ITR2_SCHPO
ID ITR2_SCHPO Reviewed; 557 AA.
AC P87110; P78901;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Myo-inositol transporter 2;
GN Name=itr2; ORFNames=SPAC20G8.03;
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], AND FUNCTION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=9560432; DOI=10.1007/s002940050334;
RA Niederberger C., Graub R., Schweingruber A.-M., Fankhauser H., Rusu M.,
RA Poitelea M., Edenharter L., Schweingruber M.E.;
RT "Exogenous inositol and genes responsible for inositol transport are
RT required for mating and sporulation in Shizosaccharomyces pombe.";
RL Curr. Genet. 33:255-261(1998).
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 MRNA] OF 166-541.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
CC -!- FUNCTION: Transporter for myo-inositol. {ECO:0000269|PubMed:9560432}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + myo-inositol(out) = H(+)(in) + myo-inositol(in);
CC Xref=Rhea:RHEA:60364, ChEBI:CHEBI:15378, ChEBI:CHEBI:17268;
CC Evidence={ECO:0000305|PubMed:9560432};
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. {ECO:0000305}.
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DR EMBL; X99105; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CU329670; CAB08597.1; -; Genomic_DNA.
DR EMBL; D89252; BAA13913.1; -; mRNA.
DR PIR; T38125; T38125.
DR PIR; T43176; T43176.
DR RefSeq; NP_593320.1; NM_001018751.2.
DR AlphaFoldDB; P87110; -.
DR SMR; P87110; -.
DR BioGRID; 278318; 3.
DR STRING; 4896.SPAC20G8.03.1; -.
DR iPTMnet; P87110; -.
DR MaxQB; P87110; -.
DR PaxDb; P87110; -.
DR PRIDE; P87110; -.
DR EnsemblFungi; SPAC20G8.03.1; SPAC20G8.03.1:pep; SPAC20G8.03.
DR GeneID; 2541827; -.
DR KEGG; spo:SPAC20G8.03; -.
DR PomBase; SPAC20G8.03; itr2.
DR VEuPathDB; FungiDB:SPAC20G8.03; -.
DR eggNOG; KOG0254; Eukaryota.
DR HOGENOM; CLU_001265_30_5_1; -.
DR InParanoid; P87110; -.
DR OMA; PECGFCA; -.
DR PhylomeDB; P87110; -.
DR PRO; PR:P87110; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005366; F:myo-inositol:proton symporter activity; IMP:PomBase.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:1904679; P:myo-inositol import across plasma membrane; IMP:PomBase.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR003663; Sugar/inositol_transpt.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR Pfam; PF00083; Sugar_tr; 1.
DR PRINTS; PR00171; SUGRTRNSPORT.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00879; SP; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 2.
PE 2: Evidence at transcript level;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..557
FT /note="Myo-inositol transporter 2"
FT /id="PRO_0000050454"
FT TOPO_DOM 1..76
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..97
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..99
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 121..123
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 145..157
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..180
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 202..209
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..240
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..261
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 262..367
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..388
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 389..396
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 397..417
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 418..432
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 433..453
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 454..468
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 469..489
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 490..498
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 499..519
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 520..557
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 24..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 271
FT /note="N -> H (in Ref. 3; BAA13913)"
FT /evidence="ECO:0000305"
FT CONFLICT 372
FT /note="I -> M (in Ref. 3; BAA13913)"
FT /evidence="ECO:0000305"
FT CONFLICT 428
FT /note="N -> H (in Ref. 3; BAA13913)"
FT /evidence="ECO:0000305"
FT CONFLICT 436
FT /note="L -> I (in Ref. 3; BAA13913)"
FT /evidence="ECO:0000305"
FT CONFLICT 526
FT /note="S -> F (in Ref. 3; BAA13913)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 557 AA; 61137 MW; 20875EC11B153175 CRC64;
MDFNNIPLAT IKSSDDKGKD FIVEMTTRPS ETKKKVPFSE DMREIPSLPN EEEANATDPQ
ANEVADENGE GFEAEKISSW IWVLSAVAGI SGLLFGYDTG VISGALAVLG SDLGHVLSSG
QKELITSATS FAALISATTS GWLADWVGRK RLLLCADAIF VIGSVIMAAS RNVAMMVVGR
FIVGYGIGLT SLIVPMYITE LAPARLRGRL VIIYVVFITG GQLIAYSLNA AFEHVHQGWR
IMFGIGAAPA LGQLISLFWT PESPRYLLRH NHVEKVYKIL SRIHPEAKPA EIAYKVSLIQ
EGVKVDFPEG NKFQHFFHSL KVLFTVPSNR RSLFIGCFLQ WFQQFSGTNA IQYFSAIIFQ
SVGFKNSISV SIVVGATNFV FTIVAFMFID RIGRRRILLC TSAVMIAGLA LCAIAYHFLP
ADTTQNTNSG WQYVVLASII IFLASYASGI GNIPWQQAEL FPMEVRALGA GFSTAINWVG
NLIISASFLT MMESITPTGT FALFAGFCFV GLVTSYFTYP ELAGMSIENI HKLLEKGFWQ
AVKESTKRVR KGRIDEA
