ID   TENS4_BOVIN             Reviewed;         716 AA.
AC   Q32PJ7;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 2.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Tensin-4;
DE   Flags: Precursor;
GN   Name=TNS4;
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 [MRNA] OF 1-126.
RX   PubMed=12140684; DOI=10.1007/s00335-001-2145-4;
RA   Sonstegard T.S., Capuco A.V., White J., Van Tassell C.P., Connor E.E.,
RA   Cho J., Sultana R., Shade L., Wray J.E., Wells K.D., Quackenbush J.;
RT   "Analysis of bovine mammary gland EST and functional annotation of the Bos
RT   taurus gene index.";
RL   Mamm. Genome 13:373-379(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 43-716.
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI08090.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BG688560; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC108089; AAI08090.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001033244.1; NM_001038155.1.
DR   AlphaFoldDB; Q32PJ7; -.
DR   SMR; Q32PJ7; -.
DR   STRING; 9913.ENSBTAP00000010461; -.
DR   PaxDb; Q32PJ7; -.
DR   PRIDE; Q32PJ7; -.
DR   GeneID; 532898; -.
DR   KEGG; bta:532898; -.
DR   CTD; 84951; -.
DR   eggNOG; KOG1930; Eukaryota.
DR   InParanoid; Q32PJ7; -.
DR   Proteomes; UP000009136; 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; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
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..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..716
FT                   /note="Tensin-4"
FT                   /id="PRO_0000248212"
FT   DOMAIN          449..556
FT                   /note="SH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT   DOMAIN          578..716
FT                   /note="Phosphatase tensin-type"
FT   REGION          119..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          158..274
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          301..322
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          334..435
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        398..423
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         248
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IZW8"
SQ   SEQUENCE   716 AA;  75888 MW;  97898D125CC77DEF CRC64;
     MSQVMSSPLL AGGPAVGLAP CEEPRRVLHP APSPSLPPPC PYYTTEGWGA QALMAPMPCK
     GPPVRLQPAP QAGANASCLL KAPGEQVSGA QEDLDSYIDF SLESLNQMIL ELDPTFQLLP
     PGPGGPEAQP TQSTTLGKKK EEPEALDIKY IEVTSTRSRC HDGPRSCCSP SVTPPFGSPR
     TGGLLLSRDL PRETRSSSES LIFSGSQGRG HQHPAPPSAV PSSHPPTSPS ISIPGMGSKA
     SGPHGLGSPL VASPSLEKGL GGQGPQLSSR VSMLSGSPAS DISYVFGSSQ SLLHSSISSH
     QSSSRSLESP SSSSSSLNNL GPVSLYTRAS DLQVPSNATP SMGQPRATRS PPLAKEHASS
     CPPSITNSMT DIPIVLINGF PEPGSPPSQR TPGPQDFVRP GATSSSMPCP ATRSHSQTLP
     EAPPTASPEG PARDMQPTMK FVMDTSKYWF KPSISREQAI ELLRKEEPGA FIVRDSSSYR
     GSFGLALKVQ EAPTPAQSRP GEDSSDLIRH FLIESSAKGV HLKGADEEPY FGSLSAFVCQ
     HSIMALALPC KLVIPQKELG GGDGASDPSA DGQASCLKKS AGCHALYLSS VSVETLSGAL
     AVEKAISATL ERDVLPTPTV VHFKVTEQGI TLTDVQRKVF FRRHYPLATL RFCGMDPEQR
     KWQKYCKPSR IFGFVAKSQT ESQENVCHLF AEYDTLQPAS QVIRLVGALL QDPERM