THOC4_MOUSE
ID THOC4_MOUSE Reviewed; 255 AA.
AC O08583; Q0VBL5; Q8CBM4; Q9JJW7;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=THO complex subunit 4;
DE Short=Tho4;
DE AltName: Full=Ally of AML-1 and LEF-1;
DE AltName: Full=Aly/REF export factor;
DE AltName: Full=REF1-I;
DE AltName: Full=RNA and export factor-binding protein 1;
DE AltName: Full=Transcriptional coactivator Aly/REF;
GN Name=Alyref; Synonyms=Aly, Ref1, Refbp1, THOC4;
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), FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Thymocyte;
RX PubMed=9119228; DOI=10.1101/gad.11.5.640;
RA Bruhn L., Munnerlyn A., Grosschedl R.;
RT "ALY, a context-dependent coactivator of LEF-1 and AML-1, is required for
RT TCRalpha enhancer function.";
RL Genes Dev. 11:640-653(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND INTERACTION WITH
RP NXF1.
RC TISSUE=Embryo;
RX PubMed=10786854; DOI=10.1017/s1355838200000078;
RA Stutz F., Bachi A., Doerks T., Braun I.C., Seraphin B., Wilm M., Bork P.,
RA Izaurralde E.;
RT "REF, an evolutionarily conserved family of hnRNP-like proteins, interacts
RT with TAP/Mex67p and participates in mRNA nuclear export.";
RL RNA 6:638-650(2000).
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 GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 190-255.
RC STRAIN=C57BL/6J; TISSUE=Urinary bladder;
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 [7]
RP FUNCTION.
RX PubMed=11158589; DOI=10.1073/pnas.98.3.1030;
RA Rodrigues J.P., Rode M., Gatfield D., Blencowe B.J., Carmo-Fonseca M.,
RA Izaurralde E.;
RT "REF proteins mediate the export of spliced and unspliced mRNAs from the
RT nucleus.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:1030-1035(2001).
RN [8]
RP 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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-85, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [10]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-38; ARG-196 AND ARG-203, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and 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).
RN [11]
RP CITRULLINATION AT ARG-140.
RX PubMed=24463520; DOI=10.1038/nature12942;
RA Christophorou M.A., Castelo-Branco G., Halley-Stott R.P., Oliveira C.S.,
RA Loos R., Radzisheuskaya A., Mowen K.A., Bertone P., Silva J.C.,
RA Zernicka-Goetz M., Nielsen M.L., Gurdon J.B., Kouzarides T.;
RT "Citrullination regulates pluripotency and histone H1 binding to
RT chromatin.";
RL Nature 507:104-108(2014).
RN [12]
RP STRUCTURE BY NMR OF 105-182.
RX PubMed=12809490; DOI=10.1021/bi034062o;
RA Perez-Alvarado G.C., Martinez-Yamout M., Allen M.M., Grosschedl R.,
RA Dyson H.J., Wright P.E.;
RT "Structure of the nuclear factor ALY: insights into post-transcriptional
RT regulatory and mRNA nuclear export processes.";
RL Biochemistry 42:7348-7357(2003).
CC -!- FUNCTION: Export adapter involved in nuclear export of spliced and
CC unspliced mRNA. Binds mRNA which is thought to be transferred to the
CC NXF1-NXT1 heterodimer for export (TAP/NFX1 pathway) (PubMed:9119228,
CC PubMed:10786854, PubMed:11158589). Component of the TREX complex which
CC is thought to couple mRNA transcription, processing and nuclear export,
CC and specifically associates with spliced mRNA and not with unspliced
CC pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-
CC independent mechanism, binds to mRNA upstream of the exon-junction
CC complex (EJC) and is recruited in a splicing- and cap-dependent manner
CC to a region near the 5' end of the mRNA where it functions in mRNA
CC export to the cytoplasm. TREX recruitment occurs via an interaction
CC between ALYREF/THOC4 and the cap-binding protein NCBP1. The TREX
CC complex is essential for the export of Kaposi's sarcoma-associated
CC herpesvirus (KSHV) intronless mRNAs and infectious virus production;
CC ALYREF/THOC4 mediates the recruitment of the TREX complex to the
CC intronless viral mRNA. Required for TREX complex assembly and for
CC linking DDX39B to the cap-binding complex (CBC). In conjunction with
CC THOC5 functions in NXF1-NXT1 mediated nuclear export of HSP70 mRNA;
CC both proteins enhance the RNA binding activity of NXF1 and are required
CC for NXF1 localization to the nuclear rim. Involved in the nuclear
CC export of intronless mRNA; proposed to be recruited to intronless mRNA
CC by ATP-bound DDX39B. Involved in transcription elongation and genome
CC stability. Involved in mRNA export of C5-methylcytosine (m5C)-
CC containing mRNAs: specifically recognizes and binds m5C mRNAs and
CC mediates their nucleo-cytoplasmic shuttling (By similarity).
