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PIGM_XENTR
ID   PIGM_XENTR              Reviewed;         419 AA.
AC   Q66IJ4;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=Phosphatidylinositol-glycan biosynthesis class M protein;
DE            Short=PIG-M;
GN   Name=pigm; ORFNames=TGas014d02.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Gastrula;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
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 (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}.
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DR   EMBL; CR760728; CAJ83771.1; -; mRNA.
DR   EMBL; BC081324; AAH81324.1; -; mRNA.
DR   RefSeq; NP_001008120.1; NM_001008119.1.
DR   AlphaFoldDB; Q66IJ4; -.
DR   STRING; 8364.ENSXETP00000013605; -.
DR   CAZy; GT50; Glycosyltransferase Family 50.
DR   PaxDb; Q66IJ4; -.
DR   DNASU; 493482; -.
DR   GeneID; 493482; -.
DR   KEGG; xtr:493482; -.
DR   CTD; 93183; -.
DR   Xenbase; XB-GENE-5730241; pigm.
DR   eggNOG; KOG3893; Eukaryota.
DR   HOGENOM; CLU_024220_3_1_1; -.
DR   InParanoid; Q66IJ4; -.
DR   OMA; HESFIYH; -.
DR   OrthoDB; 1003258at2759; -.
DR   PhylomeDB; Q66IJ4; -.
DR   TreeFam; TF314752; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000008143; Chromosome 6.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000006188; Expressed in testis and 17 other tissues.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:1990529; C:glycosylphosphatidylinositol-mannosyltransferase I complex; IBA:GO_Central.
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:0000030; F:mannosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IBA:GO_Central.
DR   InterPro; IPR007704; PIG-M.
DR   PANTHER; PTHR12886; PTHR12886; 1.
DR   Pfam; PF05007; Mannosyl_trans; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Glycosyltransferase; GPI-anchor biosynthesis;
KW   Membrane; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..419
FT                   /note="GPI mannosyltransferase 1"
FT                   /id="PRO_0000246220"
FT   TOPO_DOM        1..13
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        35..88
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        89..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        112..114
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        115..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        136..168
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        169..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        190..224
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        225..245
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        246..285
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        286..306
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        307..327
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        328..348
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        349..355
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        356..376
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        377..382
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        383..403
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        404..419
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   419 AA;  49036 MW;  ECBD805202269343 CRC64;
     MMKQAGILKI FLQHQFMFPT AFFLRSALVL FGVYQDQTML VKYTDVDYHV FTDAAEYLTQ
     GVSPYKRATY RYTPLLAWIL TPNIYVTELY GKMLFVCCDL LAAYLIHRIL VDRGIKDSAS
     LYCAIWLFNP LPMVVSSRGN AESVLAVLVL SVLYYVQKRR LIKGALIYGL SVHMKIYPIT
     YILPIALFFQ KEDFYGSQEG KRVVSNLKYI RIFRNLLQRL LSRDILLFVT VSGVTFALLT
     LFFYYRYGWE FLENTYLYHL TRRDIRHNFS PYFYMLYLTA ENNNSFILGL AAFFPQLVLL
     FVVSLAYFKD LPFCCFLHTA IFVSFNKVCT SQYFLWYLCL LPLVMPGLKM SMTNGICLII
     LWFFSQAIWL VPAYFLEFEG QNTFLYIWCA GLLFLLINTV IIVQIISNYQ LQSKKTKKT
 
 
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