CO145_CAEEL
ID CO145_CAEEL Reviewed; 294 AA.
AC Q17459;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Putative cuticle collagen 145;
DE Flags: Precursor;
GN Name=col-145; ORFNames=B0222.7;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
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).
CC -!- FUNCTION: Nematode cuticles are composed largely of collagen-like
CC proteins. The cuticle functions both as an exoskeleton and as a barrier
CC to protect the worm from its environment (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Collagen polypeptide chains are complexed within the cuticle
CC by disulfide bonds and other types of covalent cross-links.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cuticular collagen family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FO080127; CCD61420.2; -; Genomic_DNA.
DR PIR; T29838; T29838.
DR RefSeq; NP_505375.2; NM_072974.4.
DR AlphaFoldDB; Q17459; -.
DR SMR; Q17459; -.
DR BioGRID; 44335; 1.
DR DIP; DIP-24575N; -.
DR STRING; 6239.B0222.7; -.
DR PaxDb; Q17459; -.
DR PeptideAtlas; Q17459; -.
DR EnsemblMetazoa; B0222.7.1; B0222.7.1; WBGene00000718.
DR GeneID; 179297; -.
DR KEGG; cel:CELE_B0222.7; -.
DR UCSC; B0222.7; c. elegans.
DR CTD; 179297; -.
DR WormBase; B0222.7; CE48016; WBGene00000718; col-145.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00970000195960; -.
DR HOGENOM; CLU_001074_4_3_1; -.
DR InParanoid; Q17459; -.
DR OMA; TFAIMAC; -.
DR OrthoDB; 1751568at2759; -.
DR PhylomeDB; Q17459; -.
DR PRO; PR:Q17459; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00000718; Expressed in material anatomical entity and 3 other tissues.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0042302; F:structural constituent of cuticle; IEA:UniProtKB-KW.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR InterPro; IPR002486; Col_cuticle_N.
DR Pfam; PF01484; Col_cuticle_N; 1.
DR SMART; SM01088; Col_cuticle_N; 1.
PE 3: Inferred from homology;
KW Collagen; Cuticle; Disulfide bond; Reference proteome; Repeat; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..294
FT /note="Putative cuticle collagen 145"
FT /id="PRO_0000307867"
FT DOMAIN 218..276
FT /note="Collagen-like"
FT /evidence="ECO:0000255"
FT REGION 100..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 102..127
FT /note="Triple-helical region"
FT REGION 148..277
FT /note="Triple-helical region"
FT REGION 148..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..119
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..167
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 294 AA; 28744 MW; B7111C687D66D8B2 CRC64;
MEKILVTFST GAASIAVLAV LFTVPSLYNT INEVHDQVLD GVSVFRVETD SAWTEMMDIQ
ITVTPPTKPR VNPFNSVFRQ KRQTFSGLPA WCQCEPTKPT CPPGPPGPPG QPGAPGTPGA
PGPKGDDNTA TFAPLTCAPV SQDCVKCPQG PAGPAGPSGP AGPAGPDGQP GFPGQRGNDG
FPGAPGAPGD NGQPGTPGQD GFPGQPGADG QRGSGAPGAP GAPGNAGPAG PAGQDGFPGQ
DGAPGPAGPA GQDGFPGNAG SDGQPGAPGG PGLPGNDAAY CACPPRSAVF LSRH
