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JMY_XENTR
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   03-AUG-2022, entry version 57.
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.ENSXETP00000001126; -.
DR   PaxDb; A8E4X8; -.
DR   GeneID; 100127594; -.
DR   KEGG; xtr:100127594; -.
DR   CTD; 133746; -.
DR   Xenbase; XB-GENE-5832535; jmy.
DR   eggNOG; ENOG502QRHU; Eukaryota.
DR   InParanoid; A8E4X8; -.
DR   OrthoDB; 183925at2759; -.
DR   Reactome; R-XTR-6804760; Regulation of TP53 Activity through Methylation.
DR   Proteomes; UP000008143; Chromosome 1.
DR   Proteomes; UP000790000; 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; 2.
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..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
 
 
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