COL99_CAEBR
ID COL99_CAEBR Reviewed; 686 AA.
AC A8WR59;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Putative cuticle collagen 99 {ECO:0000250|UniProtKB:O76368};
DE Flags: Precursor;
GN Name=col-99 {ECO:0000312|EMBL:CAP22967.2}; ORFNames=CBG01652;
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:CAP22967.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000312|EMBL:CAP22967.2};
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:Q09457}.
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:Q09457}.
CC -!- SIMILARITY: Belongs to the cuticular collagen family. {ECO:0000255}.
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DR EMBL; HE601298; CAP22967.2; -; Genomic_DNA.
DR AlphaFoldDB; A8WR59; -.
DR STRING; 6238.CBG01652; -.
DR WormBase; CBG01652a; CBP42766; WBGene00024856; Cbr-col-99.
DR eggNOG; KOG3544; Eukaryota.
DR HOGENOM; CLU_020867_0_0_1; -.
DR InParanoid; A8WR59; -.
DR OMA; CSWKPME; -.
DR OrthoDB; 1239042at2759; -.
DR Proteomes; UP000008549; Chromosome IV.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0042302; F:structural constituent of cuticle; IEA:UniProtKB-KW.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR InterPro; IPR008160; Collagen.
DR Pfam; PF01391; Collagen; 4.
PE 3: Inferred from homology;
KW Collagen; Cuticle; Disulfide bond; Glycoprotein; Reference proteome;
KW Repeat; Signal.
FT SIGNAL 1..?
FT /evidence="ECO:0000255"
FT CHAIN ?..686
FT /note="Putative cuticle collagen 99"
FT /evidence="ECO:0000255"
FT /id="PRO_0000367043"
FT REGION 42..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..201
FT /note="Triple-helical region"
FT /evidence="ECO:0000255"
FT REGION 163..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..263
FT /note="Triple-helical region"
FT /evidence="ECO:0000255"
FT REGION 268..296
FT /note="Triple-helical region"
FT /evidence="ECO:0000255"
FT REGION 394..439
FT /note="Triple-helical region"
FT /evidence="ECO:0000255"
FT REGION 475..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..536
FT /note="Triple-helical region"
FT /evidence="ECO:0000255"
FT REGION 538..576
FT /note="Triple-helical region"
FT /evidence="ECO:0000255"
FT REGION 577..636
FT /note="Triple-helical region"
FT /evidence="ECO:0000255"
FT COMPBIAS 230..244
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..417
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..555
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 446
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 535
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 686 AA; 69737 MW; FC0674107D07A886 CRC64;
MCCYLFQQRE RERKGTLLTG EAYKLCETIT LLDVLQIEQD IPPIGNSDDN SDDVAKSRKV
RNSCMCPPGP PGERGPVGPP GLPGLPAPYY RRPRVPLSNV VFVVVIVIVF FKFQNLDESI
SRKMRAFGML YSPDGQAIQL RGMPGPPGPA GPKGLRGYPG FPGPIGLDGP RGLPGTPGSK
GERGERGPVG PPGFPGPKGD RGVMTGPFGV HGQHPAPSGP IGHHTTMNIG PPGPPGPPGP
PGPAGRDGRH GMKGDRGLPG FDGESKIGPK GETGNPGRDG IPGARGPPGE RGEKGDTAFL
STYPRGQSVS TVSSSGSQGP PGPPGPPGVC QVSQCIGVQG PPGIPGEPGR TIIGPQGPPG
EKGERGERGE TGDKGPPGTP GAASLLNGGK ALVGPPGPPG RDGRPGEKGE KGEHGLRGDM
GLPGPEGTPG KRGRRGRHGI SLVAPNGTIN EDLKKLLKTE LMPLLIEDIS ELRGKNVIPG
PPGPPGPRGH HGPIGPAGER GPQGLPGHSG ERGERGDIGP PGLPGQPGAA ESSGNQSGPR
GPPGLPGPPG EKGDLGPPGL PGQPGALGLP GHPGPMGLRG PHGTEGKQGK QGPEGPKGYP
GPMGPQGPPG NDGEPGIDGR PGPAGEKGDQ GIPGLDAPCP TGPDGLPLPY CSWKPMDGKN
DVWERRKRAT LPRSESVPEE RTYIKN
