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Q04205 (TENS_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein attributes

Sequence length1744 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May be involved in cell migration, fibrillar adhesion formation, cartilage development and in linking signal transduction pathways to the cytoskeleton.

Subunit structure

Binds to actin filaments and interacts with phosphotyrosine-containing proteins.

Subcellular location

Cell surface By similarity. Cell junctionadherens junction. Cytoplasmcytoskeleton.

Tissue specificity

Heart, gizzard, lung and skeletal muscle.

Post-translational modification

Tyrosine phosphorylated.

Sequence similarities

Contains 1 C2 tensin-type domain.

Contains 1 phosphatase tensin-type domain.

Contains 1 SH2 domain.

Sequence caution

The sequence AAA73949.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAA79215.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCell junction
Cytoplasm
Cytoskeleton
   DomainSH2 domain
   LigandActin-binding
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentadherens junction

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell surface

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 19732724. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

BCAR1P569452EBI-2607590,EBI-702093From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 17441744Tensin
PRO_0000215901

Regions

Domain58 – 230173Phosphatase tensin-type
Domain235 – 361127C2 tensin-type
Domain1472 – 1581110SH2

Experimental info

Sequence conflict491C → R in AAA73949. Ref.2
Sequence conflict491C → R in CAA79215. Ref.2
Sequence conflict611M → T in AAA73949. Ref.2
Sequence conflict611M → T in CAA79215. Ref.2
Sequence conflict881Q → PR in AAA49087. Ref.3
Sequence conflict4041A → T in AAA73949. Ref.2
Sequence conflict4041A → T in CAA79215. Ref.2
Sequence conflict4521T → A in AAA73949. Ref.2
Sequence conflict4521T → A in CAA79215. Ref.2
Sequence conflict508 – 5092DV → EL in AAA73949. Ref.2
Sequence conflict508 – 5092DV → EL in CAA79215. Ref.2
Sequence conflict5221A → P in AAA73949. Ref.2
Sequence conflict5221A → P in CAA79215. Ref.2
Sequence conflict6641R → A Ref.2
Sequence conflict6661A → T Ref.2
Sequence conflict8751P → A in AAA73949. Ref.2
Sequence conflict8751P → A in CAA79215. Ref.2
Sequence conflict9091P → T in AAA73949. Ref.2
Sequence conflict9091P → T in CAA79215. Ref.2
Sequence conflict1102 – 111312Missing Ref.3
Sequence conflict12401G → A in AAA73949. Ref.2
Sequence conflict12401G → A in CAA79215. Ref.2
Sequence conflict14801E → D in AAA73949. Ref.2
Sequence conflict14801E → D in CAA79215. Ref.2
Sequence conflict17111D → E in AAA73949. Ref.2
Sequence conflict17111D → E in CAA79215. Ref.2

Secondary structure

......................... 1744
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q04205 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 5C3C8B6211935524

FASTA1,744187,214
        10         20         30         40         50         60 
MDFGSVMNQA ATPCSPAVNY ELPSPGQSIT KQVDTPDATR SPRGGQAHCK ASRSMSVTAA 

        70         80         90        100        110        120 
MESSCELDLV YITERIIAVS YPSTAEEQSF RSNLREVAHM LKSKHGDNYV LFNLSERRHD 

       130        140        150        160        170        180 
ISKLHPKVLD FGWPDLHTPA LEKICSICKA MDTWLNAAAH NVVVLHNKGN RGRLGVVVAA 

       190        200        210        220        230        240 
YMHYSNISAS ADQALDRFAM KRFYEDKVVP VGQPSQKRYI HYFSGLLSGS IKMNNKPLFL 

       250        260        270        280        290        300 
HHVIMHGIPN FESKGGCRPF LKIYQAMQPV YTSGIYNVQG DSQTGICITI EPGLLLKGDI 

