ID Q9XUE9_CAEEL Unreviewed; 304 AA.
AC Q9XUE9;
DT 01-NOV-1999, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1999, sequence version 1.
DT 27-MAR-2024, entry version 141.
DE SubName: Full=Nematode cuticle collagen N-terminal domain-containing protein {ECO:0000313|EMBL:CAB05195.1};
GN Name=col-133 {ECO:0000313|EMBL:CAB05195.1,
GN ECO:0000313|WormBase:F52B11.4};
GN ORFNames=CELE_F52B11.4 {ECO:0000313|EMBL:CAB05195.1}, F52B11.4
GN {ECO:0000313|WormBase:F52B11.4};
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:CAB05195.1, ECO:0000313|Proteomes:UP000001940};
RN [1] {ECO:0000313|EMBL:CAB05195.1, ECO:0000313|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CAB05195.1,
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; CAB05195.1; -; Genomic_DNA.
DR PIR; T22482; T22482.
DR RefSeq; NP_502700.1; NM_070299.1.
DR AlphaFoldDB; Q9XUE9; -.
DR SMR; Q9XUE9; -.
DR IntAct; Q9XUE9; 1.
DR MINT; Q9XUE9; -.
DR STRING; 6239.F52B11.4.1; -.
DR PaxDb; 6239-F52B11-4; -.
DR PeptideAtlas; Q9XUE9; -.
DR EnsemblMetazoa; F52B11.4.1; F52B11.4.1; WBGene00000707.
DR GeneID; 186083; -.
DR KEGG; cel:CELE_F52B11.4; -.
DR UCSC; F52B11.4; c. elegans.
DR AGR; WB:WBGene00000707; -.
DR WormBase; F52B11.4; CE18724; WBGene00000707; col-133.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00970000195985; -.
DR HOGENOM; CLU_001074_4_2_1; -.
DR InParanoid; Q9XUE9; -.
DR OMA; NHEISFC; -.
DR OrthoDB; 2883930at2759; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00000707; Expressed in material anatomical entity and 3 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 InterPro; IPR008160; Collagen.
DR PANTHER; PTHR24637:SF240; 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 1: Evidence at protein level;
KW Collagen {ECO:0000313|EMBL:CAB05195.1};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Proteomics identification {ECO:0007829|PeptideAtlas:Q9XUE9};
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..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 12..64
FT /note="Nematode cuticle collagen N-terminal"
FT /evidence="ECO:0000259|SMART:SM01088"
FT REGION 72..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 112..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..161
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..244
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 304 AA; 29144 MW; 68C73E2551E72D8A CRC64;
MDEKQRLQAY RFVAYSAVTF SVVAVFSLCI TLPLVYNYVD GIKTQINHEI KFCKHSARDI
FAEVNHIRSS PKNASRFARQ AGYGGDEGVD QGSEGAQGGS CSGCCLPGAA GPAGTPGKPG
RPGRPGAAGL PGNPGRPPAQ PCEPITPPPC KPCPQGPAGA PGAPGPQGDA GAPGAPGQGS
GAGAPGPAGP KGASGAPGNP GQAGAPGQPG ADAQSESIPG APGQAGPQGP PGPAGSPGAP
GGPGQPGAPG QKGPSGAPGQ PGADGNPGAP GQPGQAGGAG EKGICPKYCA IDGGVFFEDG
TRRK
//
