ID   COL49_CAEEL             Reviewed;         283 AA.
AC   O44989;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Cuticle collagen 49 {ECO:0000303|PubMed:29604168};
DE   Flags: Precursor;
GN   Name=col-49 {ECO:0000312|WormBase:K09H9.3};
GN   ORFNames=K09H9.3 {ECO:0000312|WormBase:K09H9.3};
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, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP   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).
RN   [3] {ECO:0000305}
RP   FUNCTION, AND DEVELOPMENTAL STAGE.
RX   PubMed=29604168; DOI=10.1002/dvg.23106;
RA   Abete-Luzi P., Eisenmann D.M.;
RT   "Regulation of C. elegans L4 cuticle collagen genes by the heterochronic
RT   protein LIN-29.";
RL   Genesis 56:0-0(2018).
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:29604168}.
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:29604168}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the hypodermal cells of the tail and
CC       head, the seam cells, and in the hyp7 syncytial hypodermis in the
CC       larval L4 stage, and in the young adult (PubMed:24569038,
CC       PubMed:29604168). Not expressed in the cells of the developing vulva
CC       (PubMed:24569038). {ECO:0000269|PubMed:24569038,
CC       ECO:0000269|PubMed:29604168}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes dumpy body shape
CC       (PubMed:24569038). Defects in cuticle integrity (PubMed:24569038).
CC       {ECO:0000269|PubMed:24569038}.
CC   -!- SIMILARITY: Belongs to the cuticular collagen family. {ECO:0000305}.
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DR   EMBL; BX284601; CCD67358.1; -; Genomic_DNA.
DR   PIR; T32921; T32921.
DR   RefSeq; NP_491106.1; NM_058705.4.
DR   AlphaFoldDB; O44989; -.
DR   STRING; 6239.K09H9.3; -.
DR   EPD; O44989; -.
DR   PaxDb; O44989; -.
DR   PeptideAtlas; O44989; -.
DR   EnsemblMetazoa; K09H9.3.1; K09H9.3.1; WBGene00000626.
DR   GeneID; 187239; -.
DR   KEGG; cel:CELE_K09H9.3; -.
DR   UCSC; K09H9.3; c. elegans.
DR   CTD; 187239; -.
DR   WormBase; K09H9.3; CE18038; WBGene00000626; col-49.
DR   eggNOG; KOG3544; Eukaryota.
DR   GeneTree; ENSGT00970000196363; -.
DR   HOGENOM; CLU_001074_4_3_1; -.
DR   InParanoid; O44989; -.
DR   OMA; EDAGYCT; -.
DR   OrthoDB; 1280606at2759; -.
DR   PhylomeDB; O44989; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00000626; Expressed in material anatomical entity and 2 other tissues.
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   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; Reference proteome; Repeat; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..283
FT                   /note="Cuticle collagen 49"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000455699"
FT   DOMAIN          213..271
FT                   /note="Collagen-like"
FT                   /evidence="ECO:0000255"
FT   REGION          90..283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        139..159
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   283 AA;  28816 MW;  EAD713CE57CAA50F CRC64;
     MWKFVIGSVS TAAFFVSVCT IYFSVSMLDE LDSFRLSIRD ELEDWKEVSD DTWQRLNDMT
     SRNVPKKTNI LKEFVRGKRN VGNDQCNCAE PTKNCPAGPP GEKGSLGNPG QPGPDGVDGD
     NGVDGDVVIH DMPNPKECIK CPAGPPGPPG PPGPLGPRGD KGPSGPRGAL GDQGETGPVG
     EIGDQGPPGS AGRAGPRGQA GQPGTIAIVG LAGRPGPQGP LGEPGAQGEP GVDGKDGALG
     APGRKAENGR PGKRGKDGVA GVPGTRGKEG EDAGYCTCPP RTA