GPI8_CAEEL
ID GPI8_CAEEL Reviewed; 319 AA.
AC P49048;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 3.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Putative GPI-anchor transamidase;
DE Short=GPI transamidase;
DE EC=3.-.-.-;
DE AltName: Full=Hypersensitive to pore-forming toxin protein 4 {ECO:0000305};
DE AltName: Full=Phosphatidylinositol-glycan biosynthesis class K protein {ECO:0000312|WormBase:T05E11.6};
DE Short=PIG-K {ECO:0000305};
DE Flags: Precursor;
GN Name=pigk-1 {ECO:0000312|WormBase:T05E11.6};
GN Synonyms=hpo-4 {ECO:0000312|WormBase:T05E11.6};
GN ORFNames=T05E11.6 {ECO:0000312|WormBase:T05E11.6};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-257, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
CC -!- FUNCTION: Mediates GPI anchoring in the endoplasmic reticulum, by
CC replacing a protein's C-terminal GPI attachment signal peptide with a
CC pre-assembled GPI. During this transamidation reaction, the GPI
CC transamidase forms a carbonyl intermediate with the substrate protein
CC (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis.
CC -!- SIMILARITY: Belongs to the peptidase C13 family. {ECO:0000305}.
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DR EMBL; BX284604; CAA92977.2; -; Genomic_DNA.
DR PIR; T24525; T24525.
DR RefSeq; NP_502076.2; NM_069675.2.
DR AlphaFoldDB; P49048; -.
DR SMR; P49048; -.
DR BioGRID; 52804; 4.
DR STRING; 6239.T05E11.6; -.
DR MEROPS; C13.005; -.
DR iPTMnet; P49048; -.
DR EPD; P49048; -.
DR PaxDb; P49048; -.
DR PeptideAtlas; P49048; -.
DR EnsemblMetazoa; T05E11.6.1; T05E11.6.1; WBGene00011482.
DR UCSC; T05E11.6; c. elegans.
DR WormBase; T05E11.6; CE40776; WBGene00011482; pigk-1.
DR eggNOG; KOG1349; Eukaryota.
DR GeneTree; ENSGT00940000156273; -.
DR HOGENOM; CLU_044656_1_0_1; -.
DR InParanoid; P49048; -.
DR OMA; PGHTNNW; -.
DR OrthoDB; 1259741at2759; -.
DR PhylomeDB; P49048; -.
DR UniPathway; UPA00196; -.
DR PRO; PR:P49048; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00011482; Expressed in adult organism and 3 other tissues.
DR GO; GO:0042765; C:GPI-anchor transamidase complex; IBA:GO_Central.
DR GO; GO:0003923; F:GPI-anchor transamidase activity; IBA:GO_Central.
DR GO; GO:0016255; P:attachment of GPI anchor to protein; IBA:GO_Central.
DR GO; GO:0034394; P:protein localization to cell surface; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR028361; GPI_transamidase.
DR InterPro; IPR001096; Peptidase_C13.
DR PANTHER; PTHR48067; PTHR48067; 1.
DR Pfam; PF01650; Peptidase_C13; 1.
DR PRINTS; PR00776; HEMOGLOBNASE.
PE 1: Evidence at protein level;
KW Glycoprotein; GPI-anchor biosynthesis; Hydrolase; Protease;
KW Reference proteome; Signal; Thiol protease.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..319
FT /note="Putative GPI-anchor transamidase"
FT /id="PRO_0000215381"
FT ACT_SITE 156
FT /evidence="ECO:0000250"
FT ACT_SITE 198
FT /evidence="ECO:0000250"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
SQ SEQUENCE 319 AA; 36417 MW; D1F0BF0C0E23702D CRC64;
MRHVLLIFCA IIATEALLNT GLQLKIDELF DTPGHTNNWA VLVCTSKFWF NYRHVSNVLA
LYHSIKRLGI PDSNIIMMLA EDVPCNSRNP RPGTVYAARA GTNLYGSDVE VDYRGEEVTV
ESFIRVLTGR HHPATPRSKR LLTDHQSNVL IYLTGHGGDS FMKFQDSEEL TNVDLAYAIQ
TMFEDNRYHE MLVIADSCRS ASMYEWIDSP NVLSLSSSLT HEESYSYDVD TDIGVYVIDR
YTHYTVNFLT KEVKALNSSA NMQDYIDSCP ARKCLSNTGV RKDHYPKDVK RVRVTDFFGS
SRIFQHLSEE IVLDDEFWA
