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ELAV4_XENLA
ID   ELAV4_XENLA             Reviewed;         400 AA.
AC   Q7SZT7; Q4FZM7; Q7ZTQ4; Q91585; Q98TU5;
DT   09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=ELAV-like protein 4 {ECO:0000250|UniProtKB:P26378};
DE   AltName: Full=Protein ElrD {ECO:0000312|EMBL:AAH56021.1};
GN   Name=elavl4; Synonyms=elrD {ECO:0000312|EMBL:AAH56021.1};
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:AAA96945.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RC   TISSUE=Tadpole brain {ECO:0000312|EMBL:AAA96945.1};
RX   PubMed=7753842; DOI=10.1073/pnas.92.10.4557;
RA   Good P.J.;
RT   "A conserved family of elav-like genes in vertebrates.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:4557-4561(1995).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:AAH56021.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 12-400 (ISOFORM 1).
RC   TISSUE=Tadpole {ECO:0000312|EMBL:AAH99348.1}, and
RC   Tail bud {ECO:0000312|EMBL:AAH56021.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000305, ECO:0000312|EMBL:AAK01428.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8 (ISOFORM 2), AND ALTERNATIVE
RP   SPLICING.
RX   PubMed=11327714; DOI=10.1006/bbrc.2001.4812;
RA   Nassar F., Wegnez M.;
RT   "Characterization of two promoters of the Xenopus laevis elrD gene.";
RL   Biochem. Biophys. Res. Commun. 283:392-398(2001).
RN   [4] {ECO:0000305}
RP   TISSUE SPECIFICITY.
RX   PubMed=10473128; DOI=10.1016/s0925-4773(99)00056-8;
RA   Perron M., Furrer M.P., Wegnez M., Theodore L.;
RT   "Xenopus elav-like genes are differentially expressed during
RT   neurogenesis.";
RL   Mech. Dev. 84:139-142(1999).
RN   [5] {ECO:0000305}
RP   TISSUE SPECIFICITY.
RX   PubMed=15593335; DOI=10.1002/cne.20387;
RA   Amato M.A., Boy S., Arnault E., Girard M., Della Puppa A., Sharif A.,
RA   Perron M.;
RT   "Comparison of the expression patterns of five neural RNA binding proteins
RT   in the Xenopus retina.";
RL   J. Comp. Neurol. 481:331-339(2005).
CC   -!- FUNCTION: RNA-binding protein that is involved in the post-
CC       transcriptional regulation of mRNAs (By similarity). Plays a role in
CC       the regulation of mRNA stability, alternative splicing and translation
CC       (By similarity). Binds to AU-rich element (ARE) sequences in the 3'
CC       untranslated region (3'UTR) of target mRNAs (By similarity). Mainly
CC       play a role in neuron-specific RNA processing (By similarity).
CC       {ECO:0000250|UniProtKB:O09032, ECO:0000250|UniProtKB:P26378,
CC       ECO:0000250|UniProtKB:Q61701}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O09032}.
CC       Perikaryon {ECO:0000250|UniProtKB:Q61701}. Cell projection, axon
CC       {ECO:0000250|UniProtKB:Q61701}. Cell projection, dendrite
CC       {ECO:0000250|UniProtKB:Q61701}. Cell projection, growth cone
CC       {ECO:0000250|UniProtKB:Q61701}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=2 {ECO:0000269|PubMed:11327714}; Synonyms=ELRD2
CC       {ECO:0000269|PubMed:11327714};
CC         IsoId=Q7SZT7-1; Sequence=Displayed;
CC       Name=1 {ECO:0000269|PubMed:7753842}; Synonyms=ELRD1
CC       {ECO:0000269|PubMed:11327714};
CC         IsoId=Q7SZT7-2; Sequence=VSP_053191, VSP_053192;
CC       Name=3;
CC         IsoId=Q7SZT7-3; Sequence=VSP_053191;
CC   -!- TISSUE SPECIFICITY: Expression is neural-specific. In the retina,
CC       expressed in the ganglion cell layer from stage 28 onwards and in
CC       amacrine cells from stage 35 onwards. Expressed in the tailbud and
CC       adult brain; in tailbuds, expression is predominant in the cortical
CC       plate. {ECO:0000269|PubMed:10473128, ECO:0000269|PubMed:15593335,
CC       ECO:0000269|PubMed:7753842}.
