ID A0A8C4DXV4_DICLA Unreviewed; 1460 AA.
AC A0A8C4DXV4;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 12-OCT-2022, sequence version 2.
DT 28-JAN-2026, entry version 20.
DE RecName: Full=Thrombospondin-like N-terminal domain-containing protein {ECO:0000259|SMART:SM00210};
GN Name=LOC127378661 {ECO:0000313|Ensembl:ENSDLAP00005009554.2};
OS Dicentrarchus labrax (European seabass) (Morone labrax).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Moronidae; Dicentrarchus.
OX NCBI_TaxID=13489 {ECO:0000313|Ensembl:ENSDLAP00005009554.2, ECO:0000313|Proteomes:UP000694389};
RN [1] {ECO:0000313|Ensembl:ENSDLAP00005009554.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSDLAP00005009554.2}
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 RefSeq; XP_051283728.1; XM_051427768.1.
DR Ensembl; ENSDLAT00005010482.2; ENSDLAP00005009554.2; ENSDLAG00005005020.2.
DR GeneID; 127378661; -.
DR GeneTree; ENSGT00940000165423; -.
DR Proteomes; UP000694389; Unassembled WGS sequence.
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; 3.
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:UP000694389};
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..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1460
FT /note="Thrombospondin-like N-terminal domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035734979"
FT DOMAIN 32..221
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 226..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 591..1039
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1099..1283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..316
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..338
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..416
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..445
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..457
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..471
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..509
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..549
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..631
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..731
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 813..825
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..848
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..879
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..892
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..963
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 978..987
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 996..1008
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1022..1031
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1110..1125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1146..1155
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1156..1194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1197..1208
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1212..1221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1460 AA; 151317 MW; 506D5D3CACB678AC CRC64;
MRRRDRWSIL NWQMLLLLVV TQIKSQRRVE TGVSLDQLIG DPPPNAITRV YGPRGRAAYA
FTSAAVSGQP ARAHVPNPFY RHFSLVFYIK PSTSAASVLF SITDGPQKFM YVGVKLSAVQ
SGRQRVQFFY TEPDSEASYE AASFDVPSLV DTWSRFSLSV LEDQVTFYHG CDSEPQVVKF
ERSPDPMELD AGAGIFVGQA GGADADKFQG EIAELKVVGN PRAAERLCDD DDDSDASSGD
FGSGEGDRRQ TGHTVKTTPS SLRPVPEPPV ISSQGTWLKE TDVRFHKPLV DHSRTGSPGA
RGPSGAKGDR GEKGSKGDLG PAGPKGESGF SSGSSVSSQG GGQKGEKGAK GSSGFGYPGN
KGERGAQGPP GRPGPPGPAA EVVRLGDGSV VQQVSGPPGL PGPPGSDGPA GTPGTDGEPG
DPGEDGKAGP PGPRGFPGSP GSAGPKGDKG ERGEGEPGPR GPPGLPGPPG PGTGDRPTFF
DMEGSGFPDL DRIRGASGPP GPPGPPGPPG VSVAMGANGP VAFGPPGPPG QDGVPGLPGP
PGPPGPPGQP GLVGVKGDNG ELGLPGPSGE KQDSQDSNFF TGLFSYFAPS STGAQGDAGR
SGTPGQTGLA GLPGPMGPVG PPGPPGPPGP PYRVGFGNQD GFEGNNGLPG LRGPPGPQGP
PGIAGLPGKP GLPGIHGDKG AEGQRGPPGI PGLDGFPGQS GEKGARGDKG DTGLPGRDGG
PPGPPGPPGP PGQISYRTTS DYNDPYWNEG WQGGSSVQGR AGFPGPMGPK GDKGDSGPPG
YAPKGEKGEP GLILGPDGRP QYIGGLAGKP GESGPPGPVG PPGPHGPSGH KGEIGLPGRP
GRPGLNGARG EKGDSGIGSG YGFPGPPGPP GPPGPPGPYV PSDRFRGYDD SSRQYPALKG
EKGDPGPPGT LEIPGFRSSV DIYTLRNELK GETGNPGFKG EKGEPGGGYY DPRYGGSGVG
PPGEHGPPGP KGDSIIGPPG PQGPPGQPGR GYDGQPGPPG PPGPPGPSLP GAYRGTQTIN
IPGPPGPPGV PGLPGHSSGV TVLRSYDTMT ATARRQPEGS LVYIIDQKDL YLRVRDGVRQ
VQLGSYIALP SVDDNEVAAV EPPPLVPYSP DHHSNTDTSS HDSQRPPESP VHPDSGPQSQ
PHHPDPYYPS NPDPRYPTHT DPRYPTHTDP RYPTHTDPRY PTHTDPRYPT HTDPRYPTQP
DPRYPTQPDP RYQPDSRHQP DPRYPAPTDP RYPSYTDRLN QPDGRYSVHT AQERPTYPDT
RYAVTPQRRP PPPLPESPVH HHSTGPALHL IALNSPQTGS MQGVRGADYK CFTQAQAIGM
KGTFRAFLSA KLQDLHSIVR KADRDRVPIV NLKDEVLSDS WDGIFNEGRI KDNVPIYSFD
GKDVFSDNTW PEKMVWHGST SGGQRQVDSF CETWRVGERA LTGMASSLQS GNLLQQSSSS
CSSSYVVLCI ENSYISHSKR
//
