TENS_CHICK
ID TENS_CHICK Reviewed; 1744 AA.
AC Q04205; Q91007; Q92011;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Tensin;
GN Name=TNS;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RX PubMed=8071358; DOI=10.1016/s0021-9258(17)31791-x;
RA Lo S.H., An Q., Bao S., Wong W.K., Liu Y., Janmey P.A., Hartwig J.H.,
RA Chen L.B.;
RT "Molecular cloning of chick cardiac muscle tensin. Full-length cDNA
RT sequence, expression, and characterization.";
RL J. Biol. Chem. 269:22310-22319(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RX PubMed=7896874; DOI=10.1083/jcb.128.6.1095;
RA Chuang J.Z., Lin D.C., Lin S.;
RT "Molecular cloning, expression, and mapping of the high affinity actin-
RT capping domain of chicken cardiac tensin.";
RL J. Cell Biol. 128:1095-1109(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Chen L.B.;
RL Submitted (AUG-1991) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1469-1744.
RC TISSUE=Embryonic chondrocyte, and Embryonic heart;
RX PubMed=8223621; DOI=10.1111/j.1432-1033.1993.tb18306.x;
RA van de Werken R., Gennari M., Tavella S., Bet P., Molina F., Lin S.,
RA Cancedda R., Castagnola P.;
RT "Modulation of tensin and vimentin expression in chick embryo developing
RT cartilage and cultured differentiating chondrocytes.";
RL Eur. J. Biochem. 217:781-790(1993).
RN [5]
RP DOMAIN SH2.
RX PubMed=1708917; DOI=10.1126/science.1708917;
RA Davis S., Lu M.L., Lo S.H., Lin S., Butler J.A., Druker B.J., Roberts T.M.,
RA An Q., Chen L.B.;
RT "Presence of an SH2 domain in the actin-binding protein tensin.";
RL Science 252:712-715(1991).
CC -!- FUNCTION: May be involved in cell migration, fibrillar adhesion
CC formation, cartilage development and in linking signal transduction
CC pathways to the cytoskeleton.
CC -!- SUBUNIT: Binds to actin filaments and interacts with phosphotyrosine-
CC containing proteins.
CC -!- INTERACTION:
CC Q04205; P56945: BCAR1; Xeno; NbExp=2; IntAct=EBI-2607590, EBI-702093;
CC Q04205; Q96QB1-1: DLC1; Xeno; NbExp=7; IntAct=EBI-2607590, EBI-15638708;
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000250}. Cell junction,
CC adherens junction. Cytoplasm, cytoskeleton.
CC -!- TISSUE SPECIFICITY: Heart, gizzard, lung and skeletal muscle.
CC -!- PTM: Tyrosine phosphorylated.
CC -!- SIMILARITY: Belongs to the PTEN phosphatase protein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA73949.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA79215.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M96625; AAA59053.1; -; mRNA.
DR EMBL; L06662; AAA73949.1; ALT_INIT; mRNA.
DR EMBL; Z18529; CAA79215.1; ALT_INIT; mRNA.
DR EMBL; M74165; AAA49087.1; -; mRNA.
DR EMBL; X66286; CAA46992.1; -; mRNA.
DR PIR; A54970; A54970.
DR PIR; A57075; A57075.
DR PIR; S27939; S27939.
DR RefSeq; NP_990786.1; NM_205455.1.
DR PDB; 1WVH; X-ray; 1.50 A; A=1605-1738.
DR PDB; 2GJY; NMR; -; A=1605-1744.
DR PDBsum; 1WVH; -.
DR PDBsum; 2GJY; -.
DR AlphaFoldDB; Q04205; -.
DR BMRB; Q04205; -.
DR SMR; Q04205; -.
DR DIP; DIP-56927N; -.
DR IntAct; Q04205; 4.
DR PaxDb; Q04205; -.
DR PRIDE; Q04205; -.
DR DNASU; 396439; -.
DR GeneID; 396439; -.
DR KEGG; gga:396439; -.
DR CTD; 7145; -.
DR VEuPathDB; HostDB:geneid_396439; -.
DR InParanoid; Q04205; -.
DR OrthoDB; 172407at2759; -.
DR PhylomeDB; Q04205; -.
DR EvolutionaryTrace; Q04205; -.
DR PRO; PR:Q04205; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0010761; P:fibroblast migration; IBA:GO_Central.
DR CDD; cd01213; PTB_tensin; 1.