       310        320        330        340        350        360 
LLKCYHKKFR SPTRDVIFRV QFHTCAVHDL DIVFGKEDLD EAFRDERFPE YGKVEFVFSY 

       370        380        390        400        410        420 
GPEKIQGMEH LENGPSVSVD YNTSDPLIRW DSYENFNIQR EDSAEGTWAE PALPGKHLEK 

       430        440        450        460        470        480 
EVGHTQGPLD GSLYAKVKKK DSLHGSIGAV NTARLPLSAA PNHVEHTLSV SSDSGNSTAS 

       490        500        510        520        530        540 
TKTDRTDEPG APGAPTGHAV LSPEEKRDVD RLLVGFGLES AAPMHNHAPG PAPARLPAGP 

       550        560        570        580        590        600 
GRHVVPAQVH VNGAGTPLLA ERETDILDDE LPNQDGHSVG SLGTLSSLDG TTTASEAGFH 

       610        620        630        640        650        660 
EAPRVGSLSS LPNGPASYNG AEKMLKEGLY EAEPLSNGAY PYSNQNTLMG HHLRDPLAHL 

       670        680        690        700        710        720 
RPSRSAQEHL AGYPQRQPAS ASPAWLQPPV PQPYLYGYDL PSAHRSQSFP AVGTAKYEAN 

       730        740        750        760        770        780 
LALPQAPARS TSSREAVQRG LNSWQQQGGS RPPSQLHDGG LESHSPSLSS CSPQPSPLQP 

       790        800        810        820        830        840 
MPPHSHSMPE FPRAPSRREI EQSIEALDVL MLDLAPSVHK SQSVPSAATR QDKPAAMLSS 

       850        860        870        880        890        900 
LSAQRLSGHY AQPTPQVVQP RSFGTSVGTD PLAKPYSPGP LVPAARSTAE PDYTVHEYRE 

       910        920        930        940        950        960 
TYTPYSYQPV PEPRSYGSAP ASILPLSASY SPAGSQQLLV SSPPSPTAPA QSQLPHKGLE 

       970        980        990       1000       1010       1020 
SYEDLSRSGE EPLNLEGLVA HRVAGVQSRE KSPEESTVPA RRRTPSDSHY EKSSPEPGSP 

      1030       1040       1050       1060       1070       1080 
RSPTVLSPEV VSTIAANPGG RPKEPHLHSY KEAFEEMESA SPSSLTSGGV RSPPGLAKTP 

      1090       1100       1110       1120       1130       1140 
LSALGLKPHN PADILLHPVG ELEGEAGADS EEEPRSYVES VARTATTGRA GNLPAAQPVG 

      1150       1160       1170       1180       1190       1200 
LEVPARNGAF GNSFTVPSPV STSSPIHSVD GASLRSYPSE GSPHGTVTPP HAVAETAYRS 

      1210       1220       1230       1240       1250       1260 
PMVSQTPSAH SSYQTSSPSS FQAGTLGSPY ASPDYPDGRG GFQPDPQARQ QPQVSVVGVH 

      1270       1280       1290       1300       1310       1320 
ALPGSPRTLH RTVATNTPPS PGFGRRAANP AVASVPGSPG LGRHTVSPHA PPGSPSLARH 

      1330       1340       1350       1360       1370       1380 
QMAAVPPGSP MYGYSSPEER RPTLSRQSSA SGYQPPSTPS FPVSPAYYPG TSTPHSSSPD 

      1390       1400       1410       1420       1430       1440 
SAAYRQGSPT PQPALPEKRR MSAGERSNSL PNYATVNGKA SSPLSSGMSS PSSGSAVAFS 

      1450       1460       1470       1480       1490       1500 
HTLPDFSKFS MPDISPETRA NVKFVQDTSK YWYKPDISRE QAIALLKDRE PGAFIIRDSH 

