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P49744 (TSP4_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thrombospondin-4
Gene names
Name:Thbs4
Synonyms:Tsp-4, Tsp4
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length980 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Adhesive glycoprotein that mediates cell-to-cell and cell-to-matrix interactions and is involved in various processes including cellular proliferation, migration, adhesion and attachment, inflammatory response to CNS injury, regulation of vascular inflammation and adaptive responses of the heart to pressure overload and in myocardial function and remodeling. Binds to structural extracellular matrix (ECM) proteins and modulates the ECM in response to tissue damage, contributing to cardioprotective and adaptive ECM remodeling. Plays a role in ER stress response, via its interaction with the activating transcription factor 6 alpha (ATF6) which produces adaptive ER stress response factors and protects myocardium from pressure overload. May contribute to spinal presynaptic hypersensitivity and neuropathic pain states after peripheral nerve injury. May play a role in regulating protective astrogenesis from the subventricular zone (SVZ) niche after injury in a NOTCH1-dependent manner. Ref.2 Ref.3

Subunit structure

Homopentamer; disulfide-linked. Interacts with PTBP3 By similarity. Interacts (via EGF-like 3; calcium-binding domain) with ATF6 and facilitates its processing, activation and nuclear translocation. Interacts with NOTCH1 By similarity.

Subcellular location

Endoplasmic reticulum By similarity. Sarcoplasmic reticulum By similarity. Secreted By similarity. Secretedextracellular space By similarity. Secretedextracellular spaceextracellular matrix By similarity.

Tissue specificity

Mainly expressed in astrocytes, and in ressponse to peripheral nerve injury, significantly up-regulated in the dorsal spinal cord (at protein level). Ref.2 Ref.3

Sequence similarities

Belongs to the thrombospondin family.

Contains 4 EGF-like domains.

Contains 1 laminin G-like domain.

Contains 1 TSP C-terminal (TSPC) domain.

Contains 8 TSP type-3 repeats.

Ontologies

Keywords
   Biological processCell adhesion
Tissue remodeling
Unfolded protein response
   Cellular componentEndoplasmic reticulum
Extracellular matrix
Sarcoplasmic reticulum
Secreted
   DomainEGF-like domain
Repeat
Signal
   LigandCalcium
   Molecular functionGrowth factor
Mitogen
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbehavioral response to pain

Inferred from mutant phenotype Ref.2. Source: UniProtKB

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

nervous system development

Inferred from direct assay Ref.1. Source: RGD

neuron projection morphogenesis

Inferred from direct assay Ref.1. Source: RGD

positive regulation of cell division

Inferred from electronic annotation. Source: UniProtKB-KW

protein homooligomerization

Inferred from direct assay PubMed 10956668. Source: RGD

regulation of tissue remodeling

Inferred from sequence or structural similarity. Source: UniProtKB

response to endoplasmic reticulum stress

Inferred from sequence or structural similarity. Source: UniProtKB

response to unfolded protein

Inferred from electronic annotation. Source: UniProtKB-KW

tissue remodeling

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentendoplasmic reticulum

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular matrix

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular space

Inferred from sequence or structural similarity. Source: UniProtKB

neuromuscular junction

Inferred from direct assay Ref.1. Source: RGD

proteinaceous extracellular matrix

Inferred from direct assay Ref.1. Source: RGD

sarcoplasmic reticulum

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

collagen binding

Inferred from direct assay PubMed 10956668. Source: RGD

fibronectin binding

Inferred from direct assay PubMed 10956668. Source: RGD

laminin-1 binding

Inferred from direct assay PubMed 10956668. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4242 Potential
Chain43 – 980938Thrombospondin-4
PRO_0000035854

