GPI8_SCHPO
ID GPI8_SCHPO Reviewed; 380 AA.
AC Q9USP5;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=GPI-anchor transamidase;
DE Short=GPI transamidase;
DE EC=3.-.-.-;
DE Flags: Precursor;
GN Name=gpi8; ORFNames=SPCC11E10.02c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11124699;
RX DOI=10.1002/1097-0061(200101)18:1<33::aid-yea648>3.0.co;2-z;
RA Shams-Eldin H., Azzouz N., Eckert V., Blaschke T., Kedees M.H., Huebel A.,
RA Schwarz R.T.;
RT "The Schizosaccharomyces pombe GPI8 gene complements a Saccharomyces
RT cerevisiae GPI8 anchoring mutant.";
RL Yeast 18:33-39(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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 PIG-T homolog, PIG-U homolog and PIG-S
CC homolog. {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; AJ250428; CAC13970.1; -; mRNA.
DR EMBL; CU329672; CAB57844.1; -; Genomic_DNA.
DR PIR; T40853; T40853.
DR RefSeq; NP_588198.1; NM_001023188.2.
DR AlphaFoldDB; Q9USP5; -.
DR SMR; Q9USP5; -.
DR STRING; 4896.SPCC11E10.02c.1; -.
DR MEROPS; C13.005; -.
DR MaxQB; Q9USP5; -.
DR PaxDb; Q9USP5; -.
DR EnsemblFungi; SPCC11E10.02c.1; SPCC11E10.02c.1:pep; SPCC11E10.02c.
DR GeneID; 2539272; -.
DR KEGG; spo:SPCC11E10.02c; -.
DR PomBase; SPCC11E10.02c; gpi8.
DR VEuPathDB; FungiDB:SPCC11E10.02c; -.
DR eggNOG; KOG1349; Eukaryota.
DR HOGENOM; CLU_044656_2_1_1; -.
DR InParanoid; Q9USP5; -.
DR OMA; PGHTNNW; -.
DR PhylomeDB; Q9USP5; -.
DR UniPathway; UPA00196; -.
DR PRO; PR:Q9USP5; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0042765; C:GPI-anchor transamidase complex; ISO:PomBase.
DR GO; GO:0003923; F:GPI-anchor transamidase activity; ISO:PomBase.
DR GO; GO:0016255; P:attachment of GPI anchor to protein; ISO:PomBase.
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; Glycoprotein;
KW GPI-anchor biosynthesis; Hydrolase; Membrane; Protease; Reference proteome;
KW Signal; Thiol protease; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..380
FT /note="GPI-anchor transamidase"
FT /id="PRO_0000026531"
FT TOPO_DOM 20..354
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 376..380
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 145
FT /evidence="ECO:0000250"
FT ACT_SITE 187
FT /evidence="ECO:0000250"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 73
FT /note="Interchain (with C-182 in PIGT)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 380 AA; 43206 MW; D5069E1F76330B72 CRC64;
MIVQFVALLL LNLLQIIAAE SSHTNNWAVL ISTSRFWFNY RHTANVLGIY RSVKRLGIPD
SQIILMIADD YACNSRNLFP GTVFDNADRA LDLYGEEIEI DYKGYEVTVE AFIRLLTERV
PENTPASKRL LTNERSNILI YMTGHGGDGF IKFQDAEELS SEDLADAIEQ IHQHKRYNEI
LFMVDTCQAN SLYTKIYSPN VLAIGSSEVG TSSYSHHADI DIGVAVIDRF TFSNLEFLEN
RVDSKSKLTM QDLINSYNPY EIHSTPGVQP INLRRSPDDI LITDFFGNVR DIELHSEKIN
WMLPGENTTK PSIKRNSFVF QAQNDMQDDG KGFGISNLKS FLPPTRELKY KKHPISRIIS
AVVCISFSIG FPYYASKYLK
