ID A0A8C1A1Q7_CYPCA Unreviewed; 1389 AA.
AC A0A8C1A1Q7;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2023, sequence version 2.
DT 28-JAN-2026, entry version 20.
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:ENSCCRP00000003350.2, ECO:0000313|Proteomes:UP001108240};
RN [1] {ECO:0000313|Ensembl:ENSCCRP00000003350.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSCCRP00000003350.2}
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; ENSCCRT00000003700.2; ENSCCRP00000003350.2; ENSCCRG00000054464.1.
DR GeneTree; ENSGT00940000165423; -.
DR Proteomes; UP001108240; Unplaced.
DR GO; GO:0005587; C:collagen type IV trimer; 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: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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1389
FT /note="Thrombospondin-like N-terminal domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039897551"
FT DOMAIN 32..221
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 222..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 953..1058
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1127..1209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..252
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..358
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..418
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..449
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..509
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..551
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..563
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..589
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..632
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..648
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..689
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..736
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..751
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..778
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..898
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..923
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 953..963
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 996..1005
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1029
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1042..1053
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1131..1143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1160..1173
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1389 AA; 142648 MW; 19D6316CA3BEE7D1 CRC64;
MARRCLAFLE RFLCCVFIAL SPAAPQRREE SGVSLLQLVG DPPPDGVSKV FDDANNPSYV
FDQSSNVGQS AAAHLPNPFF RDFSLIFNIK PTSSKPGVIF SITDPTQNIM YVGVKLSAVE
KGKQYIIFYY TEPDSQSSYE AARFSVPSMV NTWTRFSISV LNERVSLYFN CDSDPQVIRF
ERSPDDMDLD AGAGVFVGHA SGADPDKFLG VIGDMRVLKD PGAAERHCEE DEDDFDANLQ
GSGDYGASGD GEGQPSVQPT PPSSRPIQQP PVTSRPLDEK QQTGSVDSSW QTSGSYGDSR
QTSGSYGSSR KTSGSYGDSR KTSVSYGDSR QTSGSYVDSE QTSGAKGDRG EKGAKGDRGL
VGLKGDAGSG SVSSGGEILV KGDAGEKGMK GNPGFGYPGS KGDRGPPGPP GPPGPPGPSA
AVEERGDGSV VQRVAGPRGP PGPPGPPGPA GADGEPGDPG EDGKAGQVGP PGFPGTPGSS
GLKGEKGERG EIQPGPRGPP GPPGPPGPPS RSDRPTFVDM EGSGFDLDSV RAMPGLPGLP
GPPGPPGPPG PSGTGSSGSG GIGPPGPPGQ NGAPGQPGLP GPSGADGKPG SPGPKGEKGD
AGELGLPGPV GEKGAIGSPG SPGLPGEGGL AGLPGPMGPV GPPGPPGPSY HVGFDDMEGS
GVHFSSVPGV RGPMGVQGPP GDPGPQGKSG LPGFPGEKGS EGPQGKDGQP GLDGFPGPQG
PRGDKGDRGD RGEPGRDGNG LPGPPGPPGP PGQITYRYSE IYDETGGPGP QGGAGLPGQA
GFPGPSGPKG DRGEPGSPGY GIKGEKGEPG LILGPDGNPL YPGGLTGQKG ERGLPGPVGP
SGPAGPSGLK GEFGMPGRPG RPGVNGYKGE KGESGSGSGY GYPGPPGPPG PPGPPGPAVP
LDRFGRYEDH SRHYPAMKGD KGDQGAPGVP GSPGFSSNFD IYALKNEMKG ERGELGLKGE
KGEPGGGFYD PRFGAVQGPP GNPGLPGPKG DSIRGPPGPQ GPPGTPGVGY DGRPGNPGPP
GPPGPPGSPS LPGAYRPQLS IPGPPGPPGP PGIPGTESGV AFLRSYDIMM ATARRQTEGA
LIYILDRSDL YLRVRDGVRQ VMLGDYKPFY GEVDNEVAAV QPPPVVHYSQ DHTANNGAEQ
ISPQHPPIEF PRREPENRNP NPPDSRYPDP RYPPYTDSRY TDPVQPERNP IVPARRPSPP
VNQPEGHVHT SGPGLHLIAL NSPQVGNMRG IRGADFLCFQ QARAVGLKGT FRAFLSSKLQ
DLYSIVRKSD RETLPIVNLK DQVLFRSWES LFSDSESRMK DNAPIYSFDG RDVLRDSAWP
EKMIWHGSSG RGHRQTDNYC ETWRAGDRAV TGLASSLQAG QLLQQTSSSC SSSYIVLCIE
NSYMTQSKK
//
