ID O16787_CAEEL Unreviewed; 315 AA.
AC O16787;
DT 01-JAN-1998, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 2.
DT 27-MAR-2024, entry version 156.
DE SubName: Full=Nematode cuticle collagen N-terminal domain-containing protein {ECO:0000313|EMBL:CCD72522.1};
GN Name=dpy-9 {ECO:0000313|EMBL:CCD72522.1,
GN ECO:0000313|WormBase:T21D12.2a};
GN ORFNames=CELE_T21D12.2 {ECO:0000313|EMBL:CCD72522.1}, T21D12.2
GN {ECO:0000313|WormBase:T21D12.2a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CCD72522.1, ECO:0000313|Proteomes:UP000001940};
RN [1] {ECO:0000313|EMBL:CCD72522.1, ECO:0000313|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CCD72522.1,
RC ECO:0000313|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RA Sulson J.E., Waterston R.;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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; BX284604; CCD72522.1; -; Genomic_DNA.
DR PIR; T28708; T28708.
DR RefSeq; NP_499889.2; NM_067488.7.
DR AlphaFoldDB; O16787; -.
DR SMR; O16787; -.
DR STRING; 6239.T21D12.2a.1; -.
DR PaxDb; 6239-T21D12-2a; -.
DR PeptideAtlas; O16787; -.
DR EnsemblMetazoa; T21D12.2a.1; T21D12.2a.1; WBGene00001071.
DR GeneID; 176846; -.
DR UCSC; T21D12.2.1; c. elegans.
DR AGR; WB:WBGene00001071; -.
DR WormBase; T21D12.2a; CE35021; WBGene00001071; dpy-9.
DR eggNOG; KOG3544; Eukaryota.
DR HOGENOM; CLU_001074_4_2_1; -.
DR InParanoid; O16787; -.
DR OMA; QDIWKQM; -.
DR OrthoDB; 2882945at2759; -.
DR PhylomeDB; O16787; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00001071; Expressed in material anatomical entity and 3 other cell types or tissues.
DR ExpressionAtlas; O16787; baseline and differential.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
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 GO; GO:0010468; P:regulation of gene expression; IMP:UniProtKB.
DR InterPro; IPR002486; Col_cuticle_N.
DR InterPro; IPR008160; Collagen.
DR PANTHER; PTHR24637:SF431; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24637; COLLAGEN; 1.
DR Pfam; PF01484; Col_cuticle_N; 1.
DR Pfam; PF01391; Collagen; 1.
DR SMART; SM01088; Col_cuticle_N; 1.
PE 4: Predicted;
KW Collagen {ECO:0000313|EMBL:CCD72522.1};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001940};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 11..61
FT /note="Nematode cuticle collagen N-terminal"
FT /evidence="ECO:0000259|SMART:SM01088"
FT REGION 88..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..298
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 315 AA; 31819 MW; D9C8A9001C4A8F29 CRC64;
MEPSNIWRTS TIVGSVVSTF AVLTVIIGLP LMHNHVQKVT TLMLTEVELC KTESQDIWKQ
MKFSRMAPNR TKRQSPYGNY GASGSGSCCA CTQGSPGPRG QPGDDGEPGR DGFPGREGDN
GIAGKYLPAP PPGTNACQKC PTGAPGPPGL PGPKGPRGPA GIEGKPGRLG EDNRPGPPGP
PGVRGEPGSP GEKGPTGDRG KVLNGAPPGP TGPPGKVGPR GLSGGKGHDG KPGLGGQPGV
RGAVGARGDA GNPGLPGPQG PKGEPGNPGT CHHCQNRAPA PSEAPGKAPP PPQDYTRPAP
ESYPSAPNGQ YLWIH
//