TSP4_BOVIN
ID TSP4_BOVIN Reviewed; 961 AA.
AC Q3SWW8;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Thrombospondin-4;
DE Flags: Precursor;
GN Name=THBS4;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Adhesive glycoprotein that mediates cell-to-cell and cell-to-
CC matrix interactions and is involved in various processes including
CC cellular proliferation, migration, adhesion and attachment,
CC inflammatory response to CNS injury, regulation of vascular
CC inflammation and adaptive responses of the heart to pressure overload
CC and in myocardial function and remodeling. Binds to structural
CC extracellular matrix (ECM) proteins and modulates the ECM in response
CC to tissue damage, contributing to cardioprotective and adaptive ECM
CC remodeling. Plays a role in ER stress response, via its interaction
CC with the activating transcription factor 6 alpha (ATF6) which produces
CC adaptive ER stress response factors and protects myocardium from
CC pressure overload. May contribute to spinal presynaptic
CC hypersensitivity and neuropathic pain states after peripheral nerve
CC injury. May play a role in regulating protective astrogenesis from the
CC subventricular zone (SVZ) niche after injury in a NOTCH1-dependent
CC manner (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homopentamer; disulfide-linked. Interacts with PTBP3 (By
CC similarity). Interacts (via EGF-like 3; calcium-binding domain) with
CC ATF6 and facilitates its processing, activation and nuclear
CC translocation. Interacts with NOTCH1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q9Z1T2}. Sarcoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q9Z1T2}. Secreted
CC {ECO:0000250|UniProtKB:Q9Z1T2}. Secreted, extracellular space
CC {ECO:0000250|UniProtKB:Q9Z1T2}. Secreted, extracellular space,
CC extracellular matrix {ECO:0000250|UniProtKB:Q9Z1T2}.
CC -!- SIMILARITY: Belongs to the thrombospondin family. {ECO:0000305}.
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DR EMBL; BC104630; AAI04631.1; -; mRNA.
DR RefSeq; NP_001029900.1; NM_001034728.1.
DR AlphaFoldDB; Q3SWW8; -.
DR SMR; Q3SWW8; -.
DR STRING; 9913.ENSBTAP00000036460; -.
DR PaxDb; Q3SWW8; -.
DR PeptideAtlas; Q3SWW8; -.
DR PRIDE; Q3SWW8; -.
DR GeneID; 541281; -.
DR KEGG; bta:541281; -.
DR CTD; 7060; -.
DR eggNOG; ENOG502QRK8; Eukaryota.
DR HOGENOM; CLU_009257_1_1_1; -.
DR InParanoid; Q3SWW8; -.
DR OrthoDB; 120983at2759; -.
DR TreeFam; TF324917; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS: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:0048266; P:behavioral response to pain; ISS: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:0034103; P:regulation of tissue remodeling; ISS:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS:UniProtKB.
DR GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
DR GO; GO:0048771; P:tissue remodeling; 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; 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; 5.
DR Pfam; PF05735; TSP_C; 1.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00179; EGF_CA; 3.
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; 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;
KW Endoplasmic reticulum; Extracellular matrix; Glycoprotein; Growth factor;
KW Mitogen; Reference proteome; Repeat; Sarcoplasmic reticulum; Secreted;
KW Signal; Tissue remodeling; Unfolded protein response.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..961
FT /note="Thrombospondin-4"
FT /id="PRO_0000283032"
FT DOMAIN 24..192
FT /note="Laminin G-like"
FT DOMAIN 286..325
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 326..363
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 379..419
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 420..462
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 463..495
FT /note="TSP type-3 1"
FT REPEAT 496..531
FT /note="TSP type-3 2"
FT REPEAT 532..554
FT /note="TSP type-3 3"
FT REPEAT 555..590
FT /note="TSP type-3 4"
FT REPEAT 591..613
FT /note="TSP type-3 5"
FT REPEAT 614..651
FT /note="TSP type-3 6"
FT REPEAT 652..691
FT /note="TSP type-3 7"
FT REPEAT 692..727
FT /note="TSP type-3 8"
FT DOMAIN 731..945
FT /note="TSP C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00635"
FT REGION 581..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 562..564
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 586..600
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..628
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 612
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 941
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 258
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 261
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 290..301
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 295..310
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 313..324
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 330..341
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 335..350
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 353..377
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 383..394
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 388..403
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 406..418
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 424..438
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 432..448
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 450..461
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 477..482
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 487..507
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 523..543
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 546..566
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 582..602
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 605..625
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 643..663
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 683..703
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 719..940
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 961 AA; 105974 MW; 5D51CA6752629A09 CRC64;
MLAPRGATFL LLHLALQPWL GAGAQATPQV FDLLPSASQR LNPSVLQPIL TDPTLNELYV
ISTFKLQSKS SATIFGLYSS ADHSKYFEFT VMGRLNKAIL RYLKNDGRIH LVVFNNLQLA
DGRRHRLLLR LTNLHRGAGS VELFLDCTRV DSIHNLPRAF SGLAQSPEAV ELRTFQRKAH
DSLEELKLVV RGSLIQVASL QDCFLQQSEP LATTNTGDFN RQFLGQMSQL NQLLGEVKDL
LRQQVKETSF LRNTIAECQA CGPLSFQSPT PNTLMPVVPA ASPTPPVRRC DSNPCFRGVR
CTDTRDGFQC GPCPEGYTGN GIVCSDVDEC RYHPCYPGVR CVNLAPGFRC DACPVGFTGP
MMQGVGISFA KTNKQVCTDI DECRNGACVL NSICINTLGS YRCGPCKPGY IGDQMRGCKM
ERNCRDPELN PCSVNAQCIE ERQGDVTCVC GVGWAGDGYI CGKDVDIDSY PDEELPCSAR
NCKKDNCKYV PNSGQEDADR DGIGDACDDD ADGDGILNEQ DNCVLTHNVD QRNSDKDIFG
DACDNCRNVL NNDQKDTDGD GKGDACDDDM DGDGIKNILD NCQKVPNSDQ EDRDGDGVGD
ACDSCPEVSN PNQSDVDNDL VGDSCDTNQD SDGDGHQDST DNCPTVINSA QLDTDKDGIG
DECDDDDDND GIPDLVPPGP DNCRLVPNPA QEDSNSDGVG DICEADFDQD QVIDRIDVCP
ENAEVTLTDF RAYQTVVLDP EGDAQIDPNW VVLNQGMEIV QTMNSDPGLA VGYTAFNGVD
FEGTFHVNTQ TDDDYAGFIF GYQDSSSFYV VMWKQTEQTY WQATPFRAVA EPGIQLKAVK
SKTGPGEHLR NSLWHTGDTS DQVRLLWKDS RNVGWKDKVS YRWFLQHRPQ VGYIRVRFYE
GSELVADSGV TIDTTMRGGR LGVFCFSQEN IIWSNLKYRC NDTIPEDFQE FQTQNFDRLD
K
