ID A0A7R9M242_9ACAR Unreviewed; 584 AA.
AC A0A7R9M242;
DT 02-JUN-2021, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 1.
DT 28-JAN-2026, entry version 16.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CAD7651648.1};
GN ORFNames=ONB1V03_LOCUS8402 {ECO:0000313|EMBL:CAD7651648.1};
OS Oppiella nova.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Sarcoptiformes; Oribatida; Brachypylina; Oppioidea; Oppiidae;
OC Oppiella.
OX NCBI_TaxID=334625 {ECO:0000313|EMBL:CAD7651648.1};
RN [1] {ECO:0000313|EMBL:CAD7651648.1}
RP NUCLEOTIDE SEQUENCE.
RA Tran Van P.;
RL Submitted (NOV-2020) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; OC919611; CAD7651648.1; -; Genomic_DNA.
DR EMBL; CAJPVJ010004786; CAG2168918.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7R9M242; -.
DR OrthoDB; 5983381at2759; -.
DR Proteomes; UP000728032; 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 Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
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; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000728032}.
FT DOMAIN 395..442
FT /note="Collagen type XV/XVIII trimerization"
FT /evidence="ECO:0000259|Pfam:PF20010"
FT DOMAIN 461..567
FT /note="Collagenase NC10/endostatin"
FT /evidence="ECO:0000259|Pfam:PF06482"
FT REGION 15..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 100..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..30
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..82
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..187
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 584 AA; 63093 MW; 5DAEAF137E175302 CRC64;
MDRPLVALIL LSYQSIGDSP GGPGGPGSPG SGDYIEGFLN GDENEPKFST PTVVDGNEQT
IPDLTNTDND QGPPPFIPPP PVPHPSIDLK GSIGDKSILE EKMPTNPEPN YITLKGEKGE
RGERGERGEK GECMERETIE TIYETQTPAP VINQCVCNVS EIISSHQIKG PKGDVGPVGP
PGPPGPPGRG STFDPDLSPG YFGAPGSGSS FSYLTRVGDP GLPGPRGLPG HKVGDPGLPG
PRGLPGHKGD KDLVLKVNRE GMAREANREG MEYPVRQGLW VPREKWDFRV SQVLRVTEER
WEFPDRLLMV LKGQAGLVAH LAHIEELKGR HLYRDMTLSR VFRCKHLSNQ NKPNFNCNLV
FVDGPPGPPG PPGEKGEPGH ATKATAAHLI VPGAVTIKNM ESLIKASANS PMGTLAFIID
EQSLLIKVNG GWQYVPLGSL VPMTSDVNEI ALGSLVPMTS DVNEIAGEIL FNSWKDLFTG
AGAPFPFPPK IYSFDGRNVL TDYSWPQKLV WHGADRSGVR NSEAYCDAWN NNSMAKVGLA
SSLLRGKLLD QEKYSCNNSF IVLCIETTSP EDRQKRHVHP SADV
//
