RBM10_MOUSE
ID RBM10_MOUSE Reviewed; 930 AA.
AC Q99KG3; Q3TIY0; Q3U5B8; Q3UKI8; Q80U75; Q8BTP8;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=RNA-binding protein 10 {ECO:0000305};
DE AltName: Full=RNA-binding motif protein 10;
GN Name=Rbm10 {ECO:0000312|MGI:MGI:2384310}; Synonyms=Kiaa0122;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Amnion, 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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-736 AND SER-738, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-733; SER-736 AND SER-738, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-733; SER-736 AND SER-738, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-733; SER-736; SER-738 AND
RP SER-797, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC 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 METHYLATION [LARGE SCALE ANALYSIS] AT ARG-902, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Not known. Binds to RNA homopolymers, with a preference for
CC poly(G) and poly(U) and little for poly(A) (By similarity). May bind to
CC specific miRNA hairpins (By similarity). {ECO:0000250|UniProtKB:P70501,
CC ECO:0000250|UniProtKB:P98175}.
CC -!- SUBUNIT: Associates with the spliceosome. Component of a large
CC chromatin remodeling complex, at least composed of MYSM1, PCAF, RBM10
CC and KIF11/TRIP5 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=4;
CC Name=1;
CC IsoId=Q99KG3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99KG3-2; Sequence=VSP_034905;
CC Name=3;
CC IsoId=Q99KG3-3; Sequence=VSP_034906;
CC Name=Ribosome biogenesis inhibitor MINAS-60;
CC IsoId=P0DW27-1; Sequence=External;
CC -!- MISCELLANEOUS: RBM10 transcripts also code for an alternative open
CC reading frame (alt-ORF) coding for the MINAS-60 (AC P0DW27) protein
CC (Probable). MINAS-60 and RBM10 ORFs are overlapping and are formed by
CC shifting the reading frame (Probable). {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65490.3; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK122208; BAC65490.3; ALT_INIT; Transcribed_RNA.
DR EMBL; AK089105; BAC40753.1; -; mRNA.
DR EMBL; AK145991; BAE26813.1; -; mRNA.
DR EMBL; AK153736; BAE32161.1; -; mRNA.
DR EMBL; AK167666; BAE39715.1; -; mRNA.
DR EMBL; AL672073; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL807240; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004674; AAH04674.1; -; mRNA.
DR CCDS; CCDS40885.1; -. [Q99KG3-1]
DR CCDS; CCDS53013.1; -. [Q99KG3-3]
DR CCDS; CCDS53014.1; -. [Q99KG3-2]
DR RefSeq; NP_001161247.1; NM_001167775.1. [Q99KG3-3]
DR RefSeq; NP_001161248.1; NM_001167776.1. [Q99KG3-2]
DR RefSeq; NP_663602.1; NM_145627.2. [Q99KG3-1]
DR RefSeq; XP_006527681.1; XM_006527618.3.
DR AlphaFoldDB; Q99KG3; -.
DR BMRB; Q99KG3; -.
DR BioGRID; 231785; 5.
DR IntAct; Q99KG3; 2.
DR MINT; Q99KG3; -.
DR STRING; 10090.ENSMUSP00000111032; -.
DR iPTMnet; Q99KG3; -.
DR PhosphoSitePlus; Q99KG3; -.
DR EPD; Q99KG3; -.
DR jPOST; Q99KG3; -.
DR MaxQB; Q99KG3; -.
DR PaxDb; Q99KG3; -.
DR PeptideAtlas; Q99KG3; -.
DR PRIDE; Q99KG3; -.
DR ProteomicsDB; 300256; -. [Q99KG3-1]
DR ProteomicsDB; 300257; -. [Q99KG3-2]
DR ProteomicsDB; 300258; -. [Q99KG3-3]
DR Antibodypedia; 11142; 208 antibodies from 29 providers.
DR DNASU; 236732; -.
DR Ensembl; ENSMUST00000064911; ENSMUSP00000068188; ENSMUSG00000031060. [Q99KG3-1]
DR Ensembl; ENSMUST00000082089; ENSMUSP00000080738; ENSMUSG00000031060. [Q99KG3-2]
DR Ensembl; ENSMUST00000084383; ENSMUSP00000111031; ENSMUSG00000031060. [Q99KG3-2]
DR Ensembl; ENSMUST00000115374; ENSMUSP00000111032; ENSMUSG00000031060. [Q99KG3-1]
DR Ensembl; ENSMUST00000115375; ENSMUSP00000111033; ENSMUSG00000031060. [Q99KG3-3]
DR Ensembl; ENSMUST00000177738; ENSMUSP00000136209; ENSMUSG00000031060. [Q99KG3-3]
DR GeneID; 236732; -.
DR KEGG; mmu:236732; -.
DR UCSC; uc009stf.2; mouse. [Q99KG3-3]
DR UCSC; uc009sth.2; mouse. [Q99KG3-1]
DR UCSC; uc009sti.2; mouse. [Q99KG3-2]
DR CTD; 8241; -.
DR MGI; MGI:2384310; Rbm10.
DR VEuPathDB; HostDB:ENSMUSG00000031060; -.
DR eggNOG; KOG0154; Eukaryota.
DR GeneTree; ENSGT00940000160369; -.
DR HOGENOM; CLU_010527_0_0_1; -.
DR InParanoid; Q99KG3; -.
DR OMA; QYYTEYY; -.
DR OrthoDB; 786674at2759; -.
DR PhylomeDB; Q99KG3; -.
DR TreeFam; TF315789; -.
