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Database: UniProt
Entry: A0A9P0I3K7_SPOLI
LinkDB: A0A9P0I3K7_SPOLI
Original site: A0A9P0I3K7_SPOLI 
ID   A0A9P0I3K7_SPOLI        Unreviewed;       558 AA.
AC   A0A9P0I3K7;
DT   13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2023, sequence version 1.
DT   28-JAN-2026, entry version 9.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CAH1638823.1};
GN   ORFNames=SPLIT_LOCUS4181 {ECO:0000313|EMBL:CAH1638823.1};
OS   Spodoptera littoralis (Egyptian cotton leafworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC   Noctuidae; Amphipyrinae; Spodoptera.
OX   NCBI_TaxID=7109 {ECO:0000313|EMBL:CAH1638823.1, ECO:0000313|Proteomes:UP001153321};
RN   [1] {ECO:0000313|EMBL:CAH1638823.1}
RP   NUCLEOTIDE SEQUENCE.
RA   King R.;
RL   Submitted (FEB-2022) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; LR824549; CAH1638823.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A9P0I3K7; -.
DR   Proteomes; UP001153321; Chromosome 18.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
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   Gene3D; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 1.
DR   Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR050149; Collagen_superfamily.
DR   InterPro; IPR010515; Collagenase_NC10/endostatin.
DR   InterPro; IPR016187; CTDL_fold.
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; 1.
DR   Pfam; PF20010; Collagen_trimer; 1.
DR   Pfam; PF06482; Endostatin; 1.
DR   SUPFAM; SSF56436; C-type lectin-like; 1.
PE   4: Predicted;
KW   Collagen {ECO:0000256|ARBA:ARBA00023119};
KW   Reference proteome {ECO:0000313|Proteomes:UP001153321}.
FT   DOMAIN          256..303
FT                   /note="Collagen type XV/XVIII trimerization"
FT                   /evidence="ECO:0000259|Pfam:PF20010"
FT   DOMAIN          346..510
FT                   /note="Collagenase NC10/endostatin"
FT                   /evidence="ECO:0000259|Pfam:PF06482"
FT   REGION          1..208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          223..253
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..148
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        160..175
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        223..235
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   558 AA;  59109 MW;  03D6A17B6B829A9E CRC64;
     MPGISGPPGS PGLKGERGER GPPGPISVTM AGSDIVTIKG DKGDAGLRGR RGRPGPSGPK
     GTAGTPGPPG PPGRPGDKGD IGLPGWIGRP GTLGPPGQPG PVGPKGEKGD PGVNILDVSM
     FKGEKGDRGF DGLPGLPGVP GPAGPPGPSG SLSEAIQYLP GPPGPPGPPG PPGPPGVSIV
     GPKGEPGFTH YEEHPVHGNT KFYGRPMSKS PLDELKALKE LKDLTNRDRD RDRHGPVQSH
     PAVHHTEEPN KSVPGAAVFQ TTEEMLKLAS SSAVGALAYV VEEQALFVKV NSGWQYVLLG
     SLVTQSAPTH PTPAPAPPPP MPAASLVHKP SLSNLVESSP VPGPSLHLAA LNEPLPGNMH
     GIRRADYACY RQGRRAGFRG TFRALLTSKI QNLNSIVRYS DRHLPVVNTQ GEILFKSFSD
     MFDGNGALAA GARIYSFNGR NVLTDSHWPQ KVIWHGSRAN GERALDSYCQ EWQNGDPTSR
     GLGSALQSHK LLAQERYPCS SHFIVLCVEV ASEINSRRKR ETIRYNTTGI LDEDDYLYNA
     EEYQQLLNEI FAQPLREN
//
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