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GPI11_CANAL
ID   GPI11_CANAL             Reviewed;         265 AA.
AC   Q5AFT2; A0A1D8PLI7; Q5AF45;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Glycosylphosphatidylinositol anchor biosynthesis protein 11;
GN   Name=GPI11; OrderedLocusNames=CAALFM_C402420CA;
GN   ORFNames=CaO19.10277, CaO19.2761;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
CC   -!- FUNCTION: Acts in the GPI biosynthetic pathway between GlcNAc-PI
CC       synthesis and GPI transfer to protein. {ECO:0000250}.
CC   -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC       biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PIGF family. {ECO:0000305}.
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DR   EMBL; CP017626; AOW29011.1; -; Genomic_DNA.
DR   RefSeq; XP_720511.1; XM_715418.1.
DR   AlphaFoldDB; Q5AFT2; -.
DR   STRING; 237561.Q5AFT2; -.
DR   PRIDE; Q5AFT2; -.
DR   GeneID; 3637849; -.
DR   KEGG; cal:CAALFM_C402420CA; -.
DR   CGD; CAL0000185478; orf19.10277.
DR   VEuPathDB; FungiDB:C4_02420C_A; -.
DR   eggNOG; KOG3144; Eukaryota.
DR   HOGENOM; CLU_069429_2_0_1; -.
DR   InParanoid; Q5AFT2; -.
DR   OrthoDB; 1182539at2759; -.
DR   UniPathway; UPA00196; -.
DR   PRO; PR:Q5AFT2; -.
DR   Proteomes; UP000000559; Chromosome 4.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0051377; F:mannose-ethanolamine phosphotransferase activity; IBA:GO_Central.
DR   GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IBA:GO_Central.
DR   InterPro; IPR009580; GPI_biosynthesis_protein_Pig-F.
DR   Pfam; PF06699; PIG-F; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Glycoprotein; GPI-anchor biosynthesis; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..265
FT                   /note="Glycosylphosphatidylinositol anchor biosynthesis
FT                   protein 11"
FT                   /id="PRO_0000191763"
FT   TRANSMEM        49..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        79..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        137..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        166..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        209..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        240..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        111
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        112
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   265 AA;  29810 MW;  0602081010A35A9D CRC64;
     MPAAIRPMKK TVSFSKDVSN NNNNLESDSD TKQSPQSYLT FIPQIKNSLL VVPFHNIFIL
     VGMFYSGLTQ DLETVMWKGF LTSIPIQVIY NYIIYINLLP LKKSTRNDHQ NNSSGSAINN
     NNNNNNNNVP LLIGSSIFVS IVLSLPLFVV IILMGAPVYK YSLKTLYLSL HLSQLIFNPL
     IILSNLNVNK IKRLFKQDHL YRIIFHHGIL SSVLLTLGGC WLGVIPIPLD WDRPWQQWPI
     TLLVGGYLGG VVGGVLSLIV NYFSH
 
 
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