ID A0A9J8A0N9_CYPCA Unreviewed; 1330 AA.
AC A0A9J8A0N9;
DT 28-JUN-2023, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2023, sequence version 1.
DT 28-JAN-2026, entry version 14.
DE RecName: Full=Thrombospondin-like N-terminal domain-containing protein {ECO:0000259|SMART:SM00210};
OS Cyprinus carpio carpio.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Cyprinus.
OX NCBI_TaxID=630221 {ECO:0000313|Ensembl:ENSCCRP00000138769.1, ECO:0000313|Proteomes:UP001108240};
RN [1] {ECO:0000313|Ensembl:ENSCCRP00000138769.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSCCRP00000138769.1}
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 Ensembl; ENSCCRT00000106785.1; ENSCCRP00000138769.1; ENSCCRG00000002061.2.
DR GeneTree; ENSGT00940000165423; -.
DR Proteomes; UP001108240; Unplaced.
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:0032836; P:glomerular basement membrane development; 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; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1060; COLLAGEN ALPHA-1(IV) CHAIN; 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:UP001108240};
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..1330
FT /note="Thrombospondin-like N-terminal domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039936102"
FT DOMAIN 32..221
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 223..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 854..997
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1066..1154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..298
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..327
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..356
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..387
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..418
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..447
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..492
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..560
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..570
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..589
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..644
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..677
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..717
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..785
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 822..837
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 885..902
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..944
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 955..968
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..990
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1330 AA; 136119 MW; FEE9CEFD1E652093 CRC64;
MARRWVAFLE LLLCCLLIAL SPAASQRREE SGVSLLQLIG DPPPVGVSKV FDHDNSPGYV
FDQSSNVGQS AAAHLPNPFF RDFSLIFNIK PTSSKPGVIF SITDPTQNIM YVGVKLSAVE
KGKQYIIFYY TEPDSESSYE AARFSVPSMV NTWTRFSISV LNERVSLYFN CDSDPQVISF
ERSPDDMDLD VGAGVFVGHA SGADPNKFLG VIGDVRVLKD PGAAERHCEE DEDDFDAGSG
DYGASGDGEG RPSIQPTPPS SRPIQQPPVT SRPLVEKQLT GGKGEKGDRG EKGAKGERGL
VGPKGDSGSG SGGSAKAEKG DPGEKGMKGS SGFGYPGSKG DRGPPGPPGP PGPPGPSAEV
ELRGDGSVLQ KVAGPRGPPG PEGPPGPAGA EGEPGDPGED GKAGQVGPPG FPGTPGSPGP
KGEKGERGES QPGPRGPPGL PGPPGPPSLS DRPTFVDMEG SGFDLDSVRA MPGLPGLPGP
PGPPGLPGPP GPGSSGPGGF GPPGPPGQNG APGQPGLPGT PGADGKPGLT GPKGEKGDSG
ELGLPGPVGE KGAKGSSGSP GLPGEGGLAG LPGPMGPVGP PGPPGPPGPR YHVGFDDMEG
SGVHFSSVPG LRGPVGIQGP PGVPGPQGTP GFPGFPGEKG SEGPQGKDGQ PGLDGFPGPQ
GPKGNKGDRG DRGEPGRDGA GLQGPPGPPG PPGQIIYGYS ENNDGGAGPR GGAGLPGQAG
FPGPVGPKGV RGEPGSPGYG IKGEKGEPGL ILGPDGNPLY HGGLTGLKGE SGLPGPVGPP
GPAGPPGLKG EFGMPGRPGR PGVNGYKGEK GESGSGSGYG YPGPPGPPGP PGPPGPALPL
DRFSRYEDYS RQYPAIKGDK GDQGAPGVPG SPGFSSNVDI YALKNEMKGE QGEPGLKGEK
GEPGGGFYDP RFGAVQGPPG NPGPTGPKGD SIRGPPGPQG PPGAPGVGYD GRPGNPGPPG
PPGPPGSPSL PGAYRPQLSI PGPPGPPGPP GVSGTGSGVT FLRSYDIMMA TARRQSEGAL
IYILDRNDLY LRVRDGVRQV MLGDYKTFYG ELDNEVAAVQ PPPVVHYSQD HTADNGAEQI
SPPHQPIEFP RREPENRNPS PTDSRYPDPQ YPPYTDPVQP HRHPVQPERN PITPARRPSP
PVNQPEGHTH TSGPGLHLIA LNSPQVGNMR GIRGADFLCF QQARAVGLKG TFRAFLSSKL
QDLYSIVRRS DRETLPIVNL KDQVLFRSWE SLFSDSESRM KDNAPIYSFD GRDVLRDSAW
PEKMIWHGSS GRGHRQTDNY CETWRAGDRA VTGLASSLQA GQLLQQTSSS CSSSYIVLCI
ENSYMTQSKK
//
