PIGV_DROPS
ID PIGV_DROPS Reviewed; 452 AA.
AC Q290J8;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=GPI mannosyltransferase 2;
DE EC=2.4.1.-;
DE AltName: Full=GPI mannosyltransferase II;
DE Short=GPI-MT-II;
GN ORFNames=GA19757;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(2005).
CC -!- FUNCTION: Mannosyltransferase involved in glycosylphosphatidylinositol-
CC anchor biosynthesis. Transfers the second mannose to the
CC glycosylphosphatidylinositol during GPI precursor assembly. Required
CC for the GPI-mediated endoplasmic reticulum exit and proper targeting to
CC the cell surface of chp. Required for GPI-mediated membrane attachment
CC of chp, qsm and Cont. Essential for microvillar stability in the
CC rhabdomere (By 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}.
CC -!- CAUTION: Was originally named veg by similarity to the D.melanogaster
CC ortholog. However, it was later shown that the veg phenotype does not
CC map to this protein. It is still not known which gene corresponds to
CC the veg phenotype. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM000071; EAL25364.1; -; Genomic_DNA.
DR RefSeq; XP_001360789.1; XM_001360752.3.
DR AlphaFoldDB; Q290J8; -.
DR STRING; 7237.FBpp0277779; -.
DR CAZy; GT76; Glycosyltransferase Family 76.
DR EnsemblMetazoa; FBtr0279341; FBpp0277779; FBgn0079753.
DR GeneID; 4804187; -.
DR KEGG; dpo:Dpse_GA19757; -.
DR eggNOG; KOG2647; Eukaryota.
DR HOGENOM; CLU_029048_3_2_1; -.
DR InParanoid; Q290J8; -.
DR OMA; EYFLHIA; -.
DR PhylomeDB; Q290J8; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000001819; Chromosome 3.
DR Bgee; FBgn0079753; Expressed in female reproductive system and 3 other tissues.
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 GO; GO:0045052; P:protein insertion into ER membrane by GPI attachment sequence; IEA:EnsemblMetazoa.
DR GO; GO:0045313; P:rhabdomere membrane biogenesis; IEA:EnsemblMetazoa.
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..452
FT /note="GPI mannosyltransferase 2"
FT /id="PRO_0000246238"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..113
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 135..161
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 183..209
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..238
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..284
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 306..327
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 349..370
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 392..398
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 399..419
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 420..426
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 427..447
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 448..452
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 452 AA; 52131 MW; 5639FB37520C552E CRC64;
MMEKVTKLAL TSRVMVLVVQ LLANFATPDH KPDVFRMPQS EGPKKNGPFP WLDELVLQSL
SGLRHWDGEY FLHIASNLYT YENTLAFYPL YPVVVRHVAQ ACQHLGIPLS RDALILLVAV
ALNVLIFCKT ANVLYKLTQR MFNDHNKSWN AALIFCFNPA SIFFSAAYSE TFFAFASFSL
MLECMRSEKD FRTFRLGAAL TGCFVCRSNG LLTLGFPLYF LARHILLSTG SVQRCWQLFK
MGLAMLVALG ILHTYYFYIY RLYCLPDVKV QHAQHVVDYA KERSFLISGQ ASVGSPWCGY
TLPFPYTYVQ SHYWDVGFLR YYKWKQLPNF LLALPMLLFM HWHCYDYIRK LVANTWSKIS
PSEYQGILKE HISFPFVLHA AVLTLVCTLY VHIQVSTRLL ASATPVFYWF AADYMPNTFQ
LSFRSKAGVL FIWCLTYSLV GTVLFSNNYP WT