ID C1HCF4_PARBA Unreviewed; 869 AA.
AC C1HCF4;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 2.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=GPI ethanolamine phosphate transferase 2 {ECO:0000256|ARBA:ARBA00020830, ECO:0000256|RuleBase:RU367106};
GN ORFNames=PAAG_08445 {ECO:0000313|EMBL:EEH38718.2};
OS Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides
OS brasiliensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502779 {ECO:0000313|EMBL:EEH38718.2, ECO:0000313|Proteomes:UP000002059};
RN [1] {ECO:0000313|EMBL:EEH38718.2, ECO:0000313|Proteomes:UP000002059}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-826 / Pb01 {ECO:0000313|Proteomes:UP000002059};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
CC -!- FUNCTION: Ethanolamine phosphate transferase involved in
CC glycosylphosphatidylinositol-anchor biosynthesis. Transfers
CC ethanolamine phosphate to the GPI second mannose.
CC {ECO:0000256|RuleBase:RU367106}.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis. {ECO:0000256|ARBA:ARBA00004687,
CC ECO:0000256|RuleBase:RU367106}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU367106}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC ECO:0000256|RuleBase:RU367106}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the PIGG/PIGN/PIGO family. PIGG subfamily.
CC {ECO:0000256|ARBA:ARBA00005315, ECO:0000256|RuleBase:RU367106}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU367106}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KN294025; EEH38718.2; -; Genomic_DNA.
DR RefSeq; XP_015701179.1; XM_015846515.1.
DR AlphaFoldDB; C1HCF4; -.
DR STRING; 502779.C1HCF4; -.
DR GeneID; 9092863; -.
DR KEGG; pbl:PAAG_08445; -.
DR VEuPathDB; FungiDB:PAAG_08445; -.
DR eggNOG; KOG2125; Eukaryota.
DR HOGENOM; CLU_004770_0_0_1; -.
DR OMA; PKYLYSM; -.
DR OrthoDB; 5479199at2759; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000002059; Partially assembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051377; F:mannose-ethanolamine phosphotransferase activity; IEA:InterPro.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd16024; GPI_EPT_2; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR002591; Phosphodiest/P_Trfase.
DR InterPro; IPR037674; PIG-G_N.
DR InterPro; IPR039527; PIGG/GPI7.
DR InterPro; IPR045687; PIGG/GPI7_C.
DR PANTHER; PTHR23072:SF0; GPI ETHANOLAMINE PHOSPHATE TRANSFERASE 2; 1.
DR PANTHER; PTHR23072; PHOSPHATIDYLINOSITOL GLYCAN-RELATED; 1.
DR Pfam; PF01663; Phosphodiest; 1.
DR Pfam; PF19316; PIGO_PIGG; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU367106};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW GPI-anchor biosynthesis {ECO:0000256|ARBA:ARBA00022502,
KW ECO:0000256|RuleBase:RU367106};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367106};
KW Reference proteome {ECO:0000313|Proteomes:UP000002059};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU367106};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU367106};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU367106}.
FT TRANSMEM 442..463
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367106"
FT TRANSMEM 470..488
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367106"
FT TRANSMEM 494..510
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367106"
FT TRANSMEM 602..620
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367106"
FT TRANSMEM 640..665
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367106"
FT DOMAIN 434..791
FT /note="GPI ethanolamine phosphate transferase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF19316"
SQ SEQUENCE 869 AA; 96420 MW; 30252C873A95F31A CRC64;
MAPKWPLFLS NLLFPLAILL FASGFFPYKP FIPGLATFSE ESNGIRSSAP FDRVVFMVVD
ALRSDFVYSE RSGFTFTQGL IQSGAALPFT AHAGAPTVTM PRVKAITTGS VPSFLDVILN
LAESDTSSTL VYQDTWLAQL RARPGGRLVM YGDDTWLKLF PGFFDRHDGT TSFFVSDFVE
VDSNVTRHVP EELKMDDWSA MIMHYLGLDH IGHKSGPNSS HMIPKQKEMD SVVRDIYNAI
ENEDHLSSTL LVLCGDHGMN DAGNHGGASP GETSPALVFI SPKIRRIQKQ GISLQPPLAD
FQYYQLIEQS DIAPTLAGLL GFPIPLNSLG VFIPQFLPMW KNNSERLDVL LENARQIGNV
VSTTFPAYKF SNCSYTSDIC TPTSDTEIAS LECDWQNALR LVHAARNDTR HSKPAEDALL
AFSRAAQDVM SGAASNYNLG RLYIGISLAS LVVALCVNSS LLVINGAEMF SVFIAVAYGV
MMFASSYVEE EQQFWYWVLS GWTFYLYAKP HIQNGDKNSE NMGASSQGRQ IGSALMFAVF
SRVMRRWNQT GQKFTAEPDI ARTFLPKHTS ILWILILLTY TDICQRMVRR TSSTEAVSFP
RLFFPVLTSF AFLFKLAFTS ADSPEILQGT VLFGPLVESI VGVSLVVQAR TVFAGMAVVL
SCMIYREIKR QWALKAFLSK TRNPSNPRLL KRNTARSTAR FPVDFHNTVS LFLVTQSRPT
NIPLFLVFRL QQLALSSMKL SDNEISITSL ILQYASFFAL GGSNSIASID LSNAYNGISN
YNVFLVGILT FWRTSFNTSS RSSEIVDLFH YDEPAGCDGV LYCAADSSFH MDGFLSQVFV
HYDVEFGTAS GCQFATWRGN IGVNLLDKI
//
