GPI18_CHAGB
ID GPI18_CHAGB Reviewed; 471 AA.
AC Q2GSI6;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 60.
DE RecName: Full=GPI mannosyltransferase 2;
DE EC=2.4.1.-;
DE AltName: Full=GPI mannosyltransferase II;
DE Short=GPI-MT-II;
DE AltName: Full=Glycosylphosphatidylinositol-anchor biosynthesis protein 18;
GN Name=GPI18; ORFNames=CHGG_09068;
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
CC -!- FUNCTION: Mannosyltransferase involved in glycosylphosphatidylinositol-
CC anchor biosynthesis. Transfers the second mannose to the
CC glycosylphosphatidylinositol during GPI precursor assembly (By
CC similarity). {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 PIGV family. {ECO:0000305}.
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DR EMBL; CH408034; EAQ85054.1; -; Genomic_DNA.
DR RefSeq; XP_001226995.1; XM_001226994.1.
DR AlphaFoldDB; Q2GSI6; -.
DR STRING; 38033.XP_001226995.1; -.
DR EnsemblFungi; EAQ85054; EAQ85054; CHGG_09068.
DR GeneID; 4395328; -.
DR eggNOG; KOG2647; Eukaryota.
DR HOGENOM; CLU_029048_0_0_1; -.
DR InParanoid; Q2GSI6; -.
DR OMA; EYFLHIA; -.
DR OrthoDB; 960696at2759; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000001056; Unassembled WGS sequence.
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:0000009; F:alpha-1,6-mannosyltransferase activity; IEA:InterPro.
DR GO; GO:0004376; F:glycolipid mannosyltransferase activity; IEA:InterPro.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR007315; PIG-V/Gpi18.
DR PANTHER; PTHR12468; PTHR12468; 1.
DR Pfam; PF04188; Mannosyl_trans2; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Glycosyltransferase; GPI-anchor biosynthesis;
KW Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..471
FT /note="GPI mannosyltransferase 2"
FT /id="PRO_0000246244"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 348..368
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 449..469
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 471 AA; 50417 MW; 5FE05A32DDC5DEE0 CRC64;
MAPKHQTPHT HAQIHTHPYR TLLTSFAAWK LFLFAIVLGS TLVGDAYDTS GGLLLQGPAN
GDAATRPAGL GTTLIARLTS WDAIYYVSAA RRDYVFEQEW AFGAGLPFVV RTLLQGLEYV
GIIDAPGAEG GRALVAEALA GILVANTAHL LSALVLYRLG QVVWRDQTLS LVAALLHVIS
PAGLFLSAPY SESSFALLSF SGYLLFALGC RAEGSSNSNN SPTRRDLYTI SAGVLFGAAT
VFRSNGLLNG APFALEVLRH LPAFVRRPTA IDTLRRLAAL GVGGAAVAAG SLGPQAAAYL
RYCIPSSSSG ASDGEENLLL PRPWCQGYLP SIFTFVQQHY WNVGFLRYWT LPNLPLFLLA
TPMLVILVKS GVDSLRGRHL PGDAKAVDGE SGRLLALIRS TAAAQVLLAV LAATTYHVQI
ITRISSGYPV WHWWLAGRLV QGDKTGSRIV MFMVIYASIQ GALFASFLPP A