ID A0A7M7IML6_NASVI Unreviewed; 1177 AA.
AC A0A7M7IML6;
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_016838931, ECO:0000313|Proteomes:UP000002358};
RN [1] {ECO:0000313|EnsemblMetazoa:XP_016838931}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JAN-2021) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR RefSeq; XP_016838931.1; XM_016983442.3.
DR AlphaFoldDB; A0A7M7IML6; -.
DR SMR; A0A7M7IML6; -.
DR EnsemblMetazoa; XM_016983442; XP_016838931; 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:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; 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:UP000002358};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1177
FT /note="Thrombospondin-like N-terminal domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5029489555"
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..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1135..1161
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 497..506
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..557
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..611
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..666
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..710
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..786
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..810
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1143..1160
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1177 AA; 123676 MW; D0BF2DC5CD98E585 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 GYDPSWKPRA IYRTEGYAMR 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
GWMGRPGTPG IPGLSGSKGE KGEPGAPSPY GSAHGIKGDK GADGFPGIPG APGMRGPPGP
AGPPGVPSQG SYIPVPGPPG PPGPPGPPGP GIGKSHIYGE RDYYGSRQGL RSSMDELKAL
RELKELKELK EHLGANAAAT RGPLETTTKI VPGAVTFQNT EAMTKMSGVS PVGTLAYIID
EQALLVRVNN GWQYIPLGTL LPITTPAPPT TASPPVNPPF EASNLINQVP VKADGTSWYP
KMLRMAALNE PFTGDMHGVR GADYACYRQA KRAGLKGTFR AFLSSRVQNV DSIVRLGDRD
LPIVNVKGDV LFNSWKEMFN GNGAYFSQNP RIYSFNGKNI LSDFTWPQKV VWHGSHTLGD
RAMDTYCDAW HSGSSDRYGL GSPLTGGRLL EQVRYSCDNK FALLCIEVTS EQTKRRRRRR
SLDEDEDEEE EDVDEEDESL LTEAEYAEQL RQLFHAD
//
