ID   A0A1I7Z4X4_9BILA        Unreviewed;       147 AA.
AC   A0A1I7Z4X4;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Collagen triple helix repeat protein {ECO:0000313|WBParaSite:L893_g22643.t1};
OS   Steinernema glaseri.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Steinernematidae;
OC   Steinernema.
OX   NCBI_TaxID=37863 {ECO:0000313|Proteomes:UP000095287, ECO:0000313|WBParaSite:L893_g22643.t1};
RN   [1] {ECO:0000313|WBParaSite:L893_g22643.t1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
CC   -!- SUBUNIT: Collagen polypeptide chains are complexed within the cuticle
CC       by disulfide bonds and other types of covalent cross-links.
CC       {ECO:0000256|ARBA:ARBA00011518}.
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DR   AlphaFoldDB; A0A1I7Z4X4; -.
DR   WBParaSite; L893_g22643.t1; L893_g22643.t1; L893_g22643.
DR   Proteomes; UP000095287; Unplaced.
DR   GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR   InterPro; IPR008160; Collagen.
DR   PANTHER; PTHR24637; COLLAGEN; 1.
DR   PANTHER; PTHR24637:SF428; SCAVENGER RECEPTOR CLASS A MEMBER 3; 1.
DR   Pfam; PF01391; Collagen; 2.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   REGION          1..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..29
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        83..114
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   147 AA;  13247 MW;  9B68CBE5010A5EBB CRC64;
     MTKQCIKCPP GEPGPPGPDG PPGPPGGPGP AGVDGAAGKP GTPGAPGPQG DKGTDGVPGT
     PGVAGPPGAN AVKQTNLPGP KGEPGAVGPP GIPGPPGFVG EAGPPGPTGP VGPAGKPGSP
     GKDGAAGPAG MAGIPGIDAQ YCPCPPR
//