GPI13_ASHGO
ID GPI13_ASHGO Reviewed; 1013 AA.
AC Q74ZS2;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=GPI ethanolamine phosphate transferase 3;
DE EC=2.-.-.-;
DE AltName: Full=Glycosylphosphatidylinositol-anchor biosynthesis protein 13;
GN Name=GPI13; OrderedLocusNames=AGR126C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 169; 174-175 AND 183.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
CC -!- FUNCTION: Involved in glycosylphosphatidylinositol-anchor biosynthesis.
CC Transfers ethanolamine phosphate to the GPI third mannose which links
CC the GPI-anchor to the C-terminus of the proteins by an amide bond.
CC Involved in cell wall biosynthesis (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PIGG/PIGN/PIGO family. PIGO subfamily.
CC {ECO:0000305}.
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DR EMBL; AE016820; AAS54616.2; -; Genomic_DNA.
DR RefSeq; NP_986792.2; NM_211854.2.
DR AlphaFoldDB; Q74ZS2; -.
DR SMR; Q74ZS2; -.
DR STRING; 33169.AAS54616; -.
DR EnsemblFungi; AAS54616; AAS54616; AGOS_AGR126C.
DR GeneID; 4623094; -.
DR KEGG; ago:AGOS_AGR126C; -.
DR eggNOG; KOG2126; Eukaryota.
DR HOGENOM; CLU_004298_1_0_1; -.
DR InParanoid; Q74ZS2; -.
DR OMA; FMNAVYW; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000000591; Chromosome VII.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0051377; F:mannose-ethanolamine phosphotransferase activity; IBA:GO_Central.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IBA:GO_Central.
DR CDD; cd16023; GPI_EPT_3; 1.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR002591; Phosphodiest/P_Trfase.
DR InterPro; IPR037675; PIG-O_N.
DR InterPro; IPR039524; PIGO/GPI13.
DR PANTHER; PTHR23071; PTHR23071; 1.
DR Pfam; PF01663; Phosphodiest; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation; Endoplasmic reticulum; Glycoprotein;
KW GPI-anchor biosynthesis; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..1013
FT /note="GPI ethanolamine phosphate transferase 3"
FT /id="PRO_0000240362"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 447..467
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 484..504
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 515..535
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 558..578
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 582..602
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 643..663
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 682..702
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 715..735
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 761..781
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 802..822
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 825..845
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 868..888
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 899..919
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 943..963
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 977..997
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 399
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 423
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 539
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 707
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 742
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 750
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 755
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1013 AA; 114501 MW; 779C5EE83B725A8D CRC64;
MQEQIEGAVD EELLKQSVLN NDEDDRRLTK LRIERFRTTH TLYIFLYSAL AALQFIAIAF
FTRGFLLSRK VLDDVANRDE STAPAKFDRL VLLVVDALRF DFVIPVDVAA EGYNSHYHNH
LRALYERWDE SILLKFLADP PTTTLQRLKG LTTGSLPTFI DAGSNFNGDV IDEDNIIKQM
CLNNKTIYFA GDDTWDALFH PYLSNVSMPY ESLNVWDLDT VDNGVISFFE DHLLNNPTEK
KEWDVLVGHM LGIDHVGHKY GPSHFSMAEK QSQVDGFIRQ IIDAVDEDTL LVVMGDHGMD
HTGNHGGDSP AELESTLWLY TKRPGTWRRQ APAAYNTTEL GRYYRAVNQI DLVPSLSLLL
GLPIPFNNLG WPIEELAHDD DEWRLFTRQT LMQLETYRNT SNSITDSSKL KILEELKINA
NSNSSDAGNY QAILLEMYKD LWARFDYYSI GTGIILLIIS LAMLITITRL IPSIVVGQML
SELVPTIIVM PLVSNVCFLG VFYVLRQPAF LQNWLWASLL ATAVGIIIGF YVPIFDRYNL
TWLVLRFGEE LSDYWSRVAA FLITLHALIF TSNSFTIWED KIVSFSLTTL GMLTLYEFVF
LPKRHSTSAI LAAALGEKEG TVSGISSGQA NSDSLPLGRF ARIVGGYHSI VLIVCTRLAS
LITICREEQG AYCTPTFTLT NNYSFSVMLG CLFLVFATPA CIKGYYNVSS SYQAAAPIWI
GMLMKSILFV NFIYWELKTF ENTSDTHGLN LTIFNLTISR IVVGVSLVAA NIGWMMGPLC
IKLNVHNNDR RSQQATILGY ANAYGAQYFL LVINFFMCIL LFNKPLAQLS LFLMCNQLLS
ILEIFDLLKL KENLIGPVAL GLLSYQQFFS TGHQATIPAV QWDMGFILTE RITFPFTHLG
IVLNTFGPHI LCGISVALLT LWKQPPGILR ANTLLARVVS NCGMLLIYQT VLCLSTFIWV
TNFRRHLMVW KIFCPRFMFA ALSLIVTQLV LTFITIAFAS GRLIKQIDRM FWK
