PIGU_SCHPO
ID PIGU_SCHPO Reviewed; 408 AA.
AC O13883; Q9UUK5;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=GPI transamidase component GAB1 homolog;
GN ORFNames=SPAC1952.01, SPAC1B3.19;
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 [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: Component of the GPI transamidase complex. May be involved in
CC the recognition of either the GPI attachment signal or the lipid
CC portion of GPI (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis.
CC -!- SUBUNIT: Forms a complex with PIG-S homolog, PIG-T homolog and GPI8.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the PIGU family. {ECO:0000305}.
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DR EMBL; CU329670; CAB11245.1; -; Genomic_DNA.
DR PIR; T37929; T37929.
DR RefSeq; XP_001713115.1; XM_001713063.2.
DR AlphaFoldDB; O13883; -.
DR SMR; O13883; -.
DR BioGRID; 280615; 2.
DR STRING; 4896.SPAC1952.01.1; -.
DR PaxDb; O13883; -.
DR EnsemblFungi; SPAC1952.01.1; SPAC1952.01.1:pep; SPAC1952.01.
DR PomBase; SPAC1952.01; -.
DR VEuPathDB; FungiDB:SPAC1952.01; -.
DR eggNOG; KOG2552; Eukaryota.
DR HOGENOM; CLU_030193_0_0_1; -.
DR InParanoid; O13883; -.
DR OMA; ALWHLWI; -.
DR PhylomeDB; O13883; -.
DR UniPathway; UPA00196; -.
DR PRO; PR:O13883; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0042765; C:GPI-anchor transamidase complex; ISO:PomBase.
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 InterPro; IPR009600; PIG-U.
DR PANTHER; PTHR13121; PTHR13121; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; GPI-anchor biosynthesis; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..408
FT /note="GPI transamidase component GAB1 homolog"
FT /id="PRO_0000121397"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..359
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 247..267
FT /note="May be involved in recognition of long-chain fatty
FT acids in GPI"
FT /evidence="ECO:0000250"
SQ SEQUENCE 408 AA; 46659 MW; F261ED1D70EE155C CRC64;
MIPNEKLKLL GLLSISFFLQ WYLANTWIAE FLYRRIEVST PVSGFLRVRE GLYLYENGLD
PYSGGVFYQS PLLLILNYCC ELLGGISVTR FVYTSISTMG GLFVYLIAKQ ARVLDPNQVL
STCSPLWISV IYLLNPLTFL PGIACSADMI LNFTTLMTIY FASCGSYAIY ACCMALTVFI
NPNALLLFFP SYLILRKCNS SIKFRQIFVV FLFYLAGLII TSGFFLNSLS FLKIPFRVYL
DSHDLTPNLG LWWYFFTEMF NEFRTFFLFV FAILPLMFVL PVSIRLYYLP LPITIALIGL
HSLFKAYPSI CDLSIFLSLL PIFNKVQDRM RYSLLTNNAI VFALVLGSAF YHSWITLGCG
NANFYYASNL ILALGLSLKI MDFLKALLLV DWYANHPQHE NIPLKQVQ
