ID A0A6A5E3P7_PERFL Unreviewed; 1282 AA.
AC A0A6A5E3P7;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 28-JAN-2026, entry version 17.
DE RecName: Full=Thrombospondin-like N-terminal domain-containing protein {ECO:0000259|SMART:SM00210};
GN ORFNames=PFLUV_G00130680 {ECO:0000313|EMBL:KAF1383317.1};
OS Perca fluviatilis (European perch).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Percoidei; Percidae; Percinae; Perca.
OX NCBI_TaxID=8168 {ECO:0000313|EMBL:KAF1383317.1, ECO:0000313|Proteomes:UP000465112};
RN [1] {ECO:0000313|EMBL:KAF1383317.1, ECO:0000313|Proteomes:UP000465112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Blood {ECO:0000313|EMBL:KAF1383317.1};
RA Roques C., Zahm M., Cabau C., Klopp C., Bouchez O., Donnadieu C., Kuhl H.,
RA Gislard M., Guendouz S., Journot L., Haffray P., Bestin A., Morvezen R.,
RA Feron R., Wen M., Jouanno E., Herpin A., Schartl M., Postlethwait J.,
RA Schaerlinger B., Chardard D., Lecocq T., Poncet C., Jaffrelo L.,
RA Lampietro C., Guiguen Y.;
RT "A chromosome-scale genome assembly of the European perch, Perca
RT fluviatilis.";
RL Submitted (JUN-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:KAF1383317.1}.
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DR EMBL; VHII01000011; KAF1383317.1; -; Genomic_DNA.
DR Proteomes; UP000465112; Chromosome 11.
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; 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; 5.
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:UP000465112};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 50..239
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 240..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 730..1003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..270
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..349
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..366
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..447
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..491
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..601
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..637
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..675
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..692
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..709
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..749
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..836
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..860
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 870..884
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 927..953
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 963..976
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 986..997
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1282 AA; 131690 MW; 59BF2E114365F428 CRC64;
MHLEFIFRPG FCIPLFAKMF QGWSLALHLV LLCWLAAALQ VIEERGPGSH LDLTEIIGVP
LPPSVSFTPG YQGFPAYKFD PEANIGRLTK TFVPGSFYRD FAIIVTVRPA TQRGGVLFAI
TDTHQKVVEL GLALTPVRGG LQSILLYYTD REQASHSHKA ASFSVPDMTD QWTRFTVVVE
HDEVRLYMDC GDGERATFHR RPERLNFSRN SGIFVANAGN TGLDKFVGSI QQLVIKDDPR
AAEEQCEDDD PYASGYTSGD DALDDRETEE EMMKNTHDKK HGTAQEEDSV PVRAPPTEVP
EVELDEYSGH QTPTEASEER LMRGRTEEPG ERSGDGHVRH GLKGERGDPG PRGPPGPPGH
PGPTPGPQWK AQPGPRGTQG PPGIPGSPGL PGKDGQAGIK GDKGDPGQRG SQGFPGLDGE
AGAKGEKGDP GVGAPGPPGL PGPPGPPRSR SVPYGADALG SGFEDLDSDT ELIRGLPGPP
GPPGPPGPPG RPDAGGTGNL SSSDTSEGLS PGLAGPPGTP GRDGLPGRPG IPGPAGKDGS
PGLPGAVGEK GNQGLSGPPG PKGECGSVST AGSSGPPGPS GPQGKRGPSG PPGPPGPPGP
PATKFFVEDM EGSGKTDMLI GAGVRGPQGP PGIPGPQGPK GEDGATGAPG LSVKGEPGDP
GPEGIPGPAG LPGARGAKGE KGNEGPKGDR GVDGLSIPGP PGLPGPPGPV INLPDLLLNV
TDGIFNFTEI RGPPGPMGPE GLPGRAGFPG PRGPKGDIGP PGVQGPAGYK GEKGEPGVTI
AADGSLLSAP RGPQGPKGNK GDRGFPGPAG LMGPIGPFGQ KGEYGFPGRP GRSGTPGRKG
DKGDAVGLPG PPGPPGPPGH PGKIIGLKGE PMRGEELAKG DKGDVGIPGE PAPGFPDGIV
GARGDQGYKG QKGEKGEDGL PGPPGLPGRS GLVGPKGESI VGPLGPVGPV GEPGAPGFGR
PGPRGPPGPA GPPGPAPAYG SGVSIPGPPG PAGPPGSPGY ANPVTIYKTS HALSRDTHRA
AEGTFAYVSE KGGELYIRAR NGWRKIQLGE LIHSGPSPSA ASQTVSRTLE SRPHRIHSQE
LQEGSRGYQP SYNVLPQTFN AVPGLHLVAL NTPLKGDMRG IRGADFQCYQ QARSMGLTAT
YRAFLSSHLQ DLSTIVRKVD RNDMPVVNLR GEVLFSSWMS IFSGNGGTFD PFTPIYSFDG
RNVMTDSAWP EKLVWHGSNT MGIRVTTNYC EAWRTADVAV TGQAALLQTG RLLGQHTRSC
SNHYIVLCIE NTYVGNTHQR RT
//
