ZYX_CAEEL
ID ZYX_CAEEL Reviewed; 603 AA.
AC Q9U3F4; H2L2F5; H2L2F6; H2L2F7; Q9U3F5;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Zyxin {ECO:0000312|WormBase:F42G4.3a};
GN Name=zyx-1 {ECO:0000312|WormBase:F42G4.3a};
GN ORFNames=F42G4.3 {ECO:0000312|WormBase:F42G4.3a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP INTERACTION WITH GLH-1 AND GLH-3.
RX PubMed=12435362; DOI=10.1006/dbio.2002.0832;
RA Smith P., Leung-Chiu W.-M., Montgomery R., Orsborn A., Kuznicki K.,
RA Gressman-Coberly E., Mutapcic L., Bennett K.;
RT "The GLH proteins, Caenorhabditis elegans P granule components, associate
RT with CSN-5 and KGB-1, proteins necessary for fertility, and with ZYX-1, a
RT predicted cytoskeletal protein.";
RL Dev. Biol. 251:333-347(2002).
RN [3] {ECO:0000305}
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH DYC-1.
RX PubMed=18094057; DOI=10.1091/mbc.e07-05-0497;
RA Lecroisey C., Martin E., Mariol M.C., Granger L., Schwab Y., Labouesse M.,
RA Segalat L., Gieseler K.;
RT "DYC-1, a protein functionally linked to dystrophin in Caenorhabditis
RT elegans is associated with the dense body, where it interacts with the
RT muscle LIM domain protein ZYX-1.";
RL Mol. Biol. Cell 19:785-796(2008).
RN [4] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=23427270; DOI=10.1091/mbc.e12-09-0679;
RA Lecroisey C., Brouilly N., Qadota H., Mariol M.C., Rochette N.C.,
RA Martin E., Benian G.M., Segalat L., Mounier N., Gieseler K.;
RT "ZYX-1, the unique zyxin protein of Caenorhabditis elegans, is involved in
RT dystrophin-dependent muscle degeneration.";
RL Mol. Biol. Cell 24:1232-1249(2013).
RN [5] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DOMAIN.
RX PubMed=25252943; DOI=10.1242/dev.108217;
RA Luo S., Schaefer A.M., Dour S., Nonet M.L.;
RT "The conserved LIM domain-containing focal adhesion protein ZYX-1 regulates
RT synapse maintenance in Caenorhabditis elegans.";
RL Development 141:3922-3933(2014).
CC -!- FUNCTION: Functions as both a mechanical stabilizer (via LIM domains)
CC of focal adhesions and as a sensor component for muscle cell damage
CC (via N-terminus) (PubMed:23427270). Regulates, stabilizes and maintains
CC posterior lateral mechanosensory (PLM) synaptic branch extension and
CC new synapse formation and growth during larval development
CC (PubMed:25252943). {ECO:0000269|PubMed:23427270,
CC ECO:0000269|PubMed:25252943}.
CC -!- SUBUNIT: Interacts with dyc-1 (PubMed:18094057, PubMed:23427270).
CC Interacts with glh-1 and glh-3 (PubMed:12435362).
CC {ECO:0000269|PubMed:12435362, ECO:0000269|PubMed:18094057,
CC ECO:0000269|PubMed:23427270}.
CC -!- INTERACTION:
CC Q9U3F4; O01836: glh-3; NbExp=2; IntAct=EBI-322208, EBI-1571750;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18094057,
CC ECO:0000269|PubMed:23427270, ECO:0000269|PubMed:25252943}. Cytoplasm
CC {ECO:0000269|PubMed:25252943}. Cytoplasm, myofibril, sarcomere, M line
CC {ECO:0000269|PubMed:18094057, ECO:0000269|PubMed:23427270}. Cell
CC projection, axon {ECO:0000269|PubMed:23427270}. Cell junction, focal
CC adhesion {ECO:0000269|PubMed:23427270}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:23427270}. Note=Shuttles between dense bodies and M
CC lines (PubMed:18094057, PubMed:23427270). Localizes to nucleus in body
CC wall muscle cells. Highly mobile in cytoplasm. Mobility seems to depend
CC on atn-1 (PubMed:23427270). {ECO:0000269|PubMed:18094057,
CC ECO:0000269|PubMed:23427270}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=5;
CC Name=a {ECO:0000312|WormBase:F42G4.3a}; Synonyms=ZYX-1A
CC {ECO:0000303|PubMed:12435362};
CC IsoId=Q9U3F4-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:F42G4.3b}; Synonyms=ZYX-1B
CC {ECO:0000303|PubMed:23427270};
CC IsoId=Q9U3F4-2; Sequence=VSP_057539;
CC Name=c {ECO:0000312|WormBase:F42G4.3c};
CC IsoId=Q9U3F4-3; Sequence=VSP_057541;
CC Name=d {ECO:0000312|WormBase:F42G4.3d};
CC IsoId=Q9U3F4-4; Sequence=VSP_057540;
CC Name=e {ECO:0000312|WormBase:F42G4.3e};
CC IsoId=Q9U3F4-5; Sequence=VSP_057542;
CC -!- TISSUE SPECIFICITY: Expressed in neurons and body wall muscle
CC (PubMed:18094057, PubMed:23427270, PubMed:25252943). Expressed in
CC pharyngeal, enteric and uterine muscles and in spermatheca
CC (PubMed:25252943). {ECO:0000269|PubMed:18094057,
CC ECO:0000269|PubMed:23427270, ECO:0000269|PubMed:25252943}.
