TES_PAPAN
ID TES_PAPAN Reviewed; 421 AA.
AC A0M8R4;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Testin;
GN Name=TES;
OS Papio anubis (Olive baboon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Papio.
OX NCBI_TaxID=9555;
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; DP000233; ABK34428.1; -; Genomic_DNA.
DR RefSeq; NP_001162184.1; NM_001168713.1.
DR AlphaFoldDB; A0M8R4; -.
DR SMR; A0M8R4; -.
DR STRING; 9555.ENSPANP00000016608; -.
DR Ensembl; ENSPANT00000006264; ENSPANP00000016607; ENSPANG00000008934.
DR GeneID; 100126668; -.
DR KEGG; panu:100126668; -.
DR CTD; 26136; -.
DR eggNOG; KOG1704; Eukaryota.
DR GeneTree; ENSGT00940000155993; -.
DR OrthoDB; 997264at2759; -.
DR Proteomes; UP000028761; Chromosome 4.
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; 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_0000278800"
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; 47957 MW; FECFE4F69C566249 CRC64;
MDLENKVKKM GLGHEQGFGA PCLKCKEKCE GFELHFWRKI CRNCKCGQEE HDVLLSNEED
RKVGKLFEDT KYTTLIAKLK SDGIPMYKRN VMILTNPVAA KKNVSINTVT YEWAPPVQNQ
ALARQYMQML PKEKQPVAGS EGAQYRKKQL AKQLPAHDQD PSKCHELSPR EVKEMEQFVK
KYKSEALGVG DVKLPCEMDA QGPKQMNIPG GDRSTPAAVG AMEDKSAEHK RTQYSCYCCK
LSMKEGDPAI YAERAGYDKL WHPACFVCST CHELLVDMIY FWKNEKLYCG RHYCDSEKPR
CAGCDELIFS NEYTQAENQN WHLKHFCCFD CDSILAGEIY VMVNDKPVCK PCYVKNHAVV
CQGCHNAIDP EVQRVSYNNF SWHASTECFL CSCCSKCLIG QKFMPVEGMV FCSVECKKMM
S