DR CDD; cd09927; SH2_Tensin_like; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR013625; PTB.
DR InterPro; IPR006020; PTB/PI_dom.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR035012; Tensin-like_SH2.
DR InterPro; IPR014020; Tensin_C2-dom.
DR InterPro; IPR029023; Tensin_phosphatase.
DR InterPro; IPR033929; Tensin_PTB.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR Pfam; PF08416; PTB; 1.
DR Pfam; PF10409; PTEN_C2; 1.
DR Pfam; PF00017; SH2; 1.
DR SMART; SM00462; PTB; 1.
DR SMART; SM01326; PTEN_C2; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SMART; SM00252; SH2; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS51182; C2_TENSIN; 1.
DR PROSITE; PS51181; PPASE_TENSIN; 1.
DR PROSITE; PS50001; SH2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Cell junction; Cytoplasm; Cytoskeleton;
KW Phosphoprotein; Reference proteome; SH2 domain.
FT CHAIN 1..1744
FT /note="Tensin"
FT /id="PRO_0000215901"
FT DOMAIN 58..230
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00590"
FT DOMAIN 235..361
FT /note="C2 tensin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00589"
FT DOMAIN 1472..1581
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT REGION 15..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 666..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 724..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 871..892
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 934..1076
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1158..1435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..753
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..789
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 934..954
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 994..1010
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1011..1031
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1199..1227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1340..1357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1364..1388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1405..1435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 49
FT /note="C -> R (in Ref. 2; AAA73949/CAA79215)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="M -> T (in Ref. 2; AAA73949/CAA79215)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="Q -> PR (in Ref. 3; AAA49087)"
FT /evidence="ECO:0000305"
FT CONFLICT 404
FT /note="A -> T (in Ref. 2; AAA73949/CAA79215)"
FT /evidence="ECO:0000305"
FT CONFLICT 452
FT /note="T -> A (in Ref. 2; AAA73949/CAA79215)"
FT /evidence="ECO:0000305"
FT CONFLICT 508..509
FT /note="DV -> EL (in Ref. 2; AAA73949/CAA79215)"
FT /evidence="ECO:0000305"
FT CONFLICT 522
FT /note="A -> P (in Ref. 2; AAA73949/CAA79215)"
FT /evidence="ECO:0000305"
FT CONFLICT 664
FT /note="R -> A (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 666
FT /note="A -> T (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 875
FT /note="P -> A (in Ref. 2; AAA73949/CAA79215)"
FT /evidence="ECO:0000305"
FT CONFLICT 909
FT /note="P -> T (in Ref. 2; AAA73949/CAA79215)"
FT /evidence="ECO:0000305"
