TSP3A_DANRE
ID TSP3A_DANRE Reviewed; 962 AA.
AC Q8JHW2; Q5U3J1;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Thrombospondin-3a;
DE Short=Thbs3a;
DE Flags: Precursor;
GN Name=thbs3a; Synonyms=thbs3, tsp3; ORFNames=zgc:103461;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000312|EMBL:AAM88772.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX PubMed=12592708; DOI=10.1080/1042517021000019278;
RA Adolph K.W.;
RT "The zebrafish thrombospondin 3 and 4 genes (thbs3 and thbs4): cDNA and
RT protein structure.";
RL DNA Seq. 13:277-285(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Adhesive glycoprotein that mediates cell-to-cell and cell-to-
CC matrix interactions. Can bind to fibrinogen, fibronectin, laminin and
CC type V collagen (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Oligomer; disulfide-linked. {ECO:0000250|UniProtKB:P49746}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically. Present
CC at the gastrulation and post-segmentation stages.
CC {ECO:0000269|PubMed:12592708}.
CC -!- SIMILARITY: Belongs to the thrombospondin family. {ECO:0000305}.
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DR EMBL; AF462310; AAM88772.1; -; mRNA.
DR EMBL; BC085524; AAH85524.1; -; mRNA.
DR RefSeq; NP_775332.1; NM_173225.1.
DR AlphaFoldDB; Q8JHW2; -.
DR SMR; Q8JHW2; -.
DR STRING; 7955.ENSDARP00000057304; -.
DR PaxDb; Q8JHW2; -.
DR GeneID; 252849; -.
DR KEGG; dre:252849; -.
DR CTD; 252849; -.
DR ZFIN; ZDB-GENE-020708-3; thbs3a.
DR eggNOG; ENOG502QRK8; Eukaryota.
DR InParanoid; Q8JHW2; -.
DR OrthoDB; 120983at2759; -.
DR PhylomeDB; Q8JHW2; -.
DR Reactome; R-DRE-186797; Signaling by PDGF.
DR PRO; PR:Q8JHW2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008201; F:heparin binding; NAS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0060231; P:mesenchymal to epithelial transition; IGI:ZFIN.
DR GO; GO:0061053; P:somite development; IGI:ZFIN.
DR Gene3D; 4.10.1080.10; -; 2.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR024665; Thbs/COMP_coiled-coil.
DR InterPro; IPR028507; Thrombospondin-3.
DR InterPro; IPR003367; Thrombospondin_3-like_rpt.
DR InterPro; IPR017897; Thrombospondin_3_rpt.
DR InterPro; IPR008859; Thrombospondin_C.
DR InterPro; IPR028974; TSP_type-3_rpt.
DR PANTHER; PTHR10199:SF114; PTHR10199:SF114; 1.
DR Pfam; PF11598; COMP; 1.
DR Pfam; PF07645; EGF_CA; 2.
DR Pfam; PF02412; TSP_3; 7.
DR Pfam; PF05735; TSP_C; 1.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF103647; SSF103647; 3.
DR SUPFAM; SSF49899; SSF49899; 2.
DR SUPFAM; SSF57184; SSF57184; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 4.
DR PROSITE; PS01187; EGF_CA; 2.
DR PROSITE; PS51234; TSP3; 8.
DR PROSITE; PS51236; TSP_CTER; 1.
PE 2: Evidence at transcript level;
KW Calcium; Cell adhesion; Disulfide bond; EGF-like domain; Glycoprotein;
KW Reference proteome; Repeat; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..962
FT /note="Thrombospondin-3a"
FT /id="PRO_0000035851"
FT DOMAIN 24..196
FT /note="Laminin G-like"
FT DOMAIN 277..318
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076,
FT ECO:0000305"
FT DOMAIN 319..358
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 373..412
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 416..458
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076,
FT ECO:0000305"
FT REPEAT 459..493
FT /note="TSP type-3 1"
FT REPEAT 494..529
FT /note="TSP type-3 2"
FT REPEAT 530..552
FT /note="TSP type-3 3"
FT REPEAT 553..588
FT /note="TSP type-3 4"
FT REPEAT 589..611
FT /note="TSP type-3 5"
FT REPEAT 612..649
FT /note="TSP type-3 6"
FT REPEAT 650..692
FT /note="TSP type-3 7"
FT REPEAT 693..728
FT /note="TSP type-3 8"
FT DOMAIN 732..946
FT /note="TSP C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00635"
FT REGION 548..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..654
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..669
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..699
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 313
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 646
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 710
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 942