CC -!- DEVELOPMENTAL STAGE: Expressed in neurons and muscle throughout
CC development. {ECO:0000269|PubMed:25252943}.
CC -!- DOMAIN: The LIM domains are sufficient for the role in PLM
CC synaptogenesis. {ECO:0000269|PubMed:25252943}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knock-down of isoform a in a dys-
CC 1/hlh-1 double mutant background reduces muscle degeneration.
CC {ECO:0000269|PubMed:23427270}.
CC -!- MISCELLANEOUS: [Isoform b]: Produced by alternative promoter usage.
CC {ECO:0000303|PubMed:25252943}.
CC -!- MISCELLANEOUS: [Isoform c]: Produced by alternative promoter usage.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform d]: Produced by alternative promoter usage.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform e]: Produced by alternative splicing of isoform
CC a. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the zyxin/ajuba family. {ECO:0000305}.
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DR EMBL; Z81082; CAB03095.2; -; Genomic_DNA.
DR EMBL; Z81082; CAB03096.2; -; Genomic_DNA.
DR EMBL; Z81082; CCE71325.1; -; Genomic_DNA.
DR EMBL; Z81082; CCE71326.1; -; Genomic_DNA.
DR EMBL; Z81082; CCE71327.1; -; Genomic_DNA.
DR PIR; C88346; C88346.
DR PIR; T22111; T22111.
DR RefSeq; NP_001254364.1; NM_001267435.1. [Q9U3F4-5]
DR RefSeq; NP_001254365.1; NM_001267436.1. [Q9U3F4-3]
DR RefSeq; NP_001254366.1; NM_001267437.1. [Q9U3F4-4]
DR RefSeq; NP_496776.1; NM_064375.6. [Q9U3F4-1]
DR RefSeq; NP_496777.2; NM_064376.5. [Q9U3F4-2]
DR AlphaFoldDB; Q9U3F4; -.
DR SMR; Q9U3F4; -.
DR DIP; DIP-25080N; -.
DR IntAct; Q9U3F4; 11.
DR STRING; 6239.F42G4.3e.2; -.
DR EPD; Q9U3F4; -.
DR PaxDb; Q9U3F4; -.
DR PeptideAtlas; Q9U3F4; -.
DR EnsemblMetazoa; F42G4.3a.1; F42G4.3a.1; WBGene00006999. [Q9U3F4-1]
DR EnsemblMetazoa; F42G4.3a.2; F42G4.3a.2; WBGene00006999. [Q9U3F4-1]
DR EnsemblMetazoa; F42G4.3b.1; F42G4.3b.1; WBGene00006999. [Q9U3F4-2]
DR EnsemblMetazoa; F42G4.3c.1; F42G4.3c.1; WBGene00006999. [Q9U3F4-3]
DR EnsemblMetazoa; F42G4.3d.1; F42G4.3d.1; WBGene00006999. [Q9U3F4-4]
DR EnsemblMetazoa; F42G4.3e.1; F42G4.3e.1; WBGene00006999. [Q9U3F4-5]
DR GeneID; 174951; -.
DR KEGG; cel:CELE_F42G4.3; -.
DR UCSC; F42G4.3a.1; c. elegans.
DR CTD; 174951; -.
DR WormBase; F42G4.3a; CE23716; WBGene00006999; zyx-1. [Q9U3F4-1]
DR WormBase; F42G4.3b; CE46653; WBGene00006999; zyx-1. [Q9U3F4-2]
DR WormBase; F42G4.3c; CE46595; WBGene00006999; zyx-1. [Q9U3F4-3]
DR WormBase; F42G4.3d; CE10324; WBGene00006999; zyx-1. [Q9U3F4-4]
DR WormBase; F42G4.3e; CE46698; WBGene00006999; zyx-1. [Q9U3F4-5]
DR eggNOG; KOG1701; Eukaryota.
DR GeneTree; ENSGT00940000168198; -.
