TENS4_MOUSE
ID TENS4_MOUSE Reviewed; 696 AA.
AC Q8BZ33; A2A552; Q3TCM8; Q7TNR5;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Tensin-4;
DE Flags: Precursor;
GN Name=Tns4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Vagina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
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; AL591366; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466556; EDL16179.1; -; Genomic_DNA.
DR EMBL; AK036834; BAC29598.1; -; mRNA.
DR EMBL; AK170638; BAE41928.1; -; mRNA.
DR EMBL; BC055820; AAH55820.1; -; mRNA.
DR CCDS; CCDS25372.1; -.
DR RefSeq; NP_766152.2; NM_172564.3.
DR AlphaFoldDB; Q8BZ33; -.
DR SMR; Q8BZ33; -.
DR STRING; 10090.ENSMUSP00000017751; -.
DR iPTMnet; Q8BZ33; -.
DR PhosphoSitePlus; Q8BZ33; -.
DR MaxQB; Q8BZ33; -.
DR PaxDb; Q8BZ33; -.
DR PeptideAtlas; Q8BZ33; -.
DR PRIDE; Q8BZ33; -.
DR ProteomicsDB; 263277; -.
DR Antibodypedia; 16494; 218 antibodies from 27 providers.
DR DNASU; 217169; -.
DR Ensembl; ENSMUST00000017751; ENSMUSP00000017751; ENSMUSG00000017607.
DR GeneID; 217169; -.
DR KEGG; mmu:217169; -.
DR UCSC; uc007lig.2; mouse.
DR CTD; 84951; -.
DR MGI; MGI:2144377; Tns4.
DR VEuPathDB; HostDB:ENSMUSG00000017607; -.
DR eggNOG; KOG1930; Eukaryota.
DR GeneTree; ENSGT00940000160142; -.
DR HOGENOM; CLU_398985_0_0_1; -.
DR InParanoid; Q8BZ33; -.
DR OMA; SQPSMKF; -.
DR OrthoDB; 172407at2759; -.
DR PhylomeDB; Q8BZ33; -.
DR TreeFam; TF315996; -.
DR Reactome; R-MMU-8875513; MET interacts with TNS proteins.
DR BioGRID-ORCS; 217169; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Tns4; mouse.
DR PRO; PR:Q8BZ33; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8BZ33; protein.
DR Bgee; ENSMUSG00000017607; Expressed in left colon and 57 other tissues.
DR Genevisible; Q8BZ33; MM.
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:MGI.
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:MGI.
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..696
FT /note="Tensin-4"
FT /id="PRO_0000248214"
FT DOMAIN 429..536
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 528..695
FT /note="Phosphatase tensin-type"
FT REGION 157..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZW8"
FT CONFLICT 268
FT /note="S -> I (in Ref. 3; BAC29598)"
FT /evidence="ECO:0000305"
FT CONFLICT 490
FT /note="H -> D (in Ref. 3; BAE41928)"
FT /evidence="ECO:0000305"
FT CONFLICT 507
FT /note="E -> K (in Ref. 3; BAE41928)"
FT /evidence="ECO:0000305"
FT CONFLICT 589
FT /note="T -> I (in Ref. 4; AAH55820)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 696 AA; 74622 MW; E2EB3F1D4DBFD079 CRC64;
MSSSLLAGGH MVSLTPCEES RMALHPTPSP GLPALCPYYT TESWGTQPLM APTLRKGSSD
RLQQAQQAEA RAHCLLQGPG EQASGASQDL ESCIDFSLEA LNQMILEIDP TFQLLPSGTA
GPQAESTNSI MSRNKKEEPE ALDIKYIEVT STRSRYLDGP QRCSSPCATP PFGSPRSGSL
FLSRDIPRET RSSSNESLIF SGNQGRGPSP LTPSSLSNAI PCRESRTSGS PLATPPGWEK
GLRAPQRGSR VSILSASPVS DVSYVFGSNQ SLPHSSLSSY PSSSRSLGSP ASSSSSLHSL
DRGSQCGRPS DAQAPSNPIL GMGQPQAVQS TPVAKEQASS CPASVTNSMA DIPIVLINGS
PEPQSPPAQR TPGHQDSVQS RVTSPSHLCQ AIKSPSKTLP DVPLPASPDG PAKDMQPTMK
FVMDTSKYWF KPSITREQAI NLLRTEKPGA FVIRDSSSYR GSFGLALKVQ ETSASAPNRP
GEDSSDLIRH FLIESSAKGV HLKGADEEPY FGSLSSFVCQ HSIMALALPC KLTIPQKELG
GAEPASDSPT HGQTSCLKIS AGCHTLYLSS VSVETLSGAL AVQKAISVTL ERDVLPTPTV
VHFKVTEQGI TLTDVQRKVF FRRHYPLSAL RFCGMDPEQR KWQKYCKPSR IFGFVAKSQT
EPQENVCHLF AEYDAVQPAS QVISLVTALL QDTERM