GPI17_YEAST
ID GPI17_YEAST Reviewed; 534 AA.
AC Q04080; D6VT61;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=GPI transamidase component GPI17;
GN Name=GPI17; OrderedLocusNames=YDR434W; ORFNames=D9461.20;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
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 [3]
RP FUNCTION.
RX PubMed=11483512; DOI=10.1093/emboj/20.15.4088;
RA Ohishi K., Inoue N., Kinoshita T.;
RT "PIG-S and PIG-T, essential for GPI anchor attachment to proteins, form a
RT complex with GAA1 and GPI8.";
RL EMBO J. 20:4088-4098(2001).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
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).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS].
RX PubMed=19756047; DOI=10.1038/msb.2009.64;
RA Kung L.A., Tao S.-C., Qian J., Smith M.G., Snyder M., Zhu H.;
RT "Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals
RT new roles for protein glycosylation in eukaryotes.";
RL Mol. Syst. Biol. 5:308-308(2009).
CC -!- FUNCTION: Component of the GPI transamidase complex. Involved in
CC transfer of GPI to proteins. {ECO:0000269|PubMed:11483512}.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis.
CC -!- SUBUNIT: Forms a complex with CDC91, GPI16, GPI8 and GAA1.
CC -!- INTERACTION:
CC Q04080; P38875: GPI16; NbExp=3; IntAct=EBI-7777, EBI-24869;
CC Q04080; P49018: GPI8; NbExp=4; IntAct=EBI-7777, EBI-7822;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:19756047}.
CC -!- MISCELLANEOUS: Present with 7520 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the PIGS family. {ECO:0000305}.
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DR EMBL; U33007; AAB64866.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12271.1; -; Genomic_DNA.
DR PIR; S69714; S69714.
DR RefSeq; NP_010722.3; NM_001180742.3.
DR AlphaFoldDB; Q04080; -.
DR SMR; Q04080; -.
DR BioGRID; 32490; 386.
DR ComplexPortal; CPX-1275; GPI-anchor transamidase complex.
DR IntAct; Q04080; 22.
DR MINT; Q04080; -.
DR STRING; 4932.YDR434W; -.
DR MaxQB; Q04080; -.
DR PaxDb; Q04080; -.
DR PRIDE; Q04080; -.
DR EnsemblFungi; YDR434W_mRNA; YDR434W; YDR434W.
DR GeneID; 852044; -.
DR KEGG; sce:YDR434W; -.
DR SGD; S000002842; GPI17.
DR VEuPathDB; FungiDB:YDR434W; -.
DR eggNOG; KOG2459; Eukaryota.
DR GeneTree; ENSGT00390000017203; -.
DR HOGENOM; CLU_010026_1_0_1; -.
DR InParanoid; Q04080; -.
DR OMA; AEHKYAV; -.
DR BioCyc; YEAST:YDR434W-MON; -.
DR UniPathway; UPA00196; -.
DR PRO; PR:Q04080; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q04080; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IC:ComplexPortal.
DR GO; GO:0042765; C:GPI-anchor transamidase complex; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IDA:SGD.
DR GO; GO:0005637; C:nuclear inner membrane; IDA:SGD.
DR GO; GO:0016255; P:attachment of GPI anchor to protein; IMP:SGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IC:ComplexPortal.
DR InterPro; IPR019540; PtdIno-glycan_biosynth_class_S.
DR PANTHER; PTHR21072; PTHR21072; 1.
DR Pfam; PF10510; PIG-S; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; GPI-anchor biosynthesis; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..534
FT /note="GPI transamidase component GPI17"
FT /id="PRO_0000218608"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..472
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 473..493
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 494..534
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 534 AA; 60814 MW; ED5841DF382099A7 CRC64;
MSNANLRKWV GFCFVAIYLF LGVPLWYKLT TVYRASLPIN YIESLQNNKF QDIHLVIPVY
VKSDTYRFPD VHDAIQVQVN HLLNSQEQRV PWSLQVLPYN ETIEQMESEG NQFHVVTLKL
DEFIGYSSAY DTKETLVYYD DAAVLSNDLP FFVAQTLVEH TFQLEWTHLN KTCEGVSTNN
DVAISYDPNI HLSVTLLSGD GNPVAWEIEP TLTDYFSPFR KFLSPLVNFT VDSSIVYHND
LNLHSLNGSC TSVTWFDLSH TIDLSELSSM AYYPEDSALN LAIVFPSASS SPDGLAFING
TRISDEITTL DWNSYLVPQW GVIIINKMPL KPNSVISEDY LEPMMYRFAT DIFQLLGLTE
GSQDLLSPYI TIDSFKRLTI LQNLDKATET LWSLVKLTQQ FQGMSIPREV SDNVIEALDL
RLQIIDLLND PGKGGDIVWN NALHLSNELV KLCEKAFFNG EMVQQNFFPQ EHMIAVYLPL
LGPISAVMFF GFYNVMKEKN QKSKKNGTER EVAKEKLELK EAQKLHAIDG EDEL
