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Database: UniProt
Entry: A0A135LY49_PENPA
LinkDB: A0A135LY49_PENPA
Original site: A0A135LY49_PENPA 
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
//
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