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PIGB_XENLA
ID   PIGB_XENLA              Reviewed;         531 AA.
AC   Q4V7R2;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 55.
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=Phosphatidylinositol-glycan biosynthesis class B protein;
DE            Short=PIG-B;
GN   Name=pigb;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Egg;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Mannosyltransferase involved in glycosylphosphatidylinositol-
CC       anchor biosynthesis. Transfers the third alpha-1,2-mannose to Man2-
CC       GlcN-acyl-PI during GPI precursor assembly (By similarity).
CC       {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; BC097762; AAH97762.1; -; mRNA.
DR   RefSeq; NP_001089512.1; NM_001096043.1.
DR   AlphaFoldDB; Q4V7R2; -.
DR   CAZy; GT22; Glycosyltransferase Family 22.
DR   DNASU; 734564; -.
DR   GeneID; 734564; -.
DR   KEGG; xla:734564; -.
DR   CTD; 734564; -.
DR   Xenbase; XB-GENE-996683; pigb.S.
DR   OrthoDB; 901894at2759; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000186698; Chromosome 3S.
DR   Bgee; 734564; Expressed in egg cell and 19 other tissues.
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:0000026; F:alpha-1,2-mannosyltransferase activity; IEA:InterPro.
DR   GO; GO:0004376; F:glycolipid mannosyltransferase activity; IEA:InterPro.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-UniPathway.
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   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Glycoprotein; Glycosyltransferase;
KW   GPI-anchor biosynthesis; Membrane; Reference proteome; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..531
FT                   /note="GPI mannosyltransferase 3"
FT                   /id="PRO_0000246254"
FT   TRANSMEM        99..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        124..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        174..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        210..230
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        249..269
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        303..323
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        328..348
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        350..370
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        375..395
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        84
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        204
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        414
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        476
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   531 AA;  61447 MW;  17F0EAF486BC0C81 CRC64;
     MEKVRSRVGW LYRRQDSQGA VQLRKRKSRL YSKEASSACP GAGLFGENTY LVLAAVGFRI
     FNCMMVQTSF VPDEYWQSLE VAHNMTFNYG YLTWEWTEGL RGFSYPLMFA AIYKVLYLLG
     KDHVWFLIWI PRLAQAVLSG IADVRLYSLV RHLENTELAK WVYFCQLCSW FTWYCATRTL
     TNTMEAVLST FALYYYPLEG SSTNSSTKYL ICVALAFLIR PTAVILWIPL LFYHFAKEKK
     KAELVVQQYL PIGILTLAAS LTVDRIFFGK WTFVQWNFLK FNVLQDLGSF YGSHPWHWYI
     TQGVPVILCT HLPFFIHGCM VTPKRYQILL VAVAWTVLTY SALSHKEFRF IYPVLPVCMV
     FCGFSFSNLK RWKKAAVGFL VLSNLFPALY TGLIHQRGAL DIMSGIQKLC KMENSSASLF
     VLMPCHSIPF YSHVHCPIKM NFLECPPDLS DSDAYIDEAD LFYVSPLAWL NAEFYNKTLL
     PTHLIMFSVL EPEIRSFLTN NNYLKSMSVF HTHLPEGRTG SHIYMYERNS K
 
 
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