ID L5MAQ8_MYODS Unreviewed; 328 AA.
AC L5MAQ8;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=GPI ethanolamine phosphate transferase 1 {ECO:0000256|RuleBase:RU367138};
DE EC=2.-.-.- {ECO:0000256|RuleBase:RU367138};
GN ORFNames=MDA_GLEAN10017744 {ECO:0000313|EMBL:ELK35461.1};
OS Myotis davidii (David's myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK35461.1, ECO:0000313|Proteomes:UP000010556};
RN [1] {ECO:0000313|Proteomes:UP000010556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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|RuleBase:RU367138}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|RuleBase:RU367138}; Multi-pass membrane protein
CC {ECO:0000256|RuleBase:RU367138}.
CC -!- SIMILARITY: Belongs to the PIGG/PIGN/PIGO family. PIGN subfamily.
CC {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; KB102342; ELK35461.1; -; Genomic_DNA.
DR AlphaFoldDB; L5MAQ8; -.
DR eggNOG; KOG2124; Eukaryota.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000010556; Unassembled WGS sequence.
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 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 PANTHER; PTHR12250:SF0; GPI ETHANOLAMINE PHOSPHATE TRANSFERASE 1; 1.
DR PANTHER; PTHR12250; PHOSPHATIDYLINOSITOL GLYCAN, CLASS N; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU367138};
KW GPI-anchor biosynthesis {ECO:0000256|RuleBase:RU367138};
KW Membrane {ECO:0000256|RuleBase:RU367138};
KW Reference proteome {ECO:0000313|Proteomes:UP000010556};
KW Transferase {ECO:0000256|RuleBase:RU367138, ECO:0000313|EMBL:ELK35461.1};
KW Transmembrane {ECO:0000256|RuleBase:RU367138};
KW Transmembrane helix {ECO:0000256|RuleBase:RU367138}.
FT TRANSMEM 260..278
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 290..309
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
SQ SEQUENCE 328 AA; 36700 MW; 59A58D2B8A401F4B CRC64;
MLLFFIVGLL VHFVFFASIF DIYFTSPLVH GMAPQFTPLP PPARRLVLIV ADGLRADALY
EFDEKGNPRA PFIRNIIMHE GSWGISHTRV PTESRPGHVA LIAGFYEDVS AVAKGWKENP
VEFDSLLNQS KYTWSWGSPD IVSMFAKGAT GNHVFTHSYD ADSEDFGAKD VTKLDTWVFD
NIKADVAPLM ASLIGVPFPL NSVGILPVNY LNNTDAFKAE SMYTNAKQIL EQFKVTSIHF
SYNTDITQFR QLCLDDIRRA FFLIFIPFVL VMCAFEAVQL TTQLSSKSIS HYVIVMCMTI
VLVFLNGLAQ LLTTKKLGLC GQPKSHLI
//
