TES_MOUSE
ID TES_MOUSE Reviewed; 423 AA.
AC P47226;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 140.
DE RecName: Full=Testin;
DE AltName: Full=TES1/TES2;
GN Name=Tes;
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 [MRNA] (ISOFORMS TES1 AND TES2).
RC TISSUE=Testis;
RX PubMed=7758969; DOI=10.1016/0378-1119(95)00088-n;
RA Divecha N., Charleston B.;
RT "Cloning and characterisation of two new cDNAs encoding murine triple LIM
RT domains.";
RL Gene 156:283-286(1995).
RN [2]
RP DISRUPTION PHENOTYPE.
RX PubMed=16033868; DOI=10.1073/pnas.0504934102;
RA Drusco A., Zanesi N., Roldo C., Trapasso F., Farber J.L., Fong L.Y.,
RA Croce C.M.;
RT "Knockout mice reveal a tumor suppressor function for Testin.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:10947-10951(2005).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=21278383; DOI=10.1074/jbc.m110.171264;
RA Boeda B., Knowles P.P., Briggs D.C., Murray-Rust J., Soriano E.,
RA Garvalov B.K., McDonald N.Q., Way M.;
RT "Molecular recognition of the Tes LIM2-3 domains by the actin-related
RT protein Arp7A.";
RL J. Biol. Chem. 286:11543-11554(2011).
CC -!- FUNCTION: Scaffold protein that may play a role in cell adhesion, cell
CC spreading and in the reorganization of the actin cytoskeleton. Plays a
CC role in the regulation of cell proliferation. May act as a tumor
CC suppressor (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts via LIM domain 1 with ZYX. Interacts (via LIM domain
CC 3) with ENAH and VASP. Interacts with ALKBH4, talin, actin, alpha-
CC actinin, GRIP1 and PXN. Interacts (via LIM domain 2) with ACTL7A (via
CC N-terminus). Heterodimer with ACTL7A; the heterodimer interacts with
CC ENAH to form a heterotrimer (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21278383}. Cell
CC junction, focal adhesion {ECO:0000250}. Note=Detected along actin
CC stress fibers (By similarity). Detected at the subacrosomal layer in
CC round spermatids. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=TES2;
CC IsoId=P47226-1; Sequence=Displayed;
CC Name=TES1;
CC IsoId=P47226-2; Sequence=VSP_003123;
CC -!- TISSUE SPECIFICITY: Detected at the acrosome of round spermatids (at
CC protein level). Isoform TES1 transcript is highly expressed in adult
CC testis and detected at low levels in other tissues. Isoform TES2
CC transcript is highly expressed in testis, kidney and spleen;
CC intermediate in thymus, submaxillary gland and lung; detected at low
CC levels in other tissues. {ECO:0000269|PubMed:21278383}.
CC -!- DOMAIN: The N-terminal and the C-terminal halves of the protein can
CC associate with each other, thereby hindering interactions with ZYX.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Increased susceptibility to carcinogen-induced
CC gastric cancer. This increase is seen both in homozygous knockout mice
CC and in heterozygous mice missing only one copy of the gene.
CC {ECO:0000269|PubMed:16033868}.
CC -!- SIMILARITY: Belongs to the prickle / espinas / testin family.
CC {ECO:0000305}.
CC -!- CAUTION: Should not be confused with rat testin which is a thiol
CC protease homolog. {ECO:0000305}.
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DR EMBL; X78990; CAA55590.1; -; mRNA.
DR EMBL; X78989; CAA55589.1; -; mRNA.
DR PIR; I48842; I48842.
DR AlphaFoldDB; P47226; -.
DR SMR; P47226; -.
DR STRING; 10090.ENSMUSP00000111127; -.
DR iPTMnet; P47226; -.
DR PhosphoSitePlus; P47226; -.
DR EPD; P47226; -.
DR MaxQB; P47226; -.
DR PaxDb; P47226; -.
DR PeptideAtlas; P47226; -.
DR PRIDE; P47226; -.
DR ProteomicsDB; 263281; -. [P47226-1]
DR ProteomicsDB; 263282; -. [P47226-2]
DR MGI; MGI:105081; Tes.
DR eggNOG; KOG1704; Eukaryota.
DR InParanoid; P47226; -.
DR PhylomeDB; P47226; -.
DR ChiTaRS; Tes; mouse.
DR PRO; PR:P47226; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P47226; protein.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR CDD; cd09413; LIM1_Testin; 1.
DR CDD; cd09416; LIM2_Testin; 1.
DR CDD; cd09419; LIM3_Testin; 1.
DR CDD; cd09829; PET_testin; 1.
DR InterPro; IPR034958; LIM1_Testin.
DR InterPro; IPR034959; LIM2_Testin.
DR InterPro; IPR034960; LIM3_Testin.
DR InterPro; IPR010442; PET_domain.
DR InterPro; IPR033724; PET_testin.
DR InterPro; IPR027683; Testin.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR24211:SF1; PTHR24211:SF1; 1.
DR Pfam; PF00412; LIM; 2.
DR Pfam; PF06297; PET; 1.
DR SMART; SM00132; LIM; 3.
DR PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR PROSITE; PS50023; LIM_DOMAIN_2; 3.
DR PROSITE; PS51303; PET; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Cytoplasm; LIM domain; Metal-binding;
KW Reference proteome; Repeat; Zinc.
FT CHAIN 1..423
FT /note="Testin"
FT /id="PRO_0000075907"
FT DOMAIN 97..204
FT /note="PET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00636"
FT DOMAIN 236..299
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 301..361
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 364..423
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..55
FT /note="Missing (in isoform TES1)"
FT /evidence="ECO:0000303|PubMed:7758969"
FT /id="VSP_003123"
SQ SEQUENCE 423 AA; 47983 MW; 376D49640322C747 CRC64;
MSATHPTRLG TRTKESNACA SQGLVRKPPW ANEGEGFELH FWRKICRNCN VVKKSMTVLL
SNEEDRKVGR LFEDTKYTTL IAKLKSDGIP MYKRNVMILT NPVAAKKNVS INTVTYEWAP
PVQNQALARQ YMQMLPKEKQ PVAGSEGAQY RKKQLAKQLP AHDQDPSKCH ELSPKEVKEM
EQFVKKYKSE ALGVGDVKFP SEMNAQGDKV HNCGNRHAPA AVASKDKSAE SKKTQYSCYC
CKHTTNEGEP AIYAERAGYD KLWHPACFIC STCGELLVDM IYFWKNGKLY CGRHYCDSEK
PRCAGCDELI FSNEYTQAEN QNWHLKHFCC FDCDHILAGK IYVMVTDKPV CKPCYVKNHA
VVCQGCHNAI DPEVQRVTYN NFSWHASTEC FLCSCCSKCL IGQKFMPVEG MVFCSVECKR
MMS
