TES_XENLA
ID TES_XENLA Reviewed; 422 AA.
AC Q7ZXE9;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Testin;
DE AltName: Full=Xtes;
GN Name=tes {ECO:0000250|UniProtKB:Q9UGI8};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000312|EMBL:AAH45027.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000312|EMBL:AAH45027.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=16554046; DOI=10.1016/j.ydbio.2006.02.004;
RA Dingwell K.S., Smith J.C.;
RT "Tes regulates neural crest migration and axial elongation in Xenopus.";
RL Dev. Biol. 293:252-267(2006).
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.
CC {ECO:0000250, ECO:0000269|PubMed:16554046}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:16554046}. Cell junction, focal adhesion
CC {ECO:0000250}. Note=Detected along actin stress fibers. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in the animal hemisphere at the 4-cell
CC stage. By stage 18, expressed in cells adjacent to the anterior neural
CC plate. In late neurula, expressed in the cranial neural crest. At tail
CC bud stages, expressed strongly in the head, ventral to the developing
CC eye, branchial arches and lateral line placodes. Also localized in the
CC otic vesicle, dorsal fin and notochord with weaker expression at
CC intersomitic junctions of tail bud embryos.
CC {ECO:0000269|PubMed:16554046}.
CC -!- DEVELOPMENTAL STAGE: Expressed maternally. Expression levels decline
CC during the cleavage stages with only weak expression by gastrula
CC stages. Levels then increase at neurula stages and are high in tail bud
CC embryos. {ECO:0000269|PubMed:16554046}.
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}.
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; BC045027; AAH45027.1; -; mRNA.
DR RefSeq; NP_001080706.1; NM_001087237.1.
DR AlphaFoldDB; Q7ZXE9; -.
DR SMR; Q7ZXE9; -.
DR DNASU; 380398; -.
DR GeneID; 380398; -.
DR CTD; 380398; -.
DR Xenbase; XB-GENE-6253774; tes.L.
DR OMA; NKLWHPA; -.
DR OrthoDB; 997264at2759; -.
DR Proteomes; UP000186698; Genome assembly.
DR Bgee; 380398; Expressed in lung and 18 other tissues.
DR GO; GO:0005938; C:cell cortex; IDA: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; IMP: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_0000283795"
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; 47731 MW; C4DB2B9CB3A788A1 CRC64;
MELENKFKKV TLGHEEGSGA PCLKCKEKCE GFELHFWRKI CRNCKCGQEE HSVLSNNEDD
RKVGKLFEDT KYTALIAKLK TDGIPTYKRN VMILTSPVAA KKDVSINTVT YEWAPPVQNQ
ALARRYMELI PKDKQPVAGS EGAQYRKKQL AKQLPAHDQD PSKCHELSPN EVKQMEQFVK
KYKNEVLGVG DVKLPKEVEA QASGAGRSTN GSLSTLTTVK STDDKVAAQK GSTYYCFRCK
ENMREGDPAV YAERAGYDKL WHPSCFVCFT CNELLVDMIY FWKNGKLYCG RHYCDSEKPR
CAGCDELIFS NEYTQAEGLN WHLKHFCCFD CDIVLAGEIY VMVNDKAVCK PCYVKNHAVS
CQGCHNAIDP EVQRVSYNGF HWHAAPECFI CSCCSKCLIG QKFMPIEGMV FCSVECKKKM
SS
