ID   TES_PIG                 Reviewed;         421 AA.
AC   Q2QLE3;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Testin;
GN   Name=TES;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12917688; DOI=10.1038/nature01858;
RA   Thomas J.W., Touchman J.W., Blakesley R.W., Bouffard G.G.,
RA   Beckstrom-Sternberg S.M., Margulies E.H., Blanchette M., Siepel A.C.,
RA   Thomas P.J., McDowell J.C., Maskeri B., Hansen N.F., Schwartz M.S.,
RA   Weber R.J., Kent W.J., Karolchik D., Bruen T.C., Bevan R., Cutler D.J.,
RA   Schwartz S., Elnitski L., Idol J.R., Prasad A.B., Lee-Lin S.-Q.,
RA   Maduro V.V.B., Summers T.J., Portnoy M.E., Dietrich N.L., Akhter N.,
RA   Ayele K., Benjamin B., Cariaga K., Brinkley C.P., Brooks S.Y., Granite S.,
RA   Guan X., Gupta J., Haghighi P., Ho S.-L., Huang M.C., Karlins E.,
RA   Laric P.L., Legaspi R., Lim M.J., Maduro Q.L., Masiello C.A.,
RA   Mastrian S.D., McCloskey J.C., Pearson R., Stantripop S., Tiongson E.E.,
RA   Tran J.T., Tsurgeon C., Vogt J.L., Walker M.A., Wetherby K.D.,
RA   Wiggins L.S., Young A.C., Zhang L.-H., Osoegawa K., Zhu B., Zhao B.,
RA   Shu C.L., De Jong P.J., Lawrence C.E., Smit A.F., Chakravarti A.,
RA   Haussler D., Green P., Miller W., Green E.D.;
RT   "Comparative analyses of multi-species sequences from targeted genomic
RT   regions.";
RL   Nature 424:788-793(2003).
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 (By similarity). Interacts (via LIM domain 2)
CC       with ACTL7A (via N-terminus). Heterodimer with ACTL7A; the heterodimer
CC       interacts with ENAH to form a heterotrimer (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell junction, focal
CC       adhesion {ECO:0000250}. Note=Detected along actin stress fibers.
CC       {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the prickle / espinas / testin family.
CC       {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; DP000017; ABA90382.1; -; Genomic_DNA.
DR   RefSeq; NP_001116672.1; NM_001123200.1.
DR   AlphaFoldDB; Q2QLE3; -.
DR   SMR; Q2QLE3; -.
DR   STRING; 9823.ENSSSCP00000017624; -.
DR   PaxDb; Q2QLE3; -.
DR   PeptideAtlas; Q2QLE3; -.
DR   PRIDE; Q2QLE3; -.
DR   Ensembl; ENSSSCT00000041361; ENSSSCP00000051115; ENSSSCG00000040344.
DR   Ensembl; ENSSSCT00015004232; ENSSSCP00015001506; ENSSSCG00015003335.
DR   Ensembl; ENSSSCT00025099837; ENSSSCP00025044005; ENSSSCG00025072605.
DR   Ensembl; ENSSSCT00030073442; ENSSSCP00030033590; ENSSSCG00030052674.
DR   Ensembl; ENSSSCT00035046583; ENSSSCP00035018623; ENSSSCG00035035158.
DR   Ensembl; ENSSSCT00040055513; ENSSSCP00040023077; ENSSSCG00040041528.
DR   Ensembl; ENSSSCT00045001949; ENSSSCP00045001240; ENSSSCG00045001254.
DR   Ensembl; ENSSSCT00050063745; ENSSSCP00050027402; ENSSSCG00050046832.
DR   Ensembl; ENSSSCT00055037001; ENSSSCP00055029411; ENSSSCG00055018908.
DR   Ensembl; ENSSSCT00060099213; ENSSSCP00060043046; ENSSSCG00060072616.
DR   Ensembl; ENSSSCT00065000699; ENSSSCP00065000158; ENSSSCG00065000607.
DR   Ensembl; ENSSSCT00070057623; ENSSSCP00070048993; ENSSSCG00070028716.
DR   GeneID; 100125376; -.
DR   KEGG; ssc:100125376; -.
DR   CTD; 26136; -.
DR   VGNC; VGNC:93884; TES.
DR   eggNOG; KOG1704; Eukaryota.
DR   GeneTree; ENSGT00940000155993; -.
DR   InParanoid; Q2QLE3; -.
DR   OMA; NKLWHPA; -.
DR   OrthoDB; 997264at2759; -.
DR   Proteomes; UP000008227; Chromosome 18.
DR   Proteomes; UP000314985; Chromosome 18.
DR   Bgee; ENSSSCG00000040344; Expressed in testis and 40 other tissues.
DR   ExpressionAtlas; Q2QLE3; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
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   3: Inferred from homology;
KW   Cell junction; Cytoplasm; LIM domain; Metal-binding; Reference proteome;
KW   Repeat; Zinc.
FT   CHAIN           1..421
FT                   /note="Testin"
FT                   /id="PRO_0000226351"
FT   DOMAIN          92..199
FT                   /note="PET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00636"
FT   DOMAIN          234..297
FT                   /note="LIM zinc-binding 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   DOMAIN          299..359
FT                   /note="LIM zinc-binding 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   DOMAIN          362..421
FT                   /note="LIM zinc-binding 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   REGION          133..164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   421 AA;  47947 MW;  7D16FC45BAEBDA50 CRC64;
     MDLEAKVKKM GLGHEQGFGA PCLKCKEKCE GFELHFWRKI CRNCKCGQEE HDVLLSNEED
     RKVGKLFEDT KYTTLIAKLK SDGIPMYKRN VMILTNPVAA KKNISINTVT YEWAPPVQNQ
     ALARQYMQML PKEKQPVAGS EGAQYRKKQL AKQLPAHDQD PSKCHELSPK EVKEMEQFVK
     KYKSEALGVG DVKLPREMNA QGPNRMCIPG GDRSTTSAVG AMEDKSAEHK TTQYSCYCCK
     LSMKEGDPAI YAERAGYDKL WHPACFVCST CHELLVDMIY FWKNDKLYCG RHYCDSEKPR
     CAGCDELIFS NEYTQAENQN WHLKHFCCFD CDNILAGEIY VMVNDKPVCK PCYVKNHAVV
     CQGCHNAIDP EVQRVTYNNF SWHASTECFL CSCCSKCLIG QKFMPVEGMV FCSVECKKMM
     S