ID   GPI8_PONAB              Reviewed;         395 AA.
AC   Q5R6L8; Q5R731;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 75.
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   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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}.
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; CR860289; CAH92429.1; -; mRNA.
DR   EMBL; CR860470; CAH92592.1; -; mRNA.
DR   RefSeq; NP_001124569.1; NM_001131097.1.
DR   AlphaFoldDB; Q5R6L8; -.
DR   SMR; Q5R6L8; -.
DR   STRING; 9601.ENSPPYP00000001424; -.
DR   MEROPS; C13.005; -.
DR   Ensembl; ENSPPYT00000042291; ENSPPYP00000042583; ENSPPYG00000001225.
DR   GeneID; 100169743; -.
DR   KEGG; pon:100169743; -.
DR   CTD; 10026; -.
DR   eggNOG; KOG1349; Eukaryota.
DR   GeneTree; ENSGT00940000156273; -.
DR   HOGENOM; CLU_044656_0_0_1; -.
DR   InParanoid; Q5R6L8; -.
DR   OrthoDB; 1259741at2759; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000001595; Chromosome 1.
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; IEA:InterPro.
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_0000230997"
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"
FT   CONFLICT        179
FT                   /note="T -> A (in Ref. 1; CAH92429)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   395 AA;  45211 MW;  960AA8B822CBA4BB CRC64;
     MAVTDSLSRA ASTLAAVLLL SFGSVAASHI EDQAEQFFRS GHTNNWAVLV CTSRFWFNYR
     HVANTLSVYR SVKRLGIPDS HIVLMLADDM ACNPRNPKPA TVFSHKNMEL NVYGDDVEVD
     YRSYEVTVEN FLRVLTGRIP PSTPRSKRLL SDDRSNILIY MTGHGGNGFL KFQDSEEITN
     IELADAFEQM WQKRRYNELL FIIDTCQGAS MYERFYSPNI MALASSQVGE DSLSHQPDPA
     IGVHLMDRYT FYVLEFLEEI NPASQTNMND LFQVCPKSLC VSTPGHRTDL FQRDPKNVLI
     TDFFGSVRKV EITTETIKLQ QDSEIMESSY KEDQMDEELM EPLKYAEQLP VAQIIHQKPK
     LKDWHPPGGF ILGLWALIIM VFFKTYGIKH MKFIF