ID F4WHR8_ACREC Unreviewed; 894 AA.
AC F4WHR8;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=GPI ethanolamine phosphate transferase 2 {ECO:0000256|ARBA:ARBA00020830};
GN ORFNames=G5I_05238 {ECO:0000313|EMBL:EGI66275.1};
OS Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS echinatior).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Acromyrmex.
OX NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN [1] {ECO:0000313|EMBL:EGI66275.1}
RP NUCLEOTIDE SEQUENCE.
RA Nygaard S., Zhang G.;
RT "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT adaptations to social evolution and fungus farming.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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; GL888167; EGI66275.1; -; Genomic_DNA.
DR AlphaFoldDB; F4WHR8; -.
DR STRING; 103372.F4WHR8; -.
DR eggNOG; KOG2125; Eukaryota.
DR InParanoid; F4WHR8; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000007755; 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:UP000007755};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EGI66275.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 374..399
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 411..429
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 441..459
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 471..492
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 498..515
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 535..552
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 579..597
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 609..625
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 645..662
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 669..689
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 762..787
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 808..829
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 841..865
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 468..615
FT /note="GPI ethanolamine phosphate transferase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF19316"
SQ SEQUENCE 894 AA; 103102 MW; E3B7F2100DFF29E6 CRC64;
MCIVFRIKTD LLYKPLIKRL IFMVIDGLRW DFIAGPIGKT AMPLTSDILT NDHGCLIQAK
LQAPTVTMPR IKAMMTGTVP NFVDVILNFG SKPLHTDNLL SQAKTHGYKL IFYGDETWLS
LFPNIFDRHD GTTSFFVTDF TEVDNNVTRH IQDELSNDDW DVMILHYLGL DHIGHVEGPF
GPSIKPKLQE MDKIVAQIAQ KVQNWNGDGE PTLFIVCGDH GIKDSGGHGG STPEETTVPI
ITIGGTMCIY EDTELKIPIK VQQLDIAVTL SAALGLPIPS TSLGSVFLDY IYNLQDDKRL
FLLNYNSRQL FDHYQKFTNE TEYIYQKYLN ITDLHLDWLN SNETQRDRND IENIALSYHA
ILDAMKEELV TSHLAIYDFS LIVIVLFVMW QMVFIAFHVE TTVWTTRKNT VFFFLMGFSL
CLGLYLYTFG NITSLCPSIK ALLFLLIIGV SYINYNLNLN NKRNVTLKIS IYRMLEIITM
MHIISFCGSS YIEEEHQTWY FFWSTLIAYF AYKYFTKLLE LMHYRNNIVG STEYYIEHCV
MLLLLFLGHI FLRKLNSTGN KWAHLPDIAQ WLKEDDSKIG MTLLLLTAFA LLIRIAYKSE
EEEYKQQSLF QNIAIAVCIY LRHMSNGAVV KIPLYSSSGI YEVQIFWGII VISLITYGYR
VIRKIKHDTY NFMSIMVFFI INMWVRISAM LHQPYNVILL PMQIIVSSII NTVLRENDSL
DRGVFLHYWL GNVFYFYQGN SNSLGSVNIA AGYVGLQSYM PFVTAVYLII NTYSAPILAY
FLLIYYWQMS EIYLQVSIVH TNKCYIAWRL LTTTVYMYFI IFQLNHLFVL SVYLPKLLYE
VTYTMTMCCS ALLTVIVIAV QHALIRFDDV HRCHICGTGL KNGHAFVQYS DNQA
//
