MEX3B_MOUSE
ID MEX3B_MOUSE Reviewed; 601 AA.
AC Q69Z36; Q2VPR1; Q6NX84; Q8K2G2;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=RNA-binding protein MEX3B;
DE AltName: Full=RING finger and KH domain-containing protein 3;
GN Name=Mex3b; Synonyms=Kiaa2009, Rkhd3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryonic tail;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 184-601.
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, Limb, and Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: RNA-binding protein. May be involved in post-transcriptional
CC regulatory mechanisms (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Cytoplasm, P-body {ECO:0000250}. Cytoplasmic granule {ECO:0000250}.
CC Note=Predominantly expressed in the cytoplasm and shuttles between the
CC cytoplasm and the nucleus through the CRM1 export pathway. Localization
CC to P-bodies is dependent on 14-3-3 (By similarity). {ECO:0000250}.
CC -!- DOMAIN: Binds RNA through its KH domains. {ECO:0000250}.
CC -!- PTM: Phosphorylation at Ser-494 creates a docking site for 14-3-3,
CC which stabilizes the protein and modulates its ability to bind RNA.
CC {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32608.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK173330; BAD32608.1; ALT_INIT; Transcribed_RNA.
DR EMBL; BC031512; AAH31512.1; -; mRNA.
DR EMBL; BC067199; AAH67199.1; -; mRNA.
DR EMBL; BC108401; AAI08402.1; -; mRNA.
DR AlphaFoldDB; Q69Z36; -.
DR SMR; Q69Z36; -.
DR STRING; 10090.ENSMUSP00000082168; -.
DR iPTMnet; Q69Z36; -.
DR PhosphoSitePlus; Q69Z36; -.
DR MaxQB; Q69Z36; -.
DR PaxDb; Q69Z36; -.
DR PRIDE; Q69Z36; -.
DR ProteomicsDB; 295554; -.
DR MGI; MGI:1918252; Mex3b.
DR eggNOG; KOG2113; Eukaryota.
DR InParanoid; Q69Z36; -.
DR PhylomeDB; Q69Z36; -.
DR ChiTaRS; Mex3b; mouse.
DR PRO; PR:Q69Z36; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q69Z36; protein.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0000932; C:P-body; ISO:MGI.
DR GO; GO:0032794; F:GTPase activating protein binding; IPI:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; ISO:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; IMP:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0006909; P:phagocytosis; IMP:MGI.
DR GO; GO:0022409; P:positive regulation of cell-cell adhesion; IMP:MGI.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IGI:MGI.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IMP:MGI.
DR GO; GO:0072697; P:protein localization to cell cortex; IMP:MGI.
DR Gene3D; 3.30.1370.10; -; 2.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00013; KH_1; 1.
DR SMART; SM00322; KH; 2.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF54791; SSF54791; 2.
DR PROSITE; PS50084; KH_TYPE_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; RNA-binding; Zinc; Zinc-finger.
FT CHAIN 1..601
FT /note="RNA-binding protein MEX3B"
FT /id="PRO_0000278785"
FT DOMAIN 98..159
FT /note="KH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 192..253
FT /note="KH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT ZN_FING 550..590
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 90..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..405
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..545
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZN04"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZN04"
FT MOD_RES 494
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZN04"
SQ SEQUENCE 601 AA; 61781 MW; 77CC73DB8DB2F08B CRC64;
MPSSLFADLE RNGSGGGGGG GGGGGGGGSG GGETLDDQRA LQLALDQLSL LGLDSDEGAS
LYDSEPRKKS VNMTECVPVP SSEHVAEIVG RQGGSGRDGD RRGFSISPTP SLEPWLPGCK
IKALRAKTNT YIKTPVRGEE PVFVVTGRKE DVAMARREII SAAEHFSMIR ASRNKNTALN
GAVPGPPNLP GQTTIQVRVP YRVVGLVVGP KGATIKRIQQ QTHTYIVTPS RDKEPVFEVT
GMPENVDRAR EEIEAHIALR TGGIIELTDE NDFHANGTDV GFDLHHGSGG SGPGSLWSKP
TPSITPTPGR KPFSSYRNDS SSSLGSASTD SYFGGGTSGS AAATSRLADY SPPSPALSFA
HNGNNNNNGN GYTYTAGEAS VPSPDGGPEL QPTFDPAPAP PPGTPLLWAQ FERSPGGGSA
APVSSSCSSS ASSSASSSSV VFPGGGASST PSNANLGLLV HRRLHPGTSC PRLSPPLHMA
TGAGEHHLAR RVRSDPGGGG LAYAAYANGL GTQLPGLPSS DTSGSSSSSS SSSSSSSSSS
GLRRKGSRDC SVCFESEVIA ALVPCGHNLF CMECANRICE KSEPECPVCH TAVTQAIRIF
S
