CO145_CAEBR
ID CO145_CAEBR Reviewed; 561 AA.
AC A8XV37;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-MAY-2016, sequence version 2.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Putative cuticle collagen 145 {ECO:0000250|UniProtKB:Q17459};
DE Flags: Precursor;
GN Name=col-145 {ECO:0000312|EMBL:CAP36504.2}; ORFNames=CBG19217;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1] {ECO:0000312|EMBL:CAP36504.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000312|EMBL:CAP36504.2};
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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|UniProtKB:Q17459}.
CC -!- SUBUNIT: Collagen polypeptide chains are complexed within the cuticle
CC by disulfide bonds and other types of covalent cross-links.
CC {ECO:0000250|UniProtKB:Q17459}.
CC -!- SIMILARITY: Belongs to the cuticular collagen family. {ECO:0000255}.
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DR EMBL; HE601047; CAP36504.2; -; Genomic_DNA.
DR AlphaFoldDB; A8XV37; -.
DR SMR; A8XV37; -.
DR STRING; 6238.CBG19217; -.
DR WormBase; CBG19217; CBP43255; WBGene00038475; Cbr-col-145.
DR eggNOG; KOG3544; Eukaryota.
DR HOGENOM; CLU_001074_4_3_1; -.
DR InParanoid; A8XV37; -.
DR OMA; ATEGFAY; -.
DR OrthoDB; 1751568at2759; -.
DR Proteomes; UP000008549; Chromosome V.
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; 1.
DR SMART; SM01088; Col_cuticle_N; 1.
PE 3: Inferred from homology;
KW Collagen; Cuticle; Disulfide bond; Reference proteome; Repeat; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..561
FT /note="Putative cuticle collagen 145"
FT /evidence="ECO:0000255"
FT /id="PRO_0000351211"
FT DOMAIN 485..543
FT /note="Collagen-like"
FT /evidence="ECO:0000255"
FT REGION 100..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 102..127
FT /note="Triple-helical region"
FT /evidence="ECO:0000255"
FT REGION 148..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..276
FT /note="Triple-helical region"
FT /evidence="ECO:0000255"
FT REGION 367..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..544
FT /note="Triple-helical region"
FT /evidence="ECO:0000255"
FT REGION 422..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
FT COMPBIAS 367..386
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 561 AA; 54598 MW; 8B4FAA42C188AB8B CRC64;
MEKILVTLST GAASIAVLAV LFTIPSLYNT INEVHDEVLD GVSVFRVETD SAWTEMMDIQ
ITVTPPTKPR VNPFNSIFRQ KRQTFSGLPA WCQCEPTKPT CPPGPPGPPG QPGQPGTPGA
PGPKGEDNTS TYAPITCAPV SQDCVKCPQG PAGPEGPAGP AGPAGPDGQP GAPGNAGNPG
SDGQPGAPGD DGQPGAPGQD GQPGAPGQDG QRGSGAPGAP GAPGNAGPAG PAGQDGAPGQ
DGQPGPAGPA GQDGAPGNAG SDGQPGAPGG PGLPGNDAAY CACPHGEDSC DHLYRSCLPR
CFGEVLDGVS VFRVETDSAW TEMMDIQVTV TPPTKPRVNP FNSVFRQKRQ TFSGLPAWCQ
CEPTKPTCPP GPPGPPGQPG QPGTPGAPGP KGEDNTATYA PITCAPVSQD CVKCPQGPAG
PTGPAGLAGP AGPDGQPGFP GQRGNDGFPG APGAPGDNGQ PGAPGQDGFP GQPGADGQRG
SGAPGAPGAP GNAGPAGPAG QDGFPGQDGQ PGPAGPAGQD GFPGNAGSDG QPGAPGGPGL
PGNDAAYCAC PPRSAVFLSR H