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EPA2B_XENLA
ID   EPA2B_XENLA             Reviewed;         218 AA.
AC   Q6TY21;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Embryonic polyadenylate-binding protein 2-B;
DE            Short=Embryonic poly(A)-binding protein 2-B;
DE            Short=XePABP2-B;
DE            Short=ePABP-2B;
DE            Short=ePABP2-B;
DE   AltName: Full=Embryonic poly(A)-binding protein type II-B;
GN   Name=Pabpn1l-b; Synonyms=epabp2-b, pabpnl1-b;
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] {ECO:0000305, ECO:0000312|EMBL:AAR26263.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP   DEVELOPMENTAL STAGE.
RC   TISSUE=Oocyte {ECO:0000269|PubMed:15083517};
RX   PubMed=15083517; DOI=10.1002/gene.20015;
RA   Good P.J., Abler L., Herring D., Sheets M.D.;
RT   "Xenopus embryonic poly(A) binding protein 2 (ePABP2) defines a new family
RT   of cytoplasmic poly(A) binding proteins expressed during the early stages
RT   of vertebrate development.";
RL   Genesis 38:166-175(2004).
RN   [2]
RP   STRUCTURE BY NMR OF 60-180, AND SUBUNIT.
RX   PubMed=18824697; DOI=10.1073/pnas.0801274105;
RA   Song J., McGivern J.V., Nichols K.W., Markley J.L., Sheets M.D.;
RT   "Structural basis for RNA recognition by a type II poly(A)-binding
RT   protein.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:15317-15322(2008).
CC   -!- FUNCTION: Binds the poly(A) tail of mRNA. Unable to interact with the
CC       cap-binding complex and is therefore unlikely to be involved in
CC       translation initiation. {ECO:0000250|UniProtKB:Q804A5,
CC       ECO:0000269|PubMed:15083517}.
CC   -!- SUBUNIT: Homodimer; Upon poly(A) binding, undergoes a dimer-monomer
CC       transition that removes the polyproline motif from the RNA recognition
CC       site and allows it to be replaced by the adenosine nucleotides of
CC       poly(A). {ECO:0000269|PubMed:18824697}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15083517}.
CC   -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC       Restricted to oogenesis, early embryogenesis and the adult ovary.
CC       Levels decrease after the onset of zygotic transcription (at protein
CC       level). {ECO:0000269|PubMed:15083517}.
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DR   EMBL; AY382837; AAR26263.1; -; mRNA.
DR   RefSeq; NP_001084418.1; NM_001090949.1.
DR   PDB; 2JWN; NMR; -; A/B=60-180.
DR   PDBsum; 2JWN; -.
DR   AlphaFoldDB; Q6TY21; -.
DR   BMRB; Q6TY21; -.
DR   SMR; Q6TY21; -.
DR   GeneID; 403372; -.
DR   KEGG; xla:403372; -.
DR   CTD; 403372; -.
DR   Xenbase; XB-GENE-1000606; pabpn1l.S.
DR   OrthoDB; 1412946at2759; -.
DR   EvolutionaryTrace; Q6TY21; -.
DR   Proteomes; UP000186698; Chromosome 4S.
DR   Bgee; 403372; Expressed in oocyte and 6 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0008143; F:poly(A) binding; IDA:UniProtKB.
DR   Gene3D; 3.30.70.330; -; 1.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00360; RRM; 1.
DR   SUPFAM; SSF54928; SSF54928; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Reference proteome; RNA-binding.
FT   CHAIN           1..218
FT                   /note="Embryonic polyadenylate-binding protein 2-B"
FT                   /id="PRO_0000239464"
FT   DOMAIN          93..170
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          169..218
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   HELIX           84..92
FT                   /evidence="ECO:0007829|PDB:2JWN"
FT   STRAND          94..100
FT                   /evidence="ECO:0007829|PDB:2JWN"
FT   HELIX           106..114
FT                   /evidence="ECO:0007829|PDB:2JWN"
FT   STRAND          119..127
FT                   /evidence="ECO:0007829|PDB:2JWN"
FT   STRAND          134..143
FT                   /evidence="ECO:0007829|PDB:2JWN"
FT   HELIX           144..151
FT                   /evidence="ECO:0007829|PDB:2JWN"
FT   TURN            152..155
FT                   /evidence="ECO:0007829|PDB:2JWN"
FT   STRAND          164..169
FT                   /evidence="ECO:0007829|PDB:2JWN"
SQ   SEQUENCE   218 AA;  24270 MW;  3571AC009E95EDBA CRC64;
     MSERVSEEPG LDKGDRAEEC ELDDPELKAI RMRVREMEEE AERLKGLSGQ DKSIGVSTRP
     CMQTTHSKMT AGAYTEGPPQ PLSAEEKKEI DKRSVYVGNV DYGSTAQDLE AHFSSCGSIN
     RITILCDKFS GHPKGYAYIE FAERNSVDAA VAMDETVFRG RTIKVLPKRT NMPGISSTDR
     GGFRGRPRGN RGNYQRGQRP RGRPFRGRGR PGPLNNPY
 
 
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