPSVFIA YLLISPIFVK PTFQSLKDVD LTTGRYDLVN
SQMYVAESST SELSEKDLTK PNLQSNDNKN SEDLESNTPP QKKSALQKVA DFLC
