ID A0A653C2G9_CALMS Unreviewed; 1050 AA.
AC A0A653C2G9;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 28-JAN-2026, entry version 18.
DE RecName: Full=Thrombospondin-like N-terminal domain-containing protein {ECO:0000259|SMART:SM00210};
GN ORFNames=CALMAC_LOCUS5678 {ECO:0000313|EMBL:VEN42064.1};
OS Callosobruchus maculatus (Southern cowpea weevil) (Pulse bruchid).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Chrysomeloidea; Chrysomelidae; Bruchinae; Bruchini; Callosobruchus.
OX NCBI_TaxID=64391 {ECO:0000313|EMBL:VEN42064.1, ECO:0000313|Proteomes:UP000410492};
RN [1] {ECO:0000313|EMBL:VEN42064.1, ECO:0000313|Proteomes:UP000410492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Sayadi A.;
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR EMBL; CAACVG010006832; VEN42064.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A653C2G9; -.
DR OrthoDB; 10060752at2759; -.
DR Proteomes; UP000410492; 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.
PE 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Reference proteome {ECO:0000313|Proteomes:UP000410492};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 4..178
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 214..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..270
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..334
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..366
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..401
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..429
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..506
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..518
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..544
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..636
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..667
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..690
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1050 AA; 109431 MW; 855E0DC7F23A162C CRC64;
MKTQYIDDDG HDGFPAFGFR AGSDVKIAHK QILPDRLSAE FSILVSAKPK SRRGGFLFAV
MNTYDTVVEL GVRVAPEGIN TTILTLFYTG PTEYYSRAIA NFTVPKFTGR WIRFAFRVAL
DNVTLFFNCL ETETVAVQRR PVELEFDSAS TLYIAQAGPT IEEPYEGALD QLKIYRDPNM
AAQQCKTNFE EFHYLDEDIN NEIYVERTDY DRTYREGSST SDDLGIFPPP PPPPDAAGRY
RGEKGDRGPR GPPGESIRGP PGPPGPPGSP GLPASEGSCS CNTTSILAAL PERSSPAYAV
EGRAGSPGPP GLPGPTGERG PPGYKGDKGD RGERGPQGAS GVQGIKGDPG RDGVQGPPGP
PGPPGPVEFE NVDESVIGGP LLRTGVPGPK GEPGKQGPSG PKGDRGAQGP KGPMGEAGHK
GERGDRGLPG EKGSIGLKGD RGDPGVDGIP GTPGKLGDKG EKGDLGPPGP PGISVGSTDI
SSVVPNLAGI KGEPGQKGEK GDRGSDGEAG IPGVPGSVGA SGGPGEKGEP GVDGAVGPVG
PPGSKGEKGD KGPPGAVIVA EGNAQIVTVK GEKGEMGKRG RRGKPGPMGP PGPPGKAGDI
GLPGWMGRPG IPGIGGQKGE KGDSGGPKGD KGDRGQDGAP GKDGIPGTPG PPGPAGPPGP
QGLPGPPSTG DIVKYVPVPG PPGPPGPPGQ PGLSIQGPKG EPGVVAAYGE AMRYNLRPGH
KSSLDELRAL RELEDLKEYS GRATAAPPLV AHIKEELPIK VVPGALTFHN KEVLVRMTEA
SPLGTMAFVI EEDALVIRVK RGWQYIALGS LLTTSAPPPP TTASPPLKLP FEASNLVNHA
IRSADGSHLR LAALNEPSTG DAHGVRGADY ACYREARRAG LRATFRAMLS SRVQNVDSLV
RLQDRKLPVV NLHGELLYHS WAEMFKGDGA PFQQQPVKIY SFSGKNVLND PTWPVKVVWH
GALPNGERAL DFSCDAWHNS SRDKVGLAAS LRSVGLLEQT PYSCDKKLII LCIEATSEGQ
KRKRRDINLR IPQTSGIDSL KIILSRSIRI
//
