ID A0A8J9VX74_9NEOP Unreviewed; 1078 AA.
AC A0A8J9VX74;
DT 03-AUG-2022, integrated into UniProtKB/TrEMBL.
DT 03-AUG-2022, sequence version 1.
DT 28-JAN-2026, entry version 13.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CAH0729565.1};
DE Flags: Fragment;
GN ORFNames=BINO364_LOCUS14636 {ECO:0000313|EMBL:CAH0729565.1};
OS Brenthis ino (lesser marbled fritillary).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Nymphalidae; Heliconiinae; Argynnini; Brenthis.
OX NCBI_TaxID=405034 {ECO:0000313|EMBL:CAH0729565.1, ECO:0000313|Proteomes:UP000838878};
RN [1] {ECO:0000313|EMBL:CAH0729565.1}
RP NUCLEOTIDE SEQUENCE.
RA Martin H S.;
RL Submitted (DEC-2021) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; OV170228; CAH0729565.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A8J9VX74; -.
DR OrthoDB; 5983381at2759; -.
DR Proteomes; UP000838878; 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 Gene3D; 2.60.120.200; -; 1.
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; IPR013320; ConA-like_dom_sf.
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; 3.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Reference proteome {ECO:0000313|Proteomes:UP000838878}.
FT DOMAIN 791..837
FT /note="Collagen type XV/XVIII trimerization"
FT /evidence="ECO:0000259|Pfam:PF20010"
FT DOMAIN 872..1043
FT /note="Collagenase NC10/endostatin"
FT /evidence="ECO:0000259|Pfam:PF06482"
FT REGION 220..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 841..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1048..1078
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..242
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..275
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..294
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..335
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..385
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..404
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..467
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..508
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..562
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..587
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..661
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..701
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..745
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1048..1060
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1061..1071
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1078
FT /evidence="ECO:0000313|EMBL:CAH0729565.1"
SQ SEQUENCE 1078 AA; 114592 MW; BDA1A5D4C70DB18D CRC64;
MTEILYIWLS INNVDAKLYK YDLLQEMIDY DSDFFEYVDD KKSAVTLTDD KFISIPISEL
STSMTELDTS FEIIAVVTLS RKKSCLFSIS TEDTIVLELC FTPSDEVLMR ISLDSDSFDS
RKTFLHVLNE EEKSTTLILQ VDVDSVSLYA NCKLIDSQSL EIRLKSLSIP EESNLIFGKI
DKLDSNFFDG QIQKLQIFSN SSYEGRFSVC DSIDDKEASV SAFTKSPDTT EDEPDDDSDT
DMLEYSTEKL DKWDKGEKGD KGDRGDRGEK GDKGEGTIGS IGPQGPIGPG GHQGPPGEKG
AEGACQCSEL VVTKLLSTMP EMRGPPGEPG PQGEDGAQGM PGLTGLQGIQ GEMGPRGFDG
EKGKPGDNGL PGKDGERGSK GEPGRNGDPG PPGPEGPMGP PGPPGEAYKE IEEAKMPIAG
EKGDIGPIGP PGSPGPKGIQ GSKGEKGEEG LKGDKGEQVI IRDKGLDGKP GPPGKPGETG
QNGIPGQPGT HGRHGEKGEK GDKGDKGEQG LPGITAKLSD ILYDDMDPIE KEAVIEKLRG
YKGDKGESGH KGDIGDTGDR GPKGSAGNDG LQGPPGEKGA HGHKGDPGPE GPKGLRGNTG
EPGPPGNVPT SAISLMKGPK GDQGEIGKTG PRGPNGHPGK KGPAGPRGYK GAKGEPGETG
HKGATGYKGE VGPVGPKGEK GETPLVDTAK LKGDKGERGE TGKSGQDGKP GKPGTCEESN
FLTVTGPPGP PGPPGPSGPP GPPGSPGISI TGPKGEPGGI ISKSTLYAFN DVNNDSNTSN
EDDDFYTAAT VIYKTSTALF KRTSITPLGT LAYILQEKIL LLKVENGWQY VLMGSFLQTR
DSHTSTSSPK FHRTTEPTNP TEGVKSSDNY IRLVALNEPY PGNMLTTTNR TGRSAAEQEC
YKQAQKFHKR STFVPFISNN VVDLISIVKS IQDRHVPVVN LYGSVLFDSW SSMFNGSGAP
LLSTTSIYSF NGKNVFIDPT WPTKALWHGS TSFGIRAKRA SCEEWQSDSS LSHGAASTLY
SNRLLEQEQY SCDNKLIVLC VETTSNARRK LRHPHPKSRK RPNDHNIETF DNRIQPGL
//
