ID A0A9J8APV2_CYPCA Unreviewed; 1310 AA.
AC A0A9J8APV2;
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:ENSCCRP00000147229.1, ECO:0000313|Proteomes:UP001108240};
RN [1] {ECO:0000313|Ensembl:ENSCCRP00000147229.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSCCRP00000147229.1}
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; ENSCCRT00000139054.1; ENSCCRP00000147229.1; 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: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: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..1310
FT /note="Thrombospondin-like N-terminal domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039906689"
FT DOMAIN 32..221
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 223..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 834..977
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1046..1134
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 756..765
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..817
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..882
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..924
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..948
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 961..970
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1310 AA; 134384 MW; 0DA69B8E2F91DE3F 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 ENGPVGPKGV 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
//
