ID TBA3_MOUSE Reviewed; 450 AA. AC P05214; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 13-AUG-1987, sequence version 1. DT 24-JAN-2024, entry version 202. DE RecName: Full=Tubulin alpha-3 chain; DE EC=3.6.5.- {ECO:0000250|UniProtKB:P68363}; DE AltName: Full=Alpha-tubulin 3/7; DE AltName: Full=Alpha-tubulin isotype M-alpha-3/7; DE AltName: Full=Tubulin alpha-3/alpha-7 chain; DE Contains: DE RecName: Full=Detyrosinated tubulin alpha-3 chain; GN Name=Tuba3a; Synonyms=Tuba3; GN and GN Name=Tuba3b; Synonyms=Tuba7; 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], AND TISSUE SPECIFICITY. RX PubMed=3785200; DOI=10.1128/mcb.6.7.2409-2419.1986; RA Villasante A., Wang D., Dobner P., Dolph P., Lewis S.A., Cowan N.J.; RT "Six mouse alpha-tubulin mRNAs encode five distinct isotypes: testis- RT specific expression of two sister genes."; RL Mol. Cell. Biol. 6:2409-2419(1986). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; 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 [3] RP PROTEIN SEQUENCE OF 230-280, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Brain, and Hippocampus; RA Lubec G., Klug S., Yang J.W., Zigmond M.; RL Submitted (JUL-2007) to UniProtKB. RN [4] RP GLUTAMYLATION. RX PubMed=15890843; DOI=10.1126/science.1113010; RA Janke C., Rogowski K., Wloga D., Regnard C., Kajava A.V., Strub J.-M., RA Temurak N., van Dijk J., Boucher D., van Dorsselaer A., Suryavanshi S., RA Gaertig J., Edde B.; RT "Tubulin polyglutamylase enzymes are members of the TTL domain protein RT family."; RL Science 308:1758-1762(2005). RN [5] RP TYROSINATION. RX PubMed=16954346; DOI=10.1083/jcb.200512058; RA Peris L., Thery M., Faure J., Saoudi Y., Lafanechere L., Chilton J.K., RA Gordon-Weeks P., Galjart N., Bornens M., Wordeman L., Wehland J., RA Andrieux A., Job D.; RT "Tubulin tyrosination is a major factor affecting the recruitment of CAP- RT Gly proteins at microtubule plus ends."; RL J. Cell Biol. 174:839-849(2006). RN [6] RP GLYCYLATION. RX PubMed=19524510; DOI=10.1016/j.cell.2009.05.020; RA Rogowski K., Juge F., van Dijk J., Wloga D., Strub J.-M., Levilliers N., RA Thomas D., Bre M.-H., Van Dorsselaer A., Gaertig J., Janke C.; RT "Evolutionary divergence of enzymatic mechanisms for posttranslational RT polyglycylation."; RL Cell 137:1076-1087(2009). RN [7] RP TYROSINATION. RX PubMed=19564401; DOI=10.1083/jcb.200902142; RA Peris L., Wagenbach M., Lafanechere L., Brocard J., Moore A.T., RA Kozielski F., Job D., Wordeman L., Andrieux A.; RT "Motor-dependent microtubule disassembly driven by tubulin tyrosination."; RL J. Cell Biol. 185:1159-1166(2009). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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 GLYCYLATION, AND GLUTAMYLATION. RX PubMed=23897886; DOI=10.1083/jcb.201305041; RA Bosch Grau M., Gonzalez Curto G., Rocha C., Magiera M.M., Marques Sousa P., RA Giordano T., Spassky N., Janke C.; RT "Tubulin glycylases and glutamylases have distinct functions in RT stabilization and motility of ependymal cilia."; RL J. Cell Biol. 202:441-451(2013). RN [10] RP DETYROSINATION. RX PubMed=26446751; DOI=10.1038/ncomms9526; RA Kerr J.P., Robison P., Shi G., Bogush A.I., Kempema A.M., Hexum J.K., RA Becerra N., Harki D.A., Martin S.S., Raiteri R., Prosser B.L., Ward C.W.; RT "Detyrosinated microtubules modulate mechanotransduction in heart and RT skeletal muscle."; RL Nat. Commun. 