DPY19_CAEBR
ID DPY19_CAEBR Reviewed; 687 AA.
AC A8Y3M2;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=C-mannosyltransferase dpy-19;
DE EC=2.4.1.-;
DE AltName: Full=Protein dumpy-19 {ECO:0000250|UniProtKB:P34413};
GN Name=dpy-19 {ECO:0000312|EMBL:CAP39491.1}; ORFNames=CBG22936;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1] {ECO:0000312|EMBL:CAP39491.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000312|EMBL:CAP39491.1};
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the dpy-19 family. {ECO:0000255}.
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DR EMBL; HE600964; CAP39491.1; -; Genomic_DNA.
DR RefSeq; XP_002643028.1; XM_002642982.1.
DR AlphaFoldDB; A8Y3M2; -.
DR STRING; 6238.CBG22936; -.
DR EnsemblMetazoa; CBG22936a.1; CBG22936a.1; WBGene00041383.
DR GeneID; 8585022; -.
DR KEGG; cbr:CBG_22936; -.
DR CTD; 8585022; -.
DR WormBase; CBG22936a; CBP05446; WBGene00041383; Cbr-dpy-19.
DR eggNOG; KOG4587; Eukaryota.
DR HOGENOM; CLU_014404_0_1_1; -.
DR InParanoid; A8Y3M2; -.
DR OMA; HDPLQGD; -.
DR OrthoDB; 1115173at2759; -.
DR Proteomes; UP000008549; Chromosome III.
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:0000030; F:mannosyltransferase activity; IBA:GO_Central.
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; IBA:GO_Central.
DR InterPro; IPR030038; Dpy-19.
DR InterPro; IPR018732; Dpy-19/Dpy-19-like.
DR PANTHER; PTHR31488; PTHR31488; 1.
DR PANTHER; PTHR31488:SF1; PTHR31488:SF1; 1.
DR Pfam; PF10034; Dpy19; 1.
PE 3: Inferred from homology;
KW Developmental protein; Differentiation; Endoplasmic reticulum;
KW Glycosyltransferase; Membrane; Neurogenesis; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..687
FT /note="C-mannosyltransferase dpy-19"
FT /id="PRO_0000365630"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 324..344
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 347..367
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 415..435
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 454..474
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 687 AA; 77918 MW; B1C01C46FA6A53E8 CRC64;
MAKKAKNSEK NGPRHSGNFS QESGISGNLW LATVVLIGLF VGFLNYQHIY TLFENDKHFS
HLADFEREMA YRTEMGLYYS YYKTIITAPS FLEGVQLITR DTVTEHGHQI NTLNRFNLYP
EVILAFLYRP FRALAKSANW QVETCWQVNR GDLRPVESCE GIGNPHYFYI TGVFVVAGTV
ATSLFYLGVL VSDSIFGGIL SVLCFAFNHG EATRVQWTPP LRESFAFPFI IGHIAILTYI
IKYRKSSTAH LLLLISAAVP ALLFWQFTQF AFFTQICSIF AAFSMDLVPL DTAKTIIKSH
LSAFFISFVM LFGNEMMIAA LYFPSIWALA TVIYISPMLA GIRLRPLYLL ILALIFGSIT
LGLKVGFSKG LGIEDDAHIF DILRSKFTSF ANFHTRLYTC SAEFDFIQYA TIEKLSSTLL
IPLALLSIGA FSWDFLSKTS LLWRTLENED SEYGEVIYNL VQLICSTTMA VLIMRLKLFM
TPHLCITVAL LANSKLLGGD KIAKTVRSSV LVGLVAMLAF RGIPNIRHQL NIKGEYSNPD
QEMLFDWIQS NTKQDAVFAG TMPVMANVKL TTLRPIVNHP HYEHVGIRDR TLKVYSMFSK
KPVAEVHQTM KKMGVNYFIF QLMNCSNDER RPECVYRGMW DEEDPKNSAR TSLCDLWILA
ANSKDNSRIS PFKIVYNPNR NYIVLKI
