ID A0AA88P2U2_9TELE Unreviewed; 1216 AA.
AC A0AA88P2U2;
DT 27-MAR-2024, integrated into UniProtKB/TrEMBL.
DT 27-MAR-2024, sequence version 1.
DT 28-JAN-2026, entry version 9.
DE RecName: Full=Thrombospondin-like N-terminal domain-containing protein {ECO:0000259|SMART:SM00210};
GN ORFNames=Q8A67_024090 {ECO:0000313|EMBL:KAK2869698.1};
OS Cirrhinus molitorella (mud carp).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Labeoninae; Labeonini; Cirrhinus.
OX NCBI_TaxID=172907 {ECO:0000313|EMBL:KAK2869698.1, ECO:0000313|Proteomes:UP001187343};
RN [1] {ECO:0000313|EMBL:KAK2869698.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Prfri {ECO:0000313|EMBL:KAK2869698.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAK2869698.1};
RA Liu H.;
RT "Chromosome-level Genome Assembly of mud carp (Cirrhinus molitorella).";
RL Submitted (AUG-2023) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAK2869698.1}.
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DR EMBL; JAUYZG010000024; KAK2869698.1; -; Genomic_DNA.
DR AlphaFoldDB; A0AA88P2U2; -.
DR Proteomes; UP001187343; Unassembled WGS sequence.
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; 4.
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:UP001187343};
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..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1216
FT /note="Thrombospondin-like N-terminal domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041646276"
FT DOMAIN 40..228
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 224..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 686..945
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..305
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..355
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..366
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..428
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..472
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..517
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..598
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..645
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..769
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..796
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 829..843
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 911..921
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 930..939
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1216 AA; 124994 MW; 260EBB1BD321AAE9 CRC64;
MGRASDSSPR IWCWTFIAVC ICSSGTALLD TDSERDSSGQ LDLTELIGVP LPPSVAFITG
FEGFPAYSFG PDANVGRLTR SFIPDPFFRD FAIVVTAKPG TRRGGVLFAI TDALQKVVHL
GVALAPVEDG SQRVILYYTE PGATRTQEAA SFKMGDLTGR WARFTLAVQG EEVKLYMDCE
EYHRVAFSRS ADGLTFQPSS GIFIGNAGGT RLERFVGSIQ QLLLTPNPSA PNEQCEEDDP
YASGYGSGDD IYDDTETRDE VKKVVEEREY TMPEDVESGP MKAPPTEPPS FSTETDDEDL
EEGSGEDIVV ISGPEEPIRS EGASQDRNVM TMQKGEKGER GPQGPPGPAG PPAPRTPGES
GARGPQGPSG PPGEPGKDGQ PGDSGKDGAP GEVGPPGFPG LPGNPGLKGD KGDPGVGVPG
PPGPPGPPGR SGTYTYPDGI EGSGSSFVDL DSDTELIRGP PGPPGPPGPP GPSVGAHPGP
IGPPGVPGKD GETGKPGLPG ENGRDGPAGK DGERGQKGEP GVPGIAGPKG DPGQPGLPGE
TGAEGPRGQP GPPGPPGKGF SFDMMDLEGS GLDGGSGFRP VLPRGPPGLP GLPGPPGPQG
KEGAVGPPGV SVKGEPGAKG DDGQPGSAGL PGRQGERGEK GDMGLKGERG LDGIGLPGPP
GPPGPVINLQ ELMLNDTEGI FNLSGIFEPQ GPLGPRGPKG DTGAPGLQGP AGLKGQKGEP
GIVSGVHAPQ GPKGLKGDSG VPGPPGQTGP IGPAGPKGEF GFPGRPGRPG MHGRKGEKGD
SDGLPGPPGP PGPPGRPGIF GCPQGTVFPI PPRPGCKKPV NSDSTQEGAS SSSSASSSAS
SSSDTLGTKV TAAKGDQGFR GEKGEAGMPG LPGRSGLAGP KGESIVGPPG HPGPRGPTGT
PGFGRTGVAG PPGPPGPPGP PGQGSGVMIP GPPGPPGPPG RAAEASSAVR RYVSLQAMRQ
SSVDEAGTLC FVIDTSKLYI KVPGGWREVQ LGGLVEMYSS PLLSQDDAEP LMLTPQFTHT
ATIHSANTLR LVALNSPLTG NLGSIHSVNK LCRTQAQAMG IRDDYKAFLS HHLQDLIDIM
QPMYRSNMPI VNLRGEVLFK NWDSIFSNHL LPVGVPLYSF DGRDVMSDPF WPQKAVWHGS
SERGKRLSAL NCESWRAGDM AITGQASFLY SGLLNQQTRS CSNHFIVLCI ETSHQHTSVQ
ELHKAQYRHR RWHHRY
//
