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LIZ1_SCHPO
ID   LIZ1_SCHPO              Reviewed;         514 AA.
AC   O43000; P78874; Q1L845;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1999, sequence version 2.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Pantothenate transporter liz1;
GN   Name=liz1; ORFNames=SPBC2G2.01c, SPBC4B4.13c;
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 SUBCELLULAR LOCATION.
RX   PubMed=9950674; DOI=10.1091/mbc.10.2.245;
RA   Moynihan E.B., Enoch T.;
RT   "Liz1p, a novel fission yeast membrane protein, is required for normal cell
RT   division when ribonucleotide reductase is inhibited.";
RL   Mol. Biol. Cell 10:245-257(1999).
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 144-448.
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).
RN   [4]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=15075270; DOI=10.1128/ec.3.2.406-412.2004;
RA   Stolz J., Caspari T., Carr A.M., Sauer N.;
RT   "Cell division defects of Schizosaccharomyces pombe liz1- mutants are
RT   caused by defects in pantothenate uptake.";
RL   Eukaryot. Cell 3:406-412(2004).
CC   -!- FUNCTION: Transports pantothenate into the cell.
CC       {ECO:0000269|PubMed:15075270}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15075270,
CC       ECO:0000269|PubMed:9950674}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:15075270, ECO:0000269|PubMed:9950674}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. Allantoate
CC       permease family. {ECO:0000305}.
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DR   EMBL; AF052688; AAC06236.1; -; Genomic_DNA.
DR   EMBL; CU329671; CAA19293.1; -; Genomic_DNA.
DR   EMBL; D89224; BAA13885.1; -; mRNA.
DR   PIR; T40485; T40485.
DR   RefSeq; NP_596430.1; NM_001022349.2.
DR   AlphaFoldDB; O43000; -.
DR   SMR; O43000; -.
DR   BioGRID; 276871; 66.
DR   STRING; 4896.SPBC2G2.01c.1; -.
DR   TCDB; 2.A.1.14.17; the major facilitator superfamily (mfs).
DR   iPTMnet; O43000; -.
DR   MaxQB; O43000; -.
DR   PaxDb; O43000; -.
DR   PRIDE; O43000; -.
DR   EnsemblFungi; SPBC2G2.01c.1; SPBC2G2.01c.1:pep; SPBC2G2.01c.
DR   PomBase; SPBC2G2.01c; liz1.
DR   VEuPathDB; FungiDB:SPBC2G2.01c; -.
DR   eggNOG; KOG2533; Eukaryota.
DR   HOGENOM; CLU_001265_4_2_1; -.
DR   InParanoid; O43000; -.
DR   OMA; AWWPLVF; -.
DR   PhylomeDB; O43000; -.
DR   PRO; PR:O43000; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
DR   GO; GO:0005887; C:integral component of plasma membrane; IC:PomBase.
DR   GO; GO:0031224; C:intrinsic component of membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:PomBase.
DR   GO; GO:0015233; F:pantothenate transmembrane transporter activity; IMP:PomBase.
DR   GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0098717; P:pantothenate import across plasma membrane; IMP:PomBase.
DR   Gene3D; 1.20.1250.20; -; 1.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..514
FT                   /note="Pantothenate transporter liz1"
FT                   /id="PRO_0000121370"
FT   TRANSMEM        24..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        72..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        98..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        128..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        159..179
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        194..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        263..283
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        300..320
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        329..349
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        357..377
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        390..410
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        423..443
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        445..447
FT                   /note="IRD -> SAI (in Ref. 3; BAA13885)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   514 AA;  57964 MW;  A4026A704EC1FECB CRC64;
     MALLNRLAKT FSPYYGLNKV EQKLLIKIDW FILSYCCVSY FINYLDRSSI NNAYLSGMQE
     DLKMHGNELQ DINVVFTCGY IIGQLPGSYA LQRVPARLWF SVMNILWGLM TIFSFAVHSV
     RALMILRFFM AVAEASTFAG THYILGAWYK ESELCKRAGI FSASGLVGTM FAGYLQTAVH
     SSLNGKGGLS GWRWLFIIDG ILTIPLSLYG LFLFPDVPET TKAPYFTEQE KELSFKRLPA
     RPKKKPLTLK AIKDIVRSWR IYGLCILWIF SGETQAIAVN VLMGQWMKWS NKFSVAQINN
     YPTVITAVGV VSTLGASVIS DKLAGNPRWP FGLFLCVITT VSATILLAWN VPDGAKFFAY
     FASGCTYAGQ AVWFSWANDI CRDNDQERGV VVFLMNMCQN IWHIWWAPIM YPNTDTPRFI
     KGLIGLLVVG GIVFVSSCIV SYMQIRDKRI KRSIQDAKDF DDVFTEHESL ELKKIGKNDE
     ESLNTTNAVK EISSPGLVIT RQRISMPKET NAQD
 
 
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