RAVR1_MOUSE
ID RAVR1_MOUSE Reviewed; 748 AA.
AC Q9CW46; Q5DTT6; Q811K0; Q8C3Z1; Q8CA14;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Ribonucleoprotein PTB-binding 1;
DE AltName: Full=Protein raver-1;
GN Name=Raver1; Synonyms=Kiaa1978;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH PTBP1; VCL AND
RP ACTN1, IDENTIFICATION IN A COMPLEX WITH VCL AND ACTN1, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Embryo;
RX PubMed=11724819; DOI=10.1083/jcb.200105044;
RA Huettelmaier S., Illenberger S., Grosheva I., Ruediger M., Singer R.H.,
RA Jockusch B.M.;
RT "Raver1, a dual compartment protein, is a ligand for PTB/hnRNPI and
RT microfilament attachment proteins.";
RL J. Cell Biol. 155:775-786(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Fetal heart, Liver, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 261-748 (ISOFORM 1).
RC TISSUE=Fetal brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs Identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 519-748 (ISOFORM 1).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Embryo, and Mammary gland;
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 [5]
RP FUNCTION.
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 [6]
RP INTERACTION WITH RAVER2, AND TISSUE SPECIFICITY.
RX PubMed=16051233; DOI=10.1016/j.febslet.2005.07.001;
RA Kleinhenz B., Fabienke M., Swiniarski S., Wittenmayer N., Kirsch J.,
RA Jockusch B.M., Arnold H.H., Illenberger S.;
RT "Raver2, a new member of the hnRNP family.";
RL FEBS Lett. 579:4254-4258(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576 AND SER-626, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-14 AND THR-469, CLEAVAGE OF INITIATOR METHIONINE [LARGE
RP SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-469; SER-576; SER-626;
RP SER-630; SER-716 AND SER-720, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP STRUCTURE BY NMR OF 61-135.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the RNA binding domain from mouse hypothetical
RT protein BAB23670.";
RL Submitted (JUN-2005) to the PDB data bank.
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. {ECO:0000269|PubMed:14633994}.
CC -!- SUBUNIT: Interacts with PTBP1, RAVER2, VCL and ACTN1. Part of a complex
CC containing RAVER1, VCL and ACTN1. {ECO:0000269|PubMed:11724819,
CC ECO:0000269|PubMed:16051233}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11724819}. Cytoplasm
CC {ECO:0000269|PubMed:11724819}. Note=Nuclear, in perinucleolar
CC structures. Shuttles between nucleus and cytoplasm. Cytoplasm, at focal
CC contacts and cell-cell contacts. Associated with myotubes during muscle
CC differentiation.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9CW46-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CW46-2; Sequence=VSP_017037, VSP_017038;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11724819,
CC ECO:0000269|PubMed:16051233}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB23670.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY275472; AAP33691.1; -; mRNA.
DR EMBL; AK004919; BAB23670.1; ALT_INIT; mRNA.
DR EMBL; AK039928; BAC30481.1; -; mRNA.
DR EMBL; AK084478; BAC39194.1; -; mRNA.
DR EMBL; AK220434; BAD90266.1; -; mRNA.
DR EMBL; BC043698; AAH43698.1; -; mRNA.
DR EMBL; BC108392; AAI08393.1; -; mRNA.
DR CCDS; CCDS40550.1; -. [Q9CW46-1]
DR RefSeq; NP_082187.1; NM_027911.3. [Q9CW46-1]
DR PDB; 1WI6; NMR; -; A=61-135.
DR PDB; 3ZZY; X-ray; 1.40 A; C/D=496-507.
DR PDB; 3ZZZ; X-ray; 1.55 A; C/D=680-692.
DR PDBsum; 1WI6; -.
DR PDBsum; 3ZZY; -.
DR PDBsum; 3ZZZ; -.
DR AlphaFoldDB; Q9CW46; -.
DR SMR; Q9CW46; -.
DR BioGRID; 214910; 32.
DR DIP; DIP-44609N; -.
DR ELM; Q9CW46; -.
DR IntAct; Q9CW46; 4.
DR MINT; Q9CW46; -.
DR STRING; 10090.ENSMUSP00000111150; -.
DR iPTMnet; Q9CW46; -.
DR PhosphoSitePlus; Q9CW46; -.
DR EPD; Q9CW46; -.
DR jPOST; Q9CW46; -.
DR MaxQB; Q9CW46; -.
DR PaxDb; Q9CW46; -.
DR PeptideAtlas; Q9CW46; -.
DR PRIDE; Q9CW46; -.
DR ProteomicsDB; 300243; -. [Q9CW46-1]
DR ProteomicsDB; 300244; -. [Q9CW46-2]
DR DNASU; 71766; -.
