GAA1_YEAST
ID GAA1_YEAST Reviewed; 614 AA.
AC P39012; D6VY88;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=GPI transamidase component GAA1;
GN Name=GAA1; Synonyms=END2; OrderedLocusNames=YLR088W; ORFNames=L9449.4;
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], AND MUTAGENESIS OF ASN-87.
RX PubMed=7730400; DOI=10.1083/jcb.129.3.629;
RA Hamburger D., Egerton M., Riezman H.;
RT "Yeast Gaa1p is required for attachment of a completed GPI anchor onto
RT proteins.";
RL J. Cell Biol. 129:629-639(1995).
RN [2]
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 [3]
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 [4]
RP SUBUNIT.
RX PubMed=11598210; DOI=10.1091/mbc.12.10.3295;
RA Fraering P., Imhof I., Meyer U., Strub J.-M., van Dorsselaer A.,
RA Vionnet C., Conzelmann A.;
RT "The GPI transamidase complex of Saccharomyces cerevisiae contains Gaa1p,
RT Gpi8p, and Gpi16p.";
RL Mol. Biol. Cell 12:3295-3306(2001).
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).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Component of the GPI transamidase complex. Required for a
CC terminal step of GPI anchor attachment onto proteins. Affects
CC endocytosis.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis.
CC -!- SUBUNIT: Forms a complex with CDC91, GPI17, GPI16 and GPI8.
CC {ECO:0000269|PubMed:11598210}.
CC -!- INTERACTION:
CC P39012; P38875: GPI16; NbExp=3; IntAct=EBI-7252, EBI-24869;
CC P39012; P49018: GPI8; NbExp=3; IntAct=EBI-7252, EBI-7822;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein.
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DR EMBL; X79409; CAA55944.1; -; Genomic_DNA.
DR EMBL; U53880; AAB67592.1; -; Genomic_DNA.
DR EMBL; Z73260; CAA97649.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09404.1; -; Genomic_DNA.
DR PIR; S45053; S45053.
DR RefSeq; NP_013189.1; NM_001181975.1.
DR AlphaFoldDB; P39012; -.
DR SMR; P39012; -.
DR BioGRID; 31361; 200.
DR ComplexPortal; CPX-1275; GPI-anchor transamidase complex.
DR DIP; DIP-4824N; -.
DR IntAct; P39012; 10.
DR MINT; P39012; -.
DR STRING; 4932.YLR088W; -.
DR MaxQB; P39012; -.
DR PaxDb; P39012; -.
DR PRIDE; P39012; -.
DR EnsemblFungi; YLR088W_mRNA; YLR088W; YLR088W.
DR GeneID; 850777; -.
DR KEGG; sce:YLR088W; -.
DR SGD; S000004078; GAA1.
DR VEuPathDB; FungiDB:YLR088W; -.
DR eggNOG; KOG3566; Eukaryota.
DR GeneTree; ENSGT00390000013685; -.
DR HOGENOM; CLU_007442_3_1_1; -.
DR InParanoid; P39012; -.
DR OMA; RESEWNI; -.
DR BioCyc; YEAST:G3O-32239-MON; -.
DR UniPathway; UPA00196; -.
DR PRO; PR:P39012; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P39012; 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; IDA:SGD.
DR GO; GO:0016255; P:attachment of GPI anchor to protein; IMP:UniProtKB.
DR GO; GO:0031505; P:fungal-type cell wall organization; IC:ComplexPortal.
DR InterPro; IPR007246; Gaa1.
DR PANTHER; PTHR13304; PTHR13304; 1.
DR Pfam; PF04114; Gaa1; 1.
DR PIRSF; PIRSF036762; GAA1; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; GPI-anchor biosynthesis; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..614
FT /note="GPI transamidase component GAA1"
FT /id="PRO_0000087417"
FT TOPO_DOM 1..19
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 41..356
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 357..377
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 378..394
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 416..464
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 465..485
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 486..535
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 536..556
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 557..577
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 578..598
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 599..614
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOTIF 610..614
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT MUTAGEN 87
FT /note="N->A: Loss of N-glycosylation."
FT /evidence="ECO:0000269|PubMed:7730400"
SQ SEQUENCE 614 AA; 69221 MW; E1B5E900AC6D2988 CRC64;
MALLEKLHRR IVDMGLVPRI IALLPVISML CALFGFISIA ILPMDGQYRR TYISENALMP
SQAYSYFRES EWNILRGYRS QIKEMVNMTS MERNNLMGSW LQEFGTKTAI YENEQYGETL
YGVMHAPRGD GTEAMVLAVP WFNSDDEFNI GGAALGVSLA RFFSRWPVWS KNIIVVFSEN
PRAALRSWVE AYHTSLDLTG GSIEAAVVLD YSSTEDFFEY VEISYDGLNG ELPNLDLVNI
AISITEHEGM KVSLHGLPSD QLTNNNFWSR LKILCLGIRD WALSGVKKPH GNEAFSGWRI
QSVTLKAHGN SGHDITTFGR IPEAMFRSIN NLLEKFHQSF FFYLLLAPRQ FVSISSYLPS
AVALSIAFAI SSLNAFINNA YANISLFSEY NLVALLVWFV SLVISFVVSQ AFLLIPSSGL
LMTISMASCF LPLILSRKIH ISEPLSYRLK NVAFLYFSLV STSLLMINFA MALLIGTLAF
PMTFVKTIVE SSSEHEVTTQ SSNPIKTEPK DEIELVENHM DTTPATPQQQ KQKLKNLVLL
ILTNPFISIT LFGLFFDDEF HGFDIINKLV SAWLDLKCWS WFVLCIGWLP CWLLILASSF
ESKSVVVRSK EKQS
