ID   TENS4_RAT               Reviewed;         718 AA.
AC   Q4V8I3;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Tensin-4;
DE   Flags: Precursor;
GN   Name=Tns4;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Placenta;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May be involved in cell migration, cartilage development and
CC       in linking signal transduction pathways to the cytoskeleton. May
CC       promote apoptosis, via its cleavage by caspase-3. Cytoplasm,
CC       cytoskeleton. {ECO:0000250}.
CC   -!- SUBUNIT: Binds to actin filaments and interacts with phosphotyrosine-
CC       containing proteins. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion {ECO:0000250}.
CC       Cytoplasm, cytoskeleton {ECO:0000250}.
CC   -!- PTM: Proteolytically cleaved by caspase-3 during apoptosis.
CC       {ECO:0000250}.
CC   -!- PTM: Tyrosine phosphorylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PTEN phosphatase protein family.
CC       {ECO:0000305}.
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DR   EMBL; BC097378; AAH97378.1; -; mRNA.
DR   RefSeq; NP_001020052.1; NM_001024881.1.
DR   AlphaFoldDB; Q4V8I3; -.
DR   SMR; Q4V8I3; -.
DR   STRING; 10116.ENSRNOP00000029109; -.
DR   PaxDb; Q4V8I3; -.
DR   PRIDE; Q4V8I3; -.
DR   GeneID; 303517; -.
DR   KEGG; rno:303517; -.
DR   UCSC; RGD:1310402; rat.
DR   CTD; 84951; -.
DR   RGD; 1310402; Tns4.
DR   eggNOG; KOG1930; Eukaryota.
DR   InParanoid; Q4V8I3; -.
DR   OrthoDB; 172407at2759; -.
DR   PhylomeDB; Q4V8I3; -.
DR   Reactome; R-RNO-8875513; MET interacts with TNS proteins.
DR   PRO; PR:Q4V8I3; -.
DR   Proteomes; UP000002494; Unplaced.
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; ISO:RGD.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0008104; P:protein localization; ISO:RGD.
DR   CDD; cd01213; PTB_tensin; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   Gene3D; 3.30.505.10; -; 1.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR013625; PTB.
DR   InterPro; IPR006020; PTB/PI_dom.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   InterPro; IPR033929; Tensin_PTB.
DR   Pfam; PF08416; PTB; 1.
DR   Pfam; PF00017; SH2; 1.
DR   SMART; SM00462; PTB; 1.
DR   SMART; SM00252; SH2; 1.
DR   SUPFAM; SSF55550; SSF55550; 1.
DR   PROSITE; PS50001; SH2; 1.
PE   2: Evidence at transcript level;
KW   Actin-binding; Apoptosis; Cell junction; Cytoplasm; Cytoskeleton;
KW   Phosphoprotein; Reference proteome; SH2 domain; Signal.
FT   SIGNAL          1..14
FT                   /evidence="ECO:0000250"
FT   CHAIN           15..718
FT                   /note="Tensin-4"
FT                   /id="PRO_0000248215"
FT   DOMAIN          451..558
FT                   /note="SH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT   DOMAIN          550..717
FT                   /note="Phosphatase tensin-type"
FT   REGION          188..244
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          272..437
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        192..225
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        272..353
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        369..425
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         230
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IZW8"
SQ   SEQUENCE   718 AA;  77245 MW;  AD76CE54CAD8E3F0 CRC64;
     MSSSLLTGGH VVSLTPHEES RMALHPTPSH DLPALCPYYT TESWGTQPLM DPTLCKGSSN
     RLQQAQQAEA RAQCLLQCPG EQASGASQDL DSCIDFSLEA LNKMILELDP TFQLLPSGIA
     GPQAEPTNSV ASRTKKEEPD ALDIKYIEVT STRSRCLDSP QRCSSPCVTP PFGSPRSGGL
     FLSRDIPRET RSSSNESLIF SGNQGRGSSP HTPSSLSNSI PCRESRASGS PLATPPGWEK
     GLRAPQWGSR VSTLSASPVS DISYVFGSNQ SLPHSSLSSY PPSSRSLGSP ASSSSSLHSL
     DRGSQCVRSS DAQVPSNPIV GMGQPQAVPS TPVAKEQASS CPPSVTNSMA DIPIVLINGN
     PEPQSPPAQQ TPRYQDSVQS RATSPSHLCQ ATKSHSKTLP DVPLTSPSHL CQATKSHSKT
     LPDVPLTASP ESPAKDMQPT MKFVMDTSKY WLKPSITREQ AINLLRTEKP GTFVIRDSSS
     YRGSFGLALK VQETPASAPN RPGEDSTDFI RHFLVESSAK GVHLKGADEE PYFGSLSAFV
     CQHSIMALAL PCKLTIPQKE LGGAEPASDS PTHGQTSCLK ISAGCHTLYL TSVSVETLSG
     ALAVQKAISV MLERDVLPTP TVVHFKVTEQ GITLTDVQRK VFFRRHYPLI ALRFCGMDPE
     QRKWQKYCKP SRIFGFVAKS QTEPQENACH LFAEYDAAQP ASQVISLVTA LLKDTERV