ID A8XAQ5_CAEBR Unreviewed; 299 AA.
AC A8XAQ5;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Protein CBR-COL-85 {ECO:0000313|EMBL:CAP29720.1};
GN Name=col-85 {ECO:0000313|WormBase:CBG10272};
GN Synonyms=Cbr-col-85 {ECO:0000313|EMBL:CAP29720.1};
GN ORFNames=CBG10272 {ECO:0000313|WormBase:CBG10272}, CBG_10272
GN {ECO:0000313|EMBL:CAP29720.1};
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP29720.1, ECO:0000313|Proteomes:UP000008549};
RN [1] {ECO:0000313|EMBL:CAP29720.1, ECO:0000313|Proteomes:UP000008549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000313|EMBL:CAP29720.1,
RC ECO:0000313|Proteomes:UP000008549};
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., 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., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- SUBUNIT: Collagen polypeptide chains are complexed within the cuticle
CC by disulfide bonds and other types of covalent cross-links.
CC {ECO:0000256|ARBA:ARBA00011518}.
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DR EMBL; HE600905; CAP29720.1; -; Genomic_DNA.
DR RefSeq; XP_002631992.1; XM_002631946.1.
DR AlphaFoldDB; A8XAQ5; -.
DR STRING; 6238.A8XAQ5; -.
DR EnsemblMetazoa; CBG10272.1; CBG10272.1; WBGene00031690.
DR GeneID; 8573991; -.
DR KEGG; cbr:CBG_10272; -.
DR CTD; 8573991; -.
DR WormBase; CBG10272; CBP02529; WBGene00031690; Cbr-col-85.
DR eggNOG; KOG3544; Eukaryota.
DR HOGENOM; CLU_001074_4_2_1; -.
DR InParanoid; A8XAQ5; -.
DR OMA; ATPMMYN; -.
DR OrthoDB; 2883462at2759; -.
DR Proteomes; UP000008549; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0042302; F:structural constituent of cuticle; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR InterPro; IPR002486; Col_cuticle_N.
DR InterPro; IPR008160; Collagen.
DR PANTHER; PTHR24637:SF319; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24637; COLLAGEN; 1.
DR Pfam; PF01484; Col_cuticle_N; 1.
DR Pfam; PF01391; Collagen; 2.
DR SMART; SM01088; Col_cuticle_N; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000008549};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 17..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 16..68
FT /note="Nematode cuticle collagen N-terminal"
FT /evidence="ECO:0000259|SMART:SM01088"
FT REGION 117..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..179
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..206
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..238
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 299 AA; 28009 MW; 18B8687878EE8D9D CRC64;
MADEKQKLAE IESLKKVAFF GISVATIATL VAIVATPMMY NYLQHVQSSL QNEVEFCRHR
TDGLWDEFSR FEVVHGKETR IKRRARAFGA ESYSTGAGGG GGGGCCSCGI GAAGPPGPPG
ADGNPGTDGA AGNPGQAGAD AEAAAAPTAA DFCFDCPPGP AGPAGNAGPP GPPGGPGAPG
NTPAGGAAGA AGPPGPPGPP GNDGAPGAPG NPGAPGAVNT VPGQQGPPGP PGPAGPPGAA
GNPGTAGYAQ PGPPGPAGDA GPDGAPGNPG QPGPAGDAGA PGSGGGCDHC PPPRTAPGY
//