THI9_SCHPO
ID THI9_SCHPO Reviewed; 591 AA.
AC Q9UT18;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Thiamine transporter thi9;
GN Name=thi9; ORFNames=SPAC9.10;
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 [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 [3]
RP FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF GLU-81, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18201975; DOI=10.1074/jbc.m708275200;
RA Vogl C., Klein C.M., Batke A.F., Schweingruber M.E., Stolz J.;
RT "Characterization of Thi9, a novel thiamine (Vitamin B1) transporter from
RT Schizosaccharomyces pombe.";
RL J. Biol. Chem. 283:7379-7389(2008).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-585, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Thiamine transporter involved in the cellular uptake of
CC thiamine. Pyrithiamine, oxythiamine, amprolium, and the thiazole part
CC of thiamine have been shown to be also substrates of thi9.
CC {ECO:0000269|PubMed:18201975}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.4 uM for thiamine {ECO:0000269|PubMed:18201975};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein. Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC superfamily. {ECO:0000305}.
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DR EMBL; CU329670; CAB57428.1; -; Genomic_DNA.
DR PIR; T39195; T39195.
DR RefSeq; NP_593353.1; NM_001018785.2.
DR AlphaFoldDB; Q9UT18; -.
DR SMR; Q9UT18; -.
DR BioGRID; 279993; 13.
DR STRING; 4896.SPAC9.10.1; -.
DR TCDB; 2.A.3.4.6; the amino acid-polyamine-organocation (apc) family.
DR iPTMnet; Q9UT18; -.
DR MaxQB; Q9UT18; -.
DR PaxDb; Q9UT18; -.
DR PRIDE; Q9UT18; -.
DR EnsemblFungi; SPAC9.10.1; SPAC9.10.1:pep; SPAC9.10.
DR GeneID; 2543578; -.
DR KEGG; spo:SPAC9.10; -.
DR PomBase; SPAC9.10; thi9.
DR VEuPathDB; FungiDB:SPAC9.10; -.
DR eggNOG; KOG1289; Eukaryota.
DR HOGENOM; CLU_004495_7_1_1; -.
DR InParanoid; Q9UT18; -.
DR OMA; AFMSTYN; -.
DR PhylomeDB; Q9UT18; -.
DR PRO; PR:Q9UT18; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0032178; C:medial membrane band; IDA:PomBase.
DR GO; GO:0005886; C:plasma membrane; IDA:PomBase.
DR GO; GO:0031520; C:plasma membrane of cell tip; IDA:PomBase.
DR GO; GO:0034216; F:high-affinity thiamine:proton symporter activity; IDA:PomBase.
DR GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR GO; GO:0140125; P:thiamine import across plasma membrane; IMP:PomBase.
DR InterPro; IPR002293; AA/rel_permease1.
DR Pfam; PF13520; AA_permease_2; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell membrane; Endoplasmic reticulum; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..591
FT /note="Thiamine transporter thi9"
FT /id="PRO_0000054169"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 397..417
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 450..470
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 545..565
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 585
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MUTAGEN 81
FT /note="E->K: Accumulates in the endoplasmic reticulum and
FT punctuate cytoplasmic structures."
FT /evidence="ECO:0000269|PubMed:18201975"
SQ SEQUENCE 591 AA; 65070 MW; FFCCD707AC7849D4 CRC64;
MPSSQISHQD PELGQTSSGS SSIKEKAEPQ LYAGPIDPAR RPDVFQEGFE DVSVTDDDND
NELLRKMGYQ PVLHRSFEFF ESFAASFASL DVVSGVRLTF SWGISFGGPA AYWSAMLVTG
FCSIVTAACL AEICSALPAA GSIYLWAAES AGPRFGRFVS FLVAWWSTTA WTTFVASITQ
STANFIFAEV STFNNPWPTN DSDVKFRAVQ WIVAEVLLVF TILLNQVPPR YYKWIFKASM
LLMFIDYVMN IIWVPVATSK KPDGFRSAKW VFTETIYDQA GYIKEVDDAN GNPIASLSKI
VPKGWQWCLS YFATAGVIVG YDASGHIAEE TKDASIKAAR GIFYSTVTSF IVAFSLAILY
LFCCPDLDTF TAILYNDNSP QPFVNFYSYL LGRGGHVVMN VVIILEIFLN GVVSVLACSR
LVFAVSRDGV LPFSNWISQV SKTGQPKNAI TVIYIVSALL LCTILPSAVA FTSLVSAAGA
PSFAAYAVLA FCRLFITRDK FPKGRWSLGW LSKPCLVITL VYNLFALVVN VSPYTYPVTG
PSFNYAVVIM GGVSIFAIIC TIVIPKSRWV ANRYRYESDS EHSASVKELK V
