ID A0A8R2DPQ9_BOMMO Unreviewed; 1188 AA.
AC A0A8R2DPQ9;
DT 12-OCT-2022, integrated into UniProtKB/TrEMBL.
DT 12-OCT-2022, sequence version 1.
DT 28-JAN-2026, entry version 14.
DE RecName: Full=Thrombospondin-like N-terminal domain-containing protein {ECO:0000259|SMART:SM00210};
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_021208105.2, 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_021208105.2}
RP IDENTIFICATION.
RC STRAIN=p50T (Dazao) {ECO:0000313|EnsemblMetazoa:XP_021208105.2};
RG EnsemblMetazoa;
RL Submitted (JUN-2022) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR AlphaFoldDB; A0A8R2DPQ9; -.
DR EnsemblMetazoa; XM_021352430.2; XP_021208105.2; LOC101737883.
DR Proteomes; UP000005204; Unassembled WGS sequence.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; IPR050938; Collagen_Structural_Proteins.
DR InterPro; IPR010515; Collagenase_NC10/endostatin.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
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; 4.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Reference proteome {ECO:0000313|Proteomes:UP000005204};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1188
FT /note="Thrombospondin-like N-terminal domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035919544"
FT DOMAIN 41..232
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 266..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 857..884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..303
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..327
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..426
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..455
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..572
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..614
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..634
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..806
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..866
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 870..882
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1188 AA; 124215 MW; C7348FA7C6FF8E18 CRC64;
MESFRYISLP LLLLVTACLA TDGLFGSSMY QNGEPFIDIP EYDLLHAIGV PFSNPKTQYF
DEGLDGFPAY GLMPGSDIKS PYRLFMPEKL YSEFSITATV RPANKDGGFL FSVVNPLETV
VQLGVQLIPS GPGLMNISLL YTDANIYAFS QTIASFVVPT FAKKWSRFAL KVSLENVTLY
LNCHEFDTVV VRRNPLELVF DSASTLYVGQ AGPLIRGAFH GAFQELKLYG SPSQAEVQCV
NTFEEIDKSG EGDEIDIDNF LVDQEEDSEG SGRYGTIPPF PPPPPGLDGY SLRLRGDKGE
RGPRGPPGES IRGPPGPPGP PGPPGPPGTA TESSGSGDDR SSVKQIFGEN YASLGQCGCN
ASTIMSLLQT APELRGSPGP PGMIGADGRA GPPGMPGQPG TPGERGPVGP RGDKGDRGDA
GTRGHEGQPG PKGEAGVDGR PGTAGPPGPP GPPGTPDYNN FESNWKPRQI YKESLMGAYG
SAIGRPGAPG PKGDSGQPGP MGPQGERGFP GQKGERGQNG AVGAKGDRGH PGPQGDRGVK
GDRGNPGFDG RPGIPGANGR PADKGEKGER GEPGPPGSPP AGVFNAADPE FMVAGSQVTG
AKGDKGEKGE KGTRGNDGPP GFPGKDGKQG ERGDIGPSGL PGMAGSPGPQ GFKGDRGERG
PPGPISVASA GTDIITIKGD KGEPGARGRR GRSGPGGARG ATGAPGPPGP AGRPGDKGDT
GLPGWMGRPG TLGPPGAPGP VGPKGEKGDP GVNILDVSMF KGEKGDRGFD GVPGVQGPPG
PPGKPASEPV QYLPGPPGPP GPPGSPGTPG VSVVGPKGEP GVSYYEEGPV HGSPKFYGRP
VLKSPLDELK ALKELKDLKD KERDRGGFSA RSQPADESSA QKTVPGAAVF QTTEEMMKLA
SSSPVGALAY VAEEQALFVK VNSGWQYVLL GSLVTQSKPP PTPAPAPLPM PAASLVHVPP
ISNLVENSPT PIGPSLRMAA LNDPLSGNMH GVRRADYACY RQARRAGLRG TFRAFLTSRI
QNLDSTVRYA DRHLPVLNTQ GDVLFKSFSD IFDGSGGIVA GTPRIYSFNG KNIITDSHWP
QKLIWHGSHA SGERALDTFC EEWQSNDPTN KGMAASLYSH KILSQERYSC NNHFAVLCIE
ATSNVSVRRK RDTHRFNTTE DSDEDYEMRP DEYEELINDI IAQPLRYN
//