Regions

Domain43 – 210168Laminin G-like
Domain304 – 34340EGF-like 1
Domain344 – 38138EGF-like 2; calcium-binding Potential
Domain397 – 43438EGF-like 3; calcium-binding Potential
Domain438 – 48144EGF-like 4
Repeat482 – 51433TSP type-3 1
Repeat515 – 55036TSP type-3 2
Repeat551 – 57323TSP type-3 3
Repeat574 – 60936TSP type-3 4
Repeat610 – 63223TSP type-3 5
Repeat633 – 67038TSP type-3 6
Repeat671 – 71040TSP type-3 7
Repeat711 – 74636TSP type-3 8
Domain750 – 964215TSP C-terminal

Amino acid modifications

Glycosylation6311N-linked (GlcNAc...) Potential
Glycosylation9601N-linked (GlcNAc...) Potential
Disulfide bond276Interchain Probable
Disulfide bond279Interchain Probable
Disulfide bond308 ↔ 319 By similarity
Disulfide bond313 ↔ 328 By similarity
Disulfide bond331 ↔ 342 By similarity
Disulfide bond348 ↔ 359 By similarity
Disulfide bond353 ↔ 368 By similarity
Disulfide bond371 ↔ 395 By similarity
Disulfide bond401 ↔ 412 By similarity
Disulfide bond406 ↔ 421 By similarity
Disulfide bond424 ↔ 436 By similarity
Disulfide bond442 ↔ 456 By similarity
Disulfide bond450 ↔ 466 By similarity
Disulfide bond468 ↔ 480 By similarity
Disulfide bond496 ↔ 501 By similarity
Disulfide bond506 ↔ 526 By similarity
Disulfide bond542 ↔ 562 By similarity
Disulfide bond565 ↔ 585 By similarity
Disulfide bond601 ↔ 621 By similarity
Disulfide bond624 ↔ 644 By similarity
Disulfide bond662 ↔ 682 By similarity
Disulfide bond702 ↔ 722 By similarity
Disulfide bond738 ↔ 959 By similarity

Sequences

Sequence LengthMass (Da)Tools
P49744 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 056D41EB6E206FCF

FASTA980108,214
        10         20         30         40         50         60 
MTMITPSSKL TLTKGNKSWS STRCGAFLLL HLVLQPWQRA GAQATPQVFD LLPSSSQRLN 

        70         80         90        100        110        120 
PAALQPVLTD PTLHELYVIS TFKLQSKSSA TIFGLYSSSD NSKYFEFTVM GRLNKAILRY 

       130        140        150        160        170        180 
LKDDGKIHLV VFNNLQLADG RRHRILLRLS NLQRGAGSVE LYLDCVQVDS VNNLPRAFSG 

       190        200        210        220        230        240 
LTQNPQAIEL RTFQRKPQDF LEELKLVVRG SLFQVASLQD CFLQQSEPLA ATGTGDFNRQ 

       250        260        270        280        290        300 
FLGQMTQLNQ LLGEVKDLLR QQVKETSFLR NTIAECQACG PLSFQSPTPN TLVPIAPPAP 

       310        320        330        340        350        360 
PTRPTRRCDS SPCFRGVRCT DTRDGFQCGP CPDGYTGNGI TCSDVDECKY HPCYPGVRCT 

       370        380        390        400        410        420 
NLAPGFRCDA CPVGFTGPMV QGVGINFAKT NKQVCTDVDE CRNGACVLNS ICINTLGSYR 

       430        440        450        460        470        480 
CGPCKPGYTG DQTRGCRTER SCRNPEQNPC SVHAQCIEER QGDVTCVCGV GWAGRAGYVC 

       490        500        510        520        530        540 
GKDVDIDSYP DEELPCSARN CKKDNCKYVP NSGQEDADRD GIGDACDEDA DGDGILNEQD 

       550        560        570        580        590        600 
NCVLTHNVDQ RNTDKDIFGD ACDNCRGVLN NDQKDTDGDG KGDACDDDMD GDGIKNILDN 

       610        620        630        640        650        660 
CPRVPNRDQQ DRDGDGVGDA CDSCPDVSNP NQSDVDNDLV GDSCDTNQDS DGDGHQDSTD 