CC {ECO:0000250|UniProtKB:Q86V81, ECO:0000269|PubMed:10786854,
CC ECO:0000269|PubMed:11158589, ECO:0000269|PubMed:9119228}.
CC -!- FUNCTION: Acts as chaperone and promotes the dimerization of
CC transcription factors containing basic leucine zipper (bZIP) domains
CC and thereby promotes transcriptional activation.
CC {ECO:0000250|UniProtKB:Q86V81}.
CC -!- SUBUNIT: Homomultimer (By similarity). Is part of several complexes
CC involved in mRNA processing and export (By similarity). Component of
CC the transcription/export (TREX) complex at least composed of
CC ALYREF/THOC4, DDX39B, SARNP/CIP29, CHTOP and the THO subcomplex; TREX
CC seems to have a dynamic structure involving ATP-dependent remodeling;
CC in the complex interacts (via C-terminus) directly with DDX39B and
CC interacts directly with THOC1 and THOC2 (By similarity). Found in mRNA
CC splicing-dependent exon junction complexes (EJC) (By similarity).
CC Identified in the spliceosome C complex (By similarity). Found in a
CC mRNP complex with UPF3A and UPF3B (By similarity). Interacts with
CC RBM8A, NCBP1, THOC5, LEF1, RUNX1, EIF4A3, RNPS1, SRRM1, IWS1 and EXOSC1
CC (By similarity). Interacts with RBM15B. Interacts with NXF1; the
CC interaction is direct (PubMed:10786854). {ECO:0000250|UniProtKB:Q86V81,
CC ECO:0000269|PubMed:10786854}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9119228}. Nucleus
CC speckle {ECO:0000250|UniProtKB:Q86V81}. Cytoplasm
CC {ECO:0000269|PubMed:9119228}. Note=Colocalizes with the core EJC,
CC ALYREF/THOC4, NXF1 and DDX39B in the nucleus and nuclear speckles.
CC Localizes to regions surrounding nuclear speckles known as perispeckles
CC in which TREX complex assembly seems to occur. Travels to the cytoplasm
CC as part of the exon junction complex (EJC) bound to mRNA.
CC {ECO:0000250|UniProtKB:Q86V81}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Refbp1-I;
CC IsoId=O08583-1; Sequence=Displayed;
CC Name=2; Synonyms=Refbp1-II;
CC IsoId=O08583-2; Sequence=VSP_008597;
CC -!- TISSUE SPECIFICITY: Highly expressed in heart, brain, spleen, lung,
CC liver, skeletal muscle, kidney and testis.
CC {ECO:0000269|PubMed:9119228}.
CC -!- PTM: Arg-50 and Arg-203 are dimethylated, probably to asymmetric
CC dimethylarginine. Arginine methylation reduces RNA binding (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}.
CC -!- SIMILARITY: Belongs to the THOC4 family. {ECO:0000305}.
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DR EMBL; U89876; AAC53117.1; -; mRNA.
DR EMBL; AJ252140; CAB76383.1; -; mRNA.
DR EMBL; AL663030; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466558; EDL34770.1; -; Genomic_DNA.
DR EMBL; BC120588; AAI20589.1; -; mRNA.
DR EMBL; BC137658; AAI37659.1; -; mRNA.
DR EMBL; AK035721; BAC29168.1; -; mRNA.
DR CCDS; CCDS25744.1; -. [O08583-1]
DR RefSeq; NP_035698.1; NM_011568.1. [O08583-1]
DR PDB; 1NO8; NMR; -; A=77-182.
DR PDBsum; 1NO8; -.
DR AlphaFoldDB; O08583; -.
DR BMRB; O08583; -.
DR SMR; O08583; -.
DR BioGRID; 204102; 44.
DR DIP; DIP-59977N; -.
DR IntAct; O08583; 9.
DR MINT; O08583; -.
DR STRING; 10090.ENSMUSP00000026125; -.
DR iPTMnet; O08583; -.
DR PhosphoSitePlus; O08583; -.
DR EPD; O08583; -.
DR jPOST; O08583; -.
DR MaxQB; O08583; -.
DR PaxDb; O08583; -.
DR PeptideAtlas; O08583; -.
DR PRIDE; O08583; -.
DR ProteomicsDB; 262919; -. [O08583-1]
DR ProteomicsDB; 262920; -. [O08583-2]
DR TopDownProteomics; O08583-1; -. [O08583-1]
DR DNASU; 21681; -.
