GPI7_ASPOR
ID GPI7_ASPOR Reviewed; 852 AA.
AC Q2U9J2;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=GPI ethanolamine phosphate transferase 2;
DE EC=2.-.-.-;
DE AltName: Full=Glycosylphosphatidylinositol-anchor biosynthesis protein 7;
GN Name=las21; Synonyms=gpi7; ORFNames=AO090701000010;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
CC -!- FUNCTION: Ethanolamine phosphate transferase involved in
CC glycosylphosphatidylinositol-anchor biosynthesis. Transfers
CC ethanolamine phosphate to the GPI second mannose (By similarity).
CC {ECO:0000250}.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PIGG/PIGN/PIGO family. PIGG subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE61773.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP007164; BAE61773.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; Q2U9J2; -.
DR SMR; Q2U9J2; -.
DR STRING; 510516.Q2U9J2; -.
DR PRIDE; Q2U9J2; -.
DR EnsemblFungi; BAE61773; BAE61773; AO090701000010.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000006564; Chromosome 5.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; -; 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; PTHR23072; 1.
DR Pfam; PF01663; Phosphodiest; 1.
DR Pfam; PF19316; PIGO_PIGG; 2.
DR SUPFAM; SSF53649; SSF53649; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Glycoprotein; GPI-anchor biosynthesis; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..852
FT /note="GPI ethanolamine phosphate transferase 2"
FT /id="PRO_0000246188"
FT TRANSMEM 458..478
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 486..506
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 516..536
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 632..652
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 676..696
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 714..734
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 750..770
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 787..807
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 824..844
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 420
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 576
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 852 AA; 94782 MW; BD20C5229A9FA095 CRC64;
MKVARSKWTI LIANILVPIS ILVFSSGFFP YKTLLTGFAT HEHTIGGQIP PGVFDKVLLL
QADFHASDFV YSQHSGFLFT QRLGGGFLIR SGAALPFTAY ASAPTVTMPR LKAITTGSVP
SFLDVILNIA EADTSSTLMH QDTWLAQLKA KGGKLVMYGD DTWLKLFPGM FHRADGTTSF
FVSDFTEVDN NVTRHIPNEL LQDDWSAFIM HYLGLDHIGH KAGPNSPYMI TKQHEMDSVV
SMVYTALEQE KHLKTTLFVL CGDHGMNEAG NHGGSSVGET SPALLFISPK FQRLETRNDS
PTEEFSDLQY YHTVEQTDIT PTLAGLLGLP IPLNSLGVFI PELLAMWDHG AKSIPLTSSS
GPHRIHMLLE NAKQLLGAVK GSFPSYSFEF DLMPVICSSQ SLIDIERVQC AWFRVLETLN
GSGANHDSEA SSEIESALLL FLRNAQKLMS SAASDYDLIR LYVGLSISGF AISLTFFPAK
RLLVNFAPAG MFLGFSILSY STMMFASSYV EEEQQFWYWI SMGWVVYLHV KYAGHFHGNS
IQKSGPANGH WPFEPSLPWF GAAALAVSYR VLRRWNQTGQ KFAAQPDITG SFFPSHQHTL
WALLSLAASD SPELLGNSFL QPVAMLTDGM HLLYHARMVL CGISLLMIYS LYAGKARETT
HKGRGKWPPS TIFHETLTLF LLMQSKVTNI PAFLVFRVQI TILASMRLST VEQTITSLLM
QYVTFYAFGG SNAISSVDIS NAYNGIGTYS VFIVGALTFI SNWAAPIWWV SASRLLRSSQ
NREEKEAHVT ILTLHMATIL MSVMAACTTL RTHLFIWTVF SPKYLYTIAW AMINHIVVNV
LGEIDWRLFM KR
