ID L5LEW6_MYODS Unreviewed; 916 AA.
AC L5LEW6;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=GPI ethanolamine phosphate transferase 2 {ECO:0000256|ARBA:ARBA00020830};
GN ORFNames=MDA_GLEAN10003934 {ECO:0000313|EMBL:ELK24421.1};
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:ELK24421.1, 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 -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis. {ECO:0000256|ARBA:ARBA00004687}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. 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}.
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DR EMBL; KB112961; ELK24421.1; -; Genomic_DNA.
DR RefSeq; XP_006771506.1; XM_006771443.2.
DR AlphaFoldDB; L5LEW6; -.
DR GeneID; 102774133; -.
DR CTD; 54872; -.
DR eggNOG; KOG2125; Eukaryota.
DR OrthoDB; 5479199at2759; -.
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: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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW GPI-anchor biosynthesis {ECO:0000256|ARBA:ARBA00022502};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000010556};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ELK24421.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 362..383
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 395..414
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 434..460
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 713..735
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 809..834
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 846..869
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 881..901
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 581..884
FT /note="GPI ethanolamine phosphate transferase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF19316"
SQ SEQUENCE 916 AA; 100863 MW; 7BA8FAA082BAB166 CRC64;
MLIDALRDDF VFGSKGVKFM PYTTYLVEKG AAHSFVAEAK PPTVTMPRVK ALMTGSLPGF
VDVVRNLNSP ALLEDNVVTQ AKAAGKRIIF YGDETWVKLF PKHFVEYDGT TSFFVSDYTE
VDDNVTRHLD KVLKRGDWDV LILHYLGLDH IGHISGPNSP LIGRKLSEMD SILMRIHTSL
LSEEREALSP SLLVLCSDHG MSESGGHGAS SLEEVNTALL LTSSAFERKP GEVRPPERVQ
QTDLAATLAV GLGLPIPQHS VGRFLFPVVQ GRALREQLRL LHLNAVQLSR LLRARIPGFE
REHGFEQFKV SERLHGNWVK LYLEENNAEI LLNMGAKARK QYLYTLKALS QALSSQEAQY
DIYSMVVGTV VVLEVLALLL LSVPQALGTT AKLEVPLSPV CSLLFYVMFL LLWATHMVVC
TSAESFCYLC SLAWPVAGVV LALVSALLCG VLSTLTRMCL RGKLLRRKAA PSHWKWSELD
FLILVGTAGH VLSLGASSFI EEEHQTWYFL ISTLCLALSH ESYRSCFLGD DEEPERRPRV
AGEFAGAASA LPDRSVSCDM LELDQARQSP SSLDGLRGRE KCMALASPWL ILGCCRLLRS
LNQTGVQWAH RPDLGHWLTS PDHQAELSVL AALSLLAIFA LVQSRCSSVA KGALALGLLG
VYCYRAATGH VLSPWQQDNK DVSRGIIEAF RVFFFLSTGT KDMLKSQVLA AGIPVKAVGL
WDVYSGLVLL TALLFRPHNL PVLVCSLLIQ TVMTKFVWRP LRHGAAEVTV MHYWFGQAFF
YFQGNSNNIA TVDISAGFVG LNTYVEVPAM FLTAFATYAG PVLWASHLVN FLSWEPNSGS
ALRRACFCYA LLSSVPVSAY VVLVTALRYH LFIWSVFSPK LLYEGVHLLV TAAVCLGFTA
VDRAGARADA GKVAHC
//
