ID   CUT2_CAEEL              Reviewed;         231 AA.
AC   P34682; P92003;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Cuticlin 2 {ECO:0000312|WormBase:F53F1.5};
DE   Flags: Precursor;
GN   Name=cut-2 {ECO:0000312|WormBase:F53F1.5};
GN   ORFNames=F53F1.5 {ECO:0000312|WormBase:F53F1.5};
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], FUNCTION, SUBCELLULAR LOCATION,
RP   DEVELOPMENTAL STAGE, DOMAIN, AND TYROSINE CROSS-LINKED.
RC   STRAIN=Bristol N2;
RX   PubMed=7935621; DOI=10.1016/0166-6851(94)90123-6;
RA   Lassandro F., Sebastiano M., Zei F., Bazzicalupo P.;
RT   "The role of dityrosine formation in the crosslinking of CUT-2, the product
RT   of a second cuticlin gene of Caenorhabditis elegans.";
RL   Mol. Biochem. Parasitol. 65:147-159(1994).
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).
CC   -!- FUNCTION: Component of the insoluble part of the cuticles.
CC       {ECO:0000269|PubMed:7935621}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:7935621}.
CC   -!- DEVELOPMENTAL STAGE: Expressed before the L1 to L2 stage molt.
CC       {ECO:0000269|PubMed:7935621}.
CC   -!- DOMAIN: The small repeats A-A-P-[AVI] are also present in many proteins
CC       constituting the protective envelope of other species.
CC       {ECO:0000305|PubMed:7935621}.
CC   -!- PTM: Tyrosine residues can be cross-linked in vitro, leading to the
CC       formation of insoluble high molecular-weight complexes.
CC       {ECO:0000269|PubMed:7935621}.
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; X74838; CAA52832.1; -; Genomic_DNA.
DR   EMBL; BX284605; CAB03133.1; -; Genomic_DNA.
DR   PIR; S37108; S37108.
DR   PIR; T22572; T22572.
DR   RefSeq; NP_506325.1; NM_073924.3.
DR   AlphaFoldDB; P34682; -.
DR   BioGRID; 44840; 2.
DR   STRING; 6239.F53F1.5; -.
DR   PeptideAtlas; P34682; -.
DR   EnsemblMetazoa; F53F1.5.1; F53F1.5.1; WBGene00009983.
DR   GeneID; 179823; -.
DR   KEGG; cel:CELE_F53F1.5; -.
DR   UCSC; F53F1.5; c. elegans.
DR   CTD; 179823; -.
DR   WormBase; F53F1.5; CE10940; WBGene00009983; cut-2.
DR   eggNOG; ENOG502QV05; Eukaryota.
DR   HOGENOM; CLU_119207_0_0_1; -.
DR   InParanoid; P34682; -.
DR   PRO; PR:P34682; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00009983; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR   GO; GO:0060106; C:cortical layer of collagen and cuticulin-based cuticle extracellular matrix; NAS:WormBase.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042302; F:structural constituent of cuticle; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Cuticle; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..231
FT                   /note="Cuticlin 2"
FT                   /id="PRO_0000021047"
FT   REPEAT          75..78
FT                   /note="1"
FT                   /evidence="ECO:0000305|PubMed:7935621"
FT   REPEAT          79..82
FT                   /note="2"
FT                   /evidence="ECO:0000305|PubMed:7935621"
FT   REPEAT          90..93
FT                   /note="3"
FT                   /evidence="ECO:0000305|PubMed:7935621"
FT   REPEAT          105..108
FT                   /note="4"
FT                   /evidence="ECO:0000305|PubMed:7935621"
FT   REPEAT          114..117
FT                   /note="5"
FT                   /evidence="ECO:0000305|PubMed:7935621"
FT   REPEAT          121..124
FT                   /note="6"
FT                   /evidence="ECO:0000305|PubMed:7935621"
FT   REPEAT          137..140
FT                   /note="7"
FT                   /evidence="ECO:0000305|PubMed:7935621"
FT   REPEAT          153..156
FT                   /note="8"
FT                   /evidence="ECO:0000305|PubMed:7935621"
FT   REPEAT          169..172
FT                   /note="9"
FT                   /evidence="ECO:0000305|PubMed:7935621"
FT   REPEAT          192..195
FT                   /note="10"
FT                   /evidence="ECO:0000305|PubMed:7935621"
FT   REPEAT          208..211
FT                   /note="11"
FT                   /evidence="ECO:0000305|PubMed:7935621"
FT   REPEAT          218..221
FT                   /note="12"
FT                   /evidence="ECO:0000305|PubMed:7935621"
FT   REGION          75..221
FT                   /note="12 X 4 AA repeats of A-A-P-[AVI]"
FT                   /evidence="ECO:0000305|PubMed:7935621"
FT   CONFLICT        148..163
FT                   /note="Missing (in Ref. 2; CAB03133)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   231 AA;  20833 MW;  A48C9C5498D8E797 CRC64;
     MQKLIVFFTT IAAAQAFLLP SGGGGGCGCA PPPPPPPCGC GAPALPPLQL PRFELPRLSL
     PSLGGGCGGP APCAAAPIAA PAGGYATAPA APVGGYATGP AFGGAAPIGG AYQAAPAFVG
     AAPVGGAYQS GPAFGGAAPA GGAYQSGPAF GGAAPAGGAY QSGPAFGGAA PAVGGAYQAG
     QAAVESAPLG GAAPAGGYQA SAPAAVEAAP AAGGYQAAAP AGGAYAGHKK N