PIGV_DROME
ID PIGV_DROME Reviewed; 449 AA.
AC Q9V7W1; A0A0B4LGQ7; B7YZR6; Q0E947; Q95TV6; Q9U3X2;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=GPI mannosyltransferase 2;
DE EC=2.4.1.-;
DE AltName: Full=GPI mannosyltransferase II;
DE Short=GPI-MT-II;
GN Name=PIG-V {ECO:0000312|FlyBase:FBgn0265174};
GN ORFNames=CG44239 {ECO:0000312|FlyBase:FBgn0265174};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11102367; DOI=10.1093/genetics/156.4.1691;
RA Prokopenko S.N., He Y., Lu Y., Bellen H.J.;
RT "Mutations affecting the development of the peripheral nervous system in
RT Drosophila: a molecular screen for novel proteins.";
RL Genetics 156:1691-1715(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF TRP-62; ASP-63; ALA-276; GLN-306 AND TRP-310.
RC STRAIN=CN BW;
RX PubMed=22575127; DOI=10.1017/s0952523812000181;
RA Rosenbaum E.E., Brehm K.S., Vasiljevic E., Gajeski A., Colley N.J.;
RT "Drosophila GPI-mannosyltransferase 2 is required for GPI anchor attachment
RT and surface expression of chaoptin.";
RL Vis. Neurosci. 29:143-156(2012).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 112-449.
RC STRAIN=Berkeley; TISSUE=Ovary;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
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. {ECO:0000269|PubMed:22575127}.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Homozygous lethal. {ECO:0000269|PubMed:22575127}.
CC -!- SIMILARITY: Belongs to the PIGV family. {ECO:0000305}.
CC -!- CAUTION: Was originally (PubMed:11102367) named veg. However, more
CC thorough studies (PubMed:22575127) found that the veg phenotype does
CC not map to this protein. It is still not known which gene corresponds
CC to the veg phenotype. {ECO:0000305|PubMed:11102367,
CC ECO:0000305|PubMed:22575127}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL13718.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF211892; AAF23239.1; -; mRNA.
DR EMBL; AE013599; AHN56304.1; -; Genomic_DNA.
DR EMBL; AE013599; AHN56305.1; -; Genomic_DNA.
DR EMBL; AE013599; AHN56306.1; -; Genomic_DNA.
DR EMBL; BT016020; AAV36905.1; -; mRNA.
DR EMBL; AY058489; AAL13718.1; ALT_INIT; mRNA.
DR RefSeq; NP_001286508.1; NM_001299579.1.
DR RefSeq; NP_001286509.1; NM_001299580.1.
DR RefSeq; NP_001286510.1; NM_001299581.1.
DR AlphaFoldDB; Q9V7W1; -.
DR STRING; 7227.FBpp0086200; -.
DR CAZy; GT76; Glycosyltransferase Family 76.
DR GlyGen; Q9V7W1; 2 sites.
DR PaxDb; Q9V7W1; -.
DR PRIDE; Q9V7W1; -.
DR DNASU; 19835383; -.
DR EnsemblMetazoa; FBtr0339071; FBpp0308217; FBgn0265174.
DR EnsemblMetazoa; FBtr0339072; FBpp0308218; FBgn0265174.
DR EnsemblMetazoa; FBtr0339073; FBpp0308219; FBgn0265174.
DR GeneID; 19835383; -.
DR KEGG; dme:Dmel_CG44239; -.
DR UCSC; CG6657-RA; d. melanogaster.
DR CTD; 19835383; -.
DR FlyBase; FBgn0265174; PIG-V.
DR VEuPathDB; VectorBase:FBgn0265174; -.
DR eggNOG; KOG2647; Eukaryota.
DR GeneTree; ENSGT00390000013174; -.
DR HOGENOM; CLU_029048_3_2_1; -.
DR InParanoid; Q9V7W1; -.
DR OMA; EYFLHIA; -.
DR OrthoDB; 960696at2759; -.
DR PhylomeDB; Q9V7W1; -.
DR Reactome; R-DME-162710; Synthesis of glycosylphosphatidylinositol (GPI).
DR UniPathway; UPA00196; -.
