YBX2A_XENLA
ID YBX2A_XENLA Reviewed; 336 AA.
AC P21574; A9JS46; B7ZQ73;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 3.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Y-box-binding protein 2-A;
DE AltName: Full=Cytoplasmic RNA-binding protein p56;
DE AltName: Full=Frog Y-box protein 2;
DE Short=FRG Y2;
DE AltName: Full=Frog Y-box protein 2-A;
DE Short=FRGY2a;
DE AltName: Full=Messenger ribonucleoprotein particle 4;
DE Short=mRNP4;
GN Name=ybx2-a; Synonyms=frgy2, frgy2-a;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=2247479; DOI=10.1073/pnas.87.22.9028;
RA Tafuri S.R., Wolffe A.P.;
RT "Xenopus Y-box transcription factors: molecular cloning, functional
RT analysis and developmental regulation.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:9028-9032(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Gastrula, and Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 5-39; 93-122 AND 213-225, AND PHOSPHORYLATION.
RC TISSUE=Oocyte;
RX PubMed=1902800; DOI=10.1016/0014-5793(91)80456-d;
RA Deschamps S., Viel A., Denis H., le Maire M.;
RT "Purification of two thermostable components of messenger ribonucleoprotein
RT particles (mRNPs) from Xenopus laevis oocytes, belonging to a novel class
RT of RNA-binding proteins.";
RL FEBS Lett. 282:110-114(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 118-336 (ISOFORM 1), PROTEIN SEQUENCE OF
RP 56-82; 95-113 AND 234-255, SUBUNIT, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP STAGE.
RC TISSUE=Ovary;
RX PubMed=1729676; DOI=10.1073/pnas.89.1.11;
RA Murray M.T., Schiller D.L., Franke W.W.;
RT "Sequence analysis of cytoplasmic mRNA-binding proteins of Xenopus oocytes
RT identifies a family of RNA-binding proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:11-15(1992).
RN [5]
RP IDENTIFICATION.
RX PubMed=1629179; DOI=10.1016/s0021-9258(19)49636-1;
RA Deschamps S., Viel A., Garrigos M., Denis H., le Maire M.;
RT "mRNP4, a major mRNA-binding protein from Xenopus oocytes is identical to
RT transcription factor FRG Y2.";
RL J. Biol. Chem. 267:13799-13802(1992).
RN [6]
RP IDENTIFICATION IN A RIBONUCLEOPROTEIN COMPLEX WITH LSM14A; DDX6 AND
RP EIF4ENIF1.
RX PubMed=17074753; DOI=10.1074/jbc.m609059200;
RA Tanaka K.J., Ogawa K., Takagi M., Imamoto N., Matsumoto K., Tsujimoto M.;
RT "RAP55, a cytoplasmic mRNP component, represses translation in Xenopus
RT oocytes.";
RL J. Biol. Chem. 281:40096-40106(2006).
RN [7]
RP IDENTIFICATION IN A RIBONUCLEOPROTEIN COMPLEX WITH CPEB1; DDX6; PAT1;
RP EIF4ENIF1; EIF4E1B AND RAP55B, AND DEVELOPMENTAL STAGE.
RX PubMed=17942399; DOI=10.1074/jbc.m704629200;
RA Minshall N., Reiter M.H., Weil D., Standart N.;
RT "CPEB interacts with an ovary-specific eIF4E and 4E-T in early Xenopus
RT oocytes.";
RL J. Biol. Chem. 282:37389-37401(2007).
RN [8]
RP IDENTIFICATION IN A RIBONUCLEOPROTEIN COMPLEX WITH ELAVL1; ELAVL2; IGF2BP3;
RP STAU1; DDX6 AND LSM14B.
RX PubMed=19458392; DOI=10.1074/jbc.m109.009928;
RA Arthur P.K., Claussen M., Koch S., Tarbashevich K., Jahn O., Pieler T.;
RT "Participation of Xenopus Elr-type proteins in vegetal mRNA localization
RT during oogenesis.";
RL J. Biol. Chem. 284:19982-19992(2009).
CC -!- FUNCTION: Has a dual function in oocytes: as a DNA-binding protein,
CC binds to the Y-box sequence (CTGATTGGCCAA) in the promoters of target
CC genes to stimulate transcription. May also function at CCAAT-containing
CC promoters that lack the consensus Y-box sequence. Also binds mRNA to
CC promote accumulation of the transcripts it contributes to produce.
CC {ECO:0000269|PubMed:2247479}.
