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Database: UniProt
Entry: A0A0K0ES79_STRER
LinkDB: A0A0K0ES79_STRER
Original site: A0A0K0ES79_STRER 
ID   A0A0K0ES79_STRER        Unreviewed;       303 AA.
AC   A0A0K0ES79;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Col_cuticle_N domain-containing protein {ECO:0000313|WBParaSite:SSTP_0001230700.1};
OS   Strongyloides stercoralis (Threadworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Strongyloides.
OX   NCBI_TaxID=6248 {ECO:0000313|WBParaSite:SSTP_0001230700.1};
RN   [1] {ECO:0000313|WBParaSite:SSTP_0001230700.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (AUG-2015) 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; A0A0K0ES79; -.
DR   STRING; 6248.A0A0K0ES79; -.
DR   WBParaSite; SSTP_0001230700.1; SSTP_0001230700.1; SSTP_0001230700.
DR   Proteomes; UP000035681; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042302; F:structural constituent of cuticle; IEA:InterPro.
DR   GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR   InterPro; IPR002486; Col_cuticle_N.
DR   PANTHER; PTHR24637; COLLAGEN; 1.
DR   PANTHER; PTHR24637:SF421; COLLAGEN-RELATED; 1.
DR   Pfam; PF01484; Col_cuticle_N; 1.
DR   SMART; SM01088; Col_cuticle_N; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035681};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          12..64
FT                   /note="Nematode cuticle collagen N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01088"
FT   REGION          113..283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        113..162
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        184..205
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        222..255
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   303 AA;  29775 MW;  E51D0DFF58D17B2A CRC64;
     MDLESRIKAY RFVAYSAVTF SIVAVLSVCV TLPMIYNYVH HVKRAMHNQV QYCKGSAKDI
     WTEINSIKKI PIITGNRTVR QAGYDSGVSG GTVSTADICE ACCLPGIAGP PGIPGKPGKP
     GKPGAPGLPG SPGKPPKQPC EPITPPPCKP CPQGPPGPSG LQGPPGDAGS PGTPGMPGSD
     GGPGNPGPKG PPGPAGSPGA PGPQGQPGTP ASSGQIIPGE PGPAGTPGPQ GPPGSPGQPG
     TPGIPGKPGP KGAPGPNGAP GNDGQPGAPG RPGTPGISGE RGICPKYCAI DGGVFFEDGT
     RRR
//
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