MEX3D_MOUSE
ID MEX3D_MOUSE Reviewed; 643 AA.
AC Q3UE17;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=RNA-binding protein MEX3D;
DE AltName: Full=RING finger and KH domain-containing protein 1;
GN Name=Mex3d; Synonyms=Rkhd1;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-427 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: RNA binding protein, may be involved in post-transcriptional
CC regulatory mechanisms. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Predominantly expressed in the cytoplasm and shuttles between the
CC cytoplasm and the nucleus through the CRM1 export pathway.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3UE17-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UE17-2; Sequence=VSP_024020;
CC -!- DOMAIN: Binds RNA through its KH domains. {ECO:0000250}.
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DR EMBL; CAAA01108096; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC152062; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK149801; BAE29094.1; -; mRNA.
DR RefSeq; NP_941017.2; NM_198615.2.
DR AlphaFoldDB; Q3UE17; -.
DR SMR; Q3UE17; -.
DR BioGRID; 231873; 2.
DR iPTMnet; Q3UE17; -.
DR PhosphoSitePlus; Q3UE17; -.
DR MaxQB; Q3UE17; -.
DR PaxDb; Q3UE17; -.
DR PRIDE; Q3UE17; -.
DR ProteomicsDB; 295555; -. [Q3UE17-1]
DR ProteomicsDB; 295556; -. [Q3UE17-2]
DR DNASU; 237400; -.
DR GeneID; 237400; -.
DR KEGG; mmu:237400; -.
DR CTD; 399664; -.
DR MGI; MGI:2681847; Mex3d.
DR eggNOG; KOG2113; Eukaryota.
DR InParanoid; Q3UE17; -.
DR OrthoDB; 814376at2759; -.
DR PhylomeDB; Q3UE17; -.
DR BioGRID-ORCS; 237400; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Mex3d; mouse.
DR PRO; PR:Q3UE17; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q3UE17; protein.
DR GO; GO:0005634; C:nucleus; ISS:BHF-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:BHF-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; ISS:BHF-UCL.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISO:MGI.
DR GO; GO:0006402; P:mRNA catabolic process; ISO:MGI.
DR GO; GO:0061157; P:mRNA destabilization; NAS:BHF-UCL.
DR GO; GO:0050779; P:RNA destabilization; ISO: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; 2.
DR SMART; SM00322; KH; 2.
DR SUPFAM; SSF54791; SSF54791; 2.
DR PROSITE; PS50084; KH_TYPE_1; 2.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; Zinc; Zinc-finger.
FT CHAIN 1..643
FT /note="RNA-binding protein MEX3D"
FT /id="PRO_0000281676"
FT DOMAIN 160..221
FT /note="KH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 253..314
FT /note="KH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT ZN_FING 592..632
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 61..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 471..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..581
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 491
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q86XN8"
FT MOD_RES 495
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..104
FT /note="MPGSTGQPDAGGAGTGTTAGDPGHPHPALAGAEDAAPRPPPEPDDAAAALRL
FT ALDQLSALGLGGARPGDEGMATRSADGATECGEDEPAPPDELEVAVAPPVTA -> MGV
FT GPSMALAPSVTCAPSMALAPSVTSAPSMALAPSVTCAPCMAVAPSVTVAPSMALTPSVT
FT LAPTMAVAS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024020"
SQ SEQUENCE 643 AA; 65329 MW; EB8EF02F788480F2 CRC64;
MPGSTGQPDA GGAGTGTTAG DPGHPHPALA GAEDAAPRPP PEPDDAAAAL RLALDQLSAL
GLGGARPGDE GMATRSADGA TECGEDEPAP PDELEVAVAP PVTASVAPGG LPLLDPDVSP
RPSPPDVFAS FAPHPAALGP STLLAEQLNV IGSRKKSVNM TECVPVPSSE HVAEIVGRQG
CKIKALRAKT NTYIKTPVRG EEPVFIVTGR KEDVEMAKRE ILSAEHFSLI RATRSKAGGL
SGATPGPPNL PGQTTIQVRV PYRVVGLVVG PKGATIKRIQ QRTHTYIVTP GRDKEPVFAV
TGMPENVDRA REEIEAHITL RTGAFTDSGP DSDFHANGTD VCLDLLGAAA SLWAKAPHPG
RRPPAATGGL RGDNALGAAS TPEPFYVGSR GGPPLPDPSP SSPYGGSGNG GFTFGGDGPS
APTGTATPED CDFGFDFLAL DLTVPATATI WAPFERAAPL PAFSGCPAVN GAPAQPNTGT
RRSSGGGAAT TPRHSPTLPE PGGLSLELPL ARRSVPDPVG AVPWRPPQSA LPPFSGSTTF
STTPSLPSTT LASSTLDTVP SEGNHKPSTT AANSSASTAA PGPPSAALAR ECVVCSEGEA
MAALVPCGHN LFCMDCAVRI CGKSEPECPA CRTPATQAIH IFS
