ID A0A151NFE4_ALLMI Unreviewed; 899 AA.
AC A0A151NFE4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
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 {ECO:0000313|EMBL:KYO35532.1};
GN ORFNames=Y1Q_0008089 {ECO:0000313|EMBL:KYO35532.1};
OS Alligator mississippiensis (American alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO35532.1};
RN [1] {ECO:0000313|EMBL:KYO35532.1, ECO:0000313|Proteomes:UP000050525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO35532.1};
RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA Ray D.A.;
RT "Sequencing three crocodilian genomes to illuminate the evolution of
RT archosaurs and amniotes.";
RL Genome Biol. 13:415-415(2012).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYO35532.1}.
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DR EMBL; AKHW03003201; KYO35532.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151NFE4; -.
DR STRING; 8496.A0A151NFE4; -.
DR eggNOG; KOG2124; Eukaryota.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000050525; 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 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:UP000050525};
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 410..429
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 450..467
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 511..531
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 537..553
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 560..578
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 584..606
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 618..635
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 647..666
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 698..714
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 755..773
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 793..816
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 828..847
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 859..880
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT DOMAIN 399..852
FT /note="GPI ethanolamine phosphate transferase 1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF04987"
SQ SEQUENCE 899 AA; 101328 MW; 4E436A40CBE116F9 CRC64;
MTPHYNPLPP PAKRLVLFVA DGLRADSLYE IEEDGSPRAP YLRNIIEDKG CWGISHTRVP
TESRPGHVAL IAGFYEDVSA VAKGWKENPV EFDSVFNESK YTWSWGSPDI LPMFAKGASG
DHVYTYCYTA EKEDFGAEDA MVLDTWVFDN VKNFFHAARS NQTMFSKVNE EKVILFLHLL
GIDTNGHAHR PNSREYKDNI RKVDEGIKEI VSLLEDFYGN DGKTAFIVTS DHGMTDWGSH
GAGHPSETLT PLIAWGAGLN YPQSVTSQAF EDNFLKEWKL ENRKRVDVNQ ADIAPLMASL
IGVPFPLNSV GILPLEYLNN SVHFKAESMF TNAVQILEQF KVKMTQKKES TLSFLFTPFK
LLSDSEQIDI LRKARSYIQK GKYNDAISLC KTLIILALEG LTYYHTYDRL FLGISIAMGF
VGWTSYVILV IIKTHTNLMR TVQNNKASSV FAYGFSAVGI FIAFFLLIQA YPWTYYIYCL
LPVPVWYAVV REFPVIQDLV TLLLTFPLHQ SIGFLFVCAL GIEILVFSFF YRSTLTVGLI
IFAGWPVITQ LWAQAKITAV SWTLLCWLLA MFPLMPVVGR EPNISLVTAA GLLILLISVS
SLPSLWKSKN KNVHHKDLAI LLFQMLSIAL SIYVVNTTHS SLQHKQGLPV INQIVSWTIL
ASSLVVPLLS PTFLFQRLLS ILLSLMSTYL LLSTGYEALF PLVLSGLMFA WINMEQETLQ
YYGLSLKPKL AILNFSYSTD ITQFRQLHLD DTRRSFFFVF FIVTAFFGTG NIASVNSFDP
ASVYCFLTVF SPFMMGGLLV LKVIIPFVLV SCAFEAVQVT TQLSSKSLFL IVLVISDIMA
LHFFFLVKDY GSWLDIGTSI SHFVLVMSFT IFMMLLNGLA QLLTTKRIEL WGLTKYHAT
//
