ID   A6NEM5_HUMAN            Unreviewed;       332 AA.
AC   A6NEM5;
DT   24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 1.
DT   16-JAN-2019, entry version 76.
DE   RecName: Full=GPI-anchor transamidase {ECO:0000256|RuleBase:RU365060};
DE            Short=GPI transamidase {ECO:0000256|RuleBase:RU365060};
DE            EC=3.-.-.- {ECO:0000256|RuleBase:RU365060};
DE   AltName: Full=Phosphatidylinositol-glycan biosynthesis class K protein {ECO:0000256|RuleBase:RU365060};
GN   Name=PIGK {ECO:0000256|RuleBase:RU365060,
GN   ECO:0000313|Ensembl:ENSP00000352041};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000352041, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000352041, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA   Hammond S., Harrison E.S., Hart E., Haugen E., Heath P.D., Holmes S.,
RA   Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J.,
RA   James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K.,
RA   Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G.,
RA   Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J.,
RA   Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L.,
RA   Matthews N.S., McLaren S., Milne S., Mistry S., Moore M.J.,
RA   Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A.,
RA   Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K.,
RA   Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G.,
RA   Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S.,
RA   Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N.,
RA   Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S.,
RA   Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L.,
RA   Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.,
RA   Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T.,
RA   Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R., Banerjee R.,
RA   Bryant S.P., Burford D.C., Burrill W.D., Clegg S.M., Dhami P.,
RA   Dovey O., Faulkner L.M., Gribble S.M., Langford C.F., Pandian R.D.,
RA   Porter K.M., Prigmore E.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [2] {ECO:0000213|PubMed:21269460}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Burckstummer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [3] {ECO:0000313|Ensembl:ENSP00000352041}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2011) to UniProtKB.
RN   [4] {ECO:0000213|PubMed:25944712}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
RA   Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
CC   -!- FUNCTION: Mediates GPI anchoring in the endoplasmic reticulum, by
CC       replacing a protein's C-terminal GPI attachment signal peptide
CC       with a pre-assembled GPI. During this transamidation reaction, the
CC       GPI transamidase forms a carbonyl intermediate with the substrate
CC       protein. {ECO:0000256|RuleBase:RU365060}.
CC   -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-
CC       anchor biosynthesis. {ECO:0000256|RuleBase:RU365060}.
CC   -!- SUBUNIT: Forms a complex with PIGT, PIGS, PIGU and GAA1.
CC       {ECO:0000256|RuleBase:RU365060}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|RuleBase:RU365060}; Single-pass type I membrane
CC       protein {ECO:0000256|RuleBase:RU365060}.
CC   -!- SIMILARITY: Belongs to the peptidase C13 family.
CC       {ECO:0000256|RuleBase:RU365060}.
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DR   EMBL; AC093433; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC113935; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL035409; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KC876885; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   ProteinModelPortal; A6NEM5; -.
DR   jPOST; A6NEM5; -.
DR   MaxQB; A6NEM5; -.
DR   PeptideAtlas; A6NEM5; -.
DR   PRIDE; A6NEM5; -.
DR   Ensembl; ENST00000359130; ENSP00000352041; ENSG00000142892.
DR   UCSC; uc001dhl.2; human.
DR   EuPathDB; HostDB:ENSG00000142892.14; -.
DR   HGNC; HGNC:8965; PIGK.
DR   OpenTargets; ENSG00000142892; -.
DR   eggNOG; KOG1349; Eukaryota.
DR   eggNOG; COG5206; LUCA.
DR   GeneTree; ENSGT00940000156273; -.
DR   HOGENOM; HOG000204398; -.
DR   HOVERGEN; HBG027488; -.
DR   UniPathway; UPA00196; -.
DR   ChiTaRS; PIGK; human.
DR   Proteomes; UP000005640; Chromosome 1.
DR   Bgee; ENSG00000142892; Expressed in 216 organ(s), highest expression level in corpus callosum.
DR   ExpressionAtlas; A6NEM5; baseline and differential.
DR   GO; GO:0042765; C:GPI-anchor transamidase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003923; F:GPI-anchor transamidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016255; P:attachment of GPI anchor to protein; IEA:UniProtKB-UniRule.
DR   InterPro; IPR028361; GPI_transamidase.
DR   InterPro; IPR001096; Peptidase_C13.
DR   PANTHER; PTHR12000; PTHR12000; 1.
DR   PANTHER; PTHR12000:SF1; PTHR12000:SF1; 1.
DR   Pfam; PF01650; Peptidase_C13; 1.
DR   PRINTS; PR00776; HEMOGLOBNASE.
PE   1: Evidence at protein level;
KW   Complete proteome {ECO:0000313|Proteomes:UP000005640};
KW   GPI-anchor biosynthesis {ECO:0000256|RuleBase:RU365060};
KW   Hydrolase {ECO:0000256|RuleBase:RU365060};
KW   Protease {ECO:0000256|RuleBase:RU365060};
KW   Proteomics identification {ECO:0000213|EPD:A6NEM5,
KW   ECO:0000213|MaxQB:A6NEM5, ECO:0000213|PeptideAtlas:A6NEM5};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW   Signal {ECO:0000256|RuleBase:RU365060};
KW   Thiol protease {ECO:0000256|RuleBase:RU365060}.
FT   SIGNAL        1     27       {ECO:0000256|RuleBase:RU365060}.
FT   CHAIN        28    332       GPI-anchor transamidase.
FT                                {ECO:0000256|RuleBase:RU365060}.
FT                                /FTId=PRO_5016190012.
SQ   SEQUENCE   332 AA;  37786 MW;  BDBEA656D0B1069B CRC64;
     MAVTDSLSRA ATVLATVLLL 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 QDSEIMESRY SS
//