ID A0A7M7IQ24_NASVI Unreviewed; 1171 AA.
AC A0A7M7IQ24;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 28-JAN-2026, entry version 18.
DE RecName: Full=Thrombospondin-like N-terminal domain-containing protein {ECO:0000259|SMART:SM00210};
OS Nasonia vitripennis (Parasitic wasp).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Proctotrupomorpha;
OC Chalcidoidea; Pteromalidae; Pteromalinae; Nasonia.
OX NCBI_TaxID=7425 {ECO:0000313|EnsemblMetazoa:XP_016838934, ECO:0000313|Proteomes:UP000002358};
RN [1] {ECO:0000313|EnsemblMetazoa:XP_016838934}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JAN-2021) to UniProtKB.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_016838934.1; XM_016983445.3.
DR AlphaFoldDB; A0A7M7IQ24; -.
DR SMR; A0A7M7IQ24; -.
DR EnsemblMetazoa; XM_016983445; XP_016838934; LOC100120859.
DR GeneID; 100120859; -.
DR CTD; 104327; -.
DR OrthoDB; 5983381at2759; -.
DR Proteomes; UP000002358; Chromosome 3.
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 CDD; cd00247; Endostatin-like; 1.
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; IPR048287; TSPN-like_N.
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; 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:UP000002358};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1171
FT /note="Thrombospondin-like N-terminal domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5029620446"
FT DOMAIN 32..228
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 246..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1129..1155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..292
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..311
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..399
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..432
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..496
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..547
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..601
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..656
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..700
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..780
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..804
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1137..1154
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1171 AA; 122908 MW; 9C2051AB1497B986 CRC64;
MSPNFRGSLP PLLLLLLLLL CAAARASQDF FGDKKETEFD LLEAAVSLID DKNLYLTDGY
DGFMSFGFRP GSEVKQPYRM YLPEKLPSEF TLVASFKPFS AKNSYLFAVL NPFETVVQLG
IRISDGPSTN QNISLIYTNS DMSTVSDEVA KFTVPRLVKR WSKIVIRVTP NEVILYLNCH
EMARQKVTRI PLELVFDTAS TLYIAQAGPH IQEKYDGLLQ SLKLHLGFPQ DLVKCNEDFD
FYSGGDGSGD HELISGSGEI DPDDVPIARG DDEVESEEVK PPPLITPPPP NPNSKEVTKG
EKGDKGEKGE SVRGPPGPPG TSYDLNDEEW IAKLPEGPPG PKGDPGDCSC NASALLTSFS
MPKLMHGEKG EPGTPGKEGK QGPLGLTGAA GPPGERGQPG PQGPKGDKGD LGNTGPEGSQ
GEKGEPGRDG APGEKGAQGP PGPPGKGEFA GYDTEGYAMR PGLPGQKGDD GKPGHPGPKG
EPGVHGAKGD KGDAGHKGMK GLHGKEGPRG VQGVKGEPGA PGVPGLPGAV GEVGRTGDKG
AKGDMGPEGK TGPAGPPGPP GHGGVSVSDV VGPGRGQKGE PGERGYKGDL GLKGEKGDKG
DFGPAGVPGI NGIQGPQGDK GEPGKDGSPG FPGTPGMKGE RGERGPPGAT TIAGTGDYVT
IKGEQGAMGP MGKRGRRGRP GPPGNEGPPG PPGPEGPPGK PGINGEIGLP GWMNNMKGRP
GTPGIPGLSG SKGEKGEPGA PSPYGSAHGI KGDKGADGFP GIPGAPGMRG PPGPAGPPGV
PSQGSYIPVP GPPGPPGPPG PPGPGIGKSH IYGERDYYGS RQGLRSSMDE LKALRELKEL
KELKEHLGAN AAATRGPLET TTKIVPGAVT FQNTEAMTKM SGVSPVGTLA YIIDEQALLV
RVNNGWQYIP LGTLLPITTP APPTTASPPV NPPFEASNLI NQVPVKADGT SWYPKMLRMA
ALNEPFTGDM HGVRGADYAC YRQAKRAGLK GTFRAFLSSR VQNVDSIVRL GDRDLPIVNV
KGDVLFNSWK EMFNGNGAYF SQNPRIYSFN GKNILSDFTW PQKVVWHGSH TLGDRAMDTY
CDAWHSGSSD RYGLGSPLTG GRLLEQVRYS CDNKFALLCI EVTSEQTKRR RRRRSLDEDE
DEEEEDVDEE DESLLTEAEY AEQLRQLFHA D
//