ID   MEX3D_HUMAN             Reviewed;         651 AA.
AC   Q86XN8; A0PJL8; A1L023; E9PAL6; Q71M49;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 3.
DT   27-MAR-2024, entry version 167.
DE   RecName: Full=RNA-binding protein MEX3D;
DE   AltName: Full=RING finger and KH domain-containing protein 1;
DE   AltName: Full=RING finger protein 193;
DE   AltName: Full=TINO;
GN   Name=MEX3D; Synonyms=KIAA2031, RKHD1, RNF193;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX   PubMed=17267406; DOI=10.1093/nar/gkm016;
RA   Buchet-Poyau K., Courchet J., Le Hir H., Seraphin B., Scoazec J.-Y.,
RA   Duret L., Domon-Dell C., Freund J.-N., Billaud M.;
RT   "Identification and characterization of human Mex-3 proteins, a novel
RT   family of evolutionarily conserved RNA-binding proteins differentially
RT   localized to processing bodies.";
RL   Nucleic Acids Res. 35:1289-1300(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA   Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA   Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA   Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA   Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA   Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA   Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA   Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA   Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA   McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA   Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA   Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA   She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA   Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 137-651 (ISOFORM 1).
RC   TISSUE=Brain;
RA   Nagase T., Kikuno R., Ohara O.;
RT   "The nucleotide sequence of a long cDNA clone isolated from human.";
RL   Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 177-651 (ISOFORM 2).
RC   TISSUE=Placenta;
RX   PubMed=14769789; DOI=10.1074/jbc.m314071200;
RA   Donnini M., Lapucci A., Papucci L., Witort E., Jacquier A., Brewer G.,
RA   Nicolin A., Capaccioli S., Schiavone N.;
RT   "Identification of TINO: a new evolutionarily conserved BCL-2 AU-rich
RT   element RNA-binding protein.";
RL   J. Biol. Chem. 279:20154-20166(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 178-651 (ISOFORM 2).
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).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-510 AND SER-514, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [7]
RP   STRUCTURE BY NMR OF 272-343.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the second KH domain in RING finger and KH domain-
RT   containing protein 1.";
RL   Submitted (SEP-2006) to the PDB data bank.
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=3;
CC       Name=1;
CC         IsoId=Q86XN8-1; Sequence=Displayed;
CC       Name=2; Synonyms=TINO;
CC         IsoId=Q86XN8-2; Sequence=VSP_024019;
CC       Name=3;
CC         IsoId=Q86XN8-3; Sequence=VSP_047662;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed in all the cell lines and
CC       tissues tested. {ECO:0000269|PubMed:17267406}.
CC   -!- DOMAIN: Binds RNA through its KH domains. {ECO:0000250}.
CC   -!- PTM: Phosphorylated. {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAQ04763.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AY950680; AAY34148.1; -; mRNA.
DR   EMBL; AC005943; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC027307; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AB107353; BAC67658.1; -; mRNA.
DR   EMBL; AF458084; AAQ04763.1; ALT_INIT; mRNA.
DR   EMBL; BC113384; AAI13385.1; -; mRNA.
DR   EMBL; BC113741; AAI13742.2; -; mRNA.
DR   CCDS; CCDS32865.2; -. [Q86XN8-1]
DR   RefSeq; NP_001167589.1; NM_001174118.1. [Q86XN8-3]
DR   RefSeq; NP_976049.3; NM_203304.3. [Q86XN8-1]
DR   PDB; 2DGR; NMR; -; A=272-341.
DR   PDBsum; 2DGR; -.
DR   AlphaFoldDB; Q86XN8; -.
DR   SMR; Q86XN8; -.
DR   BioGRID; 134376; 48.
DR   IntAct; Q86XN8; 11.
DR   STRING; 9606.ENSP00000384398; -.
DR   GlyGen; Q86XN8; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q86XN8; -.
DR   PhosphoSitePlus; Q86XN8; -.
DR   BioMuta; MEX3D; -.
DR   DMDM; 134047829; -.
DR   EPD; Q86XN8; -.
DR   jPOST; Q86XN8; -.
DR   MassIVE; Q86XN8; -.
DR   MaxQB; Q86XN8; -.
DR   PaxDb; 9606-ENSP00000384398; -.
DR   PeptideAtlas; Q86XN8; -.
DR   ProteomicsDB; 19040; -.
DR   ProteomicsDB; 70305; -. [Q86XN8-1]
DR   ProteomicsDB; 70306; -. [Q86XN8-2]
DR   Pumba; Q86XN8; -.
DR   Antibodypedia; 22752; 61 antibodies from 21 providers.
DR   DNASU; 399664; -.
DR   Ensembl; ENST00000402693.5; ENSP00000384398.3; ENSG00000181588.17. [Q86XN8-1]
DR   GeneID; 399664; -.
DR   KEGG; hsa:399664; -.
DR   MANE-Select; ENST00000402693.5; ENSP00000384398.3; NM_203304.4; NP_976049.3.
DR   UCSC; uc060rdi.1; human. [Q86XN8-1]
DR   AGR; HGNC:16734; -.
DR   CTD; 399664; -.
DR   DisGeNET; 399664; -.
DR   GeneCards; MEX3D; -.
DR   HGNC; HGNC:16734; MEX3D.
DR   HPA; ENSG00000181588; Tissue enriched (testis).
DR   MIM; 611009; gene.
DR   neXtProt; NX_Q86XN8; -.
DR   OpenTargets; ENSG00000181588; -.
DR   PharmGKB; PA162395829; -.
DR   VEuPathDB; HostDB:ENSG00000181588; -.
DR   eggNOG; KOG2113; Eukaryota.
DR   GeneTree; ENSGT00940000162613; -.
