ID   CUC3A_HAECO             Reviewed;         295 AA.
AC   P16253;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Cuticle collagen 3A3;
GN   Name=3A3;
OS   Haemonchus contortus (Barber pole worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida;
OC   Trichostrongyloidea; Haemonchidae; Haemonchus.
OX   NCBI_TaxID=6289;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   PubMed=2615789; DOI=10.1016/0166-6851(89)90104-7;
RA   Shamansky L.M., Pratt D., Boisvenue R.J., Cox G.N.;
RT   "Cuticle collagen genes of Haemonchus contortus and Caenorhabditis elegans
RT   are highly conserved.";
RL   Mol. Biochem. Parasitol. 37:73-86(1989).
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   -!- MISCELLANEOUS: This protein shows 4 potential triple-helical regions,
CC       which contain glycine as every third amino acid.
CC   -!- MISCELLANEOUS: In all nematode cuticle collagens, the polypeptide
CC       chains are complexed within the cuticle by disulfide bonds and other
CC       types of covalent cross-links.
CC   -!- SIMILARITY: Belongs to the cuticular collagen family. {ECO:0000305}.
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DR   EMBL; M32821; AAA29174.1; -; mRNA.
DR   EMBL; M32820; AAA29173.1; -; Genomic_DNA.
DR   PIR; A44984; A44984.
DR   AlphaFoldDB; P16253; -.
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   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   Collagen; Cuticle; Repeat.
FT   CHAIN           1..295
FT                   /note="Cuticle collagen 3A3"
FT                   /id="PRO_0000127607"
FT   REGION          81..278
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          98..127
FT                   /note="Triple-helical region"
FT   REGION          147..203
FT                   /note="Triple-helical region"
FT   REGION          212..277
FT                   /note="Triple-helical region"
FT   COMPBIAS        96..165
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        213..232
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        260..274
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   295 AA;  29618 MW;  85355A431B6D3311 CRC64;
     MDVIDHRIKA YRFVAYAAVG FSVVAVLSVC VTLPIVYNYV HYVRKSLHKE ASLCKISTNS
     VWDDVTVLRL AHFGNRTARQ AITSSEENGG CESCCRPGPP GPPGPPGRPG RPGRPGAPGL
     PGVPGLPPPD GSCEPVSIPP CAECPAGPPG PPGKPGPPGD PGEDGQPGPP GQDGIPGQQG
     TKGPPGPPGI PGKPGESGEV GEDAECEPVA PGDQGPPGEP GPEGPPGEPG LQGPVGMPGQ
     VGQKGESGSD GQLDFDGSPG RPGPPGPPGR PGEPGICPKY CAIDGGIFFE DGTRR