TSP4B_DANRE
ID TSP4B_DANRE Reviewed; 949 AA.
AC Q8JGW0;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Thrombospondin-4-B;
DE Short=Thbs4-B;
DE Flags: Precursor;
GN Name=thbs4b; Synonyms=thbs4, tsp4;
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:AAL82733.1};
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).
CC -!- FUNCTION: Adhesive glycoprotein that mediates cell-to-cell and cell-to-
CC matrix interactions and may be involved in various processes including
CC cellular proliferation, migration, adhesion and attachment. May play a
CC role in ER stress response (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotrimer; disulfide-linked. {ECO:0000250|UniProtKB:P35443}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250}. Sarcoplasmic
CC reticulum {ECO:0000250}. Secreted {ECO:0000250}. Secreted,
CC extracellular space {ECO:0000250}. Secreted, extracellular space,
CC extracellular matrix {ECO:0000250}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY081009; AAL82733.1; -; mRNA.
DR RefSeq; NP_775333.1; NM_173226.1.
DR AlphaFoldDB; Q8JGW0; -.
DR SMR; Q8JGW0; -.
DR STRING; 7955.ENSDARP00000093348; -.
DR PaxDb; Q8JGW0; -.
DR GeneID; 252850; -.
DR KEGG; dre:252850; -.
DR CTD; 252850; -.
DR ZFIN; ZDB-GENE-020708-4; thbs4b.
DR eggNOG; ENOG502QRK8; Eukaryota.
DR InParanoid; Q8JGW0; -.
DR OrthoDB; 120983at2759; -.
DR PhylomeDB; Q8JGW0; -.
DR Reactome; R-DRE-186797; Signaling by PDGF.
DR PRO; PR:Q8JGW0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0016529; C:sarcoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0008201; F:heparin binding; NAS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
DR GO; GO:0035989; P:tendon development; IMP: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; IPR001791; Laminin_G.
DR InterPro; IPR024665; Thbs/COMP_coiled-coil.
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 Pfam; PF11598; COMP; 1.
DR Pfam; PF07645; EGF_CA; 2.
DR Pfam; PF02412; TSP_3; 6.
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 PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 3.
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;
KW Endoplasmic reticulum; Extracellular matrix; Glycoprotein; Growth factor;
KW Mitogen; Reference proteome; Repeat; Sarcoplasmic reticulum; Secreted;
KW Signal; Unfolded protein response.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..949
FT /note="Thrombospondin-4-B"
FT /id="PRO_0000035855"
FT DOMAIN 23..198
FT /note="Laminin G-like"
FT DOMAIN 312..349
FT /note="EGF-like 1; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 365..408
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 409..451
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 452..484
FT /note="TSP type-3 1"
FT REPEAT 485..520
FT /note="TSP type-3 2"
FT REPEAT 521..543
FT /note="TSP type-3 3"
FT REPEAT 544..579
FT /note="TSP type-3 4"
FT REPEAT 580..602
FT /note="TSP type-3 5"
FT REPEAT 603..640
FT /note="TSP type-3 6"
FT REPEAT 641..680
FT /note="TSP type-3 7"
FT REPEAT 681..716
FT /note="TSP type-3 8"
FT DOMAIN 720..934
FT /note="TSP C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00635"
FT REGION 578..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..661
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 601
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 637
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 930
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 261
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:Q9R0G6,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 264
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:Q9R0G6,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 276..287
FT /evidence="ECO:0000250|UniProtKB:P35443,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 281..296
FT /evidence="ECO:0000250|UniProtKB:P35443,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 299..310
FT /evidence="ECO:0000250|UniProtKB:P35443,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 316..327
FT /evidence="ECO:0000250|UniProtKB:P35443,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 321..336
FT /evidence="ECO:0000250|UniProtKB:P35443,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 339..363
FT /evidence="ECO:0000250|UniProtKB:P35443,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 369..383
FT /evidence="ECO:0000250|UniProtKB:P35443,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 377..392
FT /evidence="ECO:0000250|UniProtKB:P35443,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 395..407
FT /evidence="ECO:0000250|UniProtKB:P35443,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 413..427
FT /evidence="ECO:0000250|UniProtKB:P35443,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 421..437
FT /evidence="ECO:0000250|UniProtKB:P35443,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 439..450
FT /evidence="ECO:0000250|UniProtKB:P35443,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 466..471
FT /evidence="ECO:0000250|UniProtKB:P35442,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 476..496
FT /evidence="ECO:0000250|UniProtKB:P35442,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 512..532
FT /evidence="ECO:0000250|UniProtKB:P35442,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 535..555
FT /evidence="ECO:0000250|UniProtKB:P35442,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 571..591
FT /evidence="ECO:0000250|UniProtKB:P35442,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 594..614
FT /evidence="ECO:0000250|UniProtKB:P35442,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 632..652
FT /evidence="ECO:0000250|UniProtKB:P35442,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 672..692
FT /evidence="ECO:0000250|UniProtKB:P35442,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 708..929
FT /evidence="ECO:0000250|UniProtKB:P35442,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 949 AA; 103991 MW; BBC9203814CA99CB CRC64;
MAGTMHLLTA VSLILMLSSA NAESTVYNLL TSPDCLPDLL HGGLAEQGVT ELYILTTFRI
QPGTGNTIFS LYNPRDNSKY FEFSVFGKAN KAILRYLRRD GRMSAVTFNK LNLADGEKHR
LLFHLKGLEV GHPGGFPHSQ GALPVPGVEL HLDCRLVETL RDLPAVFNGL NNHQAVELKT
MQGKAQEGLE ELKLAYGDSV ENVASLQDCH TQSDSVQALG LNTKQLTTQM LELTKVINEL
KDVLIQQVKE TSFLRNTISE CQACGLSGAE VVKPKCAPGV CFRDDMCIET AEGVECGPCP
DGYTGDGYSC DDVDECQFNP CFPGVRCVNM APGFRCEACP LGFTGKPLEG VGVAYAQTHK
QVCDDIDECK GPDNGGCTAN SICVNSVGSY QCGRCKTGFT GDQIRGCKPE KSCGNRLQNP
CDPNAQCTEE RDGTITCQCG IGWAGNGYLC GKDTDIDGYP DERLRCRDPT CRKDNCVTVP
NSGQEDADGD GKGDACDPDA DGDGILNEQD NCWLTPNINQ QNSDKDSHGD ACDNCVRVDN
PDQRDTDSDG LGDACDDDMD GDGLKNFLDN CQRVKNRDQL DRDGDGVGDA CDSCPDIPNP
NQSDIDNDLV GDSCDTNQDS DGDGHQDSKD NCPMVINSSQ LDTDKDGIGD ECDDDDDNDG
IPDSLPPGPD NCRLVPNPEQ IDDNNDGVGD ICESDFDQDK VIDRIDNCPE NAEITLTDFR
AYQTVVLDPE GDAQIDPNWV VLNQGMEIVQ TMNSDPGLAV GYTAFSGVDF EGTFHVNTVT
DDDYAGFIFG YQDSSSFYVV MWKQTEQTYW QATPFRAVAE PGIQLKAVKS KTGPGEHLRN
SLWHTGDTND QVRLLWKDPR NVGWKDKVSY RWYLQHRPQV GYIRVRFYEG TELVADSGVT
IDTTMRGGRL GVFCFSQENI IWSNLKYRCN DTIPEDFQEF STQHGMDPL
