TES_RABIT
ID TES_RABIT Reviewed; 421 AA.
AC Q09YN8;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Testin;
GN Name=TES;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
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 (SEP-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; DP000006; AAY89009.1; -; Genomic_DNA.
DR RefSeq; NP_001164512.1; NM_001171041.1.
DR AlphaFoldDB; Q09YN8; -.
DR SMR; Q09YN8; -.
DR STRING; 9986.ENSOCUP00000007339; -.
DR GeneID; 100126564; -.
DR KEGG; ocu:100126564; -.
DR CTD; 26136; -.
DR eggNOG; KOG1704; Eukaryota.
DR InParanoid; Q09YN8; -.
DR OrthoDB; 997264at2759; -.
DR Proteomes; UP000001811; 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; 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_0000260335"
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; 47833 MW; 9FAD2819E94C3201 CRC64;
MDLDSKMKKM GLGHEQGFGA PCLKCKEKCE GFELHFWRKI CRNCKCGQEE HDVLLSNEED
RKVGRLFEDT KYTTLIAKLK TDGIPMYKRN VMILTNPVAA KKNVSINTVT YEWAPPVQNQ
ALARQYMQML PKEKQPVAGS EGAQYRKKQL AKQLPAHDQD PSKCHELSPK EVKEMEQFVK
KYKSEALGVG DVKLPYEMGG PSPDKLYIPA GDRSTPAALG PMESKPAECK GTQYFCYCCK
LSMKEGDPAI YAERAGYDKL WHPACFVCST CSELLVDMIY FWKNGKLFCG RHYCDSEKPR
CAGCDELIFS NEYTQAENQN WHLKHFCCFD CDNILAGEIY VMVNDKPVCK PCYVKNHAVV
CQGCHNAIDP EVQRVTYNDF SWHASTQCFL CSCCSKCLIG QKFMPVEGMV FCSVECKKMM
S