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 269
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:Q9R0G6,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 272
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:Q9R0G6,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 281..292
FT /evidence="ECO:0000250|UniProtKB:P49746,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 286..303
FT /evidence="ECO:0000250|UniProtKB:P49746,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 306..317
FT /evidence="ECO:0000250|UniProtKB:P49746,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 323..335
FT /evidence="ECO:0000250|UniProtKB:P49746,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 329..344
FT /evidence="ECO:0000250|UniProtKB:P49746,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 347..371
FT /evidence="ECO:0000250|UniProtKB:P49746,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 377..390
FT /evidence="ECO:0000250|UniProtKB:P49746,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 384..399
FT /evidence="ECO:0000250|UniProtKB:P49746,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 402..414
FT /evidence="ECO:0000250|UniProtKB:P49746,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 420..434
FT /evidence="ECO:0000250|UniProtKB:P49746,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 428..444
FT /evidence="ECO:0000250|UniProtKB:P49746,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 446..457
FT /evidence="ECO:0000250|UniProtKB:P49746,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 473..480
FT /evidence="ECO:0000250|UniProtKB:P35442,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 485..505
FT /evidence="ECO:0000250|UniProtKB:P35442,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 521..541
FT /evidence="ECO:0000250|UniProtKB:P35442,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 544..564
FT /evidence="ECO:0000250|UniProtKB:P35442,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 580..600
FT /evidence="ECO:0000250|UniProtKB:P35442,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 603..623
FT /evidence="ECO:0000250|UniProtKB:P35442,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 641..661
FT /evidence="ECO:0000250|UniProtKB:P35442,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 684..704
FT /evidence="ECO:0000250|UniProtKB:P35442,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 720..941
FT /evidence="ECO:0000250|UniProtKB:P35442,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT CONFLICT 2
FT /note="E -> K (in Ref. 1; AAM88772)"
FT /evidence="ECO:0000305"
FT CONFLICT 17
FT /note="S -> F (in Ref. 1; AAM88772)"
FT /evidence="ECO:0000305"
FT CONFLICT 393
FT /note="I -> T (in Ref. 1; AAM88772)"
FT /evidence="ECO:0000305"
FT CONFLICT 430
FT /note="A -> T (in Ref. 1; AAM88772)"
FT /evidence="ECO:0000305"
FT CONFLICT 796
FT /note="C -> Y (in Ref. 1; AAM88772)"
FT /evidence="ECO:0000305"
FT CONFLICT 799
FT /note="S -> F (in Ref. 1; AAM88772)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 962 AA; 105591 MW; 15D18A2A4E67373E CRC64;
MEQMFVHIWV SLVVLMSVWS AQSDKKQDVP VIDVLGLEDV KQTVAAVEKL SLALKTLSDV
YVMSTFRLPP KLGGVLLGLY NKQDNKKYLE VAIMSKINKV LVRYVREDGK LHTVNMQSPN
VADGRPQSLI LRVGGLRREY LSLELYVNCR LADSAQRLPP LVDLPRDAEL VEIRNGHKAY
ARMQGSMDTL KLALGGTVAQ AGALTDCPFQ GDASSYNIVN GEVNSILGDH TKALIGQLII
FNQILGELRE DIREQVKEMS LVRNAILECQ MCGFHEPRSR CQPNPCFKGV SCMETFEYPG
YRCGPCPDGM TGNGTHCQDI DECSEAQPCY TPGACVNTAR GFTCESCPPG MWGPPLSGVG
VEYAKSHRQE CSDIDECVDL ANACTPNSVC INIIGSFRCG QCKTGYVGNQ TAGCFPRKSC
SSLSFNPCDA NAHCVMQRNG DVSCACNVGW AGNGHTCGKD TDIDGYPDRS LPCMDNHKHC
RQDNCVYTPN SGQEDADNDG IGDQCDEDAD GDGIKNVEDN CRLVSNKDQQ NSDTDSFGDA
CDNCPTVPNI DQKDTDSNGE GDACDDDIDG DGIQNVLDNC PKVPNPMQTD RDRDGVGDAC
DSCPEISNPM QTDVDNDLVG DVCDTNQDTD GDGHQDTRDN CPDIPNSSQL DSDNDGIGDD
CDEDDDNDGI PDNHAINGIG PDNCRLISNP NQKDSDSNGV GDVCENDFDN DSVMDLVDVC
PESAEVTLTD FRAYQTVILD PEGDAQIDPN WVVLNQGMEI VQTMNSDPGL AVGYTAFNGV
DFEGTFHVNT VTDDDCAGSI FGYQDSSSFY VVMWKQTEQT YWQSIPFRAM AEPGLQLKAV
KSRTGPGEFL RNALWHAGDT DGEVKLLWKD PRNVGWLDKT SYRWQLSHRP QVGYIRVKLY
EGSEMVADSD VVIDTSMRGG RLGVFCFSQE NIIWSNLRYR CNDTVPEDFS SHRKQVLMHI
KV
