ID A0A9J7Z5C2_CYPCA Unreviewed; 1252 AA.
AC A0A9J7Z5C2;
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:ENSCCRP00000127502.1, ECO:0000313|Proteomes:UP001108240};
RN [1] {ECO:0000313|Ensembl:ENSCCRP00000127502.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSCCRP00000127502.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
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DR AlphaFoldDB; A0A9J7Z5C2; -.
DR Ensembl; ENSCCRT00000148340.1; ENSCCRP00000127502.1; ENSCCRG00000021532.2.
DR GeneTree; ENSGT00940000158212; -.
DR OMA; CHCSSAY; -.
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 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:SF1082; COLLAGEN TRIPLE HELIX REPEAT; 1.
DR Pfam; PF01391; Collagen; 2.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
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..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..1252
FT /note="Thrombospondin-like N-terminal domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039937264"
FT DOMAIN 42..230
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 229..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 275..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 685..960
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..307
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..376
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..394
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..407
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..430
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..472
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..519
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..584
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..600
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..653
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..774
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..798
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 861..875
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 876..896
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 924..934
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 944..953
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1252 AA; 129081 MW; B0216FBDE712F4C6 CRC64;
MGRACDSSLL SRVWCWSLIT VCLCSSASAS QHFDSERDSR AQLDLTELIG VPLPPSVAFI
TGFEGFPAYS FGPDANVGRL TRSFIPDPFY RDFAIIVTAK PSTRRGGVLF AITDALQKIV
HLGVSLAPVE DGSQHVVLYY TEPGAAHTKE AASFKMGDLT GRWVRFTLAV QGEEVRLYMD
CEEHHRVAFR RSPDGLTFQP SSGIFIGNAG GTRLERFVGS IQQLLLTADP SAPNEQCEED
DPYASGYGSG GDIFDDTETP SEVKKVFEER EYTMLEDIES GPMRAPPTES PSFITETDDE
DLEEGSGEDI IIISGPKEPI RSEGASQDRN VITMQKGEKG ERGPEGPPGP AGPAAPHAPG
EPGPRGPQGP PGPPGEPGQD GQPGDPAKDG APGEAGPPGF PGLPGDPGPK GDKGDPGVGI
PGPPGPPGPP GTFKYPDGIA GSGSSYVDLD SDTELIRGPP GPPGPPGRPG LPGPSVGAQP
GPVGPPGAPG KDGETGKPGL PGENGRDGQT GKEGEKGQKG EPGLPGIMGP KGDAGQPGLP
GQTGSEGPRG QPGPPGPPGK GFSFDMMDLE GSGLDGSSGF SPVLPRGPPG LPGLPGPPGP
QGKEGAVGPP GVSVKGEPGA KGDDGQPGSS GLPGRQGERG EKGDMGQKGE RGLDGIGLPG
PPGPPGPVIN LHELMLNDTE GFFNLSGIFE PQGPSGPRGP KGDTGAPGVQ GPPGLKGQKG
EPGIVSGVHA PQGPKGLKGD GGVPGPPGQT GPIGPAGPKG EFGFPGRPGR PGINGRKGEK
GNSVGLPGPP GPPGPPGRPG IFSCPKGTVF PVPPRPGCKM PVNSDSTQEG ASSSSSGQEK
DLPSSSSSSS SSGNTLVTKV TVDKGDQGFR GEKGEAGMPG LPGLPGRSGS AGPRGESVVG
PPGHPGPRGH PGAPGFGRSG VAGPPGPPGP PGPPGQHGSG VMIPGPPGPP GPPGRAAEAS
SAVRKYVSLQ AMRQQSSAVE DGTLSFVIDT SKLYIKVPGG WREVQLGGLI ETYSSPVLSQ
DDAGPLILTS QIRHTPKIHT RNAAGPLILT SQIRHTPKIH TRNALRLVAL NTPLTGNLGS
IHSVNKLCQT QAQAMGIRDD YKAFLSHHLQ DLIDTVQPMY RTNMPIVNLR GELLFKNWDS
IFSDHLLPLG VPLYSFDGRD VMSDPFWPQK AVWHGSSEKG KRLSALNCES WRAGDMAITG
QASFLYSGLL NQQTRSCSNR FIVLCIETSH DHQTLQELHT AQVRHRRWFH RY
//
