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Database: UniProt
Entry: A0A3P7K4H9_LITSI
LinkDB: A0A3P7K4H9_LITSI
Original site: A0A3P7K4H9_LITSI 
ID   A0A3P7K4H9_LITSI        Unreviewed;       298 AA.
AC   A0A3P7K4H9;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   18-JUN-2025, entry version 25.
DE   RecName: Full=Collagen type XV/XVIII trimerization domain-containing protein {ECO:0000259|Pfam:PF20010};
GN   ORFNames=NLS_LOCUS9763 {ECO:0000313|EMBL:VDM92372.1};
OS   Litomosoides sigmodontis (Filarial nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Litomosoides.
OX   NCBI_TaxID=42156 {ECO:0000313|EMBL:VDM92372.1, ECO:0000313|Proteomes:UP000277928};
RN   [1] {ECO:0000313|EMBL:VDM92372.1, ECO:0000313|Proteomes:UP000277928}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Laetsch R D., Stevens L., Kumar S., Blaxter L. M.;
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; UYRX01001907; VDM92372.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3P7K4H9; -.
DR   STRING; 42156.A0A3P7K4H9; -.
DR   OMA; IECKQAR; -.
DR   OrthoDB; 5983381at2759; -.
DR   Proteomes; UP000277928; Unassembled WGS sequence.
DR   GO; GO:0031012; C:extracellular matrix; IEA:TreeGrafter.
DR   GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR   GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IEA:TreeGrafter.
DR   GO; GO:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
DR   Gene3D; 3.40.1620.70; -; 1.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR050149; Collagen_superfamily.
DR   InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR   PANTHER; PTHR24023:SF1112; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR   Pfam; PF01391; Collagen; 2.
DR   Pfam; PF20010; Collagen_trimer; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000277928};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          198..243
FT                   /note="Collagen type XV/XVIII trimerization"
FT                   /evidence="ECO:0000259|Pfam:PF20010"
FT   REGION          1..131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          144..189
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..19
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..34
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..87
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..115
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        152..162
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        164..180
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   298 AA;  31486 MW;  0D35DFEFC185211C CRC64;
     MVLVNVEKGE KGDKGDRGEP GPPGPMGPEG PPGTCPSNCQ PGRDGRDGIP GKPGDVGSVG
     PIGPPGRRGP PGPPGIGEPG FPGPPGAPGR CERLHPDDIA RIVSDPRLKG EKGDCHTGMP
     IHHPGVGTET NHYHQHRYAM KGEKGERGET GRMGPMGPIG QPGSPGPPGL PGPPGPPGLS
     GPPSIAYPQP MHTAPGGVHV YPTTIELFTA SHGMPIGSLT FSISSQQLYV RVNGGFKDIK
     LEGFHPIMEH RPTVEIEFEP PNDSLMRYWV SYCWSMSWSS AHVVYVCKCE LWLFVGAW
//
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