ID A0AAY5K4F7_ESOLU Unreviewed; 1350 AA.
AC A0AAY5K4F7;
DT 05-FEB-2025, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2025, sequence version 1.
DT 28-JAN-2026, entry version 5.
DE RecName: Full=Thrombospondin-like N-terminal domain-containing protein {ECO:0000259|SMART:SM00210};
GN Name=DVL3 {ECO:0000313|Ensembl:ENSELUP00000083676.1};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000083676.1, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000083676.1, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Myers G., Karagic N., Meyer A., Pippel M., Reichard M., Winkler S.,
RA Tracey A., Sims Y., Howe K., Rhie A., Formenti G., Durbin R., Fedrigo O.,
RA Jarvis E.D.;
RT "Esox lucius (northern pike) genome, fEsoLuc1, primary haplotype.";
RL Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSELUP00000083676.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSELUP00000083676.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- SIMILARITY: Belongs to the multiplexin collagen family.
CC {ECO:0000256|ARBA:ARBA00061275}.
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DR Ensembl; ENSELUT00000103748.1; ENSELUP00000083676.1; ENSELUG00000037313.1.
DR GeneTree; ENSGT00940000165423; -.
DR Proteomes; UP000265140; Chromosome 16.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00247; Endostatin-like; 1.
DR FunFam; 3.10.100.10:FF:000008; collagen alpha-1(XVIII) chain isoform X1; 1.
DR FunFam; 3.40.1620.70:FF:000003; Collagen type XVIII alpha 1; 1.
DR FunFam; 2.60.120.200:FF:000039; Collagen XV alpha 1 chain; 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 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Reference proteome {ECO:0000313|Proteomes:UP000265140};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..1350
FT /note="Thrombospondin-like N-terminal domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5044283790"
FT DOMAIN 32..221
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 221..1007
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1070..1172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..269
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..302
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..315
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..333
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..360
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..400
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..438
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..453
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..493
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..506
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..516
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..531
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..591
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..654
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..680
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..695
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 708..728
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 782..791
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 829..842
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 889..906
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 942..951
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 962..975
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 990..1001
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1076..1091
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1137..1147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1350 AA; 137999 MW; 6760C0EFA13CCD32 CRC64;
MKTRCFAWLE TLVCCVLVIL APAGSQWADE SGVSLLQLIG DPPPDEITKV YGPDNTPGYL
FSSDANTGQL ARAHLPNPFY RDFSLLFNLK PQSTKGGVIF SVTDVSQQIM YVGVKLSPVK
ANRQNVVFYY TEPGSQESYV AATFPVQSMA DQWNRFSISV LDDKVTFYIN CDDRPQVMRF
ERSPDEMELD AGAGVFVGQA GGADPDKFLG VIGELRVVGD PQAAERQCDE EGDDYDAASG
DDGSGGGERI PEEKTKTPTT PPPSRPIQQP PVTRKQPLSP KKETGPGGSK GEKGDRGDKG
DRGPSGPKGD SGSESATRGG TRAEKGEPGE KGTKGQAGFG YPGSKGDPGP PGPPGPPGLP
GPSAEVQSRG DGSLVQTVAG PRGPAGPPGT AGPQGPAGAD GEPGDPGEDG SQGPVGPPGF
PGTPGDPGLK GEKGDRGEGQ PGPRGPPGPP GPPASSRNDR PTFADMEGSG FPDIETLRGP
PGLPGPPGPP GPPGKIEGLG GVGSLGPPGK DGAPGKPGLP GLPGVDGRPG PAGASGEKGD
PGELGLPGAV GAKGAQGLTG MPGTPGQTGL AGLPGPMGPV GLPGPPGPPG PSYNIGFDDM
EGSGVGLASG LPGPRGPEGR QGPPGTPGLP GQPGFPGIPG EKGSDGPQGK DGRPGLDGFP
GPNGQKGDRG DKGDRGEPGR DGSGQPGPPG LPGPPGQIIY QTSSSDRGVV GAAGPQGEAG
PPGQAGFPGP VGPKGNMGDP GPPGYGVKGE KGESGSIIGP DGNPLFIGGV SGQKGDRGPS
GPVGPPGPYG PPGMKGEFGM PGRPGRPGVN GYKGEKGDAA VPGFGYPGAP GPPGPPGPPG
PAVPVDRFNG YDTSRNYPAT KGEKGDAGTP GLPGTPGVAS NFDIFAFKNE LRGERGDKGV
KGEKGEPGGG YYDPRFGGQQ GPPGPPGNPG LMGPKGDSIK GPPGPQGPPG APGIGYDGRP
GNPGPPGPPG PPGSPSLPGA YRPTHTISIP GPPGPAGPPG SPGQSSAVTV LRSYETMVAT
AKRQSEGTLI YIVDKSDLYI RVGNGLRQVL LGEYRPFYRD LDNEVAEVQP PPVVNYPQSQ
DHSANSGSEH FSQGGAATHP IQPPHRQPVQ PSIRNPDPRY PPQYDPHTDG RYNPLHPESR
YPTEPEIRYP VTSQRRPVPP PVHQPASHTH TSGPGLHLIA LNTPHMGNMR GIRGADFLCF
QQARAVGLKG TFRAFLSSKL QDLYSIVRKS DRDSLPIINL KDQVLFNSWE SMFSKSGGRM
KENAPIYSFD GRDIFRDSAW PEKMVWHGSS TEGHRQTDNY CETWRAGDRA VTGLASSLQS
GQLLQQSSSS CSSSYIVLCI ENSYISHSKK
//
