RNPC3_HUMAN
ID RNPC3_HUMAN Reviewed; 517 AA.
AC Q96LT9; A8K1C9; D3DT74; Q5TZ87; Q96FK7; Q96JI8; Q9NSU7; Q9NXX2;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=RNA-binding region-containing protein 3;
DE AltName: Full=RNA-binding motif protein 40;
DE Short=RNA-binding protein 40;
DE AltName: Full=U11/U12 small nuclear ribonucleoprotein 65 kDa protein;
DE Short=U11/U12 snRNP 65 kDa protein;
DE Short=U11/U12-65K;
GN Name=RNPC3; Synonyms=KIAA1839, RBM40, RNP, SNRNP65;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Fetal brain;
RX PubMed=14974681; DOI=10.1023/b:bigi.0000006032.04031.d0;
RA Zhao E., Li J., Xie Y., Jin W., Zhang Z., Chen J., Zeng L., Yin G.,
RA Qian J., Wu H., Ying K., Zhao R.C., Mao Y.;
RT "Cloning and identification of a novel human RNPC3 gene that encodes a
RT protein with two RRM domains and is expressed in the cell nucleus.";
RL Biochem. Genet. 41:315-323(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION IN A COMPLEX WITH
RP THE U11/U12 SPLICEOSOME, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15146077; DOI=10.1261/rna.7320604;
RA Will C.L., Schneider C., Hossbach M., Urlaub H., Rauhut R., Elbashir S.,
RA Tuschl T., Luehrmann R.;
RT "The human 18S U11/U12 snRNP contains a set of novel proteins not found in
RT the U2-dependent spliceosome.";
RL RNA 10:929-941(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11347906; DOI=10.1093/dnares/8.2.85;
RA Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 8:85-95(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Adipose tissue, Brain, and Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 225-517 (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [9]
RP FUNCTION, INTERACTION WITH PDCD7, IDENTIFICATION IN A COMPLEX WITH U12
RP SNRNA, AND RNA-BINDING.
RX PubMed=16096647; DOI=10.1038/sj.emboj.7600765;
RA Benecke H., Luehrmann R., Will C.L.;
RT "The U11/U12 snRNP 65K protein acts as a molecular bridge, binding the U12
RT snRNA and U11-59K protein.";
RL EMBO J. 24:3057-3069(2005).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND SER-108, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 380-517, SUBUNIT, AND FUNCTION.
RX PubMed=19447915; DOI=10.1261/rna.1359909;
RA Netter C., Weber G., Benecke H., Wahl M.C.;
RT "Functional stabilization of an RNA recognition motif by a noncanonical N-
RT terminal expansion.";
RL RNA 15:1305-1313(2009).
RN [14]
RP INVOLVEMENT IN IGHD5, VARIANTS IGHD5 THR-474 AND 502-ARG--CYS-517 DEL, AND
RP FUNCTION.
RX PubMed=24480542; DOI=10.1002/emmm.201303573;
RA Argente J., Flores R., Gutierrez-Arumi A., Verma B., Martos-Moreno G.A.,
RA Cusco I., Oghabian A., Chowen J.A., Frilander M.J., Perez-Jurado L.A.;
RT "Defective minor spliceosome mRNA processing results in isolated familial
RT growth hormone deficiency.";
RL EMBO Mol. Med. 6:299-306(2014).
RN [15]
RP CHARACTERIZATION OF VARIANTS IGHD5 THR-474 AND 502-ARG--CYS-517 DEL,
RP FUNCTION, AND STRUCTURE BY NMR OF 381-516.
RX PubMed=29255062; DOI=10.1261/rna.062844.117;
RA Norppa A.J., Kauppala T.M., Heikkinen H.A., Verma B., Iwai H.,
RA Frilander M.J.;
RT "Mutations in the U11/U12-65K protein associated with isolated growth
RT hormone deficiency lead to structural destabilization and impaired binding
RT of U12 snRNA.";
RL RNA 24:396-409(2018).
CC -!- FUNCTION: Participates in pre-mRNA U12-dependent splicing, performed by
CC the minor spliceosome which removes U12-type introns. U12-type introns
CC comprises less than 1% of all non-coding sequences. Binds to the 3'-
CC stem-loop of m(7)G-capped U12 snRNA. {ECO:0000269|PubMed:16096647,
CC ECO:0000269|PubMed:19447915, ECO:0000269|PubMed:24480542,
CC ECO:0000269|PubMed:29255062}.
CC -!- SUBUNIT: Component of the U11/U12 snRNPs that are part of the U12-type
CC spliceosome. Found in a complex with m(7)G-capped U12 snRNA. Interacts
CC with PDCD7. {ECO:0000269|PubMed:15146077, ECO:0000269|PubMed:16096647,
CC ECO:0000269|PubMed:19447915}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14974681}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96LT9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96LT9-2; Sequence=VSP_053413;
CC -!- TISSUE SPECIFICITY: Highly expressed in pancreas and kidney. Detected
CC at lower levels in heart, brain, placenta, lung, liver, spleen, thymus,
CC prostate, testis, ovary, small intestine, colon and leukocytes.