DR BioGRID-ORCS; 19835383; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 19835383; -.
DR PRO; PR:Q9V7W1; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0265174; Expressed in oviduct (Drosophila) and 26 other tissues.
DR Genevisible; Q9V7W1; DM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:FlyBase.
DR GO; GO:0031501; C:mannosyltransferase complex; IBA:GO_Central.
DR GO; GO:0000009; F:alpha-1,6-mannosyltransferase activity; ISS:FlyBase.
DR GO; GO:0004376; F:glycolipid mannosyltransferase activity; IEA:InterPro.
DR GO; GO:0000030; F:mannosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IMP:FlyBase.
DR GO; GO:0045052; P:protein insertion into ER membrane by GPI attachment sequence; IGI:FlyBase.
DR GO; GO:0045313; P:rhabdomere membrane biogenesis; IMP:FlyBase.
DR InterPro; IPR007315; PIG-V/Gpi18.
DR PANTHER; PTHR12468; PTHR12468; 1.
DR Pfam; PF04188; Mannosyl_trans2; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase;
KW GPI-anchor biosynthesis; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..449
FT /note="GPI mannosyltransferase 2"
FT /id="PRO_0000246237"
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..82
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 104..109
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 131..148
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..196
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 218..235
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 257..368
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 369..389
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 390..423
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 424..444
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 445..449
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 62
FT /note="W->L: No phenotype; when associated with V-276."
FT /evidence="ECO:0000269|PubMed:22575127"
FT MUTAGEN 63
FT /note="D->A: Shows reduced levels of chp and ninaE, small
FT rhabdomeres with severely disorganized microvilli and
FT retinal degeneration; when associated with V-276."
FT /evidence="ECO:0000269|PubMed:22575127"
FT MUTAGEN 276
FT /note="A->V: Displays defects in chp trafficking to the
FT membrane and mislocalization of ninaE, Rh3 and Rh4 in
FT photoreceptors. Shows reduced levels of chp and ninaE,
FT small rhabdomeres with severely disorganized microvilli and
FT retinal degeneration; when associated with or without A-63
FT or L-310. Mild photoreceptor cell and microvillar
FT disorganization; when associated with A-306. No phenotype;
FT when associated with L-62."
FT /evidence="ECO:0000269|PubMed:22575127"
FT MUTAGEN 306
FT /note="Q->A: Mild photoreceptor cell and microvillar
FT disorganization; when associated with V-276."
FT /evidence="ECO:0000269|PubMed:22575127"
FT MUTAGEN 310
FT /note="W->L: Shows reduced levels of chp and ninaE, small
FT rhabdomeres with severely disorganized microvilli and
FT retinal degeneration; when associated with V-276."
FT /evidence="ECO:0000269|PubMed:22575127"
FT CONFLICT 41
FT /note="S -> P (in Ref. 1; AAF23239)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="V -> M (in Ref. 1; AAF23239)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="F -> L (in Ref. 1; AAF23239 and 6; AAL13718)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 449 AA; 51544 MW; 8B3145FC9B766D83 CRC64;
MTEKVTKLAL ASRLIVLLVQ LVANGALPEH KPDVFRMPVS SDQNASWIDK VIKRCLGGLR
HWDGEYFLHI AENLYSYENT LAFYPLYPVV VRHVGQAVEA IGISLSQESI LLVVAVALNF
WLFCESANLL FQLTQVLFND LNKSWNAALI YCFNPATIFF TAAYSETFFA YSSLHLMLEC
SKPTGSFRYL RLGTALAACL LCRSNGLITL GYPLYFFGRQ LLLKNKEPNT CMQLTQMTLT
ILGAIGILHT YYFYIYRLYC LPNTRPNHPQ HIVDYAVERK YLLSGQGSEG SPWCQYTLPF
PYTYVQSHYW DVGFLRYYKW KQLPNFLLAL PMLSFMHWHC YDYMQHLAKA VWAKLTPSGF
KELIRDHTTF PFVLHAAILT LVCTVYVHIQ VSTRLLASAT PVFYWFAADH MPKTLAQLKL
RSKAGALFVW CTTYSLVGTV LFSNNYPWT
