TSP3B_DANRE
ID TSP3B_DANRE Reviewed; 929 AA.
AC Q1L8P7;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Thrombospondin-3b;
DE Short=Thbs3b;
DE Flags: Precursor;
GN Name=thbs3b {ECO:0000312|ZFIN:ZDB-GENE-060503-84}; ORFNames=si:dkey-81h8.2;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
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|UniProtKB:Q05895}.
CC -!- SUBUNIT: Oligomer; disulfide-linked. {ECO:0000250|UniProtKB:Q05895}.
CC -!- SIMILARITY: Belongs to the thrombospondin family. {ECO:0000255}.
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DR EMBL; CR749746; CAK11219.1; -; Genomic_DNA.
DR RefSeq; NP_001038679.1; NM_001045214.1.
DR AlphaFoldDB; Q1L8P7; -.
DR SMR; Q1L8P7; -.
DR STRING; 7955.ENSDARP00000085258; -.
DR PaxDb; Q1L8P7; -.
DR PRIDE; Q1L8P7; -.
DR Ensembl; ENSDART00000090825; ENSDARP00000085258; ENSDARG00000012060.
DR GeneID; 571317; -.
DR KEGG; dre:571317; -.
DR CTD; 571317; -.
DR ZFIN; ZDB-GENE-060503-84; thbs3b.
DR eggNOG; ENOG502QRK8; Eukaryota.
DR GeneTree; ENSGT00940000159283; -.
DR InParanoid; Q1L8P7; -.
DR PhylomeDB; Q1L8P7; -.
DR TreeFam; TF324917; -.
DR PRO; PR:Q1L8P7; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 19.
DR Bgee; ENSDARG00000012060; Expressed in pharyngeal gill and 8 other tissues.
DR ExpressionAtlas; Q1L8P7; baseline.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008201; F:heparin binding; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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; 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; 1.
DR Pfam; PF02412; TSP_3; 6.
DR Pfam; PF05735; TSP_C; 1.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF103647; SSF103647; 3.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS51234; TSP3; 8.
DR PROSITE; PS51236; TSP_CTER; 1.
PE 3: Inferred from homology;
KW Calcium; Cell adhesion; Disulfide bond; EGF-like domain; Glycoprotein;
KW Reference proteome; Repeat; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..929
FT /note="Thrombospondin-3b"
FT /evidence="ECO:0000255"
FT /id="PRO_0000247618"
FT DOMAIN 24..192
FT /note="Laminin G-like"
FT DOMAIN 345..384
FT /note="EGF-like 1; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 388..430
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 431..465
FT /note="TSP type-3 1"
FT REPEAT 466..501
FT /note="TSP type-3 2"
FT REPEAT 502..524
FT /note="TSP type-3 3"
FT REPEAT 525..560
FT /note="TSP type-3 4"
FT REPEAT 561..583
FT /note="TSP type-3 5"
FT REPEAT 584..621
FT /note="TSP type-3 6"
FT REPEAT 622..661
FT /note="TSP type-3 7"
FT REPEAT 662..697
FT /note="TSP type-3 8"
FT DOMAIN 701..915
FT /note="TSP C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00635"
FT REGION 602..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..626
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..642
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 381
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 618
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 911
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 265
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:Q9R0G6,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 268
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:Q9R0G6,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 277..288
FT /evidence="ECO:0000250|UniProtKB:P49746,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 282..299
FT /evidence="ECO:0000250|UniProtKB:P49746,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 319..343
FT /evidence="ECO:0000250|UniProtKB:P49746,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 349..362
FT /evidence="ECO:0000250|UniProtKB:P49746,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 356..371
FT /evidence="ECO:0000250|UniProtKB:P49746,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 374..386
FT /evidence="ECO:0000250|UniProtKB:P49746,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 392..406
FT /evidence="ECO:0000250|UniProtKB:P49746,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 400..416
FT /evidence="ECO:0000250|UniProtKB:P49746,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 418..429
FT /evidence="ECO:0000250|UniProtKB:P49746,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 445..452
FT /evidence="ECO:0000250|UniProtKB:P35442,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 457..477
FT /evidence="ECO:0000250|UniProtKB:P35442,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 493..513
FT /evidence="ECO:0000250|UniProtKB:P35442,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 516..536
FT /evidence="ECO:0000250|UniProtKB:P35442,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 552..572
FT /evidence="ECO:0000250|UniProtKB:P35442,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 575..595
FT /evidence="ECO:0000250|UniProtKB:P35442,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 613..633
FT /evidence="ECO:0000250|UniProtKB:P35442,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 653..673
FT /evidence="ECO:0000250|UniProtKB:P35442,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 689..910
FT /evidence="ECO:0000250|UniProtKB:P35442,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 929 AA; 101154 MW; 4D8364BFA6EA2731 CRC64;
MELRKIVPNL LVLYVAVHFS QSSEIKVINV LELHDVRQTA AAIENLSGAL QTVGDLYITS
TFMLPPKLGG VLFGLYDKQD NKKYLEIAVV GKINKLLVRY LRSDGKAHTV NLQNPALAEG
RTQSLILRIG GLRRSHINLE LYVNCRLVDS AQGLPSFVGL PSEAESVDVR TGQKSYARIQ
GLVESVKLAL GGSLATAGLL IDCPFQGDSA INNAVVSDIN AILGDHTKAL IGQLIIFNQI
MGELREDIRE QTKEMSLIRN TILECQVCGF HEPQSRCLPN PCYTGVSCME SMMYPGYQCG
PCPEELCVNT AKGFSCQSCP IGFTGPTLKG VGLEFAKRHK QHCVDIDECA ELSGSCVPNS
VCINTVGSFK CGQCKAGFVG NQTVGCFARR TCETLGYSPC DVNSHCVMGR NSDVSCVCNV
GWAGNGNICG PDSDIDGYPD EPLPCMDNDK HCRADNCANT PNSGQEDTDG DGIGDQCDED
ADGDGIKNVE DNCRLVPNKD QQNSDTDSYG DACDNCPNVP NGDQLDTDGN GKGDICDTDI
DGDGIPNVLD NCPKIPNPMQ TDRDGDGVGD ACDSCPEVND PLQSDMDNDL VGDVCDTNKD
IDGDGYQDTR DNCPEVPNSS QLDSDNDGIG DECDDDDDND GIPDILPPGP DNCRLVPNPS
QIDTDANGVG DVCETDFDND KVTDLLDACP ESAEVTMTDF RAFQTVILDP EGDAQIDPNW
VVLNQGMEIV QTMNSDPGLA VGYTAFNGVD FEGTIHVNTA TDDDYVGFIF GYQDSSSFYV
VMWKQTEQTY WQNLPFKALA QPGIQLKAVK SRTGPGEYLR NALWHTGDTT GEVTLLWKDP
RNVGWKDRAS YRWHLSHRPQ VGYIRLRLYE GTALVADSGV VIDSTMRGGR LGVFCFSQEN
VIWSNLGYRC NDSIPDDFML YHKQMKLRT
