ID   ZYX_CHICK               Reviewed;         542 AA.
AC   Q04584;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Zyxin;
GN   Name=ZYX;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=1469049; DOI=10.1083/jcb.119.6.1573;
RA   Sadler I., Crawford A.W., Michelsen J.W., Beckerle M.C.;
RT   "Zyxin and cCRP: two interactive LIM domain proteins associated with the
RT   cytoskeleton.";
RL   J. Cell Biol. 119:1573-1587(1992).
CC   -!- FUNCTION: Adhesion plaque protein. Binds alpha-actinin and the CRP
CC       protein. May be a component of a signal transduction pathway that
CC       mediates adhesion-stimulated changes in gene expression.
CC       {ECO:0000269|PubMed:1469049}.
CC   -!- INTERACTION:
CC       Q04584; P05094-2: ACTN1; NbExp=4; IntAct=EBI-6222189, EBI-6049246;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC       {ECO:0000250}. Cell junction, focal adhesion {ECO:0000250}. Nucleus
CC       {ECO:0000250}. Note=Associates with the actin cytoskeleton near the
CC       adhesion plaques. Enters the nucleus in the presence of HESX1 (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the zyxin/ajuba family. {ECO:0000305}.
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DR   EMBL; X69190; CAA48936.1; -; mRNA.
DR   PIR; A44358; A44358.
DR   RefSeq; NP_001004386.1; NM_001004386.1.
DR   AlphaFoldDB; Q04584; -.
DR   SMR; Q04584; -.
DR   ELM; Q04584; -.
DR   IntAct; Q04584; 1.
DR   STRING; 9031.ENSGALP00000023626; -.
DR   PaxDb; Q04584; -.
DR   Ensembl; ENSGALT00000023672; ENSGALP00000023626; ENSGALG00000014688.
DR   Ensembl; ENSGALT00000099039; ENSGALP00000074295; ENSGALG00000014688.
DR   GeneID; 418300; -.
DR   KEGG; gga:418300; -.
DR   CTD; 7791; -.
DR   VEuPathDB; HostDB:geneid_418300; -.
DR   eggNOG; KOG1701; Eukaryota.
DR   GeneTree; ENSGT00940000154273; -.
DR   HOGENOM; CLU_001357_10_2_1; -.
DR   InParanoid; Q04584; -.
DR   OrthoDB; 642235at2759; -.
DR   PhylomeDB; Q04584; -.
DR   TreeFam; TF320310; -.
DR   PRO; PR:Q04584; -.
DR   Proteomes; UP000000539; Chromosome 1.
DR   Bgee; ENSGALG00000014688; Expressed in granulocyte and 13 other tissues.
DR   ExpressionAtlas; Q04584; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:AgBase.
DR   GO; GO:0005925; C:focal adhesion; IDA:AgBase.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0001725; C:stress fiber; IDA:AgBase.
DR   GO; GO:0051393; F:alpha-actinin binding; IPI:AgBase.
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: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   1: Evidence at protein level;
KW   Cell adhesion; Cell junction; Cytoplasm; Cytoskeleton; LIM domain;
KW   Metal-binding; Nucleus; Reference proteome; Repeat; Zinc.
FT   CHAIN           1..542
FT                   /note="Zyxin"
FT                   /id="PRO_0000075915"
FT   DOMAIN          352..411
FT                   /note="LIM zinc-binding 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   DOMAIN          412..471
FT                   /note="LIM zinc-binding 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   DOMAIN          472..538
FT                   /note="LIM zinc-binding 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   REGION          22..319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..61
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        100..136
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        208..235
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        243..267
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VARIANT         463
FT                   /note="D -> V"
SQ   SEQUENCE   542 AA;  58538 MW;  9D898AC180C680FC CRC64;
     MASPGTPGTR MTTTVSINIS TPSFYNPQKK FAPVVAPKPK VNPFKTGGTS ESSQPQPPGT
     GAQRAQIGRV GEIPVSVTAE ELPLPPPPPP GEELSFSSNC AFPPPPPPFE EPFPPAPDEA
     FPSPPPPPPP MFDEGPALQI PPGSTGSVEK PLAPKAHVEI SSAPRDPTPP FPSKFTPKPS
     GTLSSKPPGL DSTPAPAPWA APQQRKEPLA SVPPPPSLPS QPTAKFTPPP VASSPGSKPG
     ATVPMAPSNS TRYPTSLQTQ FTAPSPSGPL SRPQPPNFTY AQQWERPQVQ EKPVPTEKSA
     AVKDMRRPTA DPPKGNSPLT MKEVEELELL TQKLMKDMDH PPPVEAATSE LCGFCRKPLS
     RTQPAVRALD CLFHVECFTC FKCEKQLQGQ QFYNVDEKPF CEDCYAGTLE KCSVCKQTIT
     DRMLKATGNS YHPQCFTCVM CHTPLEGASF IVDQANQPHC VDDYHRKYAP RCSVCSEPIM
     PEPGKDETVR VVALEKNFHM KCYKCEDCGR PLSIEADENG CFPLDGHVLC MKCHTVRAKT
     AC