ID   TES_CHICK               Reviewed;         422 AA.
AC   Q90YH9;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Testin;
GN   Name=TES;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=B-cell;
RA   Griffith E.M., Coutts A., Black D.M.;
RT   "Characterisation of the chick TES gene.";
RL   Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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. May play
CC       a role in the regulation of cell proliferation. May inhibit cell growth
CC       (By similarity). {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 other
CC       proteins. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the prickle / espinas / testin family.
CC       {ECO:0000305}.
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DR   EMBL; AJ315664; CAC42398.1; -; mRNA.
DR   EMBL; DP000235; AAR16239.1; -; Genomic_DNA.
DR   RefSeq; NP_989954.1; NM_204623.1.
DR   AlphaFoldDB; Q90YH9; -.
DR   SMR; Q90YH9; -.
DR   STRING; 9031.ENSGALP00000015293; -.
DR   PaxDb; Q90YH9; -.
DR   PRIDE; Q90YH9; -.
DR   GeneID; 395332; -.
DR   KEGG; gga:395332; -.
DR   CTD; 26136; -.
DR   VEuPathDB; HostDB:geneid_395332; -.
DR   eggNOG; KOG1704; Eukaryota.
DR   HOGENOM; CLU_008937_1_1_1; -.
DR   InParanoid; Q90YH9; -.
DR   OrthoDB; 997264at2759; -.
DR   PhylomeDB; Q90YH9; -.
DR   TreeFam; TF313265; -.
DR   PRO; PR:Q90YH9; -.
DR   Proteomes; UP000000539; Unplaced.
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; IEA:Ensembl.
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   2: Evidence at transcript level;
KW   Cell junction; Cytoplasm; LIM domain; Metal-binding; Reference proteome;
KW   Repeat; Zinc.
FT   CHAIN           1..422
FT                   /note="Testin"
FT                   /id="PRO_0000278803"
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..422
FT                   /note="LIM zinc-binding 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   REGION          198..224
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        202..216
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   422 AA;  47983 MW;  8A66B49D5372C42F CRC64;
     MDLESKVKKM GLGHEQGFGA PCLKCKDKCE GFELHFWRKI CRNCKCGQEE HDVLTSNEED
     RKVGKLFEDT KYTTLIAKLK NDGIPMYKRN VMILTNPVPA KKNISINTVT YEWAPPVQNQ
     TLARQYMQML PKEKQPVAGS EGAQYRKKQL AKQLPAHDQD PSKCHELSPN EVKQMEQFVK
     KYKNEALGVG DVKLPGELET KATDKNNVNS GDRSTSAAVG AMEDKSADQK ASQYSCYRCK
     LNMKEGDPAV YAERAGYDKL WHPACFVCCT CSELLVDMIY FWKNGNLYCG RHYCDSEKPR
     CAGCDELIFS NEYTQAEGQN WHLKHFCCFD CDCVLAGEIY VMVNDKPVCR PCYVKKHAAI
     CQGCHNAIDP EVQRVTYNNF NWHATQECFL CSCCSKCLIG QKFMPVEGMV FCSVECKKKM
     MS