RAVR1_RAT
ID RAVR1_RAT Reviewed; 748 AA.
AC Q5XI28;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Ribonucleoprotein PTB-binding 1;
DE AltName: Full=Protein raver-1;
GN Name=Raver1; Synonyms=Raver1h;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [2]
RP TISSUE SPECIFICITY.
RX PubMed=14633994; DOI=10.1093/emboj/cdg609;
RA Gromak N., Rideau A., Southby J., Scadden A.D.J., Gooding C.,
RA Huettelmaier S., Singer R.H., Smith C.W.J.;
RT "The PTB interacting protein raver1 regulates alpha-tropomyosin alternative
RT splicing.";
RL EMBO J. 22:6356-6364(2003).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; THR-31; SER-576 AND
RP SER-626, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Cooperates with PTBP1 to modulate regulated alternative
CC splicing events. Promotes exon skipping. Cooperates with PTBP1 to
CC modulate switching between mutually exclusive exons during maturation
CC of the TPM1 pre-mRNA (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PTBP1, RAVER2, VCL and ACTN1. Part of a complex
CC containing RAVER1, VCL and ACTN1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Note=Nuclear, in perinucleolar structures. Shuttles between nucleus and
CC cytoplasm. Cytoplasm, at focal contacts and cell-cell contacts.
CC Associated with myotubes during muscle differentiation (By similarity).
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Detected in aorta, brain, gut, heart,
CC kidney, liver, spleen, uterus and skeletal muscle.
CC {ECO:0000269|PubMed:14633994}.
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DR EMBL; BC083865; AAH83865.1; -; mRNA.
DR RefSeq; NP_001013961.1; NM_001013939.1.
DR AlphaFoldDB; Q5XI28; -.
DR SMR; Q5XI28; -.
DR IntAct; Q5XI28; 4.
DR STRING; 10116.ENSRNOP00000048510; -.
DR iPTMnet; Q5XI28; -.
DR PhosphoSitePlus; Q5XI28; -.
DR jPOST; Q5XI28; -.
DR PaxDb; Q5XI28; -.
DR PRIDE; Q5XI28; -.
DR Ensembl; ENSRNOT00000046983; ENSRNOP00000048510; ENSRNOG00000020710.
DR GeneID; 298705; -.
DR KEGG; rno:298705; -.
DR UCSC; RGD:1359190; rat.
DR CTD; 125950; -.
DR RGD; 1359190; Raver1.
DR eggNOG; KOG0123; Eukaryota.
DR GeneTree; ENSGT00940000160550; -.
DR HOGENOM; CLU_016492_1_0_1; -.
DR InParanoid; Q5XI28; -.
DR OMA; HNMQPNY; -.
DR OrthoDB; 249777at2759; -.
DR PhylomeDB; Q5XI28; -.
DR TreeFam; TF331660; -.
DR PRO; PR:Q5XI28; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000020710; Expressed in thymus and 19 other tissues.
DR Genevisible; Q5XI28; RN.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IBA:GO_Central.
DR CDD; cd12663; RRM1_RAVER1; 1.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR034635; RAVER1.
DR InterPro; IPR034633; RAVER1_RRM1.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR23189:SF46; PTHR23189:SF46; 1.
DR Pfam; PF00076; RRM_1; 3.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 3.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8IY67"
FT CHAIN 2..748
FT /note="Ribonucleoprotein PTB-binding 1"
FT /id="PRO_0000081489"
FT DOMAIN 59..130
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 132..210
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 221..299
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..401
FT /note="Interaction with PTBP1"
FT /evidence="ECO:0000250"
FT REGION 390..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 45..60
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 743..746
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 22..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY67"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY67"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 31
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 469
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY67"
FT MOD_RES 480
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY67"
FT MOD_RES 576
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 626
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 630
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CW46"
FT MOD_RES 716
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CW46"
FT MOD_RES 720
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CW46"
SQ SEQUENCE 748 AA; 79289 MW; 74B1712833F93451 CRC64;
MAADVSVTHR PPLSPEAEAE AETPETVDRR TPEQELPPLD PEEIRKRLEH TERQFRNRRK
ILIRGLPGDV TNQEVHDLLS DYELKYCFVD KYKGTAFVTL LNGEQAEAAI NTFHQSRLRE
RELSVQLQPT DALLCVANLP PSLTQAQFEE LVRPFGSLER CFLVYSERTG HSKGYGFAEY
MKKDSAARAK SDLLGKPLGP RTLYVHWTDA GQLTPALLHS RCLCVDHLPP GFNDVDALRQ
ALSAVYTPTF CQLASGQDGQ LKGFAVLEYE TAEMAEAAQQ RADGLALGGS HLRVSFCAPG
PPGRSMLAAL IAAQATALNR GKGLLPEPNI LQLLNNLGPS ASLQLLLNPL LHGGASGKQG
LLGAPPAMPL LSGPALSTAL LQLALQSQNQ SQSQSQKKPG ILGDSPLGTL QAGAQPSNSL
LGELSAGGGL APELPPRRGK PQPLLPPLLG PSGGDREPMG LGPPASQLTP PPAPMGLRGS
SLRGLPKDSG PLPTPPGVSL LGEPPKDYRI PLNPYLNLHS LLPSSNLAGK ETRGWGGSGR
GRRPAEPPLP SPAVPGGGNA SNNGSKAFPM KPRLLSPIAS NRLPPEPGLP DSYSFDYPTD
VGPRRLFSHP RESNLGAHGP SRHKMSPPPS SFSEPRSGGG SGGPLSHFYS GSPTSYFTSG
LQAGLKQSHL NKAVGSSPMG SSEGLLGLGP GPNGHSHLLK TPLGGQKRSF SHLLPSPEPS
PEGSYVGQHS QGLGGHYADS YLKRKRIF
