AAT1_SCHPO
ID AAT1_SCHPO Reviewed; 579 AA.
AC Q9P5N2;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Amino acid transporter 1;
GN Name=aat1; ORFNames=SPBC359.03c;
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 [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]
RP SUBCELLULAR LOCATION.
RX PubMed=12136010; DOI=10.1093/genetics/161.3.1053;
RA Matsumoto S., Bandyopadhyay A., Kwiatkowski D.J., Maitra U., Matsumoto T.;
RT "Role of the Tsc1-Tsc2 complex in signaling and transport across the cell
RT membrane in the fission yeast Schizosaccharomyces pombe.";
RL Genetics 161:1053-1063(2002).
RN [3]
RP FUNCTION.
RX PubMed=15797925; DOI=10.1242/jcs.02305;
RA Pardo M., Nurse P.;
RT "The nuclear rim protein Amo1 is required for proper microtubule
RT cytoskeleton organisation in fission yeast.";
RL J. Cell Sci. 118:1705-1714(2005).
RN [4]
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).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=20388730; DOI=10.1242/jcs.059139;
RA Nakase M., Tani M., Morita T., Kitamoto H.K., Kashiwazaki J., Nakamura T.,
RA Hosomi A., Tanaka N., Takegawa K.;
RT "Mannosylinositol phosphorylceramide is a major sphingolipid component and
RT is required for proper localization of plasma-membrane proteins in
RT Schizosaccharomyces pombe.";
RL J. Cell Sci. 123:1578-1587(2010).
CC -!- FUNCTION: Probable amino acid transporter that may play a role in
CC function in microtubule organization since it causes microtubule
CC defects when overexpressed. {ECO:0000269|PubMed:15797925}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane
CC protein. Cell membrane; Multi-pass membrane protein. Note=When the
CC cells were shifted to a nitrogen-free medium, aat1 was transported from
CC the Golgi apparatus to the plasma membrane within 30 minutes.
CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC superfamily. {ECO:0000305}.
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DR EMBL; CU329671; CAB91572.1; -; Genomic_DNA.
DR RefSeq; NP_595053.1; NM_001020959.2.
DR AlphaFoldDB; Q9P5N2; -.
DR SMR; Q9P5N2; -.
DR BioGRID; 277557; 8.
DR STRING; 4896.SPBC359.03c.1; -.
DR iPTMnet; Q9P5N2; -.
DR MaxQB; Q9P5N2; -.
DR PaxDb; Q9P5N2; -.
DR PRIDE; Q9P5N2; -.
DR EnsemblFungi; SPBC359.03c.1; SPBC359.03c.1:pep; SPBC359.03c.
DR GeneID; 2541042; -.
DR KEGG; spo:SPBC359.03c; -.
DR PomBase; SPBC359.03c; aat1.
DR VEuPathDB; FungiDB:SPBC359.03c; -.
DR eggNOG; KOG1286; Eukaryota.
DR HOGENOM; CLU_007946_12_0_1; -.
DR InParanoid; Q9P5N2; -.
DR PhylomeDB; Q9P5N2; -.
DR PRO; PR:Q9P5N2; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0051286; C:cell tip; HDA:PomBase.
DR GO; GO:0000324; C:fungal-type vacuole; IDA:PomBase.
DR GO; GO:0005794; C:Golgi apparatus; IDA:PomBase.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:PomBase.
DR GO; GO:0031520; C:plasma membrane of cell tip; IDA:PomBase.
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; Cell membrane; Golgi apparatus; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..579
FT /note="Amino acid transporter 1"
FT /id="PRO_0000054173"
FT TOPO_DOM 1..83
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 105..108
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..161
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 162..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..186
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 208..215
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 237..265
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 287..303
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 325..347
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 348..368
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 369..401
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 423..431
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 432..452
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 453..471
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 472..492
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 493..513
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 514..534
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 535..579
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 579 AA; 63259 MW; C60DF4BE64397CD3 CRC64;
MSAKDYDFDI ESVLPEEKAP QVSEAKKDYI SQESTVLSGQ VDFVEPEHKG FFQNLIDGFK
PAREADGNGG PALKRGLSTR HMQLMSIGGA IGSGLYVGSG SALADGGPAS VIINYILIGI
MMFFVIYALG EMAVAYPVAG SFNTYATRFI DPAWGFAVSW NYFFNYFVTF PFELTTCAIT
FTFWTDVNCA VWISIFLVVV IGINLFGVRV FGEVEFVLAL IKVVATVGFI ILAIIINCGG
VPTDHRGYIG GSIIKQKPFR HGFKGFCSVY TTAAFSFSGT EIVGLAAAEV GDPRKTLPGA
VKQVFWRVAI FYIVSLILIG LLISPDDPKL MGNGSASVSP FVLAIQEANI KGLPSVFNAV
IIISVISVTN SSTYTAGRTL HGMANLKQAP AFFKYTDRLG RPLIAMIVVL SFGFFAYINE
ANNNGNDISD TVFDWLLAIS GLSNFFTWGS ICLSHIMFRL AFKKQGHSLK ELGFVSPMGI
WGSVIGLGFN ILCLMAEFYV SLFPIGGSPN ANDFFQGYLA ACITLVFFIG YKIYDRSHIP
SLDKLDITTG LKTYEYEETK DSSDTGRFRF FKKIINTVC
