ID JMY_XENTR Reviewed; 843 AA.
AC A8E4X8;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Junction-mediating and -regulatory protein;
GN Name=jmy;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (SEP-2007) 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; BC153370; AAI53371.1; -; mRNA.
DR RefSeq; NP_001106426.1; NM_001112955.1.
DR AlphaFoldDB; A8E4X8; -.
DR SMR; A8E4X8; -.
DR STRING; 8364.ENSXETP00000011125; -.
DR PaxDb; 8364-ENSXETP00000001126; -.
DR GeneID; 100127594; -.
DR KEGG; xtr:100127594; -.
DR AGR; Xenbase:XB-GENE-5832535; -.
DR CTD; 133746; -.
DR Xenbase; XB-GENE-5832535; jmy.
DR eggNOG; ENOG502QRHU; Eukaryota.
DR InParanoid; A8E4X8; -.
DR OMA; PGEECSW; -.
DR OrthoDB; 5354952at2759; -.
DR Proteomes; UP000008143; Chromosome 1.
DR GO; GO:0000421; C:autophagosome membrane; ISS:UniProtKB.
DR GO; GO:0031252; C:cell leading edge; ISS:UniProtKB.
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:0008017; F:microtubule binding; ISS:UniProtKB.
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 InterPro; IPR031738; JMY/WHAMM.
DR InterPro; IPR031808; JMY/WHAMM_N.
DR InterPro; IPR003124; WH2_dom.
DR PANTHER; PTHR23330:SF8; JUNCTION-MEDIATING AND -REGULATORY PROTEIN; 1.
DR PANTHER; PTHR23330; P300 TRANSCRIPTIONAL COFACTOR JMY-RELATED; 1.
DR Pfam; PF15871; JMY; 1.
DR Pfam; PF15920; WHAMM-JMY_N; 1.
DR SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 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..843
FT /note="Junction-mediating and -regulatory protein"
FT /id="PRO_0000324614"
FT DOMAIN 776..793
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 49..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 652..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 821..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 190..225
FT /evidence="ECO:0000255"
FT COILED 359..385
FT /evidence="ECO:0000255"
FT COILED 416..487
FT /evidence="ECO:0000255"
FT COMPBIAS 577..600
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..632
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..682
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 829..843
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 843 AA; 96693 MW; 70A8BE6CA32875F0 CRC64;
MSFNLEDTLE SDWVAVRPNV FEEKERRKFV FIVAWNEVEG KFAITCHNRT AQRQRSADKA
GGRSPARQQQ RDSPAQSPAR KAREEPEEGE EEECSWAGLF SFQDLRAVHQ QLCSVSSELE
PCLPTFPEEP SGVWSVLFGP SELSEAEVED LGRQLRLYLG HALDTSGWKI LSQVLFADSD
DPEEYYQSLS ELRHKGYEEG LQRARKRLQE LLEKHKTTEV MVDLLDLYQL EDEAYSNVVE
ATTELYQYLL QPFRDMRELA MLRRQQIKIS IENDYLGPRR IESLKKEDAD WQKKAHMAVL
SIQDLTVKYF EITARAQKAV FDRMRGDQKK FGKTAWAAAV ERVEKLQYGV AKETLQLMRA
KEICLEQKKH ALKDQMQSLQ GGTEAIAVLD ELEADYYDHQ LQLYEVQFEI LKCEELLLTA
QLESIKRQIS EKTDEVVYYD TYESMEAMLA TEDMAASIHI QRVELQKLQQ KVRQLEAKRG
RISAKKAYLR NKKEICIAKH SEKIQQRLHS DEGYRAAQLK QEKQEDEEER KSTWVSQERQ
KTLDRLRTFK QRHPGQVVLK STRLRFSHER RRSTIRTTSS TDAPQSLSVS IQTQGLSDLG
DTEVLQPIKT QKPETTTQLE DSSLPPNAIT SELPLMTSLP TFTHEKLEPE ISTLQPSSLP
ASPPPPPPPL PPPPPPPLPP SKQDTDTLEI RVIHVKKETE EKDGAKPVSG PLAQLFDSSQ
LLNARKTLKK TGALEGIQRR RVSSPMDEVL ASLKRGSFHL KKVEQRALPP FPDEDESNNI
LAQIRKGVKL KKVQKEALRE SFTLLPDTDP LTRSIHEALR RIKEASPESE DEEESLPCTD
WEN
//