CC -!- SUBUNIT: Possibly forms a heterodimer with p54 in the 6S and 15S mRNA-
CC binding particles. The principle component of multiple messenger
CC ribonucleoprotein (mRNP) complexes. Component of a ribonucleoprotein
CC (RNP) complex, composed at least of elavl1/elrA and/or elavl2/elrB,
CC igf2bp3/vg1RBP, ddx6/Xp54, ybx2/frgy2, lsm14b/rap55b and, in a subset
CC of RNP complexes, stau1/staufen. Component of a ribonucleoprotein (RNP)
CC complex, at least composed of lsm14a/rap55a, ybx2/frgy2, ddx6/Xp54 and
CC eif4enif1/4E-T. Does not appear to directly bind lsm14a/rap55a.
CC Component of a ribonucleoprotein (RNP) complex, at least composed of
CC cpeb1, lsm14b/rap55b, ddx6/Xp54, ybx2/frgy2, pat1/P100, eif4enif1/4E-T
CC and eif4e1b. Interaction with cpeb1 is RNA-dependent.
CC {ECO:0000269|PubMed:17074753, ECO:0000269|PubMed:1729676,
CC ECO:0000269|PubMed:17942399, ECO:0000269|PubMed:19458392}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1729676}.
CC Note=Either free or associated with ribonucleoprotein particles.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P21574-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P21574-2; Sequence=VSP_038730;
CC -!- TISSUE SPECIFICITY: In adults, expression is restricted to the ovary
CC and testis. {ECO:0000269|PubMed:2247479}.
CC -!- DEVELOPMENTAL STAGE: Expressed maternally. {ECO:0000269|PubMed:1729676,
CC ECO:0000269|PubMed:17942399, ECO:0000269|PubMed:2247479}.
CC -!- PTM: Phosphorylation activates in vitro RNA binding.
CC {ECO:0000269|PubMed:1902800}.
CC -!- CAUTION: PubMed:2247479 report a decline in expression during
CC oogenesis, but PubMed:1729676 show expression is maintained at a high
CC level throughout oogenesis. {ECO:0000305}.
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DR EMBL; M59454; AAA49716.1; -; mRNA.
DR EMBL; BC155914; AAI55915.1; -; mRNA.
DR EMBL; BC169704; AAI69704.1; -; mRNA.
DR EMBL; BC169706; AAI69706.1; -; mRNA.
DR PIR; B38274; B38274.
DR RefSeq; NP_001081274.1; NM_001087805.1. [P21574-1]
DR AlphaFoldDB; P21574; -.
DR SMR; P21574; -.
DR BioGRID; 99085; 2.
DR GeneID; 397746; -.
DR KEGG; xla:397746; -.
DR CTD; 397746; -.
DR Xenbase; XB-GENE-6252609; ybx2.L.
DR OMA; GQTQSDQ; -.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 397746; Expressed in testis and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR CDD; cd04458; CSP_CDS; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR011129; CSD.
DR InterPro; IPR019844; CSD_1.
DR InterPro; IPR002059; CSP_DNA-bd.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR Pfam; PF00313; CSD; 1.
DR PRINTS; PR00050; COLDSHOCK.
DR SMART; SM00357; CSP; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR PROSITE; PS00352; CSD_1; 1.
DR PROSITE; PS51857; CSD_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Direct protein sequencing; DNA-binding;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein; RNA-binding;
KW Transcription; Transcription regulation.
FT CHAIN 1..336
FT /note="Y-box-binding protein 2-A"
FT /id="PRO_0000100227"
FT DOMAIN 44..108
FT /note="CSD"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 103..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 322..336
FT /note="SSAPDPGIADTPAPE -> VPALFHLPAALDSMGIFGTLQ (in isoform
FT 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_038730"
FT CONFLICT 254
FT /note="T -> A (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 336 AA; 37233 MW; BFD5989DD86DA2FC CRC64;
MSEAEAQEPE PVPQPESEPE IQKPGIAAAR NQANKKVLAT QVQGTVKWFN VRNGYGFINR
NDTKEDVFVH QTAIKKNNPR KFLRSVGDGE TVEFDVVEGE KGAEAANVTG PGGVPVKGSR
FAPNRRRFRR RFYRPRADTA GESGGEGVSP EQMSEGERGE ETSPQQRPQR RRPPPFFYRR
RFRRGPRPNN QQNQGAEVTE QSENKDPVAP TSEALASGDD PQRPPPRRFR QRFRRPFRPR
PAPQQTPEGG DGETKAESGE DPRPEPQRQR NRPYVQRRRR QGATQVAATA QGEGKAEPTQ
HPASEEGTPS DSPTDDGAPV QSSAPDPGIA DTPAPE
