ID A0A484BZD7_PERFV Unreviewed; 1302 AA.
AC A0A484BZD7;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 28-JAN-2026, entry version 21.
DE RecName: Full=Thrombospondin-like N-terminal domain-containing protein {ECO:0000259|SMART:SM00210};
GN ORFNames=EPR50_G00241370 {ECO:0000313|EMBL:TDG96395.1};
OS Perca flavescens (American yellow perch) (Morone flavescens).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Percoidei; Percidae; Percinae; Perca.
OX NCBI_TaxID=8167 {ECO:0000313|EMBL:TDG96395.1, ECO:0000313|Proteomes:UP000295070};
RN [1] {ECO:0000313|EMBL:TDG96395.1, ECO:0000313|Proteomes:UP000295070}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YP-PL-M2 {ECO:0000313|EMBL:TDG96395.1};
RC TISSUE=Blood {ECO:0000313|EMBL:TDG96395.1};
RA Feron R., Morvezen R., Bestin A., Haffray P., Klopp C., Zahm M., Cabau C.,
RA Roques C., Donnadieu C., Bouchez O., Christie M., Larson W., Guiguen Y.;
RT "A chromosome-scale genome assembly of the yellow perch, Perca
RT flavescens.";
RL Submitted (JAN-2019) 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:TDG96395.1}.
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DR EMBL; SCKG01000024; TDG96395.1; -; Genomic_DNA.
DR STRING; 8167.A0A484BZD7; -.
DR Proteomes; UP000295070; Chromosome 24.
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 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:UP000295070};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 4..193
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 198..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 829..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 988..1126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..296
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..336
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..374
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..427
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..467
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..505
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..538
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..568
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..625
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..640
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..656
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..728
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..759
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..780
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 844..862
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 877..886
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..906
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 921..930
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1009..1024
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1038..1068
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1302 AA; 131801 MW; D1AD3D195016D6DA CRC64;
MPNCISLLQL IGDPPPDEIG RSYGPGGETA YVFTPAAVSG QPALAHVPNP FHRHFSLLFH
VKPSTPAAAV LFSITDGPQK LMYIGVKLGA VRSGRQAVQF FYTEPDSEAS YQAASFQVPS
LVDTWSRFSL AVFEEQVTFY LGCDSEPQVV KFERSPDPME LDTGAGIFVG QAGGADTDKF
QGEIADLRVV GNPRAAERLC DDEDDSDAAS GDFGSGDGDR RQTGNTVKTT PASLRPVPEP
PLISSTGTRL KETGPGGAKG EKGDKGAKGS VGDTGPAGPK GDSGSSITSS GSSSQGGERG
QKGEKGAKGS SGFGYSGNKG ERGAPGPPGL PGPPGPAAEV VRLGDGSVVQ QVSGPPGPPG
PPGSDGAPGP AGTDGEPGDP GEDGKAGPAG PRGLPGNTGS AGAKGQKGEV GEGQPGPRGP
PGLPGPPGSG TGDRPTFFDM EGSGFPDLDK IRGARGPPGP PGPPGPPGVS VALGPNGPVV
FGPPGPPGQD GAPGLPGPPG PPGKPGQPGL RGEKGDSGDL GLPGAAGAKG AQGDLGAQGT
SGQIGLAGLP GPMGPVGPPG PPGPPGPPYG VGHDGYETNN GWSGLSGPPG PQGRAGLPGN
HGDKGSEGPR GPPGIPGLDG LPGQPGERGD RGEKGERGLP GRDGVLPGPP GPPGPPGQVI
YQTSDGPSGP KGEKGDSGPP GYAPKGEKGE PGIILGPDGR PQYLGGLAGR PGDSGPPGPV
GPPGPHGPPG HKGEIGFPGR PGRPGLNGAT GQKGDSGTAS GSGYPGPPGP PGPPGPPGPS
VPSDRLGGLD SRYYQALKGE KGDRGLPGTL EIQGAGGTID IYTLRNELKG ETGSPGYKGE
KGEPGGGYYD PRYGGSGVGA PGVPGPPGPR GDSIVGPPGP QGPPGQPGRG YDGQPGPPGP
PGPPGASLPG SYRGTQTINI PGPPGPPGVP GLPGQSSGVT VFRSYDTMTA IARRQPEGSL
VYIIEQTDLY LRVRDGIRQV QLGGYIALPS DDGNDVAAVE PPPVVPYSPD HHSNTDTSAH
DSQRPPESPV HPGSGHQSHP DPRYPSHPDP RYPTHPDPRY QPDARYQPDP RFPAPTDPRF
PSYSERVNQP DGRYSVHTAP DARYPVTPQR RPPPPVPQTP VHHHTSGPGL HLIALNVPQT
GGMRGIRGAD YQCFTQAQAI GMKGTFRAFL SAKLQDLHSI VRRADRDRFP IVNLKDEVLF
DSWEAIFNGG RMKDNVPIYS FDGKDVLSDG TWPDKMMWHG STGGGQAHAD SYCEMWRVGE
RALSGMASSL QSGSLLQQSS SSCSNSYAVL CVENSYVGHA KR
//
