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GPI10_ASHGO
ID   GPI10_ASHGO             Reviewed;         595 AA.
AC   Q75BG9;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=GPI mannosyltransferase 3;
DE            EC=2.4.1.-;
DE   AltName: Full=GPI mannosyltransferase III;
DE            Short=GPI-MT-III;
DE   AltName: Full=Glycosylphosphatidylinositol-anchor biosynthesis protein 10;
GN   Name=GPI10; OrderedLocusNames=ADL281C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: Mannosyltransferase involved in glycosylphosphatidylinositol-
CC       anchor biosynthesis. Transfers the third mannose to Man2-GlcN-acyl-PI
CC       during GPI precursor assembly (By similarity). {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 glycosyltransferase 22 family. PIGB
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AE016817; AAS51639.1; -; Genomic_DNA.
DR   RefSeq; NP_983815.1; NM_209168.1.
DR   AlphaFoldDB; Q75BG9; -.
DR   STRING; 33169.AAS51639; -.
DR   CAZy; GT22; Glycosyltransferase Family 22.
DR   EnsemblFungi; AAS51639; AAS51639; AGOS_ADL281C.
DR   GeneID; 4619950; -.
DR   KEGG; ago:AGOS_ADL281C; -.
DR   eggNOG; KOG1771; Eukaryota.
DR   HOGENOM; CLU_012353_2_0_1; -.
DR   InParanoid; Q75BG9; -.
DR   OMA; HEWPDYL; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000000591; Chromosome IV.
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:0000026; F:alpha-1,2-mannosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0004376; F:glycolipid mannosyltransferase activity; IEA:InterPro.
DR   GO; GO:0000030; F:mannosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IBA:GO_Central.
DR   InterPro; IPR005599; GPI_mannosylTrfase.
DR   InterPro; IPR039521; PIG-B/GPI10.
DR   PANTHER; PTHR22760; PTHR22760; 1.
DR   PANTHER; PTHR22760:SF4; PTHR22760:SF4; 1.
DR   Pfam; PF03901; Glyco_transf_22; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Glycosyltransferase; GPI-anchor biosynthesis;
KW   Membrane; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..595
FT                   /note="GPI mannosyltransferase 3"
FT                   /id="PRO_0000246257"
FT   TRANSMEM        58..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        85..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        128..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        185..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        212..232
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        235..255
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        260..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        289..309
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        319..339
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        413..433
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   595 AA;  67312 MW;  8DB50002FC3803E6 CRC64;
     MKERSILRTL FLWRLINALS IRSFFQADEY WQSLEPAHVK AFGYGGLTWE WQHGLRSYAF
     PMLFEMSYYV AWILGVATRM ALQGLAHATA LCGAVVPSGA AGVAAMKAVW ELPEAAQELV
     EYYGVLYGPR VVMAAVAACG EFYSVLLVRK LYLRVADKGD DQKGDAAPVS RLALMLTMTN
     FFNCFFATRT FINSFEMTLT AVALYHWDWS GGLDVGSLGF SASLAVAAFA CLQRPTNVLI
     WAVLGLFLVL NLVRSRRWQL LLTLVAKVAA AGALAVCANI AIDYYFYGGV LLPLLRFIEF
     NVTTPLAAFY GRAPWHFHLL QSVPLIVGYA LPFFVGALLT HNFRRGNAGL LGSPIMQIKC
     VVVLNIALYS CIDHKEFRFL YPLQPLFLSL SALEMHTWLQ HHHARGTAWL KRVQSLLYVL
     PVLSITAALV LNTAHEAGVV SVMDYLHSAV PSAESIGFIM PCHSTPWQSH LHRNDLGKLW
     AISCQPPLDL LHQEDAGDQL LTYMDESDHL YENIPEFIHK NFPPVFRRDL RSPGRQYAYE
     WPEFLVVFEH MDEAFMKEYL KDSNYVEVKR FFNTLSHWDS RRAGDVIVYH KSPWY
 
 
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