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Database: UniProt
Entry: A0A8R2GBS2_BOMMO
LinkDB: A0A8R2GBS2_BOMMO
Original site: A0A8R2GBS2_BOMMO 
ID   A0A8R2GBS2_BOMMO        Unreviewed;      1008 AA.
AC   A0A8R2GBS2;
DT   12-OCT-2022, integrated into UniProtKB/TrEMBL.
DT   12-OCT-2022, sequence version 1.
DT   28-JAN-2026, entry version 13.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:XP_012551551.3};
OS   Bombyx mori (Silk moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Bombycidae; Bombycinae; Bombyx.
OX   NCBI_TaxID=7091 {ECO:0000313|EnsemblMetazoa:XP_012551551.3, ECO:0000313|Proteomes:UP000005204};
RN   [1] {ECO:0000313|Proteomes:UP000005204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=p50T {ECO:0000313|Proteomes:UP000005204};
RX   PubMed=19121390; DOI=10.1016/j.ibmb.2008.11.004;
RG   International Silkworm Genome Consortium;
RT   "The genome of a lepidopteran model insect, the silkworm Bombyx mori.";
RL   Insect Biochem. Mol. Biol. 38:1036-1045(2008).
RN   [2] {ECO:0000313|EnsemblMetazoa:XP_012551551.3}
RP   IDENTIFICATION.
RC   STRAIN=p50T (Dazao) {ECO:0000313|EnsemblMetazoa:XP_012551551.3};
RG   EnsemblMetazoa;
RL   Submitted (JUN-2022) to UniProtKB.
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DR   RefSeq; XP_012551551.3; XM_012696097.4.
DR   AlphaFoldDB; A0A8R2GBS2; -.
DR   EnsemblMetazoa; XM_012696097.3; XP_012551551.3; LOC101738279.
DR   GeneID; 101738279; -.
DR   KEGG; bmor:101738279; -.
DR   Proteomes; UP000005204; Unassembled WGS sequence.
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:UP000005204};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..1008
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5035855350"
FT   DOMAIN          738..781
FT                   /note="Collagen type XV/XVIII trimerization"
FT                   /evidence="ECO:0000259|Pfam:PF20010"
FT   DOMAIN          809..978
FT                   /note="Collagenase NC10/endostatin"
FT                   /evidence="ECO:0000259|Pfam:PF06482"
FT   REGION          225..502
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          533..714
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        225..235
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        242..259
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        463..475
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        485..497
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        533..545
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        563..575
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        623..647
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        653..662
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        671..687
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1008 AA;  107641 MW;  E8D2B453AFBC3E4F CRC64;
     MAGILYTLFS ILLFQRAISS YLSGGYNLLR LDQLPSDIPT TVAPDGFPAP NFANQSVTIP
     ISDIIEIGDY LPTPFIINAV IKLDELTATC LFQFKNNVAD TYFSLCMEPA SESLVRFIFN
     GLDTSPIETV VKVDKDSWTK YTFEIDRTSL TTRLDCILLF KQSTERPTMD VLFEPDSTLV
     LGESPYSEKN FMGSIKEIKI YPDSNEETIK NICNEDFKLP SIFNEENEES TDNVEEPQYI
     KNPEKGEKGD KGEKGEKGQK GHQCLKGEPG NSVIGPEGSQ GPVGPLGPPG PVGKRGPKGE
     CECSPNLVST LLETMPEMRG PPGEAGPRGE PGLPGLHGEK GPEGPAGKPG LDGRVGEPGH
     DGVPGRNGKP GEPGPPGKDG APGRDGEPGL RGPPGPPGPG FMETEEEKKA RQIRIPGPKG
     EQGSPGLPGY PGPKGETGSK GDKGEIGQQG AKGEEGIMGQ MGEKGKKGDK GDAGVDGRPG
     MHGNHGVDGR TGDKGDKGAP GLAGLPASLA SILDEEMDEL TKAAIIEKFR GFKGEHGDKG
     DKGSKGDQGN TGLAGEPGKD GRTGSTGPRG PTGPRGKQGP MGPRGYKGAR GAPGPVGKVP
     ASEIALLKGA TGPPGPKGST GEKGQKGDKA PEIDVSKLKG EKGDRGLEGS PGKPGPIGPV
     GPPGICEKSS PQPPIPGPPG PPGPPGSPGR DGEAGQPGAS IIGPKGEPGF TMTSNNIDET
     VDFDSNDDEA FFKSYTIIFK TYKGLLKRTS KTPVGTLAYV LDEQILLLRV EYGWQNVNIG
     SMYQPSRSAP RLVPYNQPSK SPNDKRYIRL AALNEPYSGR METHLNRVGY SAINYECHRQ
     SMRDYNGTFV AVLSNRVTDL ISLVKPSERN IPVTNLKGEI LYPSWSSIFD GARSMHGQSK
     ANIYSFDNRN VYVDQQWPKK MVWIGADTLG NRSTKAYCDE WSSDSQQMFG TASPLDKLLE
     QRLLSCDNKL IVLCVELSSQ ASRHNHKKRW PKKRVTYDKR IRKPFAGT
//
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