PIGV1_CAEEL
ID PIGV1_CAEEL Reviewed; 672 AA.
AC O02164;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=GPI mannosyltransferase pigv-1 {ECO:0000305};
DE EC=2.4.1.- {ECO:0000250|UniProtKB:Q9NUD9};
DE AltName: Full=Phosphatidylinositol-glycan anchor biosynthesis class V protein 1 homolog {ECO:0000312|WormBase:T09B4.1};
GN Name=pigv-1 {ECO:0000312|WormBase:T09B4.1};
GN ORFNames=T09B4.1 {ECO:0000312|WormBase:T09B4.1};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP GLY-361.
RX PubMed=25807459; DOI=10.1371/journal.pgen.1005082;
RA Budirahardja Y., Doan T.D., Zaidel-Bar R.;
RT "Glycosyl phosphatidylinositol anchor biosynthesis is essential for
RT maintaining epithelial integrity during Caenorhabditis elegans
RT embryogenesis.";
RL PLoS Genet. 11:E1005082-E1005082(2015).
CC -!- FUNCTION: Alpha-1,6-mannosyltransferase involved in
CC glycosylphosphatidylinositol-anchor biosynthesis (By similarity).
CC Transfers the second mannose to the glycosylphosphatidylinositol during
CC GPI precursor assembly (By similarity). Required for maintenance of
CC epithelial integrity during embryogenesis (PubMed:25807459).
CC {ECO:0000250|UniProtKB:Q9NUD9, ECO:0000269|PubMed:25807459}.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis. {ECO:0000250|UniProtKB:Q9NUD9}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:25807459}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in epithelial tissues including the
CC epidermis, pharynx, intestine, rectum and excretory cell during
CC embryogenesis. {ECO:0000269|PubMed:25807459}.
CC -!- SIMILARITY: Belongs to the PIGV family. {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; BX284601; CCD71986.1; -; Genomic_DNA.
DR PIR; T25876; T25876.
DR RefSeq; NP_491783.1; NM_059382.4.
DR AlphaFoldDB; O02164; -.
DR STRING; 6239.T09B4.1.1; -.
DR CAZy; GT76; Glycosyltransferase Family 76.
DR EPD; O02164; -.
DR PaxDb; O02164; -.
DR PeptideAtlas; O02164; -.
DR EnsemblMetazoa; T09B4.1.1; T09B4.1.1; WBGene00020375.
DR GeneID; 172305; -.
DR KEGG; cel:CELE_T09B4.1; -.
DR UCSC; T09B4.1; c. elegans.
DR CTD; 172305; -.
DR WormBase; T09B4.1; CE13457; WBGene00020375; pigv-1.
DR eggNOG; KOG2647; Eukaryota.
DR GeneTree; ENSGT00390000013174; -.
DR HOGENOM; CLU_026116_0_0_1; -.
DR InParanoid; O02164; -.
DR OMA; MAHAAWL; -.
DR OrthoDB; 960696at2759; -.
DR PhylomeDB; O02164; -.
DR Reactome; R-CEL-162710; Synthesis of glycosylphosphatidylinositol (GPI).
DR UniPathway; UPA00196; -.
DR PRO; PR:O02164; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00020375; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031501; C:mannosyltransferase complex; IBA:GO_Central.
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:0000030; F:mannosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IBA:GO_Central.
DR InterPro; IPR007315; PIG-V/Gpi18.
DR PANTHER; PTHR12468; PTHR12468; 1.
DR Pfam; PF04188; Mannosyl_trans2; 2.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycosyltransferase; GPI-anchor biosynthesis;
KW Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..672
FT /note="GPI mannosyltransferase pigv-1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000433599"
FT TOPO_DOM 1..134
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 156..239
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 261..277
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 299..319
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 320..345
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 346..366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 367..423
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 424..444
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 445..520
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 521..541
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 542..569
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 570..590
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 591..592
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 593..613
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 614..648
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 649..669
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 670..672
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT REGION 82..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 361
FT /note="G->E: In qm34; temperature sensitive mutant
FT resulting in elongation arrest and over 80% embryonic
FT lethality at 25 degrees Celsius due to epithelial defects
FT during elongation with cysts forming inside the embryo
FT and/or cells leaking out from the embryo body."
FT /evidence="ECO:0000269|PubMed:25807459"
SQ SEQUENCE 672 AA; 78256 MW; 0BD9F02AC49C7700 CRC64;
MRRREPGRDV KRAAEEEFIE LERRTDTYED AVLNEDPQMK GFRFPSILSF PVPNKTIETG
VTDENPFSAR KSAFFTNRLI GREESDSSSS REDSPLGSTE TGESCSTTDD EESKEKRIEY
RDSQTQRCLG FCFRQLFFSR MWVFILQFIA SYYAGDRFRT DGFNLVDKLI EPGQSVFGDV
VVRRGLMGLR RWDAQQFLFI AEHHYIFEHS LAFFAGFPET VNYVRVGVNN GMESVFGWTF
PPWVTITLAA VFVNLFCFLL CGMTLYQVVL IMTRSVKISL LAVSIFAFNP ASIFFSSAYS
ESMFFTMTLT GFVFMLFGLR GKGFWHRMLK GFTGTICFGL TFAVRSNGLL NFLYVAWIWC
GTLLWDEEMP IPDCHKLIST LAATKNERYK QEWQAKFWRF QQKRKQNRKV FRWTDPNFSR
CVTLFIVIVC AISATLLFFT PYVFMTNFTA DEFCKPQDSH KQAVETIAKT VRLSPKTVSV
KNAWEKTTWC KKPKLFGIIA RYYGEIQTKY WSVKFFGYWK IKKIPCFLMM LPAAILTVLA
IKSSWNDVFL NKRWNNIWVL TARSDHSLPM AIHSSVLLFV AIFYINSEVF TRIIFSSSPF
IYIYIATYID KLTQGTIAGN RLWQYFESPG ILPFFVFRRV WQDGWRGKLL YIYILGYFVF
GTMAHSAWLP FT
