ID A0A9N7UE71_PLEPL Unreviewed; 1397 AA.
AC A0A9N7UE71;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 08-OCT-2025, entry version 11.
DE RecName: Full=Thrombospondin-like N-terminal domain-containing protein {ECO:0000259|SMART:SM00210};
GN ORFNames=PLEPLA_LOCUS16564 {ECO:0000313|EMBL:CAB1428591.1};
OS Pleuronectes platessa (European plaice).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Pleuronectidae;
OC Pleuronectes.
OX NCBI_TaxID=8262 {ECO:0000313|EMBL:CAB1428591.1, ECO:0000313|Proteomes:UP001153269};
RN [1] {ECO:0000313|EMBL:CAB1428591.1}
RP NUCLEOTIDE SEQUENCE.
RA Weist P.;
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CAB1428591.1}.
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DR EMBL; CADEAL010001068; CAB1428591.1; -; Genomic_DNA.
DR Proteomes; UP001153269; 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: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; 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; 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 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:UP001153269};
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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1397
FT /note="Thrombospondin-like N-terminal domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5040311950"
FT DOMAIN 183..372
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 33..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 849..1117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..53
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..403
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..478
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..493
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..529
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..573
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..612
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..659
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 746..755
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..810
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 932..942
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 957..966
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1074..1089
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1097..1106
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1397 AA; 142942 MW; B3DCAC6EA88B3A3C CRC64;
MGTLCLSFAL LFLFCSPARA QWWSLIWANP KTSSESSPPS IPPSTTSPSI SSPGFSETPW
TTGQVGVKDG VRKESVEGGT ETEGSVLAPT AVPGELLSGL STAEPGRLSA EENAGADSKT
RPQNKPLKHW KSGECYWAVF PMYILKSVPS MKTPLLWLKD AKDVELNEEV VPSFPVERGS
GGHLDLTELI GVPLPPSVSF TPGYEGFPAY IFGPEANIGR LTKTFVPGSF YKDFAIIVTV
RPSSQRGGML FAITDAGQQV VELGLALTPV RGGLQSILLY YTDRGQVSHS HKAAAFSVPD
MTDQWTRFTV VVEHNEVRLY MDCGEAERAT FHRSPESLTF SHNSGIFVAN AGNTGLDKFV
GSIQQLVIKD DPRVAEEQCE DDDPYASGFA SGDDALDDRE TEEEMTKSKH GTAQGEDSFP
VRAPPTEAPE GELEEFSGRM TPTESNEEMI GGPHQTEEAG ERSGDGHVRP EIKGERGDPG
PPGPPGPPGP TPRPGQTHPG SRGTKGPAGT PGSTGLPGRD GQKGHKGDTG DPGQSGPQGF
PGLDGKAGPS GDKGDSGIGV PGPPGLPGPP GPPRSRSVPY GADALGSGFE DLDSDTELIR
GPPGPPGPPG PPGASGSDML PDTAEGLPSG HDGPSGVPGR DGAAGKPGTP GPAGKDGAPG
LQGAGGEKGD QGLTGLSGPK GECGSLGTAG LPGAEGPMGP QGERGLIGPP GLPGPPGPQA
TKFFVEDMEG SGKSDMLLGA GVKGPQGPPG LPGPQGPEGE DGAPGSPGLS VKGEPGDPGA
EGLQGPAGLP GVRGVKGEKG NHGPKGDRGA DGLSIPGSPG PPGLPGPSFN LQDLLLNVTD
GIFNFTEIRG APGPMGPRGP KGEIGPEGIQ GPSGLKGEKG EAGVTIAADG SLLSAPRGPQ
GPKGIKGDRG YQGPSGVMGP IGPTGLKGEY GFPGRAGRPG LPGRKGDRGE ADGLQGPPGP
PGPPGIPGRI LGLKGESVTR GDSAGAKGDK GDEGMPGEPG TSESGFLDGI VGARGNQGNK
GEKGERGDTA GPGPPGMPGR SGLVGPKGES IVGPQGPIGP PGVPGAPGFG RPGPRGPAGP
TGPPGPAPPY GSADSVPGPP GPPGPPGSSG SSGSGNLVTV YKSTHALIRE SQRAPEGTLA
YVSERGGELY IKRRNSWRKI QLGELLHHGP SSSAESQTLS VPGEYSRTHR SHSQELQEGG
RGYQPSFNVL PQTFNAVPGL HLVALNSPLK GDMRGIRGAD FQCYQQARSV GLTATYRAFL
SSHLQDLSTI VRKADRNDMP VVNLRGEVLF SSWMSIFSGN GGTFNPSTPI YSFDGRNVMT
DSAWPEKLVW HGSSTVGIRL THNYCEAWRT GDMAVTGQAA LLQTGRLLGQ HTQSCSNPYV
VLCIENTYVG NTHLRRT
//