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L14BA_XENLA
ID   L14BA_XENLA             Reviewed;         422 AA.
AC   Q68FI1;
DT   09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Protein LSM14 homolog B-A;
DE   AltName: Full=RNA-associated protein 46 {ECO:0000303|PubMed:19458392};
DE            Short=xRAP46 {ECO:0000303|PubMed:19458392};
DE   AltName: Full=RNA-associated protein 55B-A;
DE            Short=RAP55B-A;
DE            Short=xRAP55B {ECO:0000303|PubMed:17942399, ECO:0000303|PubMed:18723115};
GN   Name=lsm14b-a;
GN   Synonyms=rap46 {ECO:0000303|PubMed:19458392},
GN   rap55b {ECO:0000303|PubMed:17942399, ECO:0000303|PubMed:18723115},
GN   rap55b-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] {ECO:0000312|EMBL:AAH79811.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney {ECO:0000312|EMBL:AAH79811.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305}
RP   IDENTIFICATION IN A RIBONUCLEOPROTEIN COMPLEX WITH CPEB1; DDX6; PAT1;
RP   EIF4ENIF1; EIF4E1B AND YBX2, 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   [3] {ECO:0000305}
RP   IDENTIFICATION IN A RIBONUCLEOPROTEIN COMPLEX WITH ELAVL1; ELAVL2; IGF2BP3;
RP   STAU1; DDX6 AND YBX2.
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).
RN   [4] {ECO:0000305}
RP   REVIEW.
RX   PubMed=18631138; DOI=10.1042/bst0360671;
RA   Standart N., Minshall N.;
RT   "Translational control in early development: CPEB, P-bodies and germinal
RT   granules.";
RL   Biochem. Soc. Trans. 36:671-676(2008).
RN   [5] {ECO:0000305}
RP   REVIEW.
RX   PubMed=18723115; DOI=10.1016/j.biocel.2008.06.015;
RA   Marnef A., Sommerville J., Ladomery M.R.;
RT   "RAP55: insights into an evolutionarily conserved protein family.";
RL   Int. J. Biochem. Cell Biol. 41:977-981(2009).
CC   -!- FUNCTION: May be involved in the storage of translationally inactive
CC       mRNAs and protect them from degradation (By similarity). Plays a role
CC       in control of mRNA translation (PubMed:18631138).
CC       {ECO:0000250|UniProtKB:Q8CGC4, ECO:0000269|PubMed:18631138}.
CC   -!- SUBUNIT: Component of a ribonucleoprotein (RNP) complex, at least
CC       composed of cpeb1, lsm14b/rap55b, ddx6/Xp54, ybx2/frgy2, pat1/P100,
CC       eif4enif1/4E-T and eif4e1b. Different translationally-repressed mRNP
CC       complexes probably exist that contain either lsm14a/rap55a or
CC       lsm14b/rap55b depending on the developmental stage. Component of a
CC       ribonucleoprotein (RNP) complex, composed at least of elavl1/elrA
CC       and/or elavl2/elrB, igf2bp3/vg1RBP, ddx6/Xp54, ybx2/frgy2,
CC       lsm14b/rap55b and, in a subset of RNP complexes, stau1/staufen.
CC       {ECO:0000269|PubMed:17942399, ECO:0000269|PubMed:19458392}.
CC   -!- DEVELOPMENTAL STAGE: Expressed maternally. Expression declines during
CC       oocyte maturation. {ECO:0000269|PubMed:17942399}.
CC   -!- SIMILARITY: Belongs to the LSM14 family. {ECO:0000255}.
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DR   EMBL; BC079811; AAH79811.1; -; mRNA.
DR   RefSeq; NP_001087455.1; NM_001093986.1.
DR   AlphaFoldDB; Q68FI1; -.
DR   SMR; Q68FI1; -.
DR   BioGRID; 104139; 2.
DR   MaxQB; Q68FI1; -.
DR   DNASU; 447279; -.
DR   GeneID; 447279; -.
DR   KEGG; xla:447279; -.
DR   CTD; 447279; -.
DR   Xenbase; XB-GENE-17341157; lsm14b.L.
DR   OMA; HPRWSPY; -.
DR   OrthoDB; 1569369at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10L.
DR   Bgee; 447279; Expressed in liver and 19 other tissues.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IPI:UniProtKB.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   CDD; cd01736; LSm14_N; 1.
DR   InterPro; IPR025762; DFDF.
DR   InterPro; IPR019050; FDF_dom.
DR   InterPro; IPR025761; FFD_box.
DR   InterPro; IPR025609; Lsm14-like_N.
DR   InterPro; IPR010920; LSM_dom_sf.
DR   InterPro; IPR025768; TFG_box.
DR   Pfam; PF09532; FDF; 1.
DR   Pfam; PF12701; LSM14; 1.
DR   SMART; SM01199; FDF; 1.
DR   SMART; SM01271; LSM14; 1.
DR   SUPFAM; SSF50182; SSF50182; 1.
DR   PROSITE; PS51512; DFDF; 1.
DR   PROSITE; PS51513; FFD; 1.
DR   PROSITE; PS51536; TFG; 1.
PE   1: Evidence at protein level;
KW   Developmental protein; Reference proteome; Ribonucleoprotein;
KW   Translation regulation.
FT   CHAIN           1..422
FT                   /note="Protein LSM14 homolog B-A"
FT                   /id="PRO_0000391381"
FT   DOMAIN          278..314
FT                   /note="DFDF"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00845"
FT   REGION          145..290
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          309..354
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          394..422
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           349..365
FT                   /note="FFD box"
FT   MOTIF           367..387
FT                   /note="TFG box"
FT   COMPBIAS        198..212
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        309..331
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        407..422
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   422 AA;  46102 MW;  CF95D40DAE6BC557 CRC64;
     MSSGTPYIGS KISLISKAQI RYEGILYTID TENSTVALAK VRSFGTEDRP TDRPAPPREE
     VYEYIIFRGS DIKDITVCEP PKASHALPQD PAIVQSSLGS APAASYQPSV PYSPFRGMPT
     YSQLAATSLL SQQYAASLGL EKLGSPTASA GASSSCSSPS PQPVAPEPDV PAEPPQLSQN
     AGYPSIPVRK SPMVEQAVQT GPLENQAQKK VQQAKGAPVG QRGVRQSGPQ SQPAPLNVPP
     PAAPVLGTIN DENRRPPRRR SGNRRTRNRS RGQNRPTTVK ENPIKFEGDF DFETANAQFN
     REELDKEFKD KLNFKEEKPE KEGEEKTDSG VETQNSDGNP EEDPLGPNTY YDRSKSFFDN
     ISSEMKSRRT TWAEERKLNT ETFGVSGRFL RGRSFRGGFR GGRGSAAPRR NQTTQRAGTG
     RV
 
 
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