ID   DPY2_CAEEL              Reviewed;         360 AA.
AC   P35799; Q22477;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Cuticle collagen dpy-2;
DE   AltName: Full=Protein dumpy-2;
DE   Flags: Precursor;
GN   Name=dpy-2; ORFNames=T14B4.6;
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 GLY-129; GLY-183;
RP   GLY-247 AND GLY-253.
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].
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. Mutations in dpy-2 affects
CC       the body shape.
CC   -!- SUBUNIT: Collagen polypeptide chains are complexed within the cuticle
CC       by disulfide bonds and other types of covalent cross-links.
CC   -!- SIMILARITY: Belongs to the cuticular collagen 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; L12706; AAA17398.2; -; Genomic_DNA.
DR   EMBL; FO080626; CCD65274.1; -; Genomic_DNA.
DR   PIR; T28888; T28888.
DR   PIR; T37285; T37285.
DR   RefSeq; NP_495367.1; NM_062966.5.
DR   AlphaFoldDB; P35799; -.
DR   BioGRID; 39445; 5.
DR   IntAct; P35799; 1.
DR   STRING; 6239.T14B4.6; -.
DR   EPD; P35799; -.
DR   PaxDb; P35799; -.
DR   PeptideAtlas; P35799; -.
DR   EnsemblMetazoa; T14B4.6.1; T14B4.6.1; WBGene00001064.
DR   GeneID; 174107; -.
DR   KEGG; cel:CELE_T14B4.6; -.
DR   UCSC; T14B4.6; c. elegans.
DR   CTD; 174107; -.
DR   WormBase; T14B4.6; CE04953; WBGene00001064; dpy-2.
DR   eggNOG; KOG3544; Eukaryota.
DR   GeneTree; ENSGT00970000196743; -.
DR   HOGENOM; CLU_001074_4_2_1; -.
DR   InParanoid; P35799; -.
DR   OrthoDB; 1181208at2759; -.
DR   PhylomeDB; P35799; -.
DR   PRO; PR:P35799; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00001064; Expressed in embryo and 3 other tissues.
DR   GO; GO:0005581; C:collagen trimer; ISS:WormBase.
DR   GO; GO:0042329; F:structural constituent of collagen and cuticulin-based cuticle; ISS:WormBase.
DR   GO; GO:0042338; P:cuticle development involved in collagen and cuticulin-based cuticle molting cycle; IMP:WormBase.
DR   GO; GO:0040032; P:post-embryonic body morphogenesis; IMP:WormBase.
DR   GO; GO:0040014; P:regulation of multicellular organism growth; IMP:WormBase.
DR   InterPro; IPR002486; Col_cuticle_N.
DR   InterPro; IPR008160; Collagen.
DR   Pfam; PF01484; Col_cuticle_N; 1.
DR   Pfam; PF01391; Collagen; 1.
DR   SMART; SM01088; Col_cuticle_N; 1.
PE   1: Evidence at protein level;
KW   Collagen; Cuticle; Disulfide bond; Reference proteome; Repeat; Signal.
FT   SIGNAL          1..?
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..360
FT                   /note="Cuticle collagen dpy-2"
FT                   /id="PRO_0000006428"
FT   REGION          123..152
FT                   /note="Triple-helical region"
FT   REGION          127..158
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          174..360
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          174..230
FT                   /note="Triple-helical region"
FT   REGION          238..303
FT                   /note="Triple-helical region"
FT   COMPBIAS        272..286
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        292..306
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         129
FT                   /note="G->E: In dpy2(SC38)."
FT                   /evidence="ECO:0000269|PubMed:8241567"
FT   MUTAGEN         183
FT                   /note="G->R: In dpy2(E8)."
FT                   /evidence="ECO:0000269|PubMed:8241567"
FT   MUTAGEN         247
FT                   /note="G->R: In dpy2(E489)."
FT                   /evidence="ECO:0000269|PubMed:8241567"
FT   MUTAGEN         253
FT                   /note="G->R: In dpy2(Q292)."
FT                   /evidence="ECO:0000269|PubMed:8241567"
FT   CONFLICT        355..360
FT                   /note="RRIRKW -> DGYGNGESVSNHKNNGGYYHLRKFTQ (in Ref. 2;
FT                   CCD65274)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   360 AA;  36738 MW;  B827960838A22578 CRC64;
     MKSQTSGYVD PQTEEYDESR EKSYQVLIAV SGVLSITSLL ILVLFVPSMY NYVDNISRFS
     RRDFEFCQAS ANDLETEMMS VREGLLRGRN VTKRAAGYGH YNPSMLAADS PQFQECPACC
     IPGERGPSGD SGLPALPGAP GPDGAPGRPG TTPNASCIPE RVFEPPPCLP CPQGPRGVPG
     HPGFPGDPGE YGIGGRPGSD GMPGKPGDPG LAGPIGPPGE SGPIGDKGRT PEAHVIPGPP
     GDSGLPGPWG PPGSAGMPGE DGYAGTPGEK GWPGPPGAPG PGGMPGPNGP TGEQGPSGTP
     GTCVCQDTEV VMNDEKGRVP APRDNVAPGA TGGSYEPQGG NDAAAPSAIS QSQNRRIRKW