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Database: UniProt
Entry: H2ZWA6_LATCH
LinkDB: H2ZWA6_LATCH
Original site: H2ZWA6_LATCH 
ID   H2ZWA6_LATCH            Unreviewed;      1115 AA.
AC   H2ZWA6;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=GPI ethanolamine phosphate transferase 3 {ECO:0000256|ARBA:ARBA00020841};
GN   Name=PIGO {ECO:0000313|Ensembl:ENSLACP00000001677.1};
OS   Latimeria chalumnae (Coelacanth).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Coelacanthiformes; Coelacanthidae; Latimeria.
OX   NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000001677.1, ECO:0000313|Proteomes:UP000008672};
RN   [1] {ECO:0000313|Proteomes:UP000008672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT   "The draft genome of Latimeria chalumnae.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLACP00000001677.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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. PIGO subfamily.
CC       {ECO:0000256|ARBA:ARBA00008695}.
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DR   EMBL; AFYH01170037; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01170038; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01170039; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01170040; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01170041; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01170042; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01170043; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01170044; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01170045; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01170046; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_006006311.1; XM_006006249.2.
DR   RefSeq; XP_006006312.1; XM_006006250.2.
DR   AlphaFoldDB; H2ZWA6; -.
DR   STRING; 7897.ENSLACP00000001677; -.
DR   Ensembl; ENSLACT00000001690.1; ENSLACP00000001677.1; ENSLACG00000001501.1.
DR   GeneID; 102357909; -.
DR   KEGG; lcm:102357909; -.
DR   CTD; 84720; -.
DR   eggNOG; KOG2126; Eukaryota.
DR   GeneTree; ENSGT00910000144278; -.
DR   InParanoid; H2ZWA6; -.
DR   OMA; YPSFDIF; -.
DR   OrthoDB; 5479199at2759; -.
DR   TreeFam; TF354249; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000008672; Unassembled WGS sequence.
DR   Bgee; ENSLACG00000001501; Expressed in muscle tissue and 6 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:InterPro.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd16023; GPI_EPT_3; 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; IPR037675; PIG-O_N.
DR   InterPro; IPR039524; PIGO/GPI13.
DR   PANTHER; PTHR23071:SF1; GPI ETHANOLAMINE PHOSPHATE TRANSFERASE 3; 1.
DR   PANTHER; PTHR23071; PHOSPHATIDYLINOSITOL GLYCAN; 1.
DR   Pfam; PF01663; Phosphodiest; 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:UP000008672};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        453..471
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        483..504
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        560..578
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        590..609
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        642..662
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        689..709
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        721..741
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        753..781
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        860..879
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        886..906
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        975..994
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1072..1094
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   1115 AA;  123353 MW;  E5049450DECAB8C1 CRC64;
     MNKLPALIAL LWICLLFYVG IGLFMSGFLL VRVELGNRSS CADQLFAGGK SAAGTEEEPL
     GQSCWAARRF RRVAVVVIDA LSYEFAKFDP ENRSPRPYQN RLGVIHRLVS ARPRNARLYP
     FRADAPTTTM QRVKGLTTGS LPTFIDISSN FASYAIQEDN LIQQWVQNGR KVVFMGDDTW
     DGLFPNQFSK SYFFPSFNVK DLHTVDNGVL RHLYPSVKDG NWDVLIAHFL GVDHCGHRYG
     PDQPAMADKL DQMNDMLGSL IDQLQNDTLL MVLGDHGMTD DGGHGGDSEK EVNAALFVYS
     ALPLFREEAD QAPESIPQID LVPTLALLTG IPIPYSNIGK VIPDLFRWSN ERDALSPDFT
     LVEALWINVK QVNRFLDSYS LAATDLPQDQ LQRLKELFAS AGSEYAALHA RRSQPLPNLT
     RRLQKLVSDL QLYLKEARET CQASWARFQP LRMLIGILIL AATCLLCYVV SETADRPGLY
     HGVSLSPIAW GAAVGLAFGT WQVVSGSGLE PWAAPCLAAL ASQLGFCVHL WRLRSQESGQ
     SLSERPSPLR PSPLQSSKPW AGFSVPLVIL FLRCASVFSN SFVVAEGQAV LFLLKSLLVS
     TVAGLHWAGK LSAPNPVTHP NFGPETPKQS IWQAYKRESV HLLGFLAAFL VCVNFSVVFH
     GCREEQAACQ PSPFLTPLSG LQDQQARNWN YALCLAPLAG LVLLPRLWLR HYGNLNNGGP
     AILFVRWGVP LAALLLSFYW AMNSAPESSY GKLLVLVRSA VVVFPHLMYG LVALGLLVAW
     WSPMTVFLKV TGRSAEDEEA ELVTASRGTL GAEGNLLHVI PQIYRKMQRN LRNRLGAGEG
     AAGGEEEQRP VAAAYGLGSV YSAAVLIVVW LLALLLLLLH TERMSLSFLL LFLEAFAFLQ
     LHAAFINLSA QDSGDFTVPW YAVTGWAFAA TQFFYSTGHQ PTFPTIQWNA AFVGFPEGHD
     NRIVVPAALL GMNTFASHII FAVSSPLLMF WPLVCETQGL RKRRGGKDSW GGDEEQTMEM
     RLRESPQRFT AGLLQLGARY LFAHGVQLLA SVCTAAILRR HLMVWKIFAP KFLFEAAGFV
     VTSVCSVLGI AFVMRVDVAV SRWFKQLILD QRHSR
//
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