ID   TES_XENTR               Reviewed;         422 AA.
AC   Q6DIR5;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Testin;
GN   Name=tes {ECO:0000312|EMBL:CAJ82802.1}; ORFNames=TNeu019j18.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1] {ECO:0000312|EMBL:CAJ82802.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Neurula {ECO:0000312|EMBL:CAJ82802.1};
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000312|EMBL:CAJ82802.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Tail bud {ECO:0000312|EMBL:AAH75470.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) 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. May
CC       inhibit cell growth (By similarity). Regulates cranial neural crest
CC       migration. Acts together with prickle1 to control axial elongation (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000250}. Cell
CC       junction, focal adhesion {ECO:0000250}. Note=Detected along actin
CC       stress fibers. {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; CR942607; CAJ82802.1; -; mRNA.
DR   EMBL; BC075470; AAH75470.1; -; mRNA.
DR   RefSeq; NP_001004961.1; NM_001004961.2.
DR   AlphaFoldDB; Q6DIR5; -.
DR   SMR; Q6DIR5; -.
DR   STRING; 8364.ENSXETP00000025315; -.
DR   PaxDb; Q6DIR5; -.
DR   DNASU; 448383; -.
DR   Ensembl; ENSXETT00000088298; ENSXETP00000099469; ENSXETG00000011568.
DR   GeneID; 448383; -.
DR   KEGG; xtr:448383; -.
DR   CTD; 26136; -.
DR   Xenbase; XB-GENE-1015357; tes.
DR   eggNOG; KOG1704; Eukaryota.
DR   HOGENOM; CLU_008937_1_1_1; -.
DR   InParanoid; Q6DIR5; -.
DR   OMA; NKLWHPA; -.
DR   OrthoDB; 997264at2759; -.
DR   PhylomeDB; Q6DIR5; -.
DR   TreeFam; TF313265; -.
DR   Proteomes; UP000008143; Chromosome 3.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000011568; Expressed in ovary and 11 other tissues.
DR   GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
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:0001755; P:neural crest cell migration; ISS:UniProtKB.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Cell junction; Cytoplasm; Developmental protein; LIM domain; Metal-binding;
KW   Reference proteome; Repeat; Zinc.
FT   CHAIN           1..422
FT                   /note="Testin"
FT                   /id="PRO_0000283796"
FT   DOMAIN          92..199
FT                   /note="PET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00636"
FT   DOMAIN          234..299
FT                   /note="LIM zinc-binding 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   DOMAIN          300..359
FT                   /note="LIM zinc-binding 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   DOMAIN          360..422
FT                   /note="LIM zinc-binding 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   REGION          135..165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        151..165
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   422 AA;  47846 MW;  F9C0D4E8FD4560CD CRC64;
     MELENKLKKV TLGHEEGFGA PCLKCKEKCE GFELHFWRKV CRNCKCGQEE HSILSNNEDD
     RKVGKLFEDT KYTALIAKLK TDGIPTYKRN VMILTSPVAA KKDVSINTVT YEWAPPVQNQ
     ALARRYMELI PKDKQPVAGS EGAQYRKKQL AKQLPAHDQD PSKCHELSPN EVKQMEQFVK
     KYKNEVLGVG DVKLPKEVEA QACGAGRSTN GSLSTLTTVK GTEDKVAAQK ESTYYCFRCK
     ENMREGDPAV YAERAGYDKL WHPSCFVCFT CNELLVDMIY FWKNGKLYCG RHYCDSEKPR
     CAGCDELIFS NEYTQAEGLN WHLKHFCCFD CDCVLAGEIY VMVNDKPVCK LCYVKNHAVS
     CQGCHNAIDP EVQRVSYNGF HWHAAPECFI CSCCSKCLIG QKFMPIQGMV FCSVDCKKKM
     SS