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DPY7_CAEEL
ID   DPY7_CAEEL              Reviewed;         318 AA.
AC   P34688;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Cuticle collagen dpy-7;
DE   AltName: Full=Protein dumpy-7;
DE   Flags: Precursor;
GN   Name=dpy-7; ORFNames=F46C8.6;
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-101; GLY-156;
RP   GLY-189 AND GLY-201.
RX   PubMed=1396579; DOI=10.1002/j.1460-2075.1992.tb05478.x;
RA   Johnstone I.L., Shafi Y., Barry J.D.;
RT   "Molecular analysis of mutations in the Caenorhabditis elegans collagen
RT   gene dpy-7.";
RL   EMBO J. 11:3857-3863(1992).
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-7 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}.
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DR   EMBL; X64435; CAA45773.1; -; Genomic_DNA.
DR   EMBL; FO081392; CCD71295.1; -; Genomic_DNA.
DR   PIR; S27977; S27977.
DR   RefSeq; NP_509274.1; NM_076873.4.
DR   AlphaFoldDB; P34688; -.
DR   BioGRID; 45937; 4.
DR   IntAct; P34688; 1.
DR   STRING; 6239.F46C8.6; -.
DR   EPD; P34688; -.
DR   PaxDb; P34688; -.
DR   PeptideAtlas; P34688; -.
DR   PRIDE; P34688; -.
DR   EnsemblMetazoa; F46C8.6.1; F46C8.6.1; WBGene00001069.
DR   GeneID; 181013; -.
DR   KEGG; cel:CELE_F46C8.6; -.
DR   UCSC; F46C8.6.1; c. elegans.
DR   CTD; 181013; -.
DR   WormBase; F46C8.6; CE04580; WBGene00001069; dpy-7.
DR   eggNOG; KOG3544; Eukaryota.
DR   GeneTree; ENSGT00970000196241; -.
DR   HOGENOM; CLU_001074_4_0_1; -.
DR   InParanoid; P34688; -.
DR   OMA; CTSCVQL; -.
DR   OrthoDB; 1446957at2759; -.
DR   PhylomeDB; P34688; -.
DR   PRO; PR:P34688; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00001069; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR   GO; GO:0060108; C:annular furrow extracellular matrix; IDA:WormBase.
DR   GO; GO:0060102; C:collagen and cuticulin-based cuticle extracellular matrix; IDA:WormBase.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR   GO; GO:0042329; F:structural constituent of collagen and cuticulin-based cuticle; IDA: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   InterPro; IPR002486; Col_cuticle_N.
DR   InterPro; IPR008160; Collagen.
DR   Pfam; PF01484; Col_cuticle_N; 1.
DR   Pfam; PF01391; Collagen; 2.
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           ?..318
FT                   /note="Cuticle collagen dpy-7"
FT                   /id="PRO_0000006429"
FT   REGION          101..318
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          101..130
FT                   /note="Triple-helical region"
FT   REGION          147..206
FT                   /note="Triple-helical region"
FT   REGION          209..235
FT                   /note="Triple-helical region"
FT   REGION          240..278
FT                   /note="Triple-helical region"
FT   COMPBIAS        215..229
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        244..270
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         101
FT                   /note="G->R: In dpy7(SC27)."
FT                   /evidence="ECO:0000269|PubMed:1396579"
FT   MUTAGEN         156
FT                   /note="G->R: In dpy7(E88)."
FT                   /evidence="ECO:0000269|PubMed:1396579"
FT   MUTAGEN         189
FT                   /note="G->Y: In dpy7(E1234)."
FT                   /evidence="ECO:0000269|PubMed:1396579"
FT   MUTAGEN         201
FT                   /note="G->R: In dpy7(M38)."
FT                   /evidence="ECO:0000269|PubMed:1396579"
SQ   SEQUENCE   318 AA;  31629 MW;  4EA66DA5FDC5737C CRC64;
     MEKPSSGANH VAKATVSLSI ASVLILGAVL TMLSIQLDEA HERLQNRMGS FKFVARNIWH
     DIVLVKSNGR IKRQYGGYGS DSAQSDNQQC TSCVQLRCPP GPIGPPGVSG EPGMDGANGR
     PGKPGLDGLD VPLDPEPAFP CVICPAGPPG TRGPQGEVGR PGQTGESGHP GLPGRPGKPG
     RVGDAGPQGE PGEQGEPGIK GPPGDDSIGG TGIKGPPGPP GPRGPKGPPG SNGLPSQNSG
     PPGPIGEMGP PGPPGPRGEP GPPGPFGPPG DSGEPGGHCP SSCGVQEIVA PSVSELDTND
     EPEKPARGGY SGGGYGKK
 
 
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