ID A0A0L7L1I7_OPEBR Unreviewed; 567 AA.
AC A0A0L7L1I7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 28-JAN-2026, entry version 31.
DE SubName: Full=Putative collagen alpha 1 chain {ECO:0000313|EMBL:KOB69151.1};
DE Flags: Fragment;
GN ORFNames=OBRU01_17252 {ECO:0000313|EMBL:KOB69151.1};
OS Operophtera brumata (Winter moth) (Phalaena brumata).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Geometroidea;
OC Geometridae; Larentiinae; Operophtera.
OX NCBI_TaxID=104452 {ECO:0000313|EMBL:KOB69151.1, ECO:0000313|Proteomes:UP000037510};
RN [1] {ECO:0000313|EMBL:KOB69151.1, ECO:0000313|Proteomes:UP000037510}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WM2013NL {ECO:0000313|EMBL:KOB69151.1};
RC TISSUE=Head and thorax {ECO:0000313|EMBL:KOB69151.1};
RX PubMed=26227816; DOI=10.1093/gbe/evv145;
RA Derks M.F., Smit S., Salis L., Schijlen E., Bossers A., Mateman C.,
RA Pijl A.S., de Ridder D., Groenen M.A., Visser M.E., Megens H.J.;
RT "The genome of winter moth (Operophtera brumata) provides a genomic
RT perspective on sexual dimorphism and phenology.";
RL Genome Biol. Evol. 7:2321-2332(2015).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KOB69151.1}.
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DR EMBL; JTDY01003686; KOB69151.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L7L1I7; -.
DR STRING; 104452.A0A0L7L1I7; -.
DR Proteomes; UP000037510; Unassembled WGS sequence.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
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; IPR050938; Collagen_Structural_Proteins.
DR InterPro; IPR010515; Collagenase_NC10/endostatin.
DR InterPro; IPR016187; CTDL_fold.
DR PANTHER; PTHR37456:SF6; COLLAGEN ALPHA-1(XXIII) CHAIN-LIKE ISOFORM X2; 1.
DR PANTHER; PTHR37456; SI:CH211-266K2.1; 1.
DR Pfam; PF01391; Collagen; 3.
DR Pfam; PF06482; Endostatin; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
PE 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119, ECO:0000313|EMBL:KOB69151.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037510}.
FT DOMAIN 458..566
FT /note="Collagenase NC10/endostatin"
FT /evidence="ECO:0000259|Pfam:PF06482"
FT REGION 20..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..44
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..271
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..301
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..327
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..371
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KOB69151.1"
SQ SEQUENCE 567 AA; 57159 MW; 44654C996659F75C CRC64;
VAGVCRCSLT DISQILEVMP ELKGPPGPQG TTGADGTTGA PGKTGQMGES GPPGPLGPKG
DRGERGELGA SGPEGQPGPK GDPGSDGTPG LQGPPGPPGP GESSGLYGSG NPGILGSTGE
RGPMGTPGPQ GERGYQGSKG ERGLHGPKGD KGERVSEDCL DYLDLHLHRL GEKGGRGLDG
PQGFPGNDGK SGDRGDIGPS GLPGTQGPAG LNGPKGDRGD PGPPGPVAVS RDEALLLTKG
DKGESGPRGK RGHPGPPGPR GPPGLPGPPG TPGTNGPSGD IGLPGWTGPP GTAGTPGPQG
QKGEKGDPGL GSLDLDKVKG EKGDRGFDGT AGVPGKDGPR GPPGPAGSPS NTIQYISVPG
APGPPGPPGP PGYGNDVTAD TLTDIPGVRR EGTAYRDPLD PLGENTDFDD DEDGRAIVGT
ILFKTTDSLL RLGINSPLGT LAYVIQEQAL LVRVNNGWQV QTIDSIVSWV DREIPVVNTR
GEVIFNSWGE MFDGSGALFA HAPRIYSFSG QNVLTDAAWP TKAVWHGASP NGEPAMDAYC
DAWHSSNPDK FGLASSLRSN KLLDQET
//
