Pigk
entrez
329777
canonical
uniprot
Q9CXY9
canonical
ensembl
ENSMUSG00000039047
resolver
ensp
ENSMUSP00000045351
resolver
ensp
ENSMUSP00000123772
resolver
ensp
ENSMUSP00000123899
resolver
ensp
ENSMUSP00000341990
resolver
enst
ENSMUST00000045029
resolver
enst
ENSMUST00000159899
resolver
enst
ENSMUST00000162642
resolver
genesymbol
Pigk
resolver
uniprot
F6V048
resolver
uniprot
F8WH03
resolver
uniprot
Q8BH63
resolver
uniprot
Q8BL63
resolver
uniprot
Q8BXX3
resolver
uniprot_entry
F6V048_MOUSE
resolver
uniprot_entry
F8WH03_MOUSE
resolver
uniprot_entry
GPI8_MOUSE
resolver
uniprot_entry
Q8BL63_MOUSE
resolver
uniprot_entry
Q8BXX3_MOUSE
resolver
uniprot_sec
Q8BH63
resolver
activity_regulation
ACTIVITY REGULATION: In the absence of proproteins substrates, exists in an inactive state with a disrupted catalytic site by an autoinhibitory loop. The binding of proprotein substrates, particularly the CSP region, to GPI-T triggers concerted conformational changes that alleviate the inhibition by the autoinhibitory loop. Meanwhile, proprotein residues near the omega- site induce the formation of a catalytic cleft for catalysis, following which the products are released and GPI-T reverts to the inactive state. {ECO:0000250|UniProtKB:Q92643}.
uniprot
proteins
amino_acid_sequence
MAAPCFLTLRVATLAALALLSLGSSAAGHIEDQAEQFFRSGHTNNWAVLVCTSRFWFNYRHVANTLSVYRSVKRLGIPDSHIVLMLADDMACNARNPKPATVFSHKNMELNVYGDDVEVDYRSYEVTVENFLRVLTGRVPPSTPRSKRLLSDDRSNILIYMTGHGGNGFLKFQDSEEITNIELADAFEQMWQKRRYNELLFIIDTCQGASMYERFYSPNIMALASSQVGEDSLSHQPDPAIGVHLMDRYTFYVLEFLEEINPASQTNMNDLFQVCPKSLCVSTPGHRTDLFQRDPKNVLITDFFGSVRKVEITTEKISLQWDSQVVDSSSKEDGTAEERMGPLKYAEQLPVAQIIHQKPKPRDWHPPGGFILGLWALIIMVFFKTYGIKHMKFIF
uniprot
proteins
ec_number
2.6.1.-
uniprot
proteins
function
FUNCTION: Catalytic subunit of the glycosylphosphatidylinositol-anchor (GPI-anchor) transamidase (GPI-T) complex that catalyzes the formation of the linkage between a proprotein and a GPI-anchor and participates in GPI anchored protein biosynthesis. Recognizes diverse proproteins at a C-terminal signal peptide (CSP) region that lacks consensus sequence and replaces it with a GPI-anchor via a transamidation reaction. Transamidation catalysis reaction follows a two-phase mechanism. In the acyl-enzyme phase, the carbonyl group of the proproteins's omega-site undergoes a nucleophilic attack forming an enzyme-substrate thioester bond. Followed by a general acid catalysis that allows CSP releasing, regenerating the carbonyl, and forming the acyl-enzyme intermediate. In the GPI-anchor attachment phase, the amino group of the GPI-anchor's ethanolamine phosphate, the one on third mannose (EtNP3), mediates a nucleophilic attack on the carbonyl of the acyl-enzyme intermediate, replacing the CSP, allowing GPI-anchor attachment to the omega-residue, therefore forming the product and freeing the enzyme. {ECO:0000250|UniProtKB:Q92643}.
uniprot
proteins
mass_dalton
44895
uniprot
proteins
pathway_participation
PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis. {ECO:0000250|UniProtKB:Q92643}.
uniprot
proteins
post_translational_modification
PTM: The disulfide bond between PIGK/GPI8 and PIGT is important for normal enzyme activity. {ECO:0000250|UniProtKB:Q92643}.
uniprot
proteins
protein_family
Peptidase C13 family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
21183079
uniprot
proteins
sequence_length
395
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q92643}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q92643}.
uniprot
proteins
transmembrane_region
TRANSMEM 369..385; /note="Helical"; /evidence="ECO:0000250|UniProtKB:Q92643
uniprot
proteins