CDC91_YEAST
ID CDC91_YEAST Reviewed; 394 AA.
AC P41733; D6VZ92;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=GPI transamidase component GAB1;
DE AltName: Full=Cell division control protein 91;
GN Name=GAB1; Synonyms=CDC91; OrderedLocusNames=YLR459W; ORFNames=L9122.2;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Bi E., Pringle J.R.;
RT "Sequencing and characterization of CDC91.";
RL Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBUNIT.
RX PubMed=12802054; DOI=10.1091/mbc.e02-12-0794;
RA Hong Y., Ohishi K., Kang J.Y., Tanaka S., Inoue N., Nishimura J., Maeda Y.,
RA Kinoshita T.;
RT "Human PIG-U and yeast Cdc91p are the fifth subunit of GPI transamidase
RT that attaches GPI-anchors to proteins.";
RL Mol. Biol. Cell 14:1780-1789(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
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. {ECO:0000269|PubMed:12802054}.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis.
CC -!- SUBUNIT: Forms a complex with GPI16, GPI17, GPI8 and GAA1.
CC {ECO:0000269|PubMed:12802054}.
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; L31649; AAA34487.1; -; Genomic_DNA.
DR EMBL; U22383; AAB64722.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09758.1; -; Genomic_DNA.
DR PIR; S48522; S48522.
DR RefSeq; NP_013564.1; NM_001182347.1.
DR AlphaFoldDB; P41733; -.
DR SMR; P41733; -.
DR BioGRID; 31717; 589.
DR ComplexPortal; CPX-1275; GPI-anchor transamidase complex.
DR DIP; DIP-4553N; -.
DR IntAct; P41733; 2.
DR STRING; 4932.YLR459W; -.
DR PaxDb; P41733; -.
DR PRIDE; P41733; -.
DR EnsemblFungi; YLR459W_mRNA; YLR459W; YLR459W.
DR GeneID; 851181; -.
DR KEGG; sce:YLR459W; -.
DR SGD; S000004451; GAB1.
DR VEuPathDB; FungiDB:YLR459W; -.
DR eggNOG; KOG2552; Eukaryota.
DR GeneTree; ENSGT00390000014941; -.
DR HOGENOM; CLU_030193_0_1_1; -.
DR InParanoid; P41733; -.
DR OMA; ALWHLWI; -.
DR BioCyc; YEAST:G3O-32511-MON; -.
DR UniPathway; UPA00196; -.
DR PRO; PR:P41733; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P41733; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IC:ComplexPortal.
DR GO; GO:0042765; C:GPI-anchor transamidase complex; IMP:SGD.
DR GO; GO:0016255; P:attachment of GPI anchor to protein; IMP:SGD.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0031505; P:fungal-type cell wall organization; IC:ComplexPortal.
DR GO; GO:0034394; P:protein localization to cell surface; IBA:GO_Central.
DR InterPro; IPR009600; PIG-U.
DR PANTHER; PTHR13121; PTHR13121; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Endoplasmic reticulum; GPI-anchor biosynthesis;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..394
FT /note="GPI transamidase component GAB1"
FT /id="PRO_0000121398"
FT TOPO_DOM 1..135
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 157..160
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 182..190
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 212..224
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 246..250
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 272..297
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 319..324
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 346..351
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 352..372
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 373..394
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 235..255
FT /note="May be involved in recognition of long-chain fatty
FT acids in GPI"
FT /evidence="ECO:0000250"
SQ SEQUENCE 394 AA; 44741 MW; 75F4BD39FF871A58 CRC64;
MDSTALKVAL GCIAIRLAVN SLFPSLQQQL DQSVEFSTPV TSFRSLQEGI YLLRNNIQVY
NHGVVHHPPI LIFFLSLFNS DRLISLIYAL IDGLIAYQLT EVTKAFKNLK LKVWLPGLLY
AVNPLTLLSC ISRSSIIFTN FAISSSLYCI LAEGNVLLSS VMISISGYLS VYPILLLIPL
LGMLKSWRQR ILSAIVSILS LLILLLFSYS ILGSQSWSFL TQVYGSIITF EKVFPNLGLW
WYFFIEMFDT FIPFFKAVFN IFIAVFITPF TLRYHKQPFY AFILCIGWIV LTKPYPSLGD
AGFFFSFLPF FTPLFGYLRY PIISALLFLH AIVLAPIFYH LWVVLGSGNS NFFYAISLVY
ALAIASILVD LNWAMLRIEY DNGIPNFKLK VTQI
