DPY10_CAEEL
ID DPY10_CAEEL Reviewed; 372 AA.
AC P35800; Q22476;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Cuticle collagen dpy-10;
DE AltName: Full=Protein dumpy-10;
DE Flags: Precursor;
GN Name=dpy-10; ORFNames=T14B4.7;
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], AND MUTAGENESIS OF ARG-108; GLY-153;
RP GLY-168 AND GLY-237.
RC STRAIN=Bristol N2;
RX PubMed=8241567; DOI=10.1091/mbc.4.8.803;
RA Levy A.D., Yang J., Kramer J.M.;
RT "Molecular and genetic analyses of the Caenorhabditis elegans dpy-2 and
RT dpy-10 collagen genes: a variety of molecular alterations affect organismal
RT morphology.";
RL Mol. Biol. Cell 4:803-817(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
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).
CC -!- FUNCTION: Nematode cuticles are composed largely of collagen-like
CC proteins. The cuticle functions both as an exoskeleton and as a barrier
CC to protect the worm from its environment.
CC -!- SUBUNIT: Collagen polypeptide chains are complexed within the cuticle
CC by disulfide bonds and other types of covalent cross-links.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b;
CC IsoId=P35800-1; Sequence=Displayed;
CC Name=a;
CC IsoId=P35800-2; Sequence=VSP_007377, VSP_019859;
CC -!- SIMILARITY: Belongs to the cuticular collagen family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA17395.2; Type=Erroneous gene model prediction; Evidence={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; L12692; AAA17395.2; ALT_SEQ; Genomic_DNA.
DR EMBL; FO080626; CCD65275.1; -; Genomic_DNA.
DR EMBL; FO080626; CCD65276.1; -; Genomic_DNA.
DR RefSeq; NP_001335511.1; NM_001348636.1.
DR AlphaFoldDB; P35800; -.
DR SMR; P35800; -.
DR BioGRID; 39444; 5.
DR STRING; 6239.T14B4.7b.1; -.
DR EPD; P35800; -.
DR PaxDb; P35800; -.
DR PeptideAtlas; P35800; -.
DR EnsemblMetazoa; T14B4.7.1; T14B4.7.1; WBGene00001072.
DR GeneID; 36805042; -.
DR KEGG; cel:CELE_T14B4.7; -.
DR UCSC; T14B4.7a.1; c. elegans. [P35800-1]
DR CTD; 36805042; -.
DR WormBase; T14B4.7; CE51880; WBGene00001072; dpy-10.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00970000196743; -.
DR InParanoid; P35800; -.
DR OMA; PGRNGMT; -.
DR OrthoDB; 1590584at2759; -.
DR PRO; PR:P35800; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00001072; Expressed in embryo and 4 other tissues.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR GO; GO:0042329; F:structural constituent of collagen and cuticulin-based cuticle; ISS:WormBase.
DR GO; GO:0042302; F:structural constituent of cuticle; NAS:UniProtKB.
DR GO; GO:0040002; P:collagen and cuticulin-based cuticle development; NAS:UniProtKB.
DR GO; GO:0042338; P:cuticle development involved in collagen and cuticulin-based cuticle molting cycle; IMP:WormBase.
DR GO; GO:0040011; P:locomotion; IMP:WormBase.
DR GO; GO:0040032; P:post-embryonic body morphogenesis; IMP:WormBase.
DR InterPro; IPR002486; Col_cuticle_N.
DR InterPro; IPR008160; Collagen.
DR Pfam; PF01484; Col_cuticle_N; 1.
DR Pfam; PF01391; Collagen; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Collagen; Cuticle; Disulfide bond;
KW Reference proteome; Repeat; Signal.
FT SIGNAL 1..45
FT /evidence="ECO:0000255"
FT CHAIN 46..372
FT /note="Cuticle collagen dpy-10"
FT /id="PRO_0000006430"
FT REGION 144..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..173
FT /note="Triple-helical region"
FT REGION 195..251
FT /note="Triple-helical region"
FT REGION 259..324
FT /note="Triple-helical region"
FT COMPBIAS 184..200
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..21
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_007377"
FT VAR_SEQ 69..84
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_019859"
FT MUTAGEN 108
FT /note="R->C: In dpy10(CN64)."
FT /evidence="ECO:0000269|PubMed:8241567"
FT MUTAGEN 153
FT /note="G->E: In dpy10(SC48)."
FT /evidence="ECO:0000269|PubMed:8241567"
FT MUTAGEN 168
FT /note="G->E: In dpy10(CG37)."
FT /evidence="ECO:0000269|PubMed:8241567"
FT MUTAGEN 237
FT /note="G->R: In dpy10(Q291)."
FT /evidence="ECO:0000269|PubMed:8241567"
SQ SEQUENCE 372 AA; 38530 MW; 4043F05F655F849F CRC64;
MKNNAKEDYR TFSLTTNYSR QMIYRCVTGL QIGFSLFSFI IVCVALPIMY NHVQNTITYV
DREMAYCEVR FLYFYCIKFF STLQRSNDEA ALELQYGKMR MTGNRTARGA YGSGASHGFR
PTAYGDEITG APLETECPGC CIPGPPGPRG SSGTPGKPGL PGNAGKPGMP GTTPNQTCPL
NQVREPPPCR PCPKGPPGIK GWPGFPGDVG PPGPPGLKGI DGEDGAPGET GPTGPPGYRG
GPGAPGDKGP TPEGDLKEGP PGDEGPPGPI GAPGMPGLPG RNGLTGGQGE RGWPGVSGES
GEPGYPGPEG PMGGQGPPGE PGVCVCQNVD SILLINPGPQ PRIRADDYNS DDGYGGSRGG
GDRAGYQGYG RK
