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GPI16_SCHPO
ID   GPI16_SCHPO             Reviewed;         545 AA.
AC   O94380;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=GPI transamidase component PIG-T homolog;
DE   Flags: Precursor;
GN   Name=gpi16; ORFNames=SPBC1604.15;
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).
CC   -!- FUNCTION: Component of the GPI transamidase complex. Involved in
CC       transfer of GPI to proteins (By similarity). {ECO:0000250}.
CC   -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC       biosynthesis.
CC   -!- SUBUNIT: Forms a complex with PIG-S homolog, PIG-U homolog and GPI8.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:16823372}; Single-pass type I membrane protein
CC       {ECO:0000269|PubMed:16823372}.
CC   -!- PTM: The disulfide bond between PIGK/GPI8 and PIGT is important for
CC       normal enzyme activity. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PIGT family. {ECO:0000305}.
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DR   EMBL; CU329671; CAA22348.1; -; Genomic_DNA.
DR   PIR; T39499; T39499.
DR   RefSeq; NP_596625.1; NM_001022546.2.
DR   AlphaFoldDB; O94380; -.
DR   SMR; O94380; -.
DR   STRING; 4896.SPBC1604.15.1; -.
DR   MaxQB; O94380; -.
DR   PaxDb; O94380; -.
DR   EnsemblFungi; SPBC1604.15.1; SPBC1604.15.1:pep; SPBC1604.15.
DR   GeneID; 2539759; -.
DR   KEGG; spo:SPBC1604.15; -.
DR   PomBase; SPBC1604.15; gpi16.
DR   VEuPathDB; FungiDB:SPBC1604.15; -.
DR   eggNOG; KOG2407; Eukaryota.
DR   HOGENOM; CLU_021459_2_1_1; -.
DR   InParanoid; O94380; -.
DR   OMA; LWAWIDA; -.
DR   PhylomeDB; O94380; -.
DR   UniPathway; UPA00196; -.
DR   PRO; PR:O94380; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR   GO; GO:0042765; C:GPI-anchor transamidase complex; ISO:PomBase.
DR   GO; GO:0016255; P:attachment of GPI anchor to protein; ISO:PomBase.
DR   InterPro; IPR007245; PIG-T.
DR   PANTHER; PTHR12959; PTHR12959; 1.
DR   Pfam; PF04113; Gpi16; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW   GPI-anchor biosynthesis; Membrane; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..545
FT                   /note="GPI transamidase component PIG-T homolog"
FT                   /id="PRO_0000024109"
FT   TOPO_DOM        23..493
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        494..514
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        515..545
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        168
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        227
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        336
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        391
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        467
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        182
FT                   /note="Interchain (with C-73 in PIGK/GPI8)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   545 AA;  62065 MW;  DD2C36016ABF4A9D CRC64;
     MKKNGCLLLF AYSLLSFSLT AATIDETYDE SLFIKSFSSR YSYVSFAFEI GASTDSTHSS
     VFSESSFSLF PLSIARVMDE CQVSELHIRA TRGRWDYENW KESPDNGFYS GGLGFEVWAF
     MANDPSMKYW LKLTNQLSGL LCASLNYIDS SNTYQPQLSY PGSFSFSNNT QYFASLPQED
     VCTENLSPLF KLLPCKRKAG IASLLDSHLF FDTDWHSFSI DVYPSENQSL ASVKMGIIIQ
     AVVDVERNGR RKGKTTFQPP SEYCHDEDMD SLHCLMSGYS TEHHTVDDLF HKVPKERCLL
     SSTFSDVFVS NGDKIDTFSL DEAANIQIPI QSTSDNHTVT VDRSLSNDGN HWGSLSSTIY
     NPSSSPRTIV YFEKFPWFVR VYLHTLTITL NGTRINTKDF IEKLYYQPLR DRKAGTMMEI
     QFSIPPHTNL IVHFNVEKTP LRLDEYPPDA NRGYNLPPAI ISVFDENNTK LCSLRTAALL
     MFIPTPDFSM PYNVIIFTST VIALTFGGIF NLLTRRFVPQ QSKFQNRQPS MLQRLKEKIF
     HKKRG
 
 
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