ID   TES_EULMM               Reviewed;         421 AA.
AC   Q2IBH0;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=Testin;
GN   Name=TES;
OS   Eulemur macaco macaco (Black lemur).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC   Lemuridae; Eulemur.
OX   NCBI_TaxID=30603;
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 (NOV-2005) 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; DP000024; ABC87432.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2IBH0; -.
DR   SMR; Q2IBH0; -.
DR   PRIDE; Q2IBH0; -.
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; 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; Repeat; Zinc.
FT   CHAIN           1..421
FT                   /note="Testin"
FT                   /id="PRO_0000251901"
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;  48062 MW;  91B5CC2D449218F1 CRC64;
     MDLETKVKKM GLGHEQGFGA PCLKCKEKCE GFELHFWRKI CRNCKCGQEE HDILLSNEED
     RKVGKLFEDT KYTTLIAKLK SDGIPMYKRN VMILTNPVAA RKNVSINTVT YEWAPPVQNQ
     ALARQYMQML PKDKQPVAGS EGAQYRKKQL AKQLPAHDQD PSKCHELSPK EVKEMEQFVK
     KYKNEALGVG DVKLPCELDA RGPNQMYIPG GDRSTSAAVG AMEDKSAEHK NTQYSCYCCK
     MSMKEGDPAI YAERAGYDKL WHPACFVCSI CYELLVDMIY FWKDEKLYCG RHYCDSEKPR
     CAGCDELIFS NEYTQAENQN WHLKHFCCFD CDNILAGEIY VMVNDKPVCK PCYVKNHAVV
     CQGCHNAIDP EVQRVTYNNF SWHASTECFL CSCCSKCLIG QKFMPVEGMV FCSVECKKMM
     S