ID   COL34_CAEEL             Reviewed;         299 AA.
AC   P34687; Q20087;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2002, sequence version 2.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Cuticle collagen 34;
DE   AltName: Full=Abnormal ray morphology protein 4;
GN   Name=col-34; Synonyms=ram-4; ORFNames=F36A4.10;
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 [GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=1398138; DOI=10.1016/0378-1119(92)90102-u;
RA   Bird D.M.;
RT   "Sequence comparison of the Caenorhabditis elegans dpy-13 and col-34 genes,
RT   and their deduced collagen products.";
RL   Gene 120:261-266(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Yu R.Y., Chow K.L.;
RT   "RAM-4, a collagen, is involved in ray morphogenesis of Caenorhabditis
RT   elegans male tail.";
RL   Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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.
CC   -!- SUBUNIT: Collagen polypeptide chains are complexed within the cuticle
CC       by disulfide bonds and other types of covalent cross-links.
CC   -!- SIMILARITY: Belongs to the cuticular collagen family. {ECO:0000305}.
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DR   EMBL; M80650; AAA27985.1; -; Genomic_DNA.
DR   EMBL; AF410845; AAL76233.1; -; mRNA.
DR   EMBL; FO081153; CCD69528.1; -; Genomic_DNA.
DR   PIR; JC1448; JC1448.
DR   PIR; T29956; T29956.
DR   RefSeq; NP_500520.1; NM_068119.4.
DR   AlphaFoldDB; P34687; -.
DR   SMR; P34687; -.
DR   STRING; 6239.F36A4.10; -.
DR   EPD; P34687; -.
DR   PaxDb; P34687; -.
DR   PeptideAtlas; P34687; -.
DR   EnsemblMetazoa; F36A4.10.1; F36A4.10.1; WBGene00000611.
DR   GeneID; 177188; -.
DR   KEGG; cel:CELE_F36A4.10; -.
DR   UCSC; F36A4.10; c. elegans.
DR   CTD; 177188; -.
DR   WormBase; F36A4.10; CE07185; WBGene00000611; col-34.
DR   eggNOG; KOG3544; Eukaryota.
DR   GeneTree; ENSGT00970000195912; -.
DR   HOGENOM; CLU_001074_4_2_1; -.
DR   InParanoid; P34687; -.
DR   OMA; LGCNPAH; -.
DR   OrthoDB; 1554466at2759; -.
DR   PhylomeDB; P34687; -.
DR   PRO; PR:P34687; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00000611; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR   GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR   GO; GO:0042302; F:structural constituent of cuticle; NAS:UniProtKB.
DR   GO; GO:0040002; P:collagen and cuticulin-based cuticle development; NAS:UniProtKB.
DR   InterPro; IPR002486; Col_cuticle_N.
DR   InterPro; IPR008160; Collagen.
DR   Pfam; PF01484; Col_cuticle_N; 1.
DR   Pfam; PF01391; Collagen; 2.
DR   SMART; SM01088; Col_cuticle_N; 1.
PE   2: Evidence at transcript level;
KW   Collagen; Cuticle; Disulfide bond; Reference proteome; Repeat.
FT   CHAIN           1..299
FT                   /note="Cuticle collagen 34"
FT                   /id="PRO_0000127592"
FT   REGION          105..282
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          216..278
FT                   /note="Triple-helical region"
FT   COMPBIAS        105..168
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        181..202
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        211..236
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        145
FT                   /note="C -> W (in Ref. 1; AAA27985)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        189
FT                   /note="P -> K (in Ref. 1; AAA27985)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        199..210
FT                   /note="GTPGEPGVPAQS -> EHQESQECPRG (in Ref. 1; AAA27985)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   299 AA;  29336 MW;  215780080E5C7212 CRC64;
     MDLETRIKAY RFVAYSAVAF SVVAVISVCV TLPMVYNYVH HVKRTMHNEI TFCKGSAKDI
     WNEVHALKSL PNSNRTARQA YNDAAVTGGG AQSGSCESCC LPGPPGPAGT PGKPGRPGKP
     GAPGLPGNPG RPPQQPCEPI TPPPCKPCPQ GPPGPPGPPG PPGDSGEPGS PGLPGQDAAP
     GEPGPKGPPG PPGAPGAPGT PGEPGVPAQS EPLIPGEPGP PGEAGPQGPP GSPGQPGADG
     SPGQPGPKGP NGPDGQPGAD GNPGAPGPAG PPGSPGERGI CPKYCAIDGG VFFEDGTRR