6:8526-8526(2015). RN [11] RP DETYROSINATION. RX PubMed=27102488; DOI=10.1126/science.aaf0659; RA Robison P., Caporizzo M.A., Ahmadzadeh H., Bogush A.I., Chen C.Y., RA Margulies K.B., Shenoy V.B., Prosser B.L.; RT "Detyrosinated microtubules buckle and bear load in contracting RT cardiomyocytes."; RL Science 352:417-428(2016). RN [12] RP DETYROSINATION. RX PubMed=29146868; DOI=10.1126/science.aao4165; RA Aillaud C., Bosc C., Peris L., Bosson A., Heemeryck P., Van Dijk J., RA Le Friec J., Boulan B., Vossier F., Sanman L.E., Syed S., Amara N., RA Coute Y., Lafanechere L., Denarier E., Delphin C., Pelletier L., RA Humbert S., Bogyo M., Andrieux A., Rogowski K., Moutin M.J.; RT "Vasohibins/SVBP are tubulin carboxypeptidases (TCPs) that regulate neuron RT differentiation."; RL Science 358:1448-1453(2017). RN [13] RP GLYCYLATION. RX PubMed=33414192; DOI=10.1126/science.abd4914; RA Gadadhar S., Alvarez Viar G., Hansen J.N., Gong A., Kostarev A., RA Ialy-Radio C., Leboucher S., Whitfield M., Ziyyat A., Toure A., Alvarez L., RA Pigino G., Janke C.; RT "Tubulin glycylation controls axonemal dynein activity, flagellar beat, and RT male fertility."; RL Science 371:0-0(2021). CC -!- FUNCTION: Tubulin is the major constituent of microtubules, a cylinder CC consisting of laterally associated linear protofilaments composed of CC alpha- and beta-tubulin heterodimers. Microtubules grow by the addition CC of GTP-tubulin dimers to the microtubule end, where a stabilizing cap CC forms. Below the cap, tubulin dimers are in GDP-bound state, owing to CC GTPase activity of alpha-tubulin. CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; CC Evidence={ECO:0000250|UniProtKB:P68363}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; CC Evidence={ECO:0000250|UniProtKB:P68363}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P68363}; CC -!- SUBUNIT: Dimer of alpha and beta chains. A typical microtubule is a CC hollow water-filled tube with an outer diameter of 25 nm and an inner CC diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to CC form protofilaments running lengthwise along the microtubule wall with CC the beta-tubulin subunit facing the microtubule plus end conferring a CC structural polarity. Microtubules usually have 13 protofilaments but CC different protofilament numbers can be found in some organisms and CC specialized cells. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. CC -!- TISSUE SPECIFICITY: Alpha-3 and alpha-7 are identical but coded by two CC different genes, they are testis-specific. CC {ECO:0000269|PubMed:3785200}. CC -!- DOMAIN: The MREC motif may be critical for tubulin autoregulation. CC {ECO:0000250|UniProtKB:P68363}. CC -!- PTM: Some glutamate residues at the C-terminus are polyglycylated, CC resulting in polyglycine chains on the gamma-carboxyl group. CC Glycylation is mainly limited to tubulin incorporated into axonemes CC (cilia and flagella) whereas glutamylation is prevalent in neuronal CC cells, centrioles, axonemes, and the mitotic spindle. Both CC modifications can coexist on the same protein on adjacent residues, and CC lowering polyglycylation levels increases polyglutamylation, and CC reciprocally. Cilia and flagella glycylation is required for their CC stability and maintenance. Flagella glycylation controls sperm motility CC (PubMed:33414192). {ECO:0000269|PubMed:19524510, CC ECO:0000269|PubMed:23897886, ECO:0000269|PubMed:33414192}. CC -!