ID A0A1L8FSC0_XENLA Unreviewed; 966 AA.
AC A0A1L8FSC0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=GPI ethanolamine phosphate transferase 1 {ECO:0000256|ARBA:ARBA00020831, ECO:0000256|RuleBase:RU367138};
DE EC=2.-.-.- {ECO:0000256|RuleBase:RU367138};
GN Name=pign.S {ECO:0000313|RefSeq:XP_018124968.1,
GN ECO:0000313|RefSeq:XP_041423588.1, ECO:0000313|RefSeq:XP_041423589.1,
GN ECO:0000313|Xenbase:XB-GENE-6488003};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|RefSeq:XP_018124968.1};
RN [1] {ECO:0000313|RefSeq:XP_018124968.1}
RP IDENTIFICATION.
RC STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018124968.1,
RC ECO:0000313|RefSeq:XP_041423588.1};
RC TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018124968.1,
RC ECO:0000313|RefSeq:XP_041423588.1};
RG RefSeq;
RL Submitted (APR-2022) to UniProtKB.
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}.
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DR RefSeq; XP_018124966.1; XM_018269477.1.
DR RefSeq; XP_018124967.1; XM_018269478.1.
DR RefSeq; XP_018124968.1; XM_018269479.2.
DR RefSeq; XP_018124970.1; XM_018269481.1.
DR RefSeq; XP_041423588.1; XM_041567654.1.
DR RefSeq; XP_041423589.1; XM_041567655.1.
DR STRING; 8355.A0A1L8FSC0; -.
DR PaxDb; 8355-A0A1L8FSC0; -.
DR GeneID; 108720092; -.
DR KEGG; xla:108720092; -.
DR AGR; Xenbase:XB-GENE-6488003; -.
DR CTD; 108720092; -.
DR Xenbase; XB-GENE-6488003; pign.S.
DR OMA; QSYFHRE; -.
DR OrthoDB; 6598at2759; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000186698; Chromosome 6S.
DR Bgee; 108720092; Expressed in egg cell and 18 other cell types or tissues.
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 Reference proteome {ECO:0000313|Proteomes:UP000186698};
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 439..461
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 481..500
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 506..522
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 529..552
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 558..578
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 590..608
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 614..636
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 648..665
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 741..759
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 822..842
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 848..881
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 893..914
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 926..950
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT DOMAIN 428..919
FT /note="GPI ethanolamine phosphate transferase 1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF04987"
SQ SEQUENCE 966 AA; 109255 MW; 05853F9B9431941B CRC64;
MLVFFLAGLA VHLVFFASIF DIYFTSPLVH GMTPHSTSLR SPAKRLVLFV ADGLRADTFF
ELVENGTSRA PYLRNIIETR GSWGVSHTRV PTESRPGHVA LIAGFYEDVS AVAKGWKENP
VEFDSVFNES KFTWSWGSPD ILPMFAKGAS GDHVFTHCYS AESEDFATAD ATKLDTWVFE
HLKAFFSSAR SNQTLFKKLN EEKIVFFLHL LGLDTNGHAH KPGSREYKEN VKKVDEGIKE
MALLFEDFYG NDDKTAYIFT SDHGMTDWGS HGAGHPSETL TPLVAWGAGV HYPRKVQEQY
EQDSKAWKLE HLKRIDVNQA DVAPLMASLI GIPYPLNSVG VLPVAYLNNS ELFRAESMLT
NALQILEQFK VKMAQKKETT LSFLFSPFSL LSESKQLDIL RKTRSQIHRE NYKEAMALCE
TLIDLALRGL TYYHTYDRFF LGICVFVGFS GWIFYVIVVI LKTNTGITKK SSRLNKVKSS
VSVTQYAFCA MGIFITIFLI SLSCPWTYYV YCLLPILVWY AVSEEWHILI DYLQSMSPLL
IVGFLTVTFM SIEILVLSFF YRSVLTVGLI AFACWPVVMQ IWTQAKITTL NWFFLCLLLA
VFPLMPVVGK EPNITLVTTA GLLALLISLA YLWVIYSRKN TSIENMDIMM HICQMLILAL
AIYIVNTTNS SLADKHGLPI INQFVSWTTL GPSQDVMGPN PSPPTLSYWL CDPVPSNAAK
DPPSHRNTSS LVVPLFSTTA LFQRLLSIFL SLMSTYLLLS TGYEALFPLV LSSLMYTWIY
IEQETLVKYG LSFKYMLNGI DFSLSSEITQ SRQLNLDDIR RSFFLVFFII TAFFGTGNIA
SINSFDPASV YCFLTVFSPF VMGGLMMWKI LIPFILVMCA FETVQISTQI SSKSLFLIVL
VITDIMSLHF FFLVKDYGSW LDIGTSISHF VIVMSMTIFL MLLSGLVHYL TTKKIIPWRK
LKHHST
//
