COL13_CAEEL
ID COL13_CAEEL Reviewed; 316 AA.
AC P20631;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Cuticle collagen 13;
DE Flags: Precursor;
GN Name=col-13; ORFNames=F15H10.2;
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=1689778; DOI=10.1016/0022-2836(90)90360-x;
RA Park Y.-S., Kramer J.M.;
RT "Tandemly duplicated Caenorhabditis elegans collagen genes differ in their
RT modes of splicing.";
RL J. Mol. Biol. 211:395-406(1990).
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.
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; X51623; CAA35955.1; -; Genomic_DNA.
DR EMBL; Z73972; CAA98258.1; -; Genomic_DNA.
DR PIR; S08170; S08170.
DR RefSeq; NP_505677.1; NM_073276.1.
DR AlphaFoldDB; P20631; -.
DR SMR; P20631; -.
DR STRING; 6239.F15H10.2; -.
DR EPD; P20631; -.
DR PaxDb; P20631; -.
DR EnsemblMetazoa; F15H10.2.1; F15H10.2.1; WBGene00000602.
DR GeneID; 179452; -.
DR KEGG; cel:CELE_F15H10.2; -.
DR UCSC; F15H10.2; c. elegans.
DR CTD; 179452; -.
DR WormBase; F15H10.2; CE05639; WBGene00000602; col-13.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000168256; -.
DR HOGENOM; CLU_001074_4_2_1; -.
DR InParanoid; P20631; -.
DR OMA; LTDGLWQ; -.
DR OrthoDB; 1601318at2759; -.
DR PhylomeDB; P20631; -.
DR PRO; PR:P20631; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00000602; Expressed in larva 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 InterPro; IPR008160; Collagen.
DR Pfam; PF01484; Col_cuticle_N; 1.
DR Pfam; PF01391; Collagen; 2.
DR SMART; SM01088; Col_cuticle_N; 1.
PE 3: Inferred from homology;
KW Collagen; Cuticle; Disulfide bond; Reference proteome; Repeat; Signal.
FT SIGNAL 1..36
FT /evidence="ECO:0000255"
FT CHAIN 37..316
FT /note="Cuticle collagen 13"
FT /id="PRO_0000006425"
FT REGION 127..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..157
FT /note="Triple-helical region"
FT REGION 176..202
FT /note="Triple-helical region"
FT REGION 206..235
FT /note="Triple-helical region"
FT REGION 240..266
FT /note="Triple-helical region"
FT REGION 269..304
FT /note="Triple-helical region"
FT COMPBIAS 241..255
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 316 AA; 30100 MW; 00C6D08FBC4701AF CRC64;
MSEDLKQIAQ ETESLRKVAF FGIAVSTIAT LTAIIAVPML YNYMQHVQSS LQSEVEFCQH
RSNGLWDEYK RFQGVSGVEG RIKRDAYHRS LGVSGASRKA RRQSYGNDAA VGGFGGSSGG
SCCSCGSGAA GPAGSPGQDG APGNDGAPGA PGNPGQDASE DQTAGPDSFC FDCPAGPPGP
SGAPGQKGPS GAPGAPGQSG GAALPGPPGP AGPPGPAGQP GSNGNAGAPG APGQVVDVPG
TPGPAGPPGS PGPAGAPGQP GQAGSSQPGG PGPQGDAGAP GAPGAPGQAG APGQDGESGS
EGACDHCPPP RTAPGY