CC   -!- DEVELOPMENTAL STAGE: Expressed after stage 19 (late neurula).
CC       {ECO:0000269|PubMed:7753842}.
CC   -!- SIMILARITY: Belongs to the RRM elav family. {ECO:0000255}.
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DR   EMBL; U17599; AAA96945.1; -; mRNA.
DR   EMBL; BC043735; AAH43735.1; -; mRNA.
DR   EMBL; BC056021; AAH56021.1; -; mRNA.
DR   EMBL; BC099348; AAH99348.1; -; mRNA.
DR   EMBL; AF329448; AAK01428.1; -; Genomic_DNA.
DR   PIR; I51678; I51678.
DR   RefSeq; NP_001080909.1; NM_001087440.1. [Q7SZT7-1]
DR   RefSeq; XP_018111995.1; XM_018256506.1. [Q7SZT7-3]
DR   RefSeq; XP_018111999.1; XM_018256510.1. [Q7SZT7-2]
DR   AlphaFoldDB; Q7SZT7; -.
DR   SMR; Q7SZT7; -.
DR   DNASU; 386602; -.
DR   GeneID; 386602; -.
DR   KEGG; xla:386602; -.
DR   CTD; 386602; -.
DR   Xenbase; XB-GENE-948214; elavl4.L.
DR   Proteomes; UP000186698; Chromosome 4L.
DR   Bgee; 386602; Expressed in brain and 7 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR   GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR   GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   CDD; cd12650; RRM1_Hu; 1.
DR   CDD; cd12656; RRM3_HuD; 1.
DR   Gene3D; 3.30.70.330; -; 3.
DR   InterPro; IPR006548; ELAD_HU_SF.
DR   InterPro; IPR034775; ELAV/Hu_RRM1.
DR   InterPro; IPR034918; HuD_RRM3.
DR   InterPro; IPR002343; Hud_Sxl_RNA.
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; 4.
DR   PRINTS; PR00961; HUDSXLRNA.
DR   SMART; SM00360; RRM; 3.
DR   SUPFAM; SSF54928; SSF54928; 2.
DR   TIGRFAMs; TIGR01661; ELAV_HUD_SF; 1.
DR   PROSITE; PS50102; RRM; 3.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell projection; Cytoplasm; Developmental protein;
KW   Reference proteome; Repeat; Ribonucleoprotein; RNA-binding.
FT   CHAIN           1..400
FT                   /note="ELAV-like protein 4"
FT                   /id="PRO_0000391375"
FT   DOMAIN          51..158
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          166..246
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          317..395
FT                   /note="RRM 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          12..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..7
FT                   /note="MEWNGLK -> MV (in isoform 1 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:7753842, ECO:0000303|Ref.2"
FT                   /id="VSP_053191"
FT   VAR_SEQ         89..117
FT                   /note="Missing (in isoform 1)"
FT                   /evidence="ECO:0000303|PubMed:7753842, ECO:0000303|Ref.2"
FT                   /id="VSP_053192"
SQ   SEQUENCE   400 AA;  44216 MW;  32B4F265B57DDAB4 CRC64;
     MEWNGLKMII STMEPQVSNG PTSNTSNGPS SNSRNCPSPM QTGAATDDSK TNLIVNYLPQ
     NMTQEEFRSL FGSIGEIESC KLVRDKITGT QFEENFKDLA TGTKWKPLTE EGPIFGKGQS
     LGYGFVNYID PKDAEKAINT LNGLRLQTKT IKVSYARPSS ASIRDANLYV SGLPKTMTQK
     ELEQLFSQYG RIITSRILVD QVTGVSRGVG FIRFDKRIEA EEAIKGLNGQ KPSGAAEPIT
     VKFANNPSQK TSQALLSQLY QSPNRRYPGP LHHQAQRFRL DNLLNMAYGV KRFSPITIDG
     MTSLVGMNIP GHTGTGWCIF VYNLSPDSDE SVLWQLFGPF GAVNNVKVIR DFNTNKCKGF
     GFVTMTNYDE AAMAIASLNG YRLGDRVLQV SFKTNKTHKS
 
 
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