ID   GPI8_BOVIN              Reviewed;         395 AA.
AC   Q3MHZ7;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=GPI-anchor transamidase;
DE            Short=GPI transamidase;
DE            EC=3.-.-.-;
DE   AltName: Full=Phosphatidylinositol-glycan biosynthesis class K protein;
DE            Short=PIG-K;
DE   Flags: Precursor;
GN   Name=PIGK;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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   -!- SUBUNIT: Forms a complex with PIGT, PIGS, PIGU and GAA1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Single-pass type I membrane protein {ECO:0000250}.
CC   -!- PTM: The disulfide bond between PIGK/GPI8 and PIGT is important for
CC       normal enzyme activity. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase C13 family. {ECO:0000305}.
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DR   EMBL; BC104506; AAI04507.1; -; mRNA.
DR   RefSeq; NP_001071348.1; NM_001077880.1.
DR   AlphaFoldDB; Q3MHZ7; -.
DR   SMR; Q3MHZ7; -.
DR   STRING; 9913.ENSBTAP00000041428; -.
DR   MEROPS; C13.005; -.
DR   PaxDb; Q3MHZ7; -.
DR   PRIDE; Q3MHZ7; -.
DR   Ensembl; ENSBTAT00000043893; ENSBTAP00000041428; ENSBTAG00000031012.
DR   GeneID; 508700; -.
DR   KEGG; bta:508700; -.
DR   CTD; 10026; -.
DR   VEuPathDB; HostDB:ENSBTAG00000031012; -.
DR   VGNC; VGNC:32870; PIGK.
DR   eggNOG; KOG1349; Eukaryota.
DR   GeneTree; ENSGT00940000156273; -.
DR   HOGENOM; CLU_044656_1_0_1; -.
DR   InParanoid; Q3MHZ7; -.
DR   OMA; PGHTNNW; -.
DR   OrthoDB; 1259741at2759; -.
DR   TreeFam; TF300848; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000009136; Chromosome 3.
DR   Bgee; ENSBTAG00000031012; Expressed in caput epididymis and 109 other tissues.
DR   ExpressionAtlas; Q3MHZ7; baseline and differential.
DR   GO; GO:0042765; C:GPI-anchor transamidase complex; ISS:UniProtKB.
DR   GO; GO:0003923; F:GPI-anchor transamidase activity; ISS:UniProtKB.
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   PIRSF; PIRSF500138; GPI8; 1.
DR   PIRSF; PIRSF019663; Legumain; 1.
DR   PRINTS; PR00776; HEMOGLOBNASE.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Endoplasmic reticulum; GPI-anchor biosynthesis; Hydrolase;
KW   Membrane; Protease; Reference proteome; Signal; Thiol protease;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000250"
FT   CHAIN           28..395
FT                   /note="GPI-anchor transamidase"
FT                   /id="PRO_0000230995"
FT   TOPO_DOM        28..367
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        368..388
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        389..395
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          311..321
FT                   /note="Essential for GPI attachment"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        164
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        206
FT                   /evidence="ECO:0000250"
FT   DISULFID        92
FT                   /note="Interchain (with C-186 in PIGT)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   395 AA;  45173 MW;  DF8C724BDFFB0B82 CRC64;
     MVDTCFLSRG LTTLAGLLLL PFGSLAASQI EDQAEQFFRS GHTNNWAVLV CTSRFWFNYR
     HVANTLSVYR SVKRLGIPDS HIVLMLADDM ACNPRNPKPA TVYSHKNMEL NVYGDDVEVD
     YRSYEVTVEN FLRVLTGRIP SSTPRSKRLL SDDRSNILIY MTGHGGNGFL KFQDSEEITN
     IELADAFEQM WQKRRYNELL FIIDTCQGAS MYERFYSPNI MALASSQVGE DSLSHQPDPA
     VGVHLMDRYT FYVLEFLEEI NPASQTNMND LFQVCPRSLC VSTPGHRTDL FQRDPKNVLI
     TDFFGSVRKV EITTETISLQ PDSGVVESSY KKDQMVEELM EPLKYAEQLP VAQIIHQKPK
     LKDWHPPGGF ILGLWALIIM VFFKTYGIKH MKFIF