ID A0A8R2HPR0_BOMMO Unreviewed; 1165 AA.
AC A0A8R2HPR0;
DT 12-OCT-2022, integrated into UniProtKB/TrEMBL.
DT 12-OCT-2022, sequence version 1.
DT 28-JAN-2026, entry version 12.
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_021208110.2, 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_021208110.2}
RP IDENTIFICATION.
RC STRAIN=p50T (Dazao) {ECO:0000313|EnsemblMetazoa:XP_021208110.2};
RG EnsemblMetazoa;
RL Submitted (JUN-2022) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR AlphaFoldDB; A0A8R2HPR0; -.
DR SMR; A0A8R2HPR0; -.
DR EnsemblMetazoa; XM_021352435.2; XP_021208110.2; 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; 3.
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..1165
FT /note="Thrombospondin-like N-terminal domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035871965"
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 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 797..809
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1165 AA; 121525 MW; 32D11084E5281BA8 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
GLPGWMNSKG RPGTLGPPGA PGPVGPKGEK GDPGVNILDV SMFKGEKGDR GFDGVPGVQG
PPGPPGKPAS EPVQYLPGPP GPPGPPGSPG TPGVSVVGPK GEPGVSYYEE GPVHGSPKFY
GRPGFSARSQ PADESSAQKT VPGAAVFQTT EEMMKLASSS PVGALAYVAE EQALFVKVNS
GWQYVLLGSL VTQSKPPPTP APAPLPMPAA SLVHVPPISN LVENSPTPIG PSLRMAALND
PLSGNMHGVR RADYACYRQA RRAGLRGTFR AFLTSRIQNL DSTVRYADRH LPVLNTQGDV
LFKSFSDIFD GSGGIVAGTP RIYSFNGKNI ITDSHWPQKL IWHGSHASGE RALDTFCEEW
QSNDPTNKGM AASLYSHKIL SQERYSCNNH FAVLCIEATS NVSVRRKRDT HRFNTTEDSD
EDYEMRPDEY EELINDIIAQ PLRYN
//