- PTM: Some glutamate residues at the C-terminus are polyglutamylated, CC resulting in polyglutamate chains on the gamma-carboxyl group CC (PubMed:15890843). Polyglutamylation plays a key role in microtubule CC severing by spastin (SPAST). SPAST preferentially recognizes and acts CC on microtubules decorated with short polyglutamate tails: severing CC activity by SPAST increases as the number of glutamates per tubulin CC rises from one to eight, but decreases beyond this glutamylation CC threshold (By similarity). Glutamylation is also involved in cilia CC motility (PubMed:23897886). {ECO:0000250|UniProtKB:Q71U36, CC ECO:0000269|PubMed:15890843, ECO:0000269|PubMed:23897886}. CC -!- PTM: Acetylation of alpha chains at Lys-40 is located inside the CC microtubule lumen. This modification has been correlated with increased CC microtubule stability, intracellular transport and ciliary assembly. CC {ECO:0000250|UniProtKB:Q71U36}. CC -!- PTM: Methylation of alpha chains at Lys-40 is found in mitotic CC microtubules and is required for normal mitosis and cytokinesis CC contributing to genomic stability. {ECO:0000250|UniProtKB:P68363}. CC -!- PTM: Nitration of Tyr-450 is irreversible and interferes with normal CC dynein intracellular distribution. {ECO:0000250|UniProtKB:Q71U36}. CC -!- PTM: Undergoes a tyrosination/detyrosination cycle, the cyclic removal CC and re-addition of a C-terminal tyrosine residue by the enzymes tubulin CC tyrosine carboxypeptidase (MATCAP, VASH1 or VASH2) and tubulin tyrosine CC ligase (TTL), respectively. {ECO:0000269|PubMed:16954346, CC ECO:0000269|PubMed:19564401, ECO:0000269|PubMed:26446751, CC ECO:0000269|PubMed:27102488, ECO:0000269|PubMed:29146868}. CC -!- PTM: [Tubulin alpha-3 chain]: Tyrosination promotes microtubule CC interaction with CAP-Gly domain-containing proteins such as CLIP1, CC CLIP2 and DCTN1 (PubMed:16954346, PubMed:19564401). Tyrosination CC regulates the initiation of dynein-dynactin motility via interaction CC with DCTN1, which brings the dynein-dynactin complex into contact with CC microtubules. In neurons, tyrosinated tubulins mediate the initiation CC of retrograde vesicle transport (By similarity). CC {ECO:0000250|UniProtKB:Q71U36, ECO:0000269|PubMed:16954346, CC ECO:0000269|PubMed:19564401}. CC -!- PTM: [Detyrosinated tubulin alpha-3 chain]: Detyrosination is involved CC in metaphase plate congression by guiding chromosomes during mitosis: CC detyrosination promotes interaction with CENPE, promoting pole-proximal CC transport of chromosomes toward the equator (By similarity). CC Detyrosination increases microtubules-dependent mechanotransduction in CC dystrophic cardiac and skeletal muscle (PubMed:26446751). In CC cardiomyocytes, detyrosinated microtubules are required to resist to CC contractile compression during contraction: detyrosination promotes CC association with desmin (DES) at force-generating sarcomeres, leading CC to buckled microtubules and mechanical resistance to contraction CC (PubMed:27102488). {ECO:0000250|UniProtKB:Q6PEY2, CC ECO:0000269|PubMed:26446751, ECO:0000269|PubMed:27102488}. CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M13442; AAA40501.1; -; mRNA. DR EMBL; M13443; AAA40504.1; -; mRNA. DR EMBL; BC050769; AAH50769.1; -; mRNA. DR EMBL; BC050770; AAH50770.1; -; mRNA. DR CCDS; CCDS39640.1; -. DR CCDS; CCDS39707.1; -. DR PIR; I77426; I77426. DR RefSeq; NP_033472.1; NM_009446.3. DR RefSeq; NP_033475.1; NM_009449.3. DR PDB; 8I7O; EM; 4.50 