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Database: UniProt
Entry: A0A9N7UE71_PLEPL
LinkDB: A0A9N7UE71_PLEPL
Original site: A0A9N7UE71_PLEPL 
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
//
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