ID A0A8C1JQJ0_CYPCA Unreviewed; 1234 AA.
AC A0A8C1JQJ0;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 15.
DE RecName: Full=Thrombospondin-like N-terminal domain-containing protein {ECO:0000259|SMART:SM00210};
GN Name=LOC109106652 {ECO:0000313|Ensembl:ENSCCRP00010036037.1};
OS Cyprinus carpio (Common carp).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Cyprinus.
OX NCBI_TaxID=7962 {ECO:0000313|Ensembl:ENSCCRP00010036037.1, ECO:0000313|Proteomes:UP000694427};
RN [1] {ECO:0000313|Ensembl:ENSCCRP00010036037.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAY-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
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DR AlphaFoldDB; A0A8C1JQJ0; -.
DR Ensembl; ENSCCRT00010039582.1; ENSCCRP00010036037.1; ENSCCRG00010015391.1.
DR Ensembl; ENSCCRT00010039594.1; ENSCCRP00010036048.1; ENSCCRG00010015391.1.
DR Proteomes; UP000694427; 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; 3.
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:UP000694427};
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..1234
FT /note="Thrombospondin-like N-terminal domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5044675503"
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..964
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 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 843..858
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 867..881
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 927..937
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 947..956
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1234 AA; 126929 MW; 3FDE8107739FF14B CRC64;
MGRACDSSLL RVWCWSLITV CLCSSVSASQ HFDSERDSRA QLDLTELIGV PLPPSVAFIT
GFEGFPAYSF GPDANVGRLT RSFIPDPFYG DFAIIVTAKP STRRGGVLFA ITDALQKIVH
LGVSLAPVED GSQHVVLYYT EPGAAHTKEA ASFKMGDLTG RWARFTLAVQ GEEVRLYMDC
EEHHRVAFRR SPDGLTFQPS SGIFIGNAGG TRLERFVGSI QQLLLTADPS APNEQCEEDD
PYASGYGSGG DIFDDTETPS EVKKVFEERE YTMLEDIESG PMRAPPTESP SFITETDDED
LEEGSGEDII IISGPKEPIR SEGALQDRNV ITMQKGEKGE RGPEGPPGPA GPAAPHTPGE
PGPRGPQGPP GPPGEPGQDG QPGDPAKDGA PGEAGPPGFP GLPGDPGPKG DKGDPGVGIP
GPPGPPGPPG TFKYPDGIAG SGSSYVDLDS DTELTRGPPG 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
DSVGLPGPPG PPGPPGRPGI FSCPKGTVFP VPPRPGCKMP VNSDSTHEGA SSSSSGQEKD
LPSSSSSSSS SSSSSSSSGN TLVTKVTADK GDQGFRGEKG EAGMPGLPGR SGSAGPKGES
VVGPPGHPGP RGHPGAPGFG RSGVAGPPGP PGPPGPPGQH GSGVMIPGPP GPPGPPGRAA
EASSAVRKYV SLQAMRQQSS AVEDGTLSFV IDTSKLYIKV PGGWREVQLG GLIETYSSPV
LSQDDAGPLI LTSQIRHTPK IHTRNALRLV ALNTPLTGNL GSIHSANKLC QTQAQAMGIR
DDYKAFLSHH LQDLIDTVQP MYRTNMPIVN LRGELLFKNW DSIFSDHLLP LGVPLYSFDG
RDVMSDPFWP QKAVWHGSSE RGKRLSALNC ESWRAGDMAI TGQASFLYSG LLNQQTRSCS
NRFIVLCIET SHDHQTLQEL HTAQVRHRRW FHRY
//