CC {ECO:0000269|PubMed:14974681}.
CC -!- DISEASE: Growth hormone deficiency, isolated, 5 (IGHD5) [MIM:618160]:
CC An autosomal recessive deficiency of growth hormone characterized by
CC severe postnatal growth failure, delayed bone age without bone
CC dysplasia, and hypoplasia of the anterior pituitary.
CC {ECO:0000269|PubMed:24480542, ECO:0000269|PubMed:29255062}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA90885.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA90885.1; Type=Miscellaneous discrepancy; Note=Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAB47468.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY099329; AAM45139.1; -; mRNA.
DR EMBL; BK005195; DAA05493.1; -; mRNA.
DR EMBL; AB058742; BAB47468.1; ALT_INIT; mRNA.
DR EMBL; AK000015; BAA90885.1; ALT_SEQ; mRNA.
DR EMBL; AK057799; BAB71580.1; -; mRNA.
DR EMBL; AK289844; BAF82533.1; -; mRNA.
DR EMBL; AC095032; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC105272; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX322653; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471097; EAW72905.1; -; Genomic_DNA.
DR EMBL; CH471097; EAW72901.1; -; Genomic_DNA.
DR EMBL; CH471097; EAW72906.1; -; Genomic_DNA.
DR EMBL; BC010697; AAH10697.2; -; mRNA.
DR EMBL; AL137730; CAB70897.2; -; mRNA.
DR CCDS; CCDS781.1; -. [Q96LT9-1]
DR PIR; T46396; T46396.
DR RefSeq; NP_060089.1; NM_017619.3. [Q96LT9-1]
DR PDB; 3EGN; X-ray; 2.50 A; A=380-517.
DR PDB; 5OBN; NMR; -; A=381-516.
DR PDBsum; 3EGN; -.
DR PDBsum; 5OBN; -.
DR AlphaFoldDB; Q96LT9; -.
DR SMR; Q96LT9; -.
DR BioGRID; 120740; 39.
DR CORUM; Q96LT9; -.
DR IntAct; Q96LT9; 19.
DR MINT; Q96LT9; -.
DR STRING; 9606.ENSP00000432886; -.
DR GlyGen; Q96LT9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96LT9; -.
DR PhosphoSitePlus; Q96LT9; -.
DR BioMuta; RNPC3; -.
DR DMDM; 74760946; -.
DR EPD; Q96LT9; -.
DR jPOST; Q96LT9; -.
DR MassIVE; Q96LT9; -.
DR MaxQB; Q96LT9; -.
DR PaxDb; Q96LT9; -.
DR PeptideAtlas; Q96LT9; -.
DR PRIDE; Q96LT9; -.
DR ProteomicsDB; 1846; -.
DR ProteomicsDB; 77250; -. [Q96LT9-1]
DR Antibodypedia; 9690; 86 antibodies from 23 providers.
DR DNASU; 55599; -.
DR Ensembl; ENST00000423855.7; ENSP00000391432.1; ENSG00000185946.16. [Q96LT9-1]
DR Ensembl; ENST00000524631.5; ENSP00000437278.1; ENSG00000185946.16. [Q96LT9-2]
DR Ensembl; ENST00000533099.5; ENSP00000432886.1; ENSG00000185946.16. [Q96LT9-1]
DR GeneID; 55599; -.
DR KEGG; hsa:55599; -.
DR MANE-Select; ENST00000423855.7; ENSP00000391432.1; NM_017619.4; NP_060089.1.
DR UCSC; uc010oum.2; human. [Q96LT9-1]
DR CTD; 55599; -.
DR DisGeNET; 55599; -.
DR GeneCards; RNPC3; -.
DR HGNC; HGNC:18666; RNPC3.
DR HPA; ENSG00000185946; Low tissue specificity.
DR MalaCards; RNPC3; -.
DR MIM; 618016; gene.
DR MIM; 618160; phenotype.
DR neXtProt; NX_Q96LT9; -.
DR OpenTargets; ENSG00000185946; -.
DR Orphanet; 231662; Isolated growth hormone deficiency type IA.
DR PharmGKB; PA134865246; -.
DR VEuPathDB; HostDB:ENSG00000185946; -.
DR eggNOG; KOG4206; Eukaryota.
DR GeneTree; ENSGT00530000063786; -.
DR HOGENOM; CLU_039888_2_1_1; -.
DR InParanoid; Q96LT9; -.
DR OMA; RPINTKK; -.
DR OrthoDB; 1080666at2759; -.
DR PhylomeDB; Q96LT9; -.
DR TreeFam; TF324298; -.
DR PathwayCommons; Q96LT9; -.
DR Reactome; R-HSA-72165; mRNA Splicing - Minor Pathway.
DR SignaLink; Q96LT9; -.
DR BioGRID-ORCS; 55599; 675 hits in 1084 CRISPR screens.
