YHE1_SCHPO
ID YHE1_SCHPO Reviewed; 585 AA.
AC Q9HDV2;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Uncharacterized amino-acid permease PB2B2.01;
GN ORFNames=SPBPB2B2.01;
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] {ECO:0000312|EMBL:CAC21403.1}
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 [2] {ECO:0000305}
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:16823372}. Membrane {ECO:0000255}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC superfamily. {ECO:0000255}.
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DR EMBL; CU329671; CAC21403.1; -; Genomic_DNA.
DR RefSeq; NP_596849.1; NM_001023872.2.
DR AlphaFoldDB; Q9HDV2; -.
DR SMR; Q9HDV2; -.
DR BioGRID; 277912; 1.
DR STRING; 4896.SPBPB2B2.01.1; -.
DR MaxQB; Q9HDV2; -.
DR PaxDb; Q9HDV2; -.
DR EnsemblFungi; SPBPB2B2.01.1; SPBPB2B2.01.1:pep; SPBPB2B2.01.
DR GeneID; 2541403; -.
DR KEGG; spo:SPBPB2B2.01; -.
DR PomBase; SPBPB2B2.01; -.
DR VEuPathDB; FungiDB:SPBPB2B2.01; -.
DR eggNOG; KOG1286; Eukaryota.
DR HOGENOM; CLU_007946_12_0_1; -.
DR InParanoid; Q9HDV2; -.
DR OMA; FRENAFR; -.
DR PhylomeDB; Q9HDV2; -.
DR PRO; PR:Q9HDV2; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; ISM: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; Endoplasmic reticulum; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..585
FT /note="Uncharacterized amino-acid permease PB2B2.01"
FT /id="PRO_0000310827"
FT TOPO_DOM 1..89
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P19145, ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111..121
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P19145, ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..159
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P19145, ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..193
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P19145, ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 215..221
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P19145, ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 243..271
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P19145, ECO:0000255"
FT TRANSMEM 272..292
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 293..313
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P19145, ECO:0000255"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 335..361
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P19145, ECO:0000255"
FT TRANSMEM 362..382
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 383..407
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P19145, ECO:0000255"
FT TRANSMEM 408..428
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 429..436
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P19145, ECO:0000255"
FT TRANSMEM 437..457
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 458..486
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P19145, ECO:0000255"
FT TRANSMEM 487..507
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 508..511
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P19145, ECO:0000255"
FT TRANSMEM 512..532
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 533..585
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P19145, ECO:0000255"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 585 AA; 65129 MW; DF38EC7C463DAF6F CRC64;
MNAYVRDSES VYSESYPPEN FISNEPEKSK DKDNFNGEEV ISYVGEVETV PAKEENVFRR
FINGFKIEKN QQDSAGQGLK RRLKSRHIQM IGIGGAIGTG VWVGSSKSLY RGGAASVLID
YCIVGTMVFC TVYALGELAV AFPTRGSFVT HATRFIDESW GFALSWNYVF SFIVTIPLEL
TTGTMMIKYW TNLNSGIWVT VFIVFLFFIN IFGVKGYGEM EFIMSTIKVV AMCGFIILGI
IIDCGGVPTD HRGYMGTHIF RENAFRHKFK GFCAVFTSAA FSFSGTEYVG VAAAETENPA
KAFPVAVRQT LFRIAIFYIL SLFIVSLLIS GADPRLTSYH GVDASPFVLA IKDANIKALP
SILNAIILIS VISSANAQLY AGSRAIHSLG CNGFAPKCFT LVDREGRPLV ALLILFLFMF
LGYLVETGQY DTVFDWMLSI SGLGTLFCWG SICLAHIRYR AAMKHQNRSL KEVGFVSPFN
VYASYYAFIL VCLVLAAEFY VSIFPVGGKP DASAFFENYL SAPVILVFFI CHKLYYKTKR
ITLSNMDLET DFAYKTPVEE EEEEEKSAGS LSIKQRMKKL SDMMC
