ZYX_MOUSE
ID ZYX_MOUSE Reviewed; 564 AA.
AC Q62523; P70461; Q3UGQ3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Zyxin;
GN Name=Zyx;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ICR X Swiss Webster;
RX PubMed=8940160; DOI=10.1074/jbc.271.49.31470;
RA Macalma T., Otte J., Hensler M.E., Bockholt S.M., Louis H.A.,
RA Kalff-Suske M., Grzeschik K.H., von der Ahe D., Beckerle M.C.;
RT "Molecular characterization of human zyxin.";
RL J. Biol. Chem. 271:31470-31478(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Otte J., Heischmann A., Breier G., Beckerle M.C., von der Ahe D.;
RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144 AND SER-336, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-256 AND LYS-263, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [8]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-244, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Adhesion plaque protein. Binds alpha-actinin and the CRP
CC protein. Important for targeting TES and ENA/VASP family members to
CC focal adhesions and for the formation of actin-rich structures. May be
CC a component of a signal transduction pathway that mediates adhesion-
CC stimulated changes in gene expression (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts, via the Pro-rich regions, with the EVH1 domains of
CC ENAH, EVL and VASP. Interacts with the first LIM domain of TES.
CC Interacts with SYNPO2 (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q15942}.
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; Y07711; CAA68984.1; -; mRNA.
DR EMBL; X99063; CAA67510.1; -; mRNA.
DR EMBL; AK147812; BAE28154.1; -; mRNA.
DR EMBL; CH466533; EDL13482.1; -; Genomic_DNA.
DR CCDS; CCDS20066.1; -.
DR RefSeq; NP_001276546.1; NM_001289617.1.
DR RefSeq; NP_001276547.1; NM_001289618.1.
DR RefSeq; NP_001276548.1; NM_001289619.1.
DR RefSeq; NP_035907.1; NM_011777.3.
DR RefSeq; XP_006505999.1; XM_006505936.3.
DR AlphaFoldDB; Q62523; -.
DR SMR; Q62523; -.
DR BioGRID; 204712; 20.
DR IntAct; Q62523; 1.
DR STRING; 10090.ENSMUSP00000126622; -.
DR iPTMnet; Q62523; -.
DR PhosphoSitePlus; Q62523; -.
DR SwissPalm; Q62523; -.
DR EPD; Q62523; -.
DR jPOST; Q62523; -.
DR MaxQB; Q62523; -.
DR PaxDb; Q62523; -.
DR PeptideAtlas; Q62523; -.
DR PRIDE; Q62523; -.
DR ProteomicsDB; 275172; -.
DR Antibodypedia; 1394; 397 antibodies from 43 providers.
DR DNASU; 22793; -.
DR Ensembl; ENSMUST00000164375; ENSMUSP00000126622; ENSMUSG00000029860.
DR Ensembl; ENSMUST00000203652; ENSMUSP00000145451; ENSMUSG00000029860.
DR GeneID; 22793; -.
DR KEGG; mmu:22793; -.
DR UCSC; uc009bqz.2; mouse.
DR CTD; 7791; -.
DR MGI; MGI:103072; Zyx.
DR VEuPathDB; HostDB:ENSMUSG00000029860; -.
DR eggNOG; KOG1701; Eukaryota.
DR GeneTree; ENSGT00940000154273; -.
DR HOGENOM; CLU_001357_10_2_1; -.
DR InParanoid; Q62523; -.
DR OMA; NKPFMVT; -.
DR OrthoDB; 642235at2759; -.
DR PhylomeDB; Q62523; -.
DR TreeFam; TF320310; -.
DR BioGRID-ORCS; 22793; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Zyx; mouse.
DR PRO; PR:Q62523; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q62523; protein.
DR Bgee; ENSMUSG00000029860; Expressed in granulocyte and 241 other tissues.
DR ExpressionAtlas; Q62523; baseline and differential.
DR Genevisible; Q62523; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0005912; C:adherens junction; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005925; C:focal adhesion; IDA:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0001725; C:stress fiber; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007160; P:cell-matrix adhesion; IMP:UniProtKB.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IDA:MGI.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0050727; P:regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0043149; P:stress fiber assembly; ISO:MGI.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; 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 Acetylation; Cell adhesion; Cell junction; Cytoplasm; Cytoskeleton;
KW LIM domain; Metal-binding; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q15942"
FT CHAIN 2..564
FT /note="Zyxin"
FT /id="PRO_0000075914"
FT DOMAIN 376..435
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 436..495
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 496..562
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 30..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..79
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..135
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..216
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q15942"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15942"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15942"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15942"
FT MOD_RES 180
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15942"
FT MOD_RES 244
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 256
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 263
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 265
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15942"
FT MOD_RES 270
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15942"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15942"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15942"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT CONFLICT 215
FT /note="A -> R (in Ref. 1; CAA67510)"
FT /evidence="ECO:0000305"
FT CONFLICT 284..292
FT /note="NQKMVPPDA -> IKKWCLRMP (in Ref. 1; CAA67510)"
FT /evidence="ECO:0000305"
FT CONFLICT 484
FT /note="C -> S (in Ref. 1; CAA67510)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 564 AA; 60546 MW; 98CF20E3E6B8BE9C CRC64;
MAAPRPPPAI SVSVSAPAFY APQKKFAPVV APKPKVNPFR PGDSEPPVAA GAQRAQMGRV
GEIPPPPPED FPLPPPPLIG EGDDSEGALG GAFPPPPPPM IEEPFPPAPL EEDIFPSPPP
PLEEEGGPEA PTQLPPQPRE KVCSIDLEID SLSSLLDDMT KNDPFKARVS SGYVPPPVAT
PFVPKPSTKP APGGTAPLPP WKTPSSSQPP PQPQAKPQVQ LHVQPQAKPH VQPQPVSSAN
TQPRGPLSQA PTPAPKFAPV APKFTPVVSK FSPGAPSGPG PQPNQKMVPP DAPSSVSTGS
PQPPSFTYAQ QKEKPLVQEK QHPQPPPAQN QNQVRSPGGP GPLTLKEVEE LEQLTQQLMQ
DMEHPQRQSV AVNESCGKCN QPLARAQPAV RALGQLFHIT CFTCHQCQQQ LQGQQFYSLE
GAPYCEGCYT DTLEKCNTCG QPITDRMLRA TGKAYHPQCF TCVVCACPLE GTSFIVDQAN
QPHCVPDYHK QYAPRCSVCS EPIMPEPGRD ETVRVVALDK NFHMKCYKCE DCGKPLSIEA
DDNGCFPLDG HVLCRKCHSA RAQT