DR ChiTaRS; RNPC3; human.
DR EvolutionaryTrace; Q96LT9; -.
DR GenomeRNAi; 55599; -.
DR Pharos; Q96LT9; Tbio.
DR PRO; PR:Q96LT9; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q96LT9; protein.
DR Bgee; ENSG00000185946; Expressed in caput epididymis and 185 other tissues.
DR ExpressionAtlas; Q96LT9; baseline and differential.
DR Genevisible; Q96LT9; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005689; C:U12-type spliceosomal complex; IDA:UniProtKB.
DR GO; GO:0097157; F:pre-mRNA intronic binding; IBA:GO_Central.
DR GO; GO:0030626; F:U12 snRNA binding; IBA:GO_Central.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0008380; P:RNA splicing; IC:UniProtKB.
DR CDD; cd12238; RRM1_RBM40_like; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR034147; RBM40_RRM1.
DR InterPro; IPR045164; RBM41/RNPC3.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR16105; PTHR16105; 1.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Disease variant; Dwarfism;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; Spliceosome.
FT CHAIN 1..517
FT /note="RNA-binding region-containing protein 3"
FT /id="PRO_0000311112"
FT DOMAIN 27..102
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 420..503
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..257
FT /note="Necessary for interaction with PDCD7"
FT /evidence="ECO:0000269|PubMed:16096647"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..380
FT /note="Necessary for binding to m(7)G-capped U12 snRNA"
FT REGION 213..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..229
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..249
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 298
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_053413"
FT VARIANT 474
FT /note="P -> T (in IGHD5; impairs binding to U12 and U6atac
FT small nuclear RNAs; leads to a partial defect in the
FT folding of RRM 2 domain and reduced stability of the full-
FT length protein; dbSNP:rs370930012)"
FT /evidence="ECO:0000269|PubMed:24480542,
FT ECO:0000269|PubMed:29255062"
FT /id="VAR_081540"
FT VARIANT 502..517
FT /note="Missing (in IGHD5; reduced expression due to
FT nonsense-mediated mRNA decay; impairs binding to U12 and
FT U6atac small nuclear RNAs)"
FT /evidence="ECO:0000269|PubMed:24480542,
FT ECO:0000269|PubMed:29255062"
FT /id="VAR_081541"
FT CONFLICT 392
FT /note="R -> K (in Ref. 4; BAA90885)"
FT /evidence="ECO:0000305"
FT HELIX 391..397
FT /evidence="ECO:0007829|PDB:3EGN"
FT HELIX 401..406
FT /evidence="ECO:0007829|PDB:3EGN"
FT HELIX 408..410
FT /evidence="ECO:0007829|PDB:3EGN"
FT STRAND 420..427
FT /evidence="ECO:0007829|PDB:3EGN"
FT HELIX 433..440
FT /evidence="ECO:0007829|PDB:3EGN"
FT HELIX 441..443
FT /evidence="ECO:0007829|PDB:3EGN"
FT HELIX 449..454
FT /evidence="ECO:0007829|PDB:3EGN"
FT STRAND 456..462
FT /evidence="ECO:0007829|PDB:3EGN"
FT TURN 463..465
FT /evidence="ECO:0007829|PDB:3EGN"
FT STRAND 466..472
FT /evidence="ECO:0007829|PDB:3EGN"
FT HELIX 476..486
FT /evidence="ECO:0007829|PDB:3EGN"
FT STRAND 489..491
FT /evidence="ECO:0007829|PDB:3EGN"
FT STRAND 497..500
FT /evidence="ECO:0007829|PDB:3EGN"
SQ SEQUENCE 517 AA; 58575 MW; B71E12DB1E5BB736 CRC64;
MAAPEQPLAI SRGCTSSSSL SPPRGDRTLL VRHLPAELTA EEKEDLLKYF GAQSVRVLSD
KGRLKHTAFA TFPNEKAAIK ALTRLHQLKL LGHTLVVEFA KEQDRVHSPC PTSGSEKKKR
SDDPVEDDKE KKELGYLTVE NGIAPNHGLT FPLNSCLKYM YPPPSSTILA NIVNALASVP
KFYVQVLHLM NKMNLPTPFG PITARPPMYE DYMPLHAPLP PTSPQPPEEP PLPDEDEELS
SEESEYESTD DEDRQRMNKL MELANLQPKR PKTIKQRHVR KKRKIKDMLN TPLCPSHSSL
HPVLLPSDVF DQPQPVGNKR IEFHISTDMP AAFKKDLEKE QNCEEKNHDL PATEVDASNI
GFGKIFPKPN LDITEEIKED SDEMPSECIS RRELEKGRIS REEMETLSVF RSYEPGEPNC
RIYVKNLAKH VQEKDLKYIF GRYVDFSSET QRIMFDIRLM KEGRMKGQAF IGLPNEKAAA
KALKEANGYV LFGKPMVVQF ARSARPKQDP KEGKRKC
