ID A0A9J7YBJ4_CYPCA Unreviewed; 1182 AA.
AC A0A9J7YBJ4;
DT 28-JUN-2023, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2023, sequence version 1.
DT 28-JAN-2026, entry version 13.
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:ENSCCRP00000116238.1, ECO:0000313|Proteomes:UP001108240};
RN [1] {ECO:0000313|Ensembl:ENSCCRP00000116238.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSCCRP00000116238.1}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A9J7YBJ4; -.
DR Ensembl; ENSCCRT00000130414.1; ENSCCRP00000116238.1; 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: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; 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:SF1019; COLLAGEN ALPHA-5(IV) CHAIN ISOFORM X1; 1.
DR Pfam; PF01391; Collagen; 1.
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..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1182
FT /note="Thrombospondin-like N-terminal domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039891030"
FT DOMAIN 65..246
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 43..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 741..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 918..1006
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..308
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..366
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..397
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..409
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..427
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..520
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..553
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..705
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..754
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..796
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..820
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 833..842
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1182 AA; 124101 MW; 7B97EEC7110610A3 CRC64;
VMSKLRFWLC LFILVCLRIC HTHGWFWFDD SKENMKGAQT PAYLTTTRPT SPPRTEPPRT
AEESGVSLLQ LIGDPPPVGV SKVFDHDNSP GYVFDQSSNV GQSAAAHLPN PFFRDFSLIF
NIKPTSSKPG VIFSITDPTQ NIMYVGVKLS AVEKGKQYII FYYTEPDSES SYEAARFSVP
SMVNTWTRFS ISVLNERVSL YFNCDSDPQV ISFERSPDDM DLDVGAGVFV GHASGADPNK
FLVCTQCNEN LFYANCYIND IYHLQPTPPS SRPIQQPPVT SRPLVEKQLT GGKGEKGDRG
EKGAKGERGL VGPKGDSGSG SGGSAKAEKG DPGEKGMKGS SGFGYPGSKG DRGPPGPPGP
PGPPGPSAEV ELRGDGSVLQ KVAGPRGPPG PEGPPGPAGA EGEPAMPGLP GLPGPPGPPG
LPGPPGPGSS GPGGFGPPGP PGQNGAPGQP VSLRRHGPLE KNEIWKTVCV QDDMEGSGVH
FSSVPGLRGP VGIQGPPGVP GPQGTPGFPG FPGEKGSEGP QGKDGQPGLD GFPGPQGPKG
NKGDRGDRGE PGRDGAGLQG PPGPPGPPGQ IIYGYSENVS LYIYIGGAGL PGQAGFPGPV
GPKGVRGEPG SPGYGIKGEK GEPGLILGPD GNPLYHGGLT GLKVLYYFGP AGPPGLKGEF
GMPGRPGRPG VNGYKGEKGE SGSGSGYGYP GPPGPPGPPG PPGPALPLDR FSVSAFLFGH
FFPTGFSSNV DIYALKNEMK GEQGEPGLKG EKGEPGGGFY DPRFGAVQGP PGNPGPTGPK
GDSIRGPPGP QGPPGAPGVG YDGRPGNPGP PGPPGPPGSP SLPGAYRPQL SIPGPPGPPG
PPGVSGTGSG VTFLRSYDIM MATARRQSEG ALIYILDRND LYLRVRDGVR QVMLGDYKTF
YGELDNEVAA VQPPPVVHYS QDHTADNGAE QISPPHQPIE FPRREPENRN PSPTDSRYPD
PQYPPYTDPV QPHRHPVQPE RNPITPARRP SPPVNQPEGH THTSGPGLHL IALNSPQVGN
MRGIRGADFL CFQQARAVGL KGTFRAFLSS KLQDLYSIVR RSDRETLPIV NLKDQVLFRS
WESLFSDSES RMKDNAPIYS FDGRDVLRDS AWPEKMIWHG SSGRGHRQTD NYCETWRAGD
RAVTGLASSL QAGQLLQQTS SSCSSSYIVL CIENSYMTQS KK
//
