ID   COL10_CAEEL             Reviewed;         294 AA.
AC   Q17460;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Cuticle collagen 10;
DE   Flags: Precursor;
GN   Name=col-10; ORFNames=B0222.8;
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 [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   [2]
RP   IDENTIFICATION.
RX   PubMed=2983191; DOI=10.1128/mcb.5.2.363-372.1985;
RA   Cox G.N., Hirsh D.;
RT   "Stage-specific patterns of collagen gene expression during development of
RT   Caenorhabditis elegans.";
RL   Mol. Cell. Biol. 5:363-372(1985).
RN   [3]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=9875852; DOI=10.1016/s0092-8674(00)81722-5;
RA   Lu X., Horvitz H.R.;
RT   "lin-35 and lin-53, two genes that antagonize a C. elegans Ras pathway,
RT   encode proteins similar to Rb and its binding protein RbAp48.";
RL   Cell 95:981-991(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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Collagen polypeptide chains are complexed within the cuticle
CC       by disulfide bonds and other types of covalent cross-links.
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in hypodermal cells.
CC       {ECO:0000269|PubMed:9875852}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during larval development.
CC       {ECO:0000269|PubMed:9875852}.
CC   -!- SIMILARITY: Belongs to the cuticular collagen family. {ECO:0000305}.
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DR   EMBL; FO080127; CCD61421.1; -; Genomic_DNA.
DR   PIR; T29839; T29839.
DR   RefSeq; NP_505376.1; NM_072975.4.
DR   AlphaFoldDB; Q17460; -.
DR   SMR; Q17460; -.
DR   BioGRID; 44336; 2.
DR   DIP; DIP-25271N; -.
DR   IntAct; Q17460; 2.
DR   STRING; 6239.B0222.8; -.
DR   PaxDb; Q17460; -.
DR   EnsemblMetazoa; B0222.8.1; B0222.8.1; WBGene00000599.
DR   UCSC; B0222.8; c. elegans.
DR   WormBase; B0222.8; CE06699; WBGene00000599; col-10.
DR   eggNOG; KOG3544; Eukaryota.
DR   GeneTree; ENSGT00970000195960; -.
DR   HOGENOM; CLU_001074_4_3_1; -.
DR   InParanoid; Q17460; -.
DR   OMA; TCPPRDT; -.
DR   OrthoDB; 1595166at2759; -.
DR   PhylomeDB; Q17460; -.
DR   SignaLink; Q17460; -.
DR   PRO; PR:Q17460; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00000599; Expressed in larva and 3 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:0002164; P:larval development; NAS:UniProtKB.
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..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..294
FT                   /note="Cuticle collagen 10"
FT                   /id="PRO_0000307866"
FT   REGION          100..133
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          102..127
FT                   /note="Triple-helical region"
FT   REGION          149..278
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          153..274
FT                   /note="Triple-helical region"
FT   COMPBIAS        100..119
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        153..167
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   294 AA;  28469 MW;  A7C70A6A3DA8BA0E CRC64;
     MEKFLVTLST GAASIAVLAV LFTVPSLYNT INEVHDEVLD GVSVFRVETD SAWTEMMDIQ
     ITVTPPTKPR VNPFNSIFRQ KRQTFSGLPA WCQCEPTKPT CPPGPPGPPG QPGAPGTPGA
     PGPKGDDNTA TFAPLTCAPV SQDCVKCPEG PAGPAGPEGP AGPAGPDGQP GAPGNAGNPG
     SDGQPGAPGD NGQDGAPGQD GQPGAPGQDG QRGSGAPGGP GAPGNAGPAG PAGQDGAPGQ
     DGQPGPAGPA GQDGAPGNAG SDGQPGAPGG PGLPGNDAAY CACPPRSAVF VSRH