ID   ROL6_CAEEL              Reviewed;         348 AA.
AC   P20784;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Cuticle collagen rol-6;
DE   AltName: Full=Protein roller-6;
GN   Name=rol-6; ORFNames=T01B7.7;
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 [GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=1970117; DOI=10.1128/mcb.10.5.2081-2089.1990;
RA   Kramer J.M., French R.P., Park E.-C., Johnson J.J.;
RT   "The Caenorhabditis elegans rol-6 gene, which interacts with the sqt-1
RT   collagen gene to determine organismal morphology, encodes a collagen.";
RL   Mol. Cell. Biol. 10:2081-2089(1990).
RN   [2]
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).
RN   [3]
RP   FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF ARG-71.
RX   PubMed=21094156; DOI=10.1016/j.febslet.2010.11.020;
RA   Kim T.H., Kim Y.J., Cho J.W., Shim J.;
RT   "A novel zinc-carboxypeptidase SURO-1 regulates cuticle formation and body
RT   morphogenesis in Caenorhabditis elegans.";
RL   FEBS Lett. 585:121-127(2011).
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. Involved in body
CC       morphogenesis (PubMed:21094156). {ECO:0000269|PubMed:21094156,
CC       ECO:0000305}.
CC   -!- SUBUNIT: Collagen polypeptide chains are complexed within the cuticle
CC       by disulfide bonds and other types of covalent cross-links.
CC   -!- TISSUE SPECIFICITY: Localizes in stripes along the alae.
CC       {ECO:0000269|PubMed:21094156}.
CC   -!- SIMILARITY: Belongs to the cuticular collagen family. {ECO:0000305}.
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DR   EMBL; M34451; AAA28143.1; -; Genomic_DNA.
DR   EMBL; Z66499; CAA91300.1; -; Genomic_DNA.
DR   PIR; A34705; A34705.
DR   RefSeq; NP_495858.1; NM_063457.3.
DR   AlphaFoldDB; P20784; -.
DR   SMR; P20784; -.
DR   STRING; 6239.T01B7.7; -.
DR   EPD; P20784; -.
DR   PaxDb; P20784; -.
DR   PeptideAtlas; P20784; -.
DR   EnsemblMetazoa; T01B7.7.1; T01B7.7.1; WBGene00004397.
DR   GeneID; 174397; -.
DR   KEGG; cel:CELE_T01B7.7; -.
DR   UCSC; T01B7.7; c. elegans.
DR   CTD; 174397; -.
DR   WormBase; T01B7.7; CE03591; WBGene00004397; rol-6.
DR   eggNOG; KOG3544; Eukaryota.
DR   GeneTree; ENSGT00940000174005; -.
DR   HOGENOM; CLU_001074_4_4_1; -.
DR   InParanoid; P20784; -.
DR   OMA; CKCPGRE; -.
DR   OrthoDB; 1369687at2759; -.
DR   PhylomeDB; P20784; -.
DR   PRO; PR:P20784; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00004397; Expressed in pharyngeal muscle cell (C elegans) and 2 other tissues.
DR   GO; GO:0060102; C:collagen and cuticulin-based cuticle extracellular matrix; IDA:WormBase.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR   GO; GO:0042329; F:structural constituent of collagen and cuticulin-based cuticle; IDA:WormBase.
DR   GO; GO:0042338; P:cuticle development involved in collagen and cuticulin-based cuticle molting cycle; IMP:WormBase.
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   1: Evidence at protein level;
KW   Collagen; Cuticle; Disulfide bond; Reference proteome; Repeat.
FT   CHAIN           1..348
FT                   /note="Cuticle collagen rol-6"
FT                   /id="PRO_0000127595"
FT   REGION          76..348
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          152..178
FT                   /note="Triple-helical region"
FT   REGION          196..258
FT                   /note="Triple-helical region"
FT   REGION          261..284
FT                   /note="Triple-helical region"
FT   REGION          288..323
FT                   /note="Triple-helical region"
FT   COMPBIAS        159..176
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        326..342
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         71
FT                   /note="R->C: In su1006; body is twisted into a right-handed
FT                   helix (roller phenotype)."
FT                   /evidence="ECO:0000269|PubMed:21094156"
SQ   SEQUENCE   348 AA;  34761 MW;  2251072D1346ACD0 CRC64;
     MTLTTATSGA IVFSGATLLV SLFAAASLYS QVSNIWNELD AEIANFRSLT EDMWVDMVKL
     GAGTASNRVR RQQYGGYGAT GVQPPAPTPN PYGGYGASQP APPEKFPDGI PNGGNQPKFP
     GGGFPDGPFP NGGGPRGGNQ CQCTVENSCP PGPAGPEGEE GPDGHDGQDG VPGFDGKDAE
     DVQNTPPTGC FTCPQGPLGP QGPNGAPGLR GMRGARGQPG RPGRDGNPGM PGDCGPPGAP
     GSDGKPGSPG GKGDDGERPL GRPGPRGPPG EAGPEGPQGP TGRDAYPGQS GPQGEPGLQG
     YGGAAGEDGP EGPPGAPGLP GKDAEYCKCP GREGDAGRSA RRHRKFQL