ID A0AAY5K765_ESOLU Unreviewed; 1361 AA.
AC A0AAY5K765;
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};
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:ENSELUP00000085019.1, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000085019.1, 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:ENSELUP00000085019.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSELUP00000085019.1}
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; ENSELUT00000094780.1; ENSELUP00000085019.1; ENSELUG00000041355.1.
DR GeneTree; ENSGT00940000165423; -.
DR Proteomes; UP000265140; Chromosome 22.
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:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
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; 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:SF1112; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR Pfam; PF01391; Collagen; 2.
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..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1361
FT /note="Thrombospondin-like N-terminal domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5044328633"
FT DOMAIN 32..223
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 230..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 918..1030
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1098..1178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..320
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..335
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..362
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..502
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..526
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..543
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..594
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..630
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..681
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..708
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..724
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..758
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 841..850
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 851..863
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 866..877
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 918..932
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 936..948
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 965..974
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 986..998
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1013..1022
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1100..1110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1127..1141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1167..1176
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1361 AA; 139743 MW; A99836E355B5D41F CRC64;
MTRLDSWLSP HFCIGILLLI DTLTESQRPV PGVTLLQLIG DLPPDDSRSG PGGKPVYYFG
GADGAQAAGQ LALAHLPSPF YRDFSLVFHI MPTSPGVLFS ITDASQKFMY VGVKLSPPDA
NGRDQKVLFY YTEPESEASS LAATFTVPAL DQVSWTRFSL SVSDDKVTLF MGCDTSGKTV
KFERSPDDME LDRGAGIFVG QAGAADTDRF EGAIAELKVL GNPQAAELLC EDEDDSEGVS
GSFSGDGDRM ETGQTVKTTA PSFRPMPEPP LSPSLSDRLS QTGPAGSKGE KGDRGEKGSL
GDRGPTGPKG DAGSSSSSGS SSGGGERGEK GDKGLKGSSG FGYPGSKGDR GVPGPPGPPG
PQGPAAQVVR LGDGSVVQQV AGPVGPRGPP GVQGPSGPPG PEGEAGDPGE DGKEGPPGPR
GFPGTPGITG LKGQKGHKGD GHPGPRGLPG LPGPPGPGSG DHPTFWDMEG SGGFPDIEKM
RTLQGPPGLP GKPGPPGPPG PPVMNVGSNA TGSFGAPGLP GKDGSPGLPG PPGPPGKPGP
PGPSSVVKGK AGELGLPGPS GEKQDTSSAF SSFSSYFTRL FSSEGDGSQG SQGENGLPGQ
EGQVGLAGLP GPIGPVGPPG PPGPPGPPYP VRYRDEDGTN VPEVLGIPGP EGPPGNPGLP
GKAGFPGIPG EKGSEGPRGR DGIPGMDGFP GKWGEKGERG DKGERGLPGR EGGPPGPPGP
PGPPGQIYQT SDSYIGVYGG HEQRGPGFPG PPGLPGPMGP KGDNGAPGLP GYGAKGEKGE
PVTILGPDGR PMFLGGLRGQ PGERGLPGPE GPAGPAGPAG MKGDIGMPGR PGRPGLNGVK
GDSGGHGYPG APGPPGPPGP PGQLVPRDRF STPRYDDISQ SYPQSKGEKG DRGVPGIPGQ
PGLTTNFDIY AFKNEMKGEK GDFGTKGEKG EPAEGGYYGG GYSGLGGQPG PPGPPGPKGD
SIIGPPGPQG PPGNPGRGYE GRQGEPGPPG APGPPGPSSL PGAYRPSQTI TIPGPPGPPG
PPGANGLSSG VMMLRSYDTM TATARRQAEG TLVYLLDQAD LYMRVRDGFR QIQLGPYIAL
PPDQGNAVAA VDPPRVVYHQ PEEHSPHPDP RQPQPEGQHP VYPDPHYPTH PDPRYPTHPD
PRYPSYTDRF PGPDPVRPVY PDTRYPVTPP HRPSPPLTHT HRHTVGPSIH LIALNTPHGG
NMRGIRGADL LCFNQARAIG LKGTFRAFLS SKLQDLHSIV RKSDRGSVPI VNLKDEVLFD
SWEAVFSEVR VKDNISIYSF EGKDILTDST WPDKMIWHGS TSRGQQQVDN YCEAWRVGER
ALTGMASSLQ DGQLLQQSAS SCQNSYAVLC IENSYFGQAK R
//
