ID Q19979_CAEEL Unreviewed; 294 AA.
AC Q19979;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1996, sequence version 1.
DT 24-JAN-2024, entry version 144.
DE SubName: Full=Nematode cuticle collagen N-terminal domain-containing protein {ECO:0000313|EMBL:CAA96649.1};
GN Name=col-152 {ECO:0000313|EMBL:CAA96649.1,
GN ECO:0000313|WormBase:F32G8.5};
GN ORFNames=CELE_F32G8.5 {ECO:0000313|EMBL:CAA96649.1}, F32G8.5
GN {ECO:0000313|WormBase:F32G8.5};
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:CAA96649.1, ECO:0000313|Proteomes:UP000001940};
RN [1] {ECO:0000313|EMBL:CAA96649.1, ECO:0000313|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CAA96649.1,
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; BX284605; CAA96649.1; -; Genomic_DNA.
DR PIR; T21668; T21668.
DR RefSeq; NP_505709.1; NM_073308.1.
DR AlphaFoldDB; Q19979; -.
DR SMR; Q19979; -.
DR STRING; 6239.F32G8.5.1; -.
DR PaxDb; 6239-F32G8-5; -.
DR EnsemblMetazoa; F32G8.5.1; F32G8.5.1; WBGene00000725.
DR GeneID; 185212; -.
DR UCSC; F32G8.5; c. elegans.
DR AGR; WB:WBGene00000725; -.
DR WormBase; F32G8.5; CE05794; WBGene00000725; col-152.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000167220; -.
DR HOGENOM; CLU_001074_4_3_1; -.
DR InParanoid; Q19979; -.
DR OMA; MASTHYF; -.
DR OrthoDB; 5653239at2759; -.
DR PhylomeDB; Q19979; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00000725; Expressed in material anatomical entity and 2 other cell types or tissues.
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 InterPro; IPR002486; Col_cuticle_N.
DR PANTHER; PTHR24637:SF325; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24637; COLLAGEN; 1.
DR Pfam; PF01484; Col_cuticle_N; 1.
DR SMART; SM01088; Col_cuticle_N; 1.
PE 4: Predicted;
KW Collagen {ECO:0000313|EMBL:CAA96649.1};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001940};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 5..57
FT /note="Nematode cuticle collagen N-terminal"
FT /evidence="ECO:0000259|SMART:SM01088"
FT REGION 94..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 294 AA; 29468 MW; 8C0E9097807B73A2 CRC64;
MASIHFFTGI YSISTLLIFS SIICSAVILF EINDISNEVF NEMRAFNYYS TDAWEMMSNQ
INNSPPSQPT YFSRLARSTE QKCNCSQANN CPVGPPGPPG AAGTNGEDGS PGVAGQNGNE
GKSINAQIDT YATPSCTQCT PGPPGAPGPD GVSGPVGING RPGENGADGN PGAPGEVGAP
GDQGGAGNQG AAGKPGLPGK NGQRGSGHPG PTGPVGETGN AGNNGHPGVD GENGKPGTRG
EAGLQGKEGQ TGPIGPAGQK GENGMPGLDA GYCPCPERTY GVEPMPPARQ YEGI
//