DR   HOGENOM; CLU_025598_2_1_1; -.
DR   InParanoid; Q86XN8; -.
DR   OMA; PFERSGN; -.
DR   OrthoDB; 50983at2759; -.
DR   PhylomeDB; Q86XN8; -.
DR   TreeFam; TF315107; -.
DR   PathwayCommons; Q86XN8; -.
DR   SignaLink; Q86XN8; -.
DR   SIGNOR; Q86XN8; -.
DR   BioGRID-ORCS; 399664; 9 hits in 1194 CRISPR screens.
DR   EvolutionaryTrace; Q86XN8; -.
DR   GeneWiki; MEX3D; -.
DR   GenomeRNAi; 399664; -.
DR   Pharos; Q86XN8; Tdark.
DR   PRO; PR:Q86XN8; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q86XN8; Protein.
DR   Bgee; ENSG00000181588; Expressed in right testis and 120 other cell types or tissues.
DR   ExpressionAtlas; Q86XN8; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA: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; IDA:BHF-UCL.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0061157; P:mRNA destabilization; NAS:BHF-UCL.
DR   GO; GO:0010609; P:mRNA localization resulting in post-transcriptional regulation of gene expression; NAS:BHF-UCL.
DR   CDD; cd22423; KH-I_MEX3_rpt1; 1.
DR   CDD; cd22424; KH-I_MEX3_rpt2; 1.
DR   Gene3D; 3.30.1370.10; K Homology domain, type 1; 2.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR047228; KH-I_MEX3_rpt1.
DR   InterPro; IPR047226; KH-I_MEX3_rpt2.
DR   InterPro; IPR004087; KH_dom.
DR   InterPro; IPR004088; KH_dom_type_1.
DR   InterPro; IPR036612; KH_dom_type_1_sf.
DR   InterPro; IPR047227; MEX3.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR23285; RING FINGER AND KH DOMAIN CONTAINING PROTEIN 1; 1.
DR   PANTHER; PTHR23285:SF3; RNA-BINDING PROTEIN MEX3D; 1.
DR   Pfam; PF00013; KH_1; 2.
DR   Pfam; PF13920; zf-C3HC4_3; 1.
DR   SMART; SM00322; KH; 2.
DR   SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 2.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50084; KH_TYPE_1; 2.
DR   PROSITE; PS50089; ZF_RING_2; 1.
DR   Genevisible; Q86XN8; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cytoplasm; Metal-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; RNA-binding; Zinc; Zinc-finger.
FT   CHAIN           1..651
FT                   /note="RNA-binding protein MEX3D"
FT                   /id="PRO_0000050123"
FT   DOMAIN          179..240
FT                   /note="KH 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   DOMAIN          273..334
FT                   /note="KH 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   ZN_FING         600..640
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          1..159
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          375..394
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          401..443
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          495..531
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..53
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        127..148
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         510
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         514
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         648..651
FT                   /note="HIFS -> RVETPQPGGASALQRQY (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14769789,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_024019"
FT   VAR_SEQ         648..651
FT                   /note="HIFS -> RVETETPQPGGASALQRQY (in isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_047662"
FT   STRAND          273..279
FT                   /evidence="ECO:0007829|PDB:2DGR"
FT   HELIX           282..289
FT                   /evidence="ECO:0007829|PDB:2DGR"
FT   TURN            290..293
FT                   /evidence="ECO:0007829|PDB:2DGR"
FT   HELIX           296..302
FT                   /evidence="ECO:0007829|PDB:2DGR"
FT   STRAND          306..308
FT                   /evidence="ECO:0007829|PDB:2DGR"
FT   STRAND          312..314
FT                   /evidence="ECO:0007829|PDB:2DGR"
FT   STRAND          317..322
FT                   /evidence="ECO:0007829|PDB:2DGR"
FT   TURN            324..326
FT                   /evidence="ECO:0007829|PDB:2DGR"
FT   HELIX           327..339
FT                   /evidence="ECO:0007829|PDB:2DGR"
SQ   SEQUENCE   651 AA;  64883 MW;  5E056EE2D08BC4CD CRC64;
     MPSSLGQPDG GGGGGGGGGG VGAAGEDPGP GPAPPPEGAQ EAAPAPRPPP EPDDAAAALR
     LALDQLSALG LGGAGDTDEE GAAGDGAAAA GGADGGAAPE PVPPDGPEAG APPTLAPAVA
     PGSLPLLDPN ASPPPPPPPR PSPPDVFAGF APHPAALGPP TLLADQMSVI GSRKKSVNMT
     ECVPVPSSEH VAEIVGRQGC KIKALRAKTN TYIKTPVRGE EPVFIVTGRK EDVEMAKREI
     LSAAEHFSII RATRSKAGGL PGAAQGPPNL PGQTTIQVRV PYRVVGLVVG PKGATIKRIQ
     QRTHTYIVTP GRDKEPVFAV TGMPENVDRA REEIEAHITL RTGAFTDAGP DSDFHANGTD
     VCLDLLGAAA SLWAKTPNQG RRPPTATAGL RGDTALGAPS APEAFYAGSR GGPSVPDPGP
     ASPYSGSGNG GFAFGAEGPG APVGTAAPDD CDFGFDFDFL ALDLTVPAAA TIWAPFERAA
     PLPAFSGCST VNGAPGPPAA GARRSSGAGT PRHSPTLPEP GGLRLELPLS RRGAPDPVGA
     LSWRPPQGPV SFPGGAAFST ATSLPSSPAA AACAPLDSGA SENSRKPPSA SSAPALAREC
     VVCAEGEVMA ALVPCGHNLF CMDCAVRICG KSEPECPACR TPATQAIHIF S
//