ID   ZYX_XENLA               Reviewed;         663 AA.
AC   A5H447;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Zyxin;
GN   Name=zyx {ECO:0000250|UniProtKB:Q04584};
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:0000305, ECO:0000312|EMBL:ABM66816.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH HESX1, TISSUE
RP   SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Embryo {ECO:0000269|PubMed:18297730};
RX   PubMed=18297730; DOI=10.1002/dvdy.21471;
RA   Martynova N.Y., Eroshkin F.M., Ermolina L.V., Ermakova G.V.,
RA   Korotaeva A.L., Smurova K.M., Gyoeva F.K., Zaraisky A.G.;
RT   "The LIM-domain protein zyxin binds the homeodomain factor Xanf1/Hesx1 and
RT   modulates its activity in the anterior neural plate of Xenopus laevis
RT   embryo.";
RL   Dev. Dyn. 237:736-749(2008).
CC   -!- FUNCTION: Adhesion plaque protein. May be a component of a signal
CC       transduction pathway that mediates adhesion-stimulated changes in gene
CC       expression (By similarity). Suppresses the transcription-repressing
CC       activity of hesx1/anf1. {ECO:0000250|UniProtKB:Q04584,
CC       ECO:0000269|PubMed:18297730}.
CC   -!- SUBUNIT: Interacts (via LIM2 domain) with hesx1/anf1.
CC       {ECO:0000269|PubMed:18297730}.
CC   -!- INTERACTION:
CC       A5H447; Q91898: hesx1-b; NbExp=5; IntAct=EBI-5651620, EBI-5651634;
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. {ECO:0000250|UniProtKB:Q04584,
CC       ECO:0000250|UniProtKB:Q15942}.
CC   -!- TISSUE SPECIFICITY: At the early gastrula stage, expressed at a low
CC       level in the animal hemisphere. Expression rises by the end of
CC       gastrulation in the anterior part of the embryo, where it gradually
CC       increases by the midneurula stage. During neurulation, expression
CC       continues most intensively in the anterior part of the neural plate and
CC       around it. At later stages, intensely expressed in the brain and at
CC       lower levels in the spinal cord, eyes, nasal placodes, within somites,
CC       and around the cement gland. {ECO:0000269|PubMed:18297730}.
CC   -!- DEVELOPMENTAL STAGE: Expressed at a low level at early stages.
CC       Expression increases during gastrulation, reaches maximum levels by the
CC       middle of neurulation, and slightly decreases during later development.
CC       {ECO:0000269|PubMed:18297730}.
CC   -!- SIMILARITY: Belongs to the zyxin/ajuba family. {ECO:0000255}.
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DR   EMBL; EF051627; ABM66816.1; -; mRNA.
DR   RefSeq; NP_001092151.1; NM_001098681.1.
DR   AlphaFoldDB; A5H447; -.
DR   IntAct; A5H447; 1.
DR   GeneID; 100049724; -.
DR   KEGG; xla:100049724; -.
DR   CTD; 100049724; -.
DR   Xenbase; XB-GENE-6253946; zyx.S.
DR   OrthoDB; 642235at2759; -.
DR   Proteomes; UP000186698; Chromosome 7S.
DR   Bgee; 100049724; Expressed in neurula embryo and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IPI:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003712; F:transcription coregulator activity; IDA:UniProtKB.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:UniProtKB.
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   1: Evidence at protein level;
KW   Cell adhesion; Cell junction; Cytoplasm; Cytoskeleton; LIM domain;
KW   Metal-binding; Reference proteome; Repeat; Transcription;
KW   Transcription regulation; Zinc.
FT   CHAIN           1..663
FT                   /note="Zyxin"
FT                   /id="PRO_0000331487"
FT   DOMAIN          470..531
FT                   /note="LIM zinc-binding 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   DOMAIN          532..589
FT                   /note="LIM zinc-binding 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   DOMAIN          590..660
FT                   /note="LIM zinc-binding 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   REGION          35..438
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..111
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        119..144
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        158..211
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        227..262
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        265..282
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        295..316
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        373..390
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        422..438
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   663 AA;  70725 MW;  27158AB024B69B21 CRC64;
     MDPAAPATRM TSSFTINIST PSFYNPPKKF APVVPPKPKI NPFKAPEEPQ SLVPQENSAG
     PGLHQAFVGK VGEMPPGVDH DDFVLPPPPP SEESISPPSS SFPPPPPSFG DEGLGSPSGG
     SFPPPPPPEF SEPFPPPIEE FFPSPPPLEE CVSDTQDLPV PVPPPPPPPL PSPPAAPPPK
     PSAPCEAPKP APVFPKSSPP PAFPKPEPPS VAPKAASSIF IPKPSAPMAV APKPLAPPPV
     AAKPSGPVSF APPSPAPHTF SPDPSAPAHT FSPKTVTFSP KSAPHTFMPK PSAPVTYPQK
     TTEPPAEASQ SSPKVTPAAK HEAPPPTVPS GGRAPGFSFA QQRERPRVLE KPRANLQGSE
     PEHEPTVEVQ VERTRSLGPQ TESGRSPGAQ STGGKDMKPL PEGLRSQKPM SDGIHRTGGQ
     HSGHKVTGQQ DQTLGSQGLN MKEVEELEML TQQLMREMDK PPTAEAHSME LCGFCGRGLS
     RTETVVRAGE HLYHVACFTC SRCDQQLQGQ QYYESAGKPL CDECYQDTLE CCAVCDKKIT
     ERLLKAIGKS YHPSCFTCAV CKCSLQGEPF IVDDNKLPHC VNDYHRRYAP RCCVCGDPIA
     PEPGRDETVR VVALEKNFHM MCYKCEDCGC PLSIEADDAG CFPLDGHVLC KKCHTVRARA
     ALG