DR Ensembl; ENSMUST00000115487; ENSMUSP00000111150; ENSMUSG00000010205. [Q9CW46-1]
DR Ensembl; ENSMUST00000217359; ENSMUSP00000151195; ENSMUSG00000111497. [Q9CW46-1]
DR GeneID; 71766; -.
DR KEGG; mmu:71766; -.
DR UCSC; uc009okd.2; mouse. [Q9CW46-1]
DR CTD; 125950; -.
DR MGI; MGI:1919016; Raver1.
DR VEuPathDB; HostDB:ENSMUSG00000010205; -.
DR VEuPathDB; HostDB:ENSMUSG00000111497; -.
DR eggNOG; KOG0123; Eukaryota.
DR GeneTree; ENSGT00940000160550; -.
DR HOGENOM; CLU_016492_1_0_1; -.
DR InParanoid; Q9CW46; -.
DR OMA; HNMQPNY; -.
DR PhylomeDB; Q9CW46; -.
DR TreeFam; TF331660; -.
DR BioGRID-ORCS; 71766; 9 hits in 71 CRISPR screens.
DR EvolutionaryTrace; Q9CW46; -.
DR PRO; PR:Q9CW46; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9CW46; protein.
DR Bgee; ENSMUSG00000010205; Expressed in animal zygote and 62 other tissues.
DR ExpressionAtlas; Q9CW46; baseline and differential.
DR Genevisible; Q9CW46; MM.
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; 2.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19131326"
FT CHAIN 2..748
FT /note="Ribonucleoprotein PTB-binding 1"
FT /id="PRO_0000081488"
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..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..401
FT /note="Interaction with PTBP1"
FT /evidence="ECO:0000269|PubMed:11724819"
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..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19131326"
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:19131326"
FT MOD_RES 469
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
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:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 626
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 630
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 716
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 720
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 253..270
FT /note="LACGQDGQLKGFAVLEYE -> TCVIMASLELRDPPAFSS (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017037"
FT VAR_SEQ 271..748
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017038"
FT CONFLICT 1
FT /note="M -> K (in Ref. 1; BAB23670)"
FT /evidence="ECO:0000305"
FT CONFLICT 397
FT /note="Missing (in Ref. 3; BAD90266)"
FT /evidence="ECO:0000305"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:1WI6"
FT HELIX 72..78
FT /evidence="ECO:0007829|PDB:1WI6"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:1WI6"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:1WI6"
FT TURN 91..94
FT /evidence="ECO:0007829|PDB:1WI6"
FT STRAND 95..102
FT /evidence="ECO:0007829|PDB:1WI6"
FT HELIX 103..113
FT /evidence="ECO:0007829|PDB:1WI6"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:1WI6"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:1WI6"
FT STRAND 684..686
FT /evidence="ECO:0007829|PDB:3ZZZ"
SQ SEQUENCE 748 AA; 79382 MW; B0D775F14BD5B214 CRC64;
MAADVSVTHR PPLSPEAEAE AETPETVDRR APEQELPPLD PEEIRKRLEH TERQFRNRRK
ILIRGLPGDV TNQEVHDLLS DYELKYCFVD KYKGTAFVTL LNGEQAEAAI NTFHQSRLRE
RELSVQLQPT DALLCVANLP PSLTQAQFEE LVRPFGSLER CFLVYSERTG HSKGYGFAEY
MKKDSAARAK SDLLGKPLGP RTLYVHWTDA GQLTPALLHS RCLCVDHLPP GFSDVDALRR
ALSVVYTPTF CQLACGQDGQ LKGFAVLEYE TAEMAEAAQE RADGQALGDS HLRVSFCAPG
PPGRSMLAAL IAAQATALNR GKGLLPEPNL LQLLNNLGPS ASLQLLLNPL LHGGASGKQG
LLGAPPAMPL LSGPALSTAL LQLALQSQSQ NQSQGQKKPG ILGDSPLGTL QAGAQPSNSL
LGELSAGGGL APELPPRRGK PQPLLPPLLG PSGGDREPMG LGPPATQLTP PPAPVGLRGS
NHRGLPKDSG PLPTPPGVSL LGEPPKDYRI PLNPYLNLHS LLPSSNLAGK ETRGWGGSGR
GRRPAEPPLP SPAVPGGGSG SNNGNKAFQM KSRLLSPIAS NRLPPEPGLP DSYGFDYPTD
VGPRRLFSHP REPTLGAHGP SRHKMSPPPS SFNEPRSGGG SGGPLSHFYS GSPTSYFTSG
LQAGLKQSHL NKAVGSSPMG SSEGLLGLGP GPNGHSHLLK TPLGGQKRSF SHLLPSPEPS
PEGSYVGQHS QGLGGHYADS YLKRKRIF
