ID   COL2_CAEEL              Reviewed;         301 AA.
AC   P17656;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Cuticle collagen 2;
DE   Flags: Precursor;
GN   Name=col-2; ORFNames=W01B6.7;
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].
RC   STRAIN=Bristol N2;
RX   PubMed=7139711; DOI=10.1016/0092-8674(82)90256-2;
RA   Kramer J.M., Cox G.N., Hirsh D.;
RT   "Comparisons of the complete sequences of two collagen genes from
RT   Caenorhabditis elegans.";
RL   Cell 30:599-606(1982).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RC   STRAIN=Bristol N2;
RX   PubMed=2578467; DOI=10.1016/s0021-9258(18)89683-1;
RA   Kramer J.M., Cox G.N., Hirsh D.;
RT   "Expression of the Caenorhabditis elegans collagen genes col-1 and col-2 is
RT   developmentally regulated.";
RL   J. Biol. Chem. 260:1945-1951(1985).
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Bristol N2;
RA   Kohara Y., Shin-i T., Suzuki Y., Sugano S., Thierry-Mieg D.,
RA   Thierry-Mieg J.;
RT   "The Caenorhabditis elegans transcriptome project, a complementary view of
RT   the genome.";
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
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   -!- TISSUE SPECIFICITY: Syncytial dorsal and ventral epidermis.
CC       {ECO:0000269|PubMed:2578467}.
CC   -!- DEVELOPMENTAL STAGE: Low level expression from embryos at comma stage
CC       to adult; maximal level in dauer larvae. {ECO:0000269|PubMed:2578467}.
CC   -!- SIMILARITY: Belongs to the cuticular collagen family. {ECO:0000305}.
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DR   EMBL; J01048; AAA27990.1; -; Genomic_DNA.
DR   EMBL; V00148; CAA23464.1; -; Genomic_DNA.
DR   EMBL; Z68301; CAA92620.1; -; Genomic_DNA.
DR   EMBL; AY347575; AAP97869.1; -; mRNA.
DR   PIR; B31219; B31219.
DR   RefSeq; NP_501829.1; NM_069428.3.
DR   AlphaFoldDB; P17656; -.
DR   SMR; P17656; -.
DR   STRING; 6239.W01B6.7; -.
DR   PaxDb; P17656; -.
DR   PeptideAtlas; P17656; -.
DR   EnsemblMetazoa; W01B6.7.1; W01B6.7.1; WBGene00000593.
DR   GeneID; 177872; -.
DR   KEGG; cel:CELE_W01B6.7; -.
DR   UCSC; W01B6.7; c. elegans.
DR   CTD; 177872; -.
DR   WormBase; W01B6.7; CE03759; WBGene00000593; col-2.
DR   eggNOG; KOG3544; Eukaryota.
DR   GeneTree; ENSGT00970000195890; -.
DR   HOGENOM; CLU_001074_4_2_1; -.
DR   InParanoid; P17656; -.
DR   OMA; CDGCCNP; -.
DR   OrthoDB; 1598349at2759; -.
DR   PRO; PR:P17656; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00000593; Expressed in material anatomical entity and 2 other tissues.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR   GO; GO:0042302; F:structural constituent of cuticle; IEA:UniProtKB-KW.
DR   GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR   InterPro; IPR002486; Col_cuticle_N.
DR   Pfam; PF01484; Col_cuticle_N; 1.
DR   SMART; SM01088; Col_cuticle_N; 1.
PE   2: Evidence at transcript level;
KW   Collagen; Cuticle; Disulfide bond; Reference proteome; Repeat; Signal.
FT   SIGNAL          1..37
FT                   /evidence="ECO:0000255"
FT   CHAIN           38..301
FT                   /note="Cuticle collagen 2"
FT                   /id="PRO_0000006421"
FT   REGION          105..134
FT                   /note="Triple-helical region"
FT   REGION          109..284
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          153..176
FT                   /note="Triple-helical region"
FT   REGION          183..212
FT                   /note="Triple-helical region"
FT   REGION          215..282
FT                   /note="Triple-helical region"
FT   COMPBIAS        109..126
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        142..194
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   301 AA;  28025 MW;  33317E3BDAC302F9 CRC64;
     MDIDARIKAY KFVAYSAVTF SVVAVVSVFI TLPMVYNYVN NVKKQIHTDV NFCKVSARDI
     WSEVHLIKDA PGNNTRVARQ AYSTGGAGGG GGGGGGGCDG CCNPGPPGPG GSPGKPGKPG
     KPGAPGAPGN PGKGASAPCE PVTQPPCQPC PGGPPGPAGP AGPPGPPGPD GNPGSPAGPS
     GPGPAGPPGP AGPAGNDGAP GAPGGPGEPG ASEQGGPGEP GPAGPPGPAG PAGNDGAPGT
     GGPGPAGPKG PPGAAGAPGA DGNPGGPGTA GKPGGEGEKG ICPKYCAIDG GVFFEDGTRR
     R