      1510       1520       1530       1540       1550       1560 
SFRGAYGLAM KVASPPPTVM QQNKKGDITN ELVRHFLIET SPRGVKLKGC PNEPNFGCLS 

      1570       1580       1590       1600       1610       1620 
ALVYQHSIMP LALPCKLVIP DRDPMEEKKD AASTTNSATD LLKQGAACNV LFINSVEMES 

      1630       1640       1650       1660       1670       1680 
LTGPQAISKA VAETLVADPT PTATIVHFKV SAQGITLTDN QRKLFFRRHY PLNTVTFCDL 

      1690       1700       1710       1720       1730       1740 
DPQERKWTKT DGSGPAKLFG FVARKQGSTT DNVCHLFAEL DPDQPAAAIV NFVSRVMLGS 


GQKR 

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References

[1]"Molecular cloning of chick cardiac muscle tensin. Full-length cDNA sequence, expression, and characterization."
Lo S.H., An Q., Bao S., Wong W.K., Liu Y., Janmey P.A., Hartwig J.H., Chen L.B.
J. Biol. Chem. 269:22310-22319(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Heart.
[2]"Molecular cloning, expression, and mapping of the high affinity actin-capping domain of chicken cardiac tensin."
Chuang J.Z., Lin D.C., Lin S.
J. Cell Biol. 128:1095-1109(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Heart.
[3]Chen L.B.
Submitted (AUG-1991) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"Modulation of tensin and vimentin expression in chick embryo developing cartilage and cultured differentiating chondrocytes."
van de Werken R., Gennari M., Tavella S., Bet P., Molina F., Lin S., Cancedda R., Castagnola P.
Eur. J. Biochem. 217:781-790(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1469-1744.
Tissue: Embryonic chondrocyte and Embryonic heart.
[5]"Presence of an SH2 domain in the actin-binding protein tensin."
Davis S., Lu M.L., Lo S.H., Lin S., Butler J.A., Druker B.J., Roberts T.M., An Q., Chen L.B.
Science 252:712-715(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAIN SH2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M96625 mRNA. Translation: AAA59053.1.
L06662 mRNA. Translation: AAA73949.1. Different initiation.
Z18529 mRNA. Translation: CAA79215.1. Different initiation.
M74165 mRNA. Translation: AAA49087.1.
X66286 mRNA. Translation: CAA46992.1.
PIRA54970.
A57075.
S27939.
RefSeqNP_990786.1. NM_205455.1.
UniGeneGga.4128.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WVHX-ray1.50A1605-1738[»]
2GJYNMR-A1605-1744[»]
ProteinModelPortalQ04205.
SMRQ04205. Positions 1605-1744.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ04205. 1 interaction.

Proteomic databases

PaxDbQ04205.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID396439.
KEGGgga:396439.

Organism-specific databases

CTD7145.

Phylogenomic databases

eggNOGCOG2453.
HOGENOMHOG000060090.
HOVERGENHBG060186.
InParanoidQ04205.
KOK18080.
PhylomeDBQ04205.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
3.90.190.10. 1 hit.
InterProIPR000008. C2_dom.
IPR011993. PH_like_dom.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR013625. PTB.
IPR006020. PTB/PI_dom.
IPR000980. SH2.
IPR014020. Tensin_C2-dom.
IPR029023. Tensin_lipid_phosphatase_dom.
[Graphical view]
PfamPF08416. PTB. 1 hit.
PF10409. PTEN_C2. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]
SMARTSM00462. PTB. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view]
SUPFAMSSF49562. SSF49562. 1 hit.
SSF52799. SSF52799. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEPS51182. C2_TENSIN. 1 hit.
PS51181. PPASE_TENSIN. 1 hit.
PS50001. SH2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ04205.
NextBio20816480.

Entry information

Entry nameTENS_CHICK
AccessionPrimary (citable) accession number: Q04205
Secondary accession number(s): Q91007, Q92011
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1997
Last modified: June 11, 2014
This is version 104 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references