DPY19_CAEEL
ID DPY19_CAEEL Reviewed; 683 AA.
AC P34413;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 19-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=C-mannosyltransferase dpy-19;
DE EC=2.4.1.-;
DE AltName: Full=Protein dumpy-19;
GN Name=dpy-19; ORFNames=F22B7.10;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF GLY-185 AND LEU-218.
RX PubMed=11023868; DOI=10.1242/dev.127.21.4655;
RA Honigberg L., Kenyon C.;
RT "Establishment of left/right asymmetry in neuroblast migration by UNC-
RT 40/DCC, UNC-73/Trio and DPY-19 proteins in C. elegans.";
RL Development 127:4655-4668(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLY-185.
RX PubMed=23562325; DOI=10.1016/j.molcel.2013.03.003;
RA Buettner F.F., Ashikov A., Tiemann B., Lehle L., Bakker H.;
RT "C. elegans DPY-19 is a C-mannosyltransferase glycosylating thrombospondin
RT repeats.";
RL Mol. Cell 50:295-302(2013).
CC -!- FUNCTION: C-mannosyltransferase that mediates C-mannosylation of
CC tryptophan residues on target proteins such as unc-5 and mig-21.
CC Mediates the attachment of alpha-mannose in C-C linkage to the C2 of
CC the indole ring of tryptophan. C-mannosylation takes place in the
CC endoplasmic reticulum and frequently found in thrombospondin (TSP)
CC type-1 repeats and in the WSXWS motif of type I cytokine receptors.
CC Required to orient neuroblasts QL and QR correctly on the
CC anterior/posterior (A/P) axis: QL and QR are born in the same A/P
CC position, but polarize and migrate left/right asymmetrically, QL
CC migrates toward the posterior and QR migrates toward the anterior.
CC Required with unc-40 to express mab-5 correctly in the Q cell
CC descendants. {ECO:0000269|PubMed:11023868,
CC ECO:0000269|PubMed:23562325}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed faintly in neuroblasts QL and QR, more
CC strongly in the neighboring epidermal cells (dorsal hyp7 cells, ventral
CC P cells and lateral V cells), and in dorsal and ventral body muscle
CC cells. {ECO:0000269|PubMed:11023868}.
CC -!- DISRUPTION PHENOTYPE: Defects in the cell polarization of neuroblasts Q
CC cells. {ECO:0000269|PubMed:11023868}.
CC -!- SIMILARITY: Belongs to the dpy-19 family. {ECO:0000305}.
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DR EMBL; FO080222; CCD62139.1; -; Genomic_DNA.
DR PIR; S44629; S44629.
DR RefSeq; NP_498909.1; NM_066508.1.
DR AlphaFoldDB; P34413; -.
DR BioGRID; 56129; 7.
DR STRING; 6239.F22B7.10; -.
DR CAZy; GT98; Glycosyltransferase Family 98.
DR EPD; P34413; -.
DR PaxDb; P34413; -.
DR PeptideAtlas; P34413; -.
DR EnsemblMetazoa; F22B7.10.1; F22B7.10.1; WBGene00001078.
DR GeneID; 191628; -.
DR KEGG; cel:CELE_F22B7.10; -.
DR UCSC; F22B7.10; c. elegans.
DR CTD; 191628; -.
DR WormBase; F22B7.10; CE26462; WBGene00001078; dpy-19.
DR eggNOG; KOG4587; Eukaryota.
DR GeneTree; ENSGT00530000063023; -.
DR HOGENOM; CLU_014404_0_1_1; -.
DR InParanoid; P34413; -.
DR OMA; HDPLQGD; -.
DR OrthoDB; 1115173at2759; -.
DR PhylomeDB; P34413; -.
DR BRENDA; 2.4.1.B72; 1045.
DR PRO; PR:P34413; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00001078; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
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:0005637; C:nuclear inner membrane; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:WormBase.
DR GO; GO:0000030; F:mannosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0018406; P:protein C-linked glycosylation via 2'-alpha-mannosyl-L-tryptophan; IDA:UniProtKB.
DR InterPro; IPR030038; Dpy-19.
DR InterPro; IPR018732; Dpy-19/Dpy-19-like.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR PANTHER; PTHR31488; PTHR31488; 1.
DR PANTHER; PTHR31488:SF1; PTHR31488:SF1; 1.
DR Pfam; PF10034; Dpy19; 1.
DR SUPFAM; SSF88713; SSF88713; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Differentiation; Endoplasmic reticulum;
KW Glycosyltransferase; Membrane; Neurogenesis; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..683
FT /note="C-mannosyltransferase dpy-19"
FT /id="PRO_0000079993"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 413..433
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 467..487
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 502..522
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MUTAGEN 185
FT /note="G->D: In dpy-19(e1295); randomize the neuroblast QL
FT and QR asymmetrical pattern of mab-5 expression. Abolishes
FT C-mannosyltransferase activity in vitro."
FT /evidence="ECO:0000269|PubMed:11023868,
FT ECO:0000269|PubMed:23562325"
FT MUTAGEN 218
FT /note="L->F: In allele mu78; randomize the neuroblast QL
FT and QR asymmetrical pattern of mab-5 expression."
FT /evidence="ECO:0000269|PubMed:11023868"
SQ SEQUENCE 683 AA; 77852 MW; E307D9FA32F60A56 CRC64;
MAKKPKNSPE KSKYSSDTSS SLYSQTWLAS VVIIGLLVGY INYQHVYTLF ENDKHFSHLA
DFEREMAYRT EMGLYYSYYK TIINAPSFLE GVQEITHDTV TEHGHEINTL NRFNLYPEVI
LAFLYRPFRA FAKSANWQIE LCWQVNRGEL RPVESCEGIG NPHYFYITGV FIVAGTVASS
IFYLGVLVSD SIFGGFLSVL CFAFNHGEAT RVQWTPPLRE SFAFPFIIGH IAILTFVIKY
KKSGHSMILL LTSMAVPALL FWQFTQFAFF TQICSIFLAF SLDLIPFSTA KTVIHSHIIS
FLIGFLLLFG NEMMITALYF PSILALGMII YISPLLSNLK FRPAYVLFLA IIFASITLGL
KIGLSKGLGI EDDAHIFDIL RSKFTSFANF HTRLYTCSAE FDFIQYSTIE KLCGTLLIPL
ALISLVTFVF NFVKNTNLLW RNSEEIGENG EILYNVVQLC CSTVMAFLIM RLKLFMTPHL
CIVAALFANS KLLGGDRISK TIRVSALVGV IAILFYRGIP NIRQQLNVKG EYSNPDQEML
FDWIQHNTKQ DAVFAGTMPV MANVKLTTLR PIVNHPHYEH VGIRERTLKV YSMFSKKPIA
EVHKIMKEMG VNYFVFQLMN CSNDERRPEC VYRGMWDEED PKNSGRTALC DLWILAANSK
DNSRIAPFKI VYNANRNYIV LKI
