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Database: UniProt
Entry: A0A8R2DNN5_BOMMO
LinkDB: A0A8R2DNN5_BOMMO
Original site: A0A8R2DNN5_BOMMO 
ID   A0A8R2DNN5_BOMMO        Unreviewed;      1001 AA.
AC   A0A8R2DNN5;
DT   12-OCT-2022, integrated into UniProtKB/TrEMBL.
DT   12-OCT-2022, sequence version 1.
DT   28-JAN-2026, entry version 14.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:XP_021208068.2};
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_021208068.2, 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_021208068.2}
RP   IDENTIFICATION.
RC   STRAIN=p50T (Dazao) {ECO:0000313|EnsemblMetazoa:XP_021208068.2};
RG   EnsemblMetazoa;
RL   Submitted (JUN-2022) to UniProtKB.
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DR   RefSeq; XP_021208068.2; XM_021352393.3.
DR   AlphaFoldDB; A0A8R2DNN5; -.
DR   EnsemblMetazoa; XM_021352393.2; XP_021208068.2; LOC101738279.
DR   GeneID; 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   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; 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..1001
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5035727017"
FT   DOMAIN          731..774
FT                   /note="Collagen type XV/XVIII trimerization"
FT                   /evidence="ECO:0000259|Pfam:PF20010"
FT   DOMAIN          802..971
FT                   /note="Collagenase NC10/endostatin"
FT                   /evidence="ECO:0000259|Pfam:PF06482"
FT   REGION          217..495
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          526..709
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        217..228
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        235..252
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        456..468
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        478..490
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        526..538
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        556..568
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        616..640
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        646..655
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        664..680
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1001 AA;  106840 MW;  571D239E662B5E3E CRC64;
     MAGILYTLFS ILLFQRAISS YLSGGYNLLR LDQLPSDIPT TVAPDGFPAP NFANQSVTIP
     ISDIIEIGDY LPTPFIINAV IKLDELTATC LFQFKNNVAD TYFSLCMEPA SESLVRFIFN
     GLDTSPIETV VKVDKDSWTK YTFEIDRTSL TTRLDCILLF KQSTERPTMD VLFEPDSTLV
     LGESPYSEKN FMGSIKEIKI YPDSNEETIK NICNEFNEEN EESTDNVEEP QYIKNPEKGE
     KGDKGEKGEK GQKGHQCLKG EPGNSVIGPE GSQGPVGPLG PPGPVGKRGP KGECECSPNL
     VSTLLETMPE MRGPPGEAGP RGEPGLPGLH GEKGPEGPAG KPGLDGRVGE PGHDGVPGRN
     GKPGEPGPPG KDGAPGRDGE PGLRGPPGPP GPGFMETEEE KKARQIRIPG PKGEQGSPGL
     PGYPGPKGET GSKGDKGEIG QQGAKGEEGI MGQMGEKGKK GDKGDAGVDG RPGMHGNHGV
     DGRTGDKGDK GAPGLAGLPA SLASILDEEM DELTKAAIIE KFRGFKGEHG DKGDKGSKGD
     QGNTGLAGEP GKDGRTGSTG PRGPTGPRGK QGPMGPRGYK GARGAPGPVG KVPASEIALL
     KGATGPPGPK GSTGEKGQKG DKAPEIDVSK LKGEKGDRGL EGSPGKPGPI GPVGPPGICE
     KSSPQPPIPG PPGPPGPPGS PGRDGEAGQP GASIIGPKGE PGFTMTSNNI DETVDFDSND
     DEAFFKSYTI IFKTYKGLLK RTSKTPVGTL AYVLDEQILL LRVEYGWQNV NIGSMYQPSR
     SAPRLVPYNQ PSKSPNDKRY IRLAALNEPY SGRMETHLNR VGYSAINYEC HRQSMRDYNG
     TFVAVLSNRV TDLISLVKPS ERNIPVTNLK GEILYPSWSS IFDGARSMHG QSKANIYSFD
     NRNVYVDQQW PKKMVWIGAD TLGNRSTKAY CDEWSSDSQQ MFGTASPLDK LLEQRLLSCD
     NKLIVLCVEL SSQASRHNHK KRWPKKRVTY DKRIRKPFAG T
//
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