DR HOGENOM; CLU_452874_0_0_1; -.
DR OMA; VALNTKW; -.
DR OrthoDB; 1040359at2759; -.
DR PhylomeDB; Q9U3F4; -.
DR Reactome; R-CEL-446353; Cell-extracellular matrix interactions.
DR SignaLink; Q9U3F4; -.
DR PRO; PR:Q9U3F4; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00006999; Expressed in larva and 3 other tissues.
DR GO; GO:0015629; C:actin cytoskeleton; ISS:WormBase.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; ISS:WormBase.
DR GO; GO:0031430; C:M band; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0001725; C:stress fiber; IBA:GO_Central.
DR GO; GO:0055120; C:striated muscle dense body; IDA:WormBase.
DR GO; GO:0017151; F:DEAD/H-box RNA helicase binding; IPI:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0099558; P:maintenance of synapse structure; IMP:WormBase.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0006939; P:smooth muscle contraction; IMP:WormBase.
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 Alternative promoter usage; Alternative splicing; Cell adhesion;
KW Cell junction; Cell projection; Cytoplasm; Cytoskeleton; LIM domain;
KW Metal-binding; Neurogenesis; Nucleus; Reference proteome; Repeat; Zinc.
FT CHAIN 1..603
FT /note="Zyxin"
FT /id="PRO_0000432626"
FT DOMAIN 409..470
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 471..529
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 530..601
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 1..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 310..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..409
FT /note="MGPPPPPPPPPLLPSGEILPSRKWKTEDAPRRNNHPAPAPPKPSRPTVDASA
FT LQHAAARLRKTGYNEPVRGDVENLSDGRLDRPHQQLPDGDRTYRANLQQLAQPKTRAEI
FT PSPPTYSNQPRPLGDFHRDPNALSQFQQSREALLSSTSPTSNYSPINKFSSSTLTQYAN
FT KSPSPPSFGNSNSEATYVSPYSSKHSYPTNFRSYHKDDDYFNNTATTATTTTSSNSLNE
FT NNNSNKYGNKETVLQWSEPYDPSKIRRSQSPIRNAREMIHEYSTTNYVTEVQQPPPPPP
FT DLYQRMTQARTFLQNSLAKQLRDEGLTESQKAANRNQTGALSASSSIPFDASQIVKNSY
FT NGDEVDHLVHQMRTKLNQPADTSPSIVQYPRRQAPDSSRANYSATTSTSFSSSTTRKIM
FT NIN -> MADQED (in isoform b)"
FT /id="VSP_057539"
FT VAR_SEQ 1..358
FT /note="Missing (in isoform d)"
FT /id="VSP_057540"
FT VAR_SEQ 1..266
FT /note="Missing (in isoform c)"
FT /id="VSP_057541"
FT VAR_SEQ 575..603
FT /note="LEGQGCYPIDNHLLCKTCNGNRLRVVSST -> KECEFTKCKWFFEYGCQPP
FT DDLDINGGHLELCSGALFIRHLCCKFHKNQRYLGRHVEHNPKQFEFIPSLARLQ (in
FT isoform e)"
FT /id="VSP_057542"
SQ SEQUENCE 603 AA; 66774 MW; 05417BEEBF2292EA CRC64;
MGPPPPPPPP PLLPSGEILP SRKWKTEDAP RRNNHPAPAP PKPSRPTVDA SALQHAAARL
RKTGYNEPVR GDVENLSDGR LDRPHQQLPD GDRTYRANLQ QLAQPKTRAE IPSPPTYSNQ
PRPLGDFHRD PNALSQFQQS REALLSSTSP TSNYSPINKF SSSTLTQYAN KSPSPPSFGN
SNSEATYVSP YSSKHSYPTN FRSYHKDDDY FNNTATTATT TTSSNSLNEN NNSNKYGNKE
TVLQWSEPYD PSKIRRSQSP IRNAREMIHE YSTTNYVTEV QQPPPPPPDL YQRMTQARTF
LQNSLAKQLR DEGLTESQKA ANRNQTGALS ASSSIPFDAS QIVKNSYNGD EVDHLVHQMR
TKLNQPADTS PSIVQYPRRQ APDSSRANYS ATTSTSFSSS TTRKIMNINI CVGCGKEITG
DQPGCNAMNQ IFHVDCFKCG QCSKTLAGAS FYNIDDKPTC EGCYQNSLEK CTACNRAISD
KLLRACGGVY HVNCFVCFSC KKSLDGIPFT LDKDNNVHCV PCFHDKFAPR CALCSKPIVP
QDGEKESVRV VAMDKSFHVD CYKCEDCGMQ LSSKLEGQGC YPIDNHLLCK TCNGNRLRVV
SST
