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GPI1_SCHPO
ID   GPI1_SCHPO              Reviewed;         653 AA.
AC   O14357; P78971;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 128.
DE   RecName: Full=N-acetylglucosaminyl-phosphatidylinositol biosynthetic protein gpi1;
GN   Name=gpi1; ORFNames=SPBC30D10.11;
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 [MRNA].
RX   PubMed=9046095;
RX   DOI=10.1002/(sici)1097-0061(199702)13:2<139::aid-yea69>3.0.co;2-s;
RA   Colussi P.A., Orlean P.;
RT   "The essential Schizosaccharomyces pombe gpi1+ gene complements a bakers'
RT   yeast GPI anchoring mutant and is required for efficient cell separation.";
RL   Yeast 13:139-150(1997).
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).
CC   -!- FUNCTION: Necessary for the synthesis of N-acetylglucosaminyl-
CC       phosphatidylinositol, the very early intermediate in GPI-anchor
CC       biosynthesis.
CC   -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC       biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC49650.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U77355; AAC49650.1; ALT_INIT; mRNA.
DR   EMBL; CU329671; CAB10806.1; -; Genomic_DNA.
DR   PIR; T40185; T40185.
DR   RefSeq; NP_596274.1; NM_001022195.2.
DR   AlphaFoldDB; O14357; -.
DR   STRING; 4896.SPBC30D10.11.1; -.
DR   PaxDb; O14357; -.
DR   EnsemblFungi; SPBC30D10.11.1; SPBC30D10.11.1:pep; SPBC30D10.11.
DR   GeneID; 2540323; -.
DR   KEGG; spo:SPBC30D10.11; -.
DR   PomBase; SPBC30D10.11; gpi1.
DR   VEuPathDB; FungiDB:SPBC30D10.11; -.
DR   eggNOG; KOG1183; Eukaryota.
DR   HOGENOM; CLU_007914_2_1_1; -.
DR   InParanoid; O14357; -.
DR   OMA; YNWQLTI; -.
DR   PhylomeDB; O14357; -.
DR   Reactome; R-SPO-162710; Synthesis of glycosylphosphatidylinositol (GPI).
DR   UniPathway; UPA00196; -.
DR   PRO; PR:O14357; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR   GO; GO:0000506; C:glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex; ISO:PomBase.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0017176; F:phosphatidylinositol N-acetylglucosaminyltransferase activity; IGI:PomBase.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IGI:PomBase.
DR   InterPro; IPR007720; PigQ/GPI1.
DR   PANTHER; PTHR21329; PTHR21329; 1.
DR   Pfam; PF05024; Gpi1; 1.
PE   2: Evidence at transcript level;
KW   GPI-anchor biosynthesis; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..653
FT                   /note="N-acetylglucosaminyl-phosphatidylinositol
FT                   biosynthetic protein gpi1"
FT                   /id="PRO_0000087557"
FT   TRANSMEM        43..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        237..257
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        327..347
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        382..402
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        407..427
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        485..505
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        520..540
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        605..625
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        448
FT                   /note="L -> M (in Ref. 1; AAC49650)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   653 AA;  76432 MW;  916CF84ADEA0C66E CRC64;
     MSTTTMNIAS APIEVKRIYW PKSTISYTDS GYLVGWKYST NDLIVVTTIT SYQSFANFLV
     DYCKNQDQSV DIKSLCILGT FNCSADILPG DKYEIDCWIK VQQSTELSHP RVFDSASTPL
     KINLHIIYYH PPQPRKMQFL SLEPLSLLLL KDSFINKSNP EYESMQHQQI LLKKLKLHFP
     RRKENSWKRS LRSGLIELLN QSFEVRMLTH ENNNKKNSYV FRLFDRVSSS TFYFFNSLFA
     YFIILLRIIN EVILLAINYR PIPLSYNMMD IFVSARQVDL RLQQACFWPV QYMKLWVFRK
     SKRVAIEDYK EYIRFYNNLW LVANDMIFGI TMSSFILENL HLVVKLIENI TFEYAIKNVR
     SMVIWLVDTP AGLKLNNDIC KFIMKLSVWV IDVWSNFLLH CLPWTPFLVQ VVAISGFGGA
     SLMIALISDF LSVMTIHIHL LYLASSRLYN WQLRVIYSLL QLFRGKKRNV LRNRIDSYEY
     DLDQLLLGTI LFTVLIFFLP TIYVFYAAFA LTRVSVMTCL AICETMLAFL NHFPLFVTML
     RIKDPYRIPS GLNFEIVSFE PLKQDGFATL YLNCNSKPMS LGSMFEHYRK LARRLISHYL
     SKTTLISLLV GCPVPAIPAE QLYNIQYAML PTKRISIRKL RDLLFHQKKF PYD
 
 
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