       670        680        690        700        710        720 
NCPTVINSAQ LDTDKDGIGD ECDDDDDNDG MPDLFPPGPD NCRLVPNPAQ EDSNNDGVGD 

       730        740        750        760        770        780 
ICEADFDQDK VIDRIDVCPE NAEITLTDFR AYQTVVLDPE GDAQIDPNWV VLNQGMEIVQ 

       790        800        810        820        830        840 
TMNSDPGLAV GYTAFNGVDF EGTFHVNTQT DDDYAGFIFG YQDSSSFYVV MWKQTEQTYW 

       850        860        870        880        890        900 
QATPFRAVAE PGIQLKAVKS KTGPGEHLRN SLWHTGDTSD QVRLLWKDSR NVGWKDKVSY 

       910        920        930        940        950        960 
RWFLQHRPQV GYIRVRFYEG SELVADSGVT IDTTMRGGRL GVFCFSQENI IWSNLKYRCN 

       970        980 
DTIPEDFQEF QIQTFDRLDN 

« Hide

References

[1]"Thrombospondin-4, an extracellular matrix protein expressed in the developing and adult nervous system promotes neurite outgrowth."
Arber S., Caroni P.
J. Cell Biol. 131:1083-1094(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Lewis.
Tissue: Skeletal muscle.
[2]"Thrombospondin-4 contributes to spinal sensitization and neuropathic pain states."
Kim D.S., Li K.W., Boroujerdi A., Peter Yu Y., Zhou C.Y., Deng P., Park J., Zhang X., Lee J., Corpe M., Sharp K., Steward O., Eroglu C., Barres B., Zaucke F., Xu Z.C., Luo Z.D.
J. Neurosci. 32:8977-8987(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[3]"Thrombospondin-4 contributes to spinal cord injury-induced changes in nociception."
Zeng J., Kim D., Li K.W., Sharp K., Steward O., Zaucke F., Luo Z.D.
Eur. J. Pain 17:1458-1464(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X89963 mRNA. Translation: CAA62002.1.
UniGeneRn.11207.

3D structure databases

ProteinModelPortalP49744.
SMRP49744. Positions 236-280, 622-961.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP49744. 1 interaction.
STRING10116.ENSRNOP00000017078.

PTM databases

PhosphoSiteP49744.

Proteomic databases

PaxDbP49744.
PRIDEP49744.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCRGD:62046. rat.

Organism-specific databases

RGD62046. Thbs4.

Phylogenomic databases

eggNOGNOG12793.
HOGENOMHOG000007542.
HOVERGENHBG000636.
InParanoidP49744.
PhylomeDBP49744.

Gene expression databases

GenevestigatorP49744.

Family and domain databases

Gene3D2.60.120.200. 1 hit.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR018097. EGF_Ca-bd_CS.
IPR001791. Laminin_G.
IPR024665. Thbs/COMP_coiled-coil.
IPR003367. Thrombospondin_3-like_rpt.
IPR017897. Thrombospondin_3_rpt.
IPR008859. Thrombospondin_C.
[Graphical view]
PfamPF11598. COMP. 1 hit.
PF00008. EGF. 1 hit.
PF07645. EGF_CA. 2 hits.
PF02412. TSP_3. 6 hits.
PF05735. TSP_C. 1 hit.
[Graphical view]
SMARTSM00181. EGF. 2 hits.
SM00179. EGF_CA. 2 hits.
SM00210. TSPN. 1 hit.
[Graphical view]
SUPFAMSSF49899. SSF49899. 2 hits.
PROSITEPS01186. EGF_2. 1 hit.
PS50026. EGF_3. 4 hits.
PS01187. EGF_CA. 2 hits.
PS51234. TSP3. 8 hits.
PS51236. TSP_CTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROP49744.

Entry information

Entry nameTSP4_RAT
AccessionPrimary (citable) accession number: P49744
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families