JMY_DANRE
ID JMY_DANRE Reviewed; 846 AA.
AC Q6NVC9;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Junction-mediating and -regulatory protein;
GN Name=jmy; ORFNames=zgc:77377;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts both as a nuclear p53/TP53-cofactor and a cytoplasmic
CC regulator of actin dynamics depending on conditions. In nucleus, acts
CC as a cofactor that increases p53/TP53 response. Increases p53/TP53-
CC dependent transcription and apoptosis, suggesting an important role in
CC p53/TP53 stress response such as DNA damage. In cytoplasm, acts as a
CC nucleation-promoting factor for both branched and unbranched actin
CC filaments. Activates the Arp2/3 complex to induce branched actin
CC filament networks. Also catalyzes actin polymerization in the absence
CC of Arp2/3, creating unbranched filaments. Contributes to cell motility
CC by controlling actin dynamics. {ECO:0000250|UniProtKB:Q8N9B5,
CC ECO:0000250|UniProtKB:Q9QXM1}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9QXM1}.
CC Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q8N9B5}. Cytoplasm,
CC cytoskeleton {ECO:0000250|UniProtKB:Q8N9B5}. Endomembrane system;
CC Lipid-anchor. Cytoplasmic vesicle, autophagosome membrane
CC {ECO:0000250|UniProtKB:Q8N9B5}. Note=Localizes to the nucleus in most
CC cell types. In primary neutrophils, it colocalizes with actin filaments
CC at the leading edge and is excluded from the nucleus (By similarity).
CC {ECO:0000250|UniProtKB:Q9QXM1}.
CC -!- SIMILARITY: Belongs to the JMY family. {ECO:0000305}.
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DR EMBL; BC068186; AAH68186.1; -; mRNA.
DR RefSeq; NP_998437.1; NM_213272.1.
DR AlphaFoldDB; Q6NVC9; -.
DR STRING; 7955.ENSDARP00000119835; -.
DR PaxDb; Q6NVC9; -.
DR PRIDE; Q6NVC9; -.
DR GeneID; 406556; -.
DR KEGG; dre:406556; -.
DR CTD; 133746; -.
DR ZFIN; ZDB-GENE-040426-2433; jmy.
DR eggNOG; ENOG502QRHU; Eukaryota.
DR InParanoid; Q6NVC9; -.
DR OrthoDB; 183925at2759; -.
DR PhylomeDB; Q6NVC9; -.
DR PRO; PR:Q6NVC9; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0000421; C:autophagosome membrane; ISS:UniProtKB.
DR GO; GO:0031252; C:cell leading edge; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0071933; F:Arp2/3 complex binding; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:0070060; P:'de novo' actin filament nucleation; ISS:UniProtKB.
DR GO; GO:0070358; P:actin polymerization-dependent cell motility; ISS:UniProtKB.
DR GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; ISS:UniProtKB.
DR GO; GO:0009267; P:cellular response to starvation; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; IBA:GO_Central.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR InterPro; IPR033324; Jmy.
DR InterPro; IPR031738; JMY/WHAMM.
DR InterPro; IPR031808; JMY/WHAMM_N.
DR InterPro; IPR003124; WH2_dom.
DR PANTHER; PTHR23330:SF8; PTHR23330:SF8; 1.
DR Pfam; PF15871; JMY; 1.
DR Pfam; PF15920; WHAMM-JMY_N; 1.
DR PROSITE; PS51082; WH2; 1.
PE 2: Evidence at transcript level;
KW Actin-binding; Coiled coil; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW DNA damage; DNA repair; Lipoprotein; Membrane; Nucleus; Reference proteome.
FT CHAIN 1..846
FT /note="Junction-mediating and -regulatory protein"
FT /id="PRO_0000324613"
FT DOMAIN 779..796
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 68..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 533..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 822..846
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 216..254
FT /evidence="ECO:0000255"
FT COILED 410..513
FT /evidence="ECO:0000255"
FT COILED 545..574
FT /evidence="ECO:0000255"
FT COMPBIAS 68..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..572
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..711
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 846 AA; 96380 MW; 809755A0CF1F48D4 CRC64;
MSFAMEDAIE SGWVSVRPNV FEEKEKHKFV FIVAWNEIEG KFAVTCHNRT VQKRSAERDS
LLEAAEGELA AAADTDRRTA RPAHRSPGRE RSGGQSSPSA AAELELLDAA EDAELSARQD
SSWAGLFSFQ DLRAAHLQLC AVNADLEPCL PALPEEQTGV WSVLFGVPEM SARDTDALCF
QLQVYLGHAL DTCGWRILSQ VLFPDSEDAE EYYESLSELR QKGYEDALQR AKRRLQQLLE
QQRAVERMVE LLQLYSEQDE AYGELVEATT ELYHYLLQPF RDMRELAMLR RQQIKISLET
ERLGPRRVES LRREDEDWQR KAHTAVLSIQ DLTVKYFETT ARAQKVMYER MRADQRKFGK
AAWGAAVERM ERLQYAVSKE TLQLMRAKEI CLEQRKHGLR EEMQGLQGGE DAMARLDQLE
ALYYELQLQL YEIQFEILKN EELLLTAQLQ SLRRQMSERQ EEVVYYDTFE SPDAMKATED
PAQPQTPRDD INKLQQRTRQ LEARRGRITA KKAYLKNKKE ICIINHTQKL QQRQAGAHGV
SQQPLLQDEE DEEEQRLSRV SQERQRTLDR LRSFKQRYPG QVTLKSTRLR LAFSRKKALR
AEQMQTQTQP QTQAASVQTD DAPAPLEPPS AVPELCRPDS FLSLPPMGGA VAEAPPSAEL
TSLPPARELL LLDSSTSPMS PPPPPPPPPP PPPPMLEDFP PRSPPEPQSP LGPFSARFFD
SSQLLNARKK LRKTASLESS QWRRASSPMD EVLASLKRGS FHLRKAELRV LAPDPDEDDG
NNILAQIRKG VKLRKVRRQE RSARAIMADS ADPLTRSIHE ALRRIKEASP ESESEDDTPT
ATDWES
