ID A0A9P0DYJ4_PHACE Unreviewed; 509 AA.
AC A0A9P0DYJ4;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 28-JAN-2026, entry version 10.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CAH1180546.1};
GN ORFNames=PHAECO_LOCUS11619 {ECO:0000313|EMBL:CAH1180546.1};
OS Phaedon cochleariae (Mustard beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Chrysomeloidea; Chrysomelidae; Chrysomelinae; Chrysomelini; Phaedon.
OX NCBI_TaxID=80249 {ECO:0000313|EMBL:CAH1180546.1, ECO:0000313|Proteomes:UP001153737};
RN [1] {ECO:0000313|EMBL:CAH1180546.1}
RP NUCLEOTIDE SEQUENCE.
RA King R.;
RL Submitted (JAN-2022) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAH1180546.1}
RP NUCLEOTIDE SEQUENCE.
RG ENA_rothamsted_submissions;
RG culmorum;
RA King R.;
RL Submitted (OCT-2022) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; OU896714; CAH1180546.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A9P0DYJ4; -.
DR OrthoDB; 5983381at2759; -.
DR Proteomes; UP001153737; Chromosome 8.
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; 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; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1082; COLLAGEN TRIPLE HELIX REPEAT; 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:UP001153737}.
FT DOMAIN 224..263
FT /note="Collagen type XV/XVIII trimerization"
FT /evidence="ECO:0000259|Pfam:PF20010"
FT DOMAIN 302..468
FT /note="Collagenase NC10/endostatin"
FT /evidence="ECO:0000259|Pfam:PF06482"
FT REGION 1..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 509 AA; 52911 MW; 7A26E4ECDAF149EE CRC64;
MGPAGPKGDA GVDGAVGPVG APGSKGERGE RGPPGVAVTV PDGKEHDVVA VKGEKGEMGK
RGRRGKPGPV GPAGPPGTLG EIGLPGWMGR PGIPGVPGAK GEKGDITGTK GEKGDAGEKG
DRGADGRPGR DGNPGPPGPP PLEDAVRYVP VQGLPGPPGP PGTPGLSITG PKGEPGAPSY
GEPVHYSRPG RATASPPLAN VPYSDQASTH IVPGAIIVHK REAVARITSA SPVGTIAYIV
EEEALLVRVN NGWQYIALGA FLPVSTSAPP TTTSRPLFRP PLEASNLISH VAKTTSDASY
IRLAALNEPR TGQVHGVRGA DYACYREGRR AGLKGTFRAL LSSRTQDVSS IVRQADRRLP
VANLKGEVIF SSWSEMFSGS GAPFPHPPPA IYSFDGKHVL LDVATFPTPA VWHGALPTGE
RAPLTATCEG WHSGAGDRVG LAGELEGQLL GQTRRGCDER LVVLCVEATT EVLVQRRRRR
RREAEDYRYY GGEGALSEEE YSSLLSSIE
//
