ID G0P540_CAEBE Unreviewed; 303 AA.
AC G0P540;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Nematode cuticle collagen N-terminal domain-containing protein {ECO:0000259|SMART:SM01088};
GN ORFNames=CAEBREN_29497 {ECO:0000313|EMBL:EGT45188.1};
OS Caenorhabditis brenneri (Nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=135651 {ECO:0000313|Proteomes:UP000008068};
RN [1] {ECO:0000313|Proteomes:UP000008068}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB2801 {ECO:0000313|Proteomes:UP000008068};
RG Caenorhabditis brenneri Sequencing and Analysis Consortium;
RA Wilson R.K.;
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
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; GL380073; EGT45188.1; -; Genomic_DNA.
DR AlphaFoldDB; G0P540; -.
DR STRING; 135651.G0P540; -.
DR EnsemblMetazoa; CBN29497.1; CBN29497.1; WBGene00191462.
DR eggNOG; KOG3544; Eukaryota.
DR HOGENOM; CLU_001074_4_2_1; -.
DR InParanoid; G0P540; -.
DR Proteomes; UP000008068; 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:SF275; 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:UP000008068};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 13..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 13..65
FT /note="Nematode cuticle collagen N-terminal"
FT /evidence="ECO:0000259|SMART:SM01088"
FT REGION 72..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..169
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..202
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..276
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 303 AA; 29503 MW; B44FEF564A4F6A94 CRC64;
MDSSDGRTKA YKFVAYAAVS FSIVAVLSVV LTLPMVYNYV SHVRQQMNHE LQFCKGSAKD
IFAEVNFMKT HSGPAAPGNR TARQSGYGQP EVNPSANLQC EGCCLPGPPG PAGAPGKPGK
PGRPGAPGQP GIPGKPPTAP CEPTTPPPCK PCPQGPPGPP GPPGAPGDPG EAGTPGRPGT
DATPGLPGPR GPPGPPGEAG QPGPQGDPGA PAQSEPLTPG APGEPGDAGP AGPPGPPGAP
GNDGPAGPPG PKGSPGPDGP PGVDGQAGPP GPPGQAGTPG EKGICPKYCA LDGGVFFEDG
TRR
//
