GPI16_YEAST
ID GPI16_YEAST Reviewed; 610 AA.
AC P38875; D3DLD6;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=GPI transamidase component GPI16;
DE Flags: Precursor;
GN Name=GPI16; OrderedLocusNames=YHR188C;
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=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
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 FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
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 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).
CC -!- FUNCTION: Component of the GPI transamidase complex. Involved in
CC transfer of GPI to proteins. {ECO:0000269|PubMed:11483512,
CC ECO:0000269|PubMed:11598210}.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis.
CC -!- SUBUNIT: Forms a complex with CDC91, GPI17, GPI8 and GAA1.
CC {ECO:0000269|PubMed:11598210}.
CC -!- INTERACTION:
CC P38875; P39012: GAA1; NbExp=3; IntAct=EBI-24869, EBI-7252;
CC P38875; Q04080: GPI17; NbExp=3; IntAct=EBI-24869, EBI-7777;
CC P38875; P49018: GPI8; NbExp=3; IntAct=EBI-24869, EBI-7822;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:11598210}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:11598210}.
CC -!- PTM: The disulfide bond between GPI8 and GPI16 is important for normal
CC enzyme activity. {ECO:0000250}.
CC -!- MISCELLANEOUS: Present with 1680 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the PIGT family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-9 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB68365.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U00030; AAB68365.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006934; DAA06880.1; -; Genomic_DNA.
DR PIR; S46687; S46687.
DR RefSeq; NP_012058.1; NM_001179319.1.
DR AlphaFoldDB; P38875; -.
DR SMR; P38875; -.
DR BioGRID; 36622; 527.
DR ComplexPortal; CPX-1275; GPI-anchor transamidase complex.
DR DIP; DIP-1888N; -.
DR IntAct; P38875; 17.
DR MINT; P38875; -.
DR STRING; 4932.YHR188C; -.
DR iPTMnet; P38875; -.
DR MaxQB; P38875; -.
DR PaxDb; P38875; -.
DR PRIDE; P38875; -.
DR EnsemblFungi; YHR188C_mRNA; YHR188C; YHR188C.
DR GeneID; 856595; -.
DR KEGG; sce:YHR188C; -.
DR SGD; S000001231; GPI16.
DR VEuPathDB; FungiDB:YHR188C; -.
DR eggNOG; KOG2407; Eukaryota.
DR GeneTree; ENSGT00390000018558; -.
DR HOGENOM; CLU_021459_2_1_1; -.
DR InParanoid; P38875; -.
DR OMA; LWAWIDA; -.
DR BioCyc; YEAST:YHR188C-MON; -.
DR UniPathway; UPA00196; -.
DR PRO; PR:P38875; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38875; 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:0030176; C:integral component of endoplasmic reticulum membrane; 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; IPR007245; PIG-T.
DR PANTHER; PTHR12959; PTHR12959; 1.
DR Pfam; PF04113; Gpi16; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW GPI-anchor biosynthesis; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..610
FT /note="GPI transamidase component GPI16"
FT /id="PRO_0000024110"
FT TOPO_DOM 20..551
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 552..572
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 573..610
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11598210"
FT DISULFID 202
FT /note="Interchain (with C-85 in GPI8)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 610 AA; 68771 MW; E9613CE0EA99F963 CRC64;
MILTLAYFML GTLLLGVFAE DTVSQIGIND SLWYPYDEAL VLKPLPNNDL LLSFAFQLQS
EPFDPAVSSM SYDAYEHYTT FPRAIPPLLE STATRQFHLR FTRGFWDALS WGQLPHAGKE
AGASGVELWS QVQAMDQEQA FHNWKKLSNS LSGLFCSSLN FIDESRTTFP RRSYASDIGA
PLFNSTEKLY LMRASLPNEP ICTENLTPFI KLLPTRGKSG LTSLLDGHKL FDSLWNSISL
DIATICSEDE DALCHYEMDA RIEMVTHVPS ALARGERPIP KPLDGNTLRC DTDKPFDSYQ
CFPLPEPSQT HFKLSQLFAR PINNGNLFAN RPTRICAEVD RSTWTAFLSV DDTIFSTHDN
CFDLSNDQNE GGSGYDFILE STDTTKVTPI VPVPIHVSRS LTGNGQDRGG MRIVFHNDND
TPVKLIYFES LPWFMRVYLS SLQITSTTSP QLQENDIILD KYYLQAADRK RPGHLEFTML
IPANTDIVMT YQFDKALLQF AEYPPDANHG FEIDAAVITV LSLESSSSLY EMRTSTLLLS
LSTPDFSMPY NVIILTSTIM GLIFGMLYNL MVKRMVTVEE ADKITLQSGL KYKLLKLKEK
FLGKKKTKTD