DR Ensembl; ENSMUST00000026125; ENSMUSP00000026125; ENSMUSG00000025134. [O08583-1]
DR GeneID; 21681; -.
DR KEGG; mmu:21681; -.
DR UCSC; uc007mtl.1; mouse. [O08583-1]
DR CTD; 10189; -.
DR MGI; MGI:1341044; Alyref.
DR VEuPathDB; HostDB:ENSMUSG00000025134; -.
DR eggNOG; KOG0533; Eukaryota.
DR GeneTree; ENSGT00410000025615; -.
DR HOGENOM; CLU_052367_0_1_1; -.
DR InParanoid; O08583; -.
DR OMA; GIARVWF; -.
DR OrthoDB; 1369069at2759; -.
DR PhylomeDB; O08583; -.
DR TreeFam; TF313312; -.
DR Reactome; R-MMU-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-MMU-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-MMU-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-MMU-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-MMU-72187; mRNA 3'-end processing.
DR Reactome; R-MMU-73856; RNA Polymerase II Transcription Termination.
DR BioGRID-ORCS; 21681; 28 hits in 77 CRISPR screens.
DR ChiTaRS; Alyref; mouse.
DR EvolutionaryTrace; O08583; -.
DR PRO; PR:O08583; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; O08583; protein.
DR Bgee; ENSMUSG00000025134; Expressed in maxillary prominence and 265 other tissues.
DR Genevisible; O08583; MM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
DR GO; GO:0000781; C:chromosome, telomeric region; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0035145; C:exon-exon junction complex; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000346; C:transcription export complex; ISO:MGI.
DR GO; GO:0062153; F:C5-methylcytidine-containing RNA binding; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IDA:MGI.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:MGI.
DR GO; GO:0006406; P:mRNA export from nucleus; ISO:MGI.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0032786; P:positive regulation of DNA-templated transcription, elongation; ISO:MGI.
DR GO; GO:0000018; P:regulation of DNA recombination; ISO:MGI.
DR GO; GO:0031297; P:replication fork processing; ISO:MGI.
DR GO; GO:0006405; P:RNA export from nucleus; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR GO; GO:0046784; P:viral mRNA export from host cell nucleus; ISO:MGI.
DR DisProt; DP02371; -.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR025715; FoP_C.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF13865; FoP_duplication; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM01218; FoP_duplication; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Chaperone; Citrullination;
KW Cytoplasm; Methylation; mRNA processing; mRNA splicing; mRNA transport;
KW Nucleus; Phosphoprotein; Reference proteome; RNA-binding; Spliceosome;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q86V81"
FT CHAIN 2..255
FT /note="THO complex subunit 4"
FT /id="PRO_0000081975"
FT DOMAIN 105..182
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 16..37
FT /note="Sufficient for RNA-binding, interaction with NXF1-
FT NXT1 heterodimer"
FT /evidence="ECO:0000250"
FT REGION 185..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q86V81"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86V81"
FT MOD_RES 38
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 38
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 58
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q86V81"
FT MOD_RES 63
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q86V81"
FT MOD_RES 70
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q86V81"
FT MOD_RES 85
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86V81"
FT MOD_RES 140
FT /note="Citrulline"
FT /evidence="ECO:0000269|PubMed:24463520"
FT MOD_RES 196
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 196
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 203
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q86V81"
FT MOD_RES 203
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q86V81"
FT MOD_RES 203
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 218
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q86V81"
FT MOD_RES 233
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q86V81"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86V81"
FT VAR_SEQ 14..105
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10786854"
FT /id="VSP_008597"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:1NO8"
FT HELIX 118..128
FT /evidence="ECO:0007829|PDB:1NO8"
FT STRAND 131..137
FT /evidence="ECO:0007829|PDB:1NO8"
FT STRAND 147..153
FT /evidence="ECO:0007829|PDB:1NO8"
FT HELIX 155..165
FT /evidence="ECO:0007829|PDB:1NO8"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:1NO8"
SQ SEQUENCE 255 AA; 26940 MW; F597235EBDD47C17 CRC64;
MADKMDMSLD DIIKLNRSQR GGRGGGRGRG RAGSQGGRGG AVQAAARVNR GGGPMRNRPA
IARGAAGGGR NRPAPYSRPK QLPDKWQHDL FDSGFGGGAG VETGGKLLVS NLDFGVSDAD
IQELFAEFGT LKKAAVHYDR SGRSLGTADV HFERKADALK AMKQYNGVPL DGRPMNIQLV
TSQIDTQRRP AQSINRGGMT RNRGSGGFGG GGTRRGTRGG SRGRGRGTGR NSKQQLSAEE
LDAQLDAYNA RMDTS
