ID   ZYX_XENTR               Reviewed;         674 AA.
AC   Q0VA45;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Zyxin;
GN   Name=zyx {ECO:0000250|UniProtKB:Q04584};
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:AAI21256.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain {ECO:0000312|EMBL:AAI21256.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Adhesion plaque protein. May be a component of a signal
CC       transduction pathway that mediates adhesion-stimulated changes in gene
CC       expression. Suppresses the transcription-repressing activity of
CC       hesx1/anf1 (By similarity). {ECO:0000250|UniProtKB:A5H447,
CC       ECO:0000250|UniProtKB:Q04584}.
CC   -!- SUBUNIT: Interacts (via LIM2 domain) with hesx1/anf1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q04584,
CC       ECO:0000250|UniProtKB:Q15942}. Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:Q04584, ECO:0000250|UniProtKB:Q15942}. Cell
CC       junction, focal adhesion {ECO:0000250}. Note=Associates with the actin
CC       cytoskeleton near the adhesion plaques. Enters the nucleus in the
CC       presence of hesx1 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the zyxin/ajuba family. {ECO:0000255}.
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DR   EMBL; BC121255; AAI21256.1; -; mRNA.
DR   RefSeq; NP_001072265.1; NM_001078797.1.
DR   AlphaFoldDB; Q0VA45; -.
DR   DNASU; 779718; -.
DR   GeneID; 779718; -.
DR   KEGG; xtr:779718; -.
DR   CTD; 7791; -.
DR   Xenbase; XB-GENE-6453993; zyx.
DR   InParanoid; Q0VA45; -.
DR   Proteomes; UP000008143; Chromosome 7.
DR   Proteomes; UP000790000; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
DR   GO; GO:0001725; C:stress fiber; ISS:UniProtKB.
DR   GO; GO:0140297; F:DNA-binding transcription factor binding; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IBA:GO_Central.
DR   InterPro; IPR001781; Znf_LIM.
DR   Pfam; PF00412; LIM; 3.
DR   SMART; SM00132; LIM; 3.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 3.
PE   2: Evidence at transcript level;
KW   Cell adhesion; Cell junction; Cytoplasm; Cytoskeleton; LIM domain;
KW   Metal-binding; Reference proteome; Repeat; Transcription;
KW   Transcription regulation; Zinc.
FT   CHAIN           1..674
FT                   /note="Zyxin"
FT                   /id="PRO_0000331488"
FT   DOMAIN          481..542
FT                   /note="LIM zinc-binding 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   DOMAIN          543..600
FT                   /note="LIM zinc-binding 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   DOMAIN          601..671
FT                   /note="LIM zinc-binding 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   REGION          35..447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..144
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        160..209
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        224..271
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   674 AA;  71365 MW;  BDAA9997C66575C4 CRC64;
     MDPAAPAARM TSSFTINIST PSFYNPPKKF APVVPPKPKV NPFRAAEEPV PQENSAGPGL
     RRAFVGKVGQ IPSMAPPGGD PEDFVLPPPP PNEEPMSPPG SSFPPPPPSF GDDGPGSPLG
     LFPPPPPPEF SEPFPPPIEE SFPSPPPLEE AAGLSDTQDP PASVPPPPPP LPSPPEPAPP
     VLCEAPKPAP VLPKPPPPSA FPKPEPPQSV APKAQSSIFI PKPSPPSAVA PKPVAPPPVA
     AKPSGPGPFV GPSAAPPTHT PAPPAPAHTF SPKPVAGPTF APKSASHTFM AKPSAPVFSP
     KAATEPPTEA PQERFPASQS SPKLTPAAKH EAPPPAAKHE APPPASATRA PGFSFAQQRD
     KPRVLEKPRA NVRDLVPEPP VETRGERTLG PQAEGGRSFG AQPIGGKDTK PLPEGLRNQT
     PDGTHRVGGQ PGTHRPTPHQ DQTSGSQGLN MKEVEELEML TQQLMQEMDK PTPAAEAHTM
     ELCGFCGRGL SRTETVVRAG EHLYHVTCFT CSKCEQQLQG QQYYESAGKP LCEECYQDTL
     ECCAVCEKKI TERLLRAIGQ AYHPSCFTCA VCKCSLQGEP FIVDDNKLPH CVSDYHRRYA
     PRCTVCGDPI APEPGRDETV RVVALEKNFH MMCYKCEDCG CPLSIEADDG GCFPLDGHVL
     CKKCHTVRAR AALG