ID C3YGF2_BRAFL Unreviewed; 612 AA.
AC C3YGF2;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=GPI ethanolamine phosphate transferase 1 {ECO:0000256|ARBA:ARBA00020831, ECO:0000256|RuleBase:RU367138};
DE EC=2.-.-.- {ECO:0000256|RuleBase:RU367138};
GN ORFNames=BRAFLDRAFT_94824 {ECO:0000313|EMBL:EEN60673.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN60673.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN60673.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN60673.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
CC -!- FUNCTION: Ethanolamine phosphate transferase involved in
CC glycosylphosphatidylinositol-anchor biosynthesis. Transfers
CC ethanolamine phosphate to the first alpha-1,4-linked mannose of the
CC glycosylphosphatidylinositol precursor of GPI-anchor.
CC {ECO:0000256|RuleBase:RU367138}.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis. {ECO:0000256|ARBA:ARBA00004687,
CC ECO:0000256|RuleBase:RU367138}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU367138}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC ECO:0000256|RuleBase:RU367138}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the PIGG/PIGN/PIGO family. PIGN subfamily.
CC {ECO:0000256|ARBA:ARBA00008400, ECO:0000256|RuleBase:RU367138}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU367138}.
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DR EMBL; GG666511; EEN60673.1; -; Genomic_DNA.
DR RefSeq; XP_002604662.1; XM_002604616.1.
DR AlphaFoldDB; C3YGF2; -.
DR STRING; 7739.C3YGF2; -.
DR eggNOG; KOG2124; Eukaryota.
DR InParanoid; C3YGF2; -.
DR UniPathway; UPA00196; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051377; F:mannose-ethanolamine phosphotransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd16020; GPI_EPT_1; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR007070; GPI_EtnP_transferase_1.
DR InterPro; IPR017852; GPI_EtnP_transferase_1_C.
DR InterPro; IPR002591; Phosphodiest/P_Trfase.
DR InterPro; IPR037671; PIGN_N.
DR PANTHER; PTHR12250:SF0; GPI ETHANOLAMINE PHOSPHATE TRANSFERASE 1; 1.
DR PANTHER; PTHR12250; PHOSPHATIDYLINOSITOL GLYCAN, CLASS N; 1.
DR Pfam; PF01663; Phosphodiest; 1.
DR Pfam; PF04987; PigN; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU367138};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW GPI-anchor biosynthesis {ECO:0000256|ARBA:ARBA00022502,
KW ECO:0000256|RuleBase:RU367138};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367138};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU367138};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU367138};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU367138}.
FT TRANSMEM 456..480
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 532..558
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 573..596
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT DOMAIN 540..565
FT /note="GPI ethanolamine phosphate transferase 1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF04987"
SQ SEQUENCE 612 AA; 68218 MW; 6F547C168DC84D23 CRC64;
MLLFFLGALF VHVIYFASIF DIYFTSPLVH GMTPHSTPAP PPAKRLVLFV GDGLRADRFF
ELDKHGQTRA PYLRDIIQTR GTWGVSHTRV PTESRPGHVA LIAGFYEDVS AVAKGWKENP
VEFDSVFNQS KETWAWGSPD ILPMFAKGAT GDHVHTYMYS SEEEDFADSD PGKLDNWVFE
RVEAFLQEAH NNETLGGFLQ QSRVVLFLHL LGIDTSGHAY RPMSSEYLEN IRLVDAGIQK
TVGLLEDFYQ HDGQTAYVFT SDHGMTDWAK LVSGDSRLPD RFVGQESKCH TTTGLQFLEG
WQNHQLQRLA APLSFGPKLV SGDSRLPDRF VGQESKCHTT TGLQFLEGWQ NHQLQRLAAP
LSFGRSHGAG HPSETLTPLL AWGAGVAGPQ SGNTQDYMDG FGQEWKLENI RRCDVNQVKM
KQKRETTLSV FFIPYRGSDI YKLADYIKAN NLTLSLLGSC VLAVLSLELL ILLMVMSVYV
RHSTAASLLN KEGNPVFNRV FSWTMLDHGS ILDGDLCIQG SRCGGTGTNK KVIMIIVQTC
LFLTVLLMSD LMGLHFFFLV QDTGSWLEIG TSISHYVTVM STTIAIMLLF GVARFLTGTA
IISQQEDKTH AQ
//
