ID   TES_RHIFE               Reviewed;         421 AA.
AC   Q2IBC3;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 56.
DE   RecName: Full=Testin;
GN   Name=TES;
OS   Rhinolophus ferrumequinum (Greater horseshoe bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Rhinolophidae;
OC   Rhinolophinae; Rhinolophus.
OX   NCBI_TaxID=59479;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Antonellis A., Ayele K., Benjamin B., Blakesley R.W., Boakye A.,
RA   Bouffard G.G., Brinkley C., Brooks S., Chu G., Coleman H., Engle J.,
RA   Gestole M., Greene A., Guan X., Gupta J., Haghighi P., Han J., Hansen N.,
RA   Ho S.-L., Hu P., Hunter G., Hurle B., Idol J.R., Kwong P., Laric P.,
RA   Larson S., Lee-Lin S.-Q., Legaspi R., Madden M., Maduro Q.L., Maduro V.B.,
RA   Margulies E.H., Masiello C., Maskeri B., McDowell J., Mojidi H.A.,
RA   Mullikin J.C., Oestreicher J.S., Park M., Portnoy M.E., Prasad A., Puri O.,
RA   Reddix-Dugue N., Schandler K., Schueler M.G., Sison C., Stantripop S.,
RA   Stephen E., Taye A., Thomas J.W., Thomas P.J., Tsipouri V., Ung L.,
RA   Vogt J.L., Wetherby K.D., Young A., Green E.D.;
RT   "NISC comparative sequencing initiative.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; DP000028; ABC87469.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2IBC3; -.
DR   SMR; Q2IBC3; -.
DR   Proteomes; UP000472240; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
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; 3.
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_0000251902"
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          134..164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   421 AA;  47661 MW;  BA01B252D56F1112 CRC64;
     MDLAVKVKKM GLGHEQGFGA PCLKCKEKCE GFELHFWRKI CRNCKCGQEE HDVLLSNEED
     RKVGKLFEDT KYTTLIAKLK SDGIPMYKRN VMILTNPVAA KKNVSINTVT YEWAPPVQNQ
     ALARHYMQML PKEKQPVAGS EGAQYRKKQL AKQLPAHDQD PSKCHELSPK EVKEMEQFVK
     KYKSEALGVG DVKLPREMDA QGPPRIDSPG GDRSTAAAVG AMDGKSAEHR RTQYSCYCCK
     LSMKEGDPAI YAERAGYDKL WHPACFVCST CEELLVDMIY FWKNGKLYCG RHYCDSEKPR
     CAGCDELIFS NEYTQAENQN WHLKHFCCFD CDNILAGEIY VMVDDKPVCK PCYVKNHAVV
     CQGCHNAIDP EVQRVTYNGF SWHAAAECFL CSCCSKCLLG QKFMPVEGMV FCSVECKKMM
     S