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Database: UniProt
Entry: A0A7M7IQ24_NASVI
LinkDB: A0A7M7IQ24_NASVI
Original site: A0A7M7IQ24_NASVI 
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.
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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
//
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