FT CONFLICT 1102..1113
FT /note="Missing (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 1240
FT /note="G -> A (in Ref. 2; AAA73949/CAA79215)"
FT /evidence="ECO:0000305"
FT CONFLICT 1480
FT /note="E -> D (in Ref. 2; AAA73949/CAA79215)"
FT /evidence="ECO:0000305"
FT CONFLICT 1711
FT /note="D -> E (in Ref. 2; AAA73949/CAA79215)"
FT /evidence="ECO:0000305"
FT STRAND 1607..1619
FT /evidence="ECO:0007829|PDB:1WVH"
FT HELIX 1623..1635
FT /evidence="ECO:0007829|PDB:1WVH"
FT STRAND 1644..1651
FT /evidence="ECO:0007829|PDB:1WVH"
FT STRAND 1654..1662
FT /evidence="ECO:0007829|PDB:1WVH"
FT STRAND 1667..1671
FT /evidence="ECO:0007829|PDB:1WVH"
FT HELIX 1672..1674
FT /evidence="ECO:0007829|PDB:1WVH"
FT STRAND 1675..1680
FT /evidence="ECO:0007829|PDB:1WVH"
FT STRAND 1686..1688
FT /evidence="ECO:0007829|PDB:1WVH"
FT STRAND 1690..1693
FT /evidence="ECO:0007829|PDB:1WVH"
FT STRAND 1695..1703
FT /evidence="ECO:0007829|PDB:1WVH"
FT STRAND 1706..1709
FT /evidence="ECO:0007829|PDB:2GJY"
FT STRAND 1712..1719
FT /evidence="ECO:0007829|PDB:1WVH"
FT HELIX 1726..1737
FT /evidence="ECO:0007829|PDB:1WVH"
SQ SEQUENCE 1744 AA; 187214 MW; 5C3C8B6211935524 CRC64;
MDFGSVMNQA ATPCSPAVNY ELPSPGQSIT KQVDTPDATR SPRGGQAHCK ASRSMSVTAA
MESSCELDLV YITERIIAVS YPSTAEEQSF RSNLREVAHM LKSKHGDNYV LFNLSERRHD
ISKLHPKVLD FGWPDLHTPA LEKICSICKA MDTWLNAAAH NVVVLHNKGN RGRLGVVVAA
YMHYSNISAS ADQALDRFAM KRFYEDKVVP VGQPSQKRYI HYFSGLLSGS IKMNNKPLFL
HHVIMHGIPN FESKGGCRPF LKIYQAMQPV YTSGIYNVQG DSQTGICITI EPGLLLKGDI
LLKCYHKKFR SPTRDVIFRV QFHTCAVHDL DIVFGKEDLD EAFRDERFPE YGKVEFVFSY
GPEKIQGMEH LENGPSVSVD YNTSDPLIRW DSYENFNIQR EDSAEGTWAE PALPGKHLEK
EVGHTQGPLD GSLYAKVKKK DSLHGSIGAV NTARLPLSAA PNHVEHTLSV SSDSGNSTAS
TKTDRTDEPG APGAPTGHAV LSPEEKRDVD RLLVGFGLES AAPMHNHAPG PAPARLPAGP
GRHVVPAQVH VNGAGTPLLA ERETDILDDE LPNQDGHSVG SLGTLSSLDG TTTASEAGFH
EAPRVGSLSS LPNGPASYNG AEKMLKEGLY EAEPLSNGAY PYSNQNTLMG HHLRDPLAHL
RPSRSAQEHL AGYPQRQPAS ASPAWLQPPV PQPYLYGYDL PSAHRSQSFP AVGTAKYEAN
LALPQAPARS TSSREAVQRG LNSWQQQGGS RPPSQLHDGG LESHSPSLSS CSPQPSPLQP
MPPHSHSMPE FPRAPSRREI EQSIEALDVL MLDLAPSVHK SQSVPSAATR QDKPAAMLSS
LSAQRLSGHY AQPTPQVVQP RSFGTSVGTD PLAKPYSPGP LVPAARSTAE PDYTVHEYRE
TYTPYSYQPV PEPRSYGSAP ASILPLSASY SPAGSQQLLV SSPPSPTAPA QSQLPHKGLE
SYEDLSRSGE EPLNLEGLVA HRVAGVQSRE KSPEESTVPA RRRTPSDSHY EKSSPEPGSP
RSPTVLSPEV VSTIAANPGG RPKEPHLHSY KEAFEEMESA SPSSLTSGGV RSPPGLAKTP
LSALGLKPHN PADILLHPVG ELEGEAGADS EEEPRSYVES VARTATTGRA GNLPAAQPVG
LEVPARNGAF GNSFTVPSPV STSSPIHSVD GASLRSYPSE GSPHGTVTPP HAVAETAYRS
PMVSQTPSAH SSYQTSSPSS FQAGTLGSPY ASPDYPDGRG GFQPDPQARQ QPQVSVVGVH
ALPGSPRTLH RTVATNTPPS PGFGRRAANP AVASVPGSPG LGRHTVSPHA PPGSPSLARH
QMAAVPPGSP MYGYSSPEER RPTLSRQSSA SGYQPPSTPS FPVSPAYYPG TSTPHSSSPD
SAAYRQGSPT PQPALPEKRR MSAGERSNSL PNYATVNGKA SSPLSSGMSS PSSGSAVAFS
HTLPDFSKFS MPDISPETRA NVKFVQDTSK YWYKPDISRE QAIALLKDRE PGAFIIRDSH
SFRGAYGLAM KVASPPPTVM QQNKKGDITN ELVRHFLIET SPRGVKLKGC PNEPNFGCLS
ALVYQHSIMP LALPCKLVIP DRDPMEEKKD AASTTNSATD LLKQGAACNV LFINSVEMES
LTGPQAISKA VAETLVADPT PTATIVHFKV SAQGITLTDN QRKLFFRRHY PLNTVTFCDL
DPQERKWTKT DGSGPAKLFG FVARKQGSTT DNVCHLFAEL DPDQPAAAIV NFVSRVMLGS
GQKR
