ID A0A9J8A031_CYPCA Unreviewed; 1251 AA.
AC A0A9J8A031;
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:ENSCCRP00000138574.1, ECO:0000313|Proteomes:UP001108240};
RN [1] {ECO:0000313|Ensembl:ENSCCRP00000138574.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSCCRP00000138574.1}
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; A0A9J8A031; -.
DR Ensembl; ENSCCRT00000152312.1; ENSCCRP00000138574.1; ENSCCRG00000021532.2.
DR GeneTree; ENSGT00940000158212; -.
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..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..1251
FT /note="Thrombospondin-like N-terminal domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039928803"
FT DOMAIN 41..229
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 228..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 684..958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..306
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..375
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..393
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..406
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..429
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..471
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..518
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..583
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..599
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..652
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..773
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..797
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 860..874
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 875..895
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..933
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 943..952
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1251 AA; 128994 MW; 678DEA0F222D2102 CRC64;
MGRACDSSLL RVWCWSLITV CLCSSASASQ HFDSERDSRA QLDLTELIGV PLPPSVAFIT
GFEGFPAYSF GPDANVGRLT RSFIPDPFYR DFAIIVTAKP STRRGGVLFA ITDALQKIVH
LGVSLAPVED GSQHVVLYYT EPGAAHTKEA ASFKMGDLTG RWVRFTLAVQ GEEVRLYMDC
EEHHRVAFRR SPDGLTFQPS SGIFIGNAGG TRLERFVGSI QQLLLTADPS APNEQCEEDD
PYASGYGSGG DIFDDTETPS EVKKVFEERE YTMLEDIESG PMRAPPTESP SFITETDDED
LEEGSGEDII IISGPKEPIR SEGASQDRNV ITMQKGEKGE RGPEGPPGPA GPAAPHAPGE
PGPRGPQGPP GPPGEPGQDG QPGDPAKDGA PGEAGPPGFP GLPGDPGPKG DKGDPGVGIP
GPPGPPGPPG TFKYPDGIAG SGSSYVDLDS DTELIRGPPG PPGPPGRPGL PGPSVGAQPG
PVGPPGAPGK DGETGKPGLP GENGRDGQTG KEGEKGQKGE PGLPGIMGPK GDAGQPGLPG
QTGSEGPRGQ PGPPGPPGKG FSFDMMDLEG SGLDGSSGFS PVLPRGPPGL PGLPGPPGPQ
GKEGAVGPPG VSVKGEPGAK GDDGQPGSSG LPGRQGERGE KGDMGQKGER GLDGIGLPGP
PGPPGPVINL HELMLNDTEG FFNLSGIFEP QGPSGPRGPK GDTGAPGVQG PPGLKGQKGE
PGIVSGVHAP QGPKGLKGDG GVPGPPGQTG PIGPAGPKGE FGFPGRPGRP GINGRKGEKG
NSVGLPGPPG PPGPPGRPGI FSCPKGTVFP VPPRPGCKMP VNSDSTQEGA SSSSSGQEKD
LPSSSSSSSS SGNTLVTKVT VDKGDQGFRG EKGEAGMPGL PGLPGRSGSA GPRGESVVGP
PGHPGPRGHP GAPGFGRSGV AGPPGPPGPP GPPGQHGSGV MIPGPPGPPG PPGRAAEASS
AVRKYVSLQA MRQQSSAVED GTLSFVIDTS KLYIKVPGGW REVQLGGLIE TYSSPVLSQD
DAGPLILTSQ IRHTPKIHTR NAAGPLILTS QIRHTPKIHT RNALRLVALN TPLTGNLGSI
HSVNKLCQTQ AQAMGIRDDY KAFLSHHLQD LIDTVQPMYR TNMPIVNLRG ELLFKNWDSI
FSDHLLPLGV PLYSFDGRDV MSDPFWPQKA VWHGSSEKGK RLSALNCESW RAGDMAITGQ
ASFLYSGLLN QQTRSCSNRF IVLCIETSHD HQTLQELHTA QVRHRRWFHR Y
//
