位置:首页 > 蛋白库 > GPI14_ASPOR
GPI14_ASPOR
ID   GPI14_ASPOR             Reviewed;         415 AA.
AC   Q2TXB8;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 2.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=GPI mannosyltransferase 1;
DE            EC=2.4.1.-;
DE   AltName: Full=GPI mannosyltransferase I;
DE            Short=GPI-MT-I;
DE   AltName: Full=Glycosylphosphatidylinositol-anchor biosynthesis protein 14;
GN   Name=gpi14; ORFNames=AO090010000207;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
CC   -!- FUNCTION: Mannosyltransferase involved in glycosylphosphatidylinositol-
CC       anchor biosynthesis. Transfers the first alpha-1,4-mannose to GlcN-
CC       acyl-PI during GPI precursor assembly. Required for cell wall integrity
CC       (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 PIGM family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE66105.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP007175; BAE66105.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001827238.2; XM_001827186.2.
DR   AlphaFoldDB; Q2TXB8; -.
DR   STRING; 510516.Q2TXB8; -.
DR   CAZy; GT50; Glycosyltransferase Family 50.
DR   EnsemblFungi; BAE66105; BAE66105; AO090010000207.
DR   VEuPathDB; FungiDB:AO090010000207; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000006564; Chromosome 8.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0051751; F:alpha-1,4-mannosyltransferase activity; IEA:InterPro.
DR   GO; GO:0004376; F:glycolipid mannosyltransferase activity; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR007704; PIG-M.
DR   PANTHER; PTHR12886; PTHR12886; 1.
DR   Pfam; PF05007; Mannosyl_trans; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Endoplasmic reticulum;
KW   Glycosyltransferase; GPI-anchor biosynthesis; Membrane; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..415
FT                   /note="GPI mannosyltransferase 1"
FT                   /id="PRO_0000246225"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        82..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        134..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        158..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        222..242
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        284..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        329..349
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        354..374
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        387..407
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   415 AA;  46549 MW;  1DECEECE3B44E541 CRC64;
     MASLFERPSL VFGAAIVLRA ILLVYGAWQD AHSAVKYTDI DYMVFTDAAR YVSKGDSPYA
     RDTYRYTPLL AWLLLPTSWD GFFSFGKVLF ALSDVVAGWL IAKALTSFYG MSPPRALKYA
     SVWLLNPMVA NISTRGSSEG LLCVLVIALL WAVLNRKITL AGVLLGLSVH FKIYPFVYGP
     SIIWWLDEER EGLKSSSQKQ KPEQDDRNLL THIFNFITPS RLLLTTTALA TFSGLNISMY
     ILYDFPFAQH TYLHHLTRID HRHNFSPYSS LLYLSAAGDI QGSFESLAFI PQLLLSVVVI
     PIVLAKRSLP GAMLAQTFAF VTFNKVCTSQ YFLWYLIFLP FYLPSSSLMK NPRLGITVTA
     LWVIAQALWL QQGYYLEFLG LSSFVPGLFL ASLGFFAVNI WILGIIINDV ALEGC
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024