ID A0A135LY49_PENPA Unreviewed; 969 AA.
AC A0A135LY49;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=GPI ethanolamine phosphate transferase 1 {ECO:0000256|ARBA:ARBA00020831, ECO:0000256|RuleBase:RU367138};
DE EC=2.-.-.- {ECO:0000256|RuleBase:RU367138};
GN ORFNames=PGRI_009300 {ECO:0000313|EMBL:KXG53880.1};
OS Penicillium patulum (Penicillium griseofulvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=5078 {ECO:0000313|EMBL:KXG53880.1, ECO:0000313|Proteomes:UP000070168};
RN [1] {ECO:0000313|EMBL:KXG53880.1, ECO:0000313|Proteomes:UP000070168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG3 {ECO:0000313|EMBL:KXG53880.1,
RC ECO:0000313|Proteomes:UP000070168};
RX PubMed=26729047; DOI=10.1186/s12864-015-2347-x;
RA Banani H., Marcet-Houben M., Ballester A.R., Abbruscato P.,
RA Gonzalez-Candelas L., Gabaldon T., Spadaro D.;
RT "Genome sequencing and secondary metabolism of the postharvest pathogen
RT Penicillium griseofulvum.";
RL BMC Genomics 17:19-19(2016).
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|ARBA:ARBA00024850, 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:KXG53880.1}.
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DR EMBL; LHQR01000014; KXG53880.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135LY49; -.
DR STRING; 5078.A0A135LY49; -.
DR OMA; TISHFCI; -.
DR OrthoDB; 6598at2759; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000070168; 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:0008484; F:sulfuric ester hydrolase activity; IEA:InterPro.
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; IPR037671; PIGN_N.
DR InterPro; IPR000917; Sulfatase_N.
DR PANTHER; PTHR12250:SF0; GPI ETHANOLAMINE PHOSPHATE TRANSFERASE 1; 1.
DR PANTHER; PTHR12250; PHOSPHATIDYLINOSITOL GLYCAN, CLASS N; 1.
DR Pfam; PF04987; PigN; 2.
DR Pfam; PF00884; Sulfatase; 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:UP000070168};
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 7..30
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 463..489
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 501..520
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 554..575
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 606..624
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 645..665
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 677..696
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 708..728
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 788..807
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 827..850
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 862..881
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT TRANSMEM 893..913
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367138"
FT DOMAIN 189..316
FT /note="Sulfatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00884"
FT DOMAIN 452..598
FT /note="GPI ethanolamine phosphate transferase 1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF04987"
FT DOMAIN 598..886
FT /note="GPI ethanolamine phosphate transferase 1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF04987"
FT REGION 939..969
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 949..969
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 969 AA; 107872 MW; 46D2452FE4EF7D38 CRC64;
MARLGRVGFL ALAVVFHLIY TYSIFDIYFV SPIVSGMRSY GVERSAGTPA PAKRLVLFVA
DGLRADKAFQ AFPDPSPDAD PENNELIRLS PFIRSQVLSH GTFGVSHTRV PTESRPGHVA
LIAGLYEDVS SVTTGWKMNP VNFDSVFNQS RHTWSWGSPD ILPMFKEGAV PGKVDAEMYS
EEAEDFTVDA THLDTWVFSK VHDLFESAKT DPDLNRKLRD DKLVFFLHLL GLDTTGHSFR
PYSNEYLHNI KVVDQGVQAV TKLVEDFYGD DKTAFVFTAD HGMSDTGSHG DGHPDNTRTP
LVVWGSGVAR PQLSSTGIAA GHEDGFSADW GFDQVHRHDV AQADVAALMA YLVGLDFPVN
SVGQLPLDYL NASPKEKALA ALANTQGVLE MYRVKEEQKR DAVIRYVPYE PLSGYHENSI
EGRLARIEAL ISSGDHEEAI VISAELLRVA LEGLRYLQTY DWLFLRTIVS IGYLGWIAYA
LTTVIDLHVL HGTSDSHRTT ASISFFSSIL AALFSVFLYQ GSSWRYYFYA FFPVYFWEEV
FARRKALIAG RQIVLGHVCS FTGYLKFGLQ LLAFLGTMEA MVQSYFHREI FTVCFSLVIK
VENLDTITYG GLLMFLTGIL YLLFEDAIIG HRDPESKELN AIGRVGSRII MGIQLGMVLL
AVIVTRSSVL SLQARQGLPF GNIVVGWVVL VASLTLPFFH RLYPNSHYLH RLMIIFLTFS
PTFIILTISW EGLFYFVFCM TVVTWVRLEH AIYVHTAGTL KKPKNPGVTT VDGETFYYRA
LTLSDIRVAL FFFFLLQSAF FSTGNVASIS TFSLDSVRRL IPVFDPFAQG ALLILQILIP
FAIISANLGI LNRRLEVPPS ALFMVVMAIS DIMTLNFFFM VRDEGSWLDI GMTISHFCIA
SALCTFVAGL EFLSEQFVSG VNFAPVILGT VPIEEVTECE DRKPKKASGA KQSKSKAKGK
GKGKSGKWS
//