ID F7DPJ1_XENTR Unreviewed; 843 AA.
AC F7DPJ1;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 4.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Junction-mediating and -regulatory protein {ECO:0000313|Ensembl:ENSXETP00000001126};
GN Name=jmy {ECO:0000313|Ensembl:ENSXETP00000001126};
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 {ECO:0000313|Ensembl:ENSXETP00000001126};
RN [1] {ECO:0000313|Ensembl:ENSXETP00000001126}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000001126};
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
RN [2] {ECO:0000313|Ensembl:ENSXETP00000001126}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUN-2011) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
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DR AlphaFoldDB; F7DPJ1; -.
DR Ensembl; ENSXETT00000001126; ENSXETP00000001126; ENSXETG00000000520.
DR AGR; Xenbase:XB-GENE-5832535; -.
DR Xenbase; XB-GENE-5832535; jmy.
DR HOGENOM; CLU_012316_0_0_1; -.
DR InParanoid; F7DPJ1; -.
DR TreeFam; TF331023; -.
DR Reactome; R-XTR-6804760; Regulation of TP53 Activity through Methylation.
DR Bgee; ENSXETG00000000520; Expressed in 4-cell stage embryo and 15 other cell types or tissues.
DR ExpressionAtlas; F7DPJ1; baseline.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
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 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329}.
FT DOMAIN 776..793
FT /note="WH2"
FT /evidence="ECO:0000259|PROSITE:PS51082"
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 194..221
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 458..485
FT /evidence="ECO:0000256|SAM:Coils"
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; 96749 MW; D0A8B86CA1BA3846 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
LLNARKRLKK TGALEGIQRR RVSSPMDEVL ASLKRGSFHL KKVEQRALPP FPDEDESNNI
LAQIRKGVKL KKVQKEALRE SFTLLPDTDP LTRSIHEALR RIKEASPESE DEEESLPCTD
WEN
//