COL71_CAEEL
ID COL71_CAEEL Reviewed; 371 AA.
AC Q9N4U2;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Cuticle collagen 71 {ECO:0000303|PubMed:24569038};
GN Name=col-71 {ECO:0000312|WormBase:Y49F6B.10};
GN ORFNames=Y49F6B.10 {ECO:0000312|WormBase:Y49F6B.10};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=24569038; DOI=10.1534/g3.113.009522;
RA Jackson B.M., Abete-Luzi P., Krause M.W., Eisenmann D.M.;
RT "Use of an activated beta-catenin to identify Wnt pathway target genes in
RT caenorhabditis elegans, including a subset of collagen genes expressed in
RT late larval development.";
RL G3 (Bethesda) 4:733-747(2014).
CC -!- FUNCTION: Probable cuticular collagen-like protein (Probable). Nematode
CC cuticles are composed largely of collagen-like proteins (Probable). The
CC cuticle functions both as an exoskeleton and as a barrier to protect
CC the worm from its environment (Probable). Acts downstream of the Wnt
CC signaling pathway, perhaps in the formation of the adult cuticle
CC (PubMed:24569038). {ECO:0000269|PubMed:24569038,
CC ECO:0000305|PubMed:24569038}.
CC -!- SUBUNIT: Collagen polypeptide chains are complexed within the cuticle
CC by disulfide bonds and other types of covalent cross-links.
CC {ECO:0000305|PubMed:24569038}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}. Nucleus {ECO:0000269|PubMed:24569038}.
CC -!- DEVELOPMENTAL STAGE: Expressed in hypodermal cells and seam cells, in
CC the larval L4 stage, and in the young adult (PubMed:24569038). Not
CC expressed in the cells of the developing vulva (PubMed:24569038).
CC {ECO:0000269|PubMed:24569038}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes hypodermal or
CC cuticular rupture, typically in the anterior body region
CC (PubMed:24569038). Dumpy body shape (PubMed:24569038). Defects in
CC cuticle integrity (PubMed:24569038). {ECO:0000269|PubMed:24569038}.
CC -!- SIMILARITY: Belongs to the cuticular collagen family. {ECO:0000305}.
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DR EMBL; BX284602; CCD64720.1; -; Genomic_DNA.
DR RefSeq; NP_494562.1; NM_062161.4.
DR AlphaFoldDB; Q9N4U2; -.
DR DIP; DIP-26702N; -.
DR STRING; 6239.Y49F6B.10; -.
DR EPD; Q9N4U2; -.
DR PaxDb; Q9N4U2; -.
DR PeptideAtlas; Q9N4U2; -.
DR EnsemblMetazoa; Y49F6B.10.1; Y49F6B.10.1; WBGene00000647.
DR GeneID; 173695; -.
DR KEGG; cel:CELE_Y49F6B.10; -.
DR UCSC; Y49F6B.10; c. elegans.
DR CTD; 173695; -.
DR WormBase; Y49F6B.10; CE25334; WBGene00000647; col-71.
DR eggNOG; KOG3544; Eukaryota.
DR HOGENOM; CLU_001074_4_2_1; -.
DR InParanoid; Q9N4U2; -.
DR OMA; CNVNARQ; -.
DR OrthoDB; 1345845at2759; -.
DR PhylomeDB; Q9N4U2; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00000647; Expressed in material anatomical entity and 3 other tissues.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0042302; F:structural constituent of cuticle; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR InterPro; IPR002486; Col_cuticle_N.
DR InterPro; IPR008160; Collagen.
DR Pfam; PF01484; Col_cuticle_N; 1.
DR Pfam; PF01391; Collagen; 1.
DR SMART; SM01088; Col_cuticle_N; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Membrane; Nucleus; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..371
FT /note="Cuticle collagen 71"
FT /id="PRO_0000455700"
FT TRANSMEM 38..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 223..280
FT /note="Collagen-like"
FT /evidence="ECO:0000255"
FT REGION 108..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..187
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..225
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 371 AA; 37071 MW; F4EBB6A5C425A4F5 CRC64;
MRNAGGDKPF STPVLLREMG LKTHVDDDPK TKAYRLIGYA AVTFSTVSVI CFCVTMPVVF
TYVQSVKRQM SHEMATCNVN ARQIFDDVAA LRAGFPFAQA GNRTARQAGY DVHPSKPTPV
GYSGGDAAAA EVKGNSPAAA YEDKPFVAVG VEEGPHTATT GSDSEGTCHD CCLPGPPGPP
GPPGRPGPNG KAGANGLNGN PGRPPEAPCE PVTPPPCPPC PAGPKGAPGQ AGYPGADGQP
GSQGDNGEKG SDGAAGEKGR PGPLGKIGEP GATGETGENA ENSEPTPGPQ GPPGAIGPVG
SRGTPGHPGE DGEAGAPGAP GENGTDGENG EDGVPGVPGH DGKAGRAGER GICPKYCAKD
GGIFFEDGTR R