DR BioGRID-ORCS; 236732; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Rbm10; mouse.
DR PRO; PR:Q99KG3; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q99KG3; protein.
DR Bgee; ENSMUSG00000031060; Expressed in ureteric bud tip and 245 other tissues.
DR Genevisible; Q99KG3; MM.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035198; F:miRNA binding; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0070935; P:3'-UTR-mediated mRNA stabilization; IDA:MGI.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:MGI.
DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; IGI:MGI.
DR GO; GO:1905461; P:positive regulation of vascular associated smooth muscle cell apoptotic process; IDA:MGI.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IEA:InterPro.
DR GO; GO:1905459; P:regulation of vascular associated smooth muscle cell apoptotic process; IGI:MGI.
DR GO; GO:1905288; P:vascular associated smooth muscle cell apoptotic process; IDA:MGI.
DR GO; GO:1990874; P:vascular associated smooth muscle cell proliferation; IGI:MGI.
DR CDD; cd16167; OCRE_RBM10; 1.
DR CDD; cd12754; RRM2_RBM10; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR000467; G_patch_dom.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR041591; OCRE.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR033095; RBM10.
DR InterPro; IPR035618; RBM10_OCRE.
DR InterPro; IPR034992; RBM10_RRM2.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR PANTHER; PTHR13948:SF4; PTHR13948:SF4; 1.
DR Pfam; PF01585; G-patch; 1.
DR Pfam; PF17780; OCRE; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF00641; zf-RanBP; 1.
DR SMART; SM00443; G_patch; 1.
DR SMART; SM00360; RRM; 2.
DR SMART; SM00547; ZnF_RBZ; 1.
DR SUPFAM; SSF54928; SSF54928; 2.
DR SUPFAM; SSF90209; SSF90209; 1.
DR PROSITE; PS50174; G_PATCH; 1.
DR PROSITE; PS50102; RRM; 2.
DR PROSITE; PS01358; ZF_RANBP2_1; 1.
DR PROSITE; PS50199; ZF_RANBP2_2; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative initiation; Alternative splicing; Metal-binding;
KW Methylation; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding; Zinc; Zinc-finger.
FT CHAIN 1..930
FT /note="RNA-binding protein 10"
FT /id="PRO_0000345017"
FT DOMAIN 129..209
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 300..384
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 858..904
FT /note="G-patch"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT ZN_FING 212..242
FT /note="RanBP2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 759..784
FT /note="C2H2-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 464..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 620..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 712..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 818..861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..126
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..646
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..753
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..836
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P98175"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P98175"
FT MOD_RES 383
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P98175"
FT MOD_RES 718
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P98175"
FT MOD_RES 723
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P98175"
FT MOD_RES 733
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18630941,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 736
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 738
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 781
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P98175"
FT MOD_RES 797
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 845
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P98175"
FT MOD_RES 902
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 68..144
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12693553,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_034905"
FT VAR_SEQ 354
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_034906"
FT CONFLICT 188
FT /note="M -> V (in Ref. 2; BAE26813)"
FT /evidence="ECO:0000305"
FT CONFLICT 355
FT /note="E -> VR (in Ref. 1; BAC65490)"
FT /evidence="ECO:0000305"
FT CONFLICT 428
FT /note="P -> H (in Ref. 2; BAE39715)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 930 AA; 103494 MW; E59A2AB20AF1C08C CRC64;
MEYERRGGRG DRTGRYGATD RSQDDSGENR SRDHDYRDMD YRSYPREYGS QEGKHEYDDS
SEEQSAEDSY EASPGSETQR RRRRRHRHSP TGPPGFPRDG DYRDQDYRTE QGEEEEEEDE
EEEEEKASNI VMLRMLPQAA TEDDIRGQLQ SHGVQAREVR LMRNKSSGQS RGFAFVEFSH
LQDATRWMEA NQHSLNILGQ KVSMHYSDPK PKINEDWLCN KCGVQNFKRR EKCFKCGVPK
SEAEQKLPLG TRLDQQALPL GGRELSQGLL PLPQPYQAQG VLTSQALSQG SEPSSENAND
TIILRNLNPH STMDSILGAL APYAVLSSSN VRVIKDKQTQ LNRGFAFIQL STIVEAAQLL
QILQALHPPL TIDGKTINVE FAKGSKRDMA SNEGSRINAA SVASTAIAAA QWAISQASQG
GESAWAAPEE PPVDYSYYQQ DEGYGSSQGT DSLYAHGYLK NSKGPGMTGT KGDPAGTGPE
ASLEAGADSV SLQAFSRAQP GAAPGLYQQS AEGSSGQSTA TNSQSYTIIS PAVLKAELQS
PTQPSSSAFP PATSPTAPEA YSQYPVPDVS TYQYDETSGY YYDPQTGLYY DPNSQYYYNA
QSQQYLYWDG ERRTYIPALE QSADGHKDTG ASSKEGKEKK EKHKTKTAQQ IAKDMERWAR
SLNKQKENFK NSFQPISALR DDERRESATA DAGYAILEKK GALAERQHTS MDLPKLASDD
RPSPPRGLVA AYSGESDSEE EQERGGPERE EKLTDWQKLA CLLCRRQFPS KEALIRHQQL
SGLHKQNLEI HRRAHLSENE LEALEKNDME QMKYRDRAAE RREKYGIPEP PEPKRRKYGG
ISTASVDFEQ PTRDGLGSDN IGSRMLQAMG WKEGSGLGRK KQGIVTPIEA QTRVRGSGLG
ARGSSYGVTS TESYKETLHK TMVTRFNEAQ