A; AE/AG/AI/BE/BG/BI/CG/CI/DE/DG/EE/EG/FE/FG/GE/GG/GI/HE/HG/HI/IE/IG/II/JE/JG/KE/KG/KI/LE/LG=1-438. DR PDB; 8I7R; EM; 6.50 A; AC/AE/AG/AI/AK/AM/BC/BE/BG/BI/BK/BM/CC/CE/CG/CI/CK/CM/DA/DC/DE/DG/DI/DK/EA/EC/EE/EG/EI/EK=1-438. DR PDB; 8IYJ; EM; 3.50 A; AA/AC/AE/AG/AI/AK/AM/AO/BC/BE/BG/BI/BK/BM/BO/CC/CE/CG/CI/CK/CM/CO/CQ/DC/DE/DG/DI/DK/DM/DO=1-450. DR PDBsum; 8I7O; -. DR PDBsum; 8I7R; -. DR PDBsum; 8IYJ; -. DR AlphaFoldDB; P05214; -. DR EMDB; EMD-35823; -. DR SMR; P05214; -. DR BioGRID; 204374; 73. DR BioGRID; 204377; 1. DR IntAct; P05214; 69. DR STRING; 10090.ENSMUSP00000084713; -. DR GlyGen; P05214; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P05214; -. DR PhosphoSitePlus; P05214; -. DR SwissPalm; P05214; -. DR REPRODUCTION-2DPAGE; P05214; -. DR jPOST; P05214; -. DR PaxDb; 10090-ENSMUSP00000084713; -. DR PeptideAtlas; P05214; -. DR ProteomicsDB; 254819; -. DR Pumba; P05214; -. DR Antibodypedia; 60456; 48 antibodies from 10 providers. DR DNASU; 22144; -. DR DNASU; 22147; -. DR Ensembl; ENSMUST00000087445.7; ENSMUSP00000084713.7; ENSMUSG00000067338.7. DR Ensembl; ENSMUST00000088246.6; ENSMUSP00000085580.6; ENSMUSG00000067702.6. DR GeneID; 22144; -. DR GeneID; 22147; -. DR KEGG; mmu:22147; -. DR UCSC; uc009dui.1; mouse. DR CTD; 22147; -. DR MGI; MGI:1095406; Tuba3a. DR MGI; MGI:1095408; Tuba3b. DR VEuPathDB; HostDB:ENSMUSG00000067338; -. DR VEuPathDB; HostDB:ENSMUSG00000067702; -. DR eggNOG; KOG1376; Eukaryota. DR GeneTree; ENSGT00950000182825; -. DR HOGENOM; CLU_015718_0_0_1; -. DR InParanoid; P05214; -. DR OMA; RRMADQC; -. DR OrthoDB; 899149at2759; -. DR PhylomeDB; P05214; -. DR TreeFam; TF300314; -. DR Reactome; R-MMU-190840; Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane. DR Reactome; R-MMU-2132295; MHC class II antigen presentation. DR Reactome; R-MMU-2467813; Separation of Sister Chromatids. DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion. DR Reactome; R-MMU-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand. DR Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes. DR Reactome; R-MMU-437239; Recycling pathway of L1. DR Reactome; R-MMU-5610787; Hedgehog 'off' state. DR Reactome; R-MMU-5617833; Cilium Assembly. DR Reactome; R-MMU-5620924; Intraflagellar transport. DR Reactome; R-MMU-5626467; RHO GTPases activate IQGAPs. DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins. DR Reactome; R-MMU-6807878; COPI-mediated anterograde transport. DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic. DR Reactome; R-MMU-6811436; COPI-independent Golgi-to-ER retrograde traffic. DR Reactome; R-MMU-68877; Mitotic Prometaphase. DR Reactome; R-MMU-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint. DR Reactome; R-MMU-8955332; Carboxyterminal post-translational modifications of tubulin. DR Reactome; R-MMU-9646399; Aggrephagy. DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation. DR Reactome; R-MMU-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III. DR Reactome; R-MMU-983189; Kinesins. DR Reactome; R-MMU-9833482; PKR-mediated signaling. DR BioGRID-ORCS; 22144; 1 hit in 79 CRISPR screens. DR BioGRID-ORCS; 22147; 4 hits in 80 CRISPR screens. DR ChiTaRS; Tuba3a; mouse. DR ChiTaRS; Tuba3b; mouse. DR PRO; PR:P05214; -. DR Proteomes; UP000000589; Chromosome 6. DR RNAct; P05214; Protein. DR Bgee; ENSMUSG00000067338; Expressed in spermatocyte and 51 other cell types or tissues. DR ExpressionAtlas; P05214; baseline and differential. DR Genevisible; P05214; MM. DR GO; GO:0036064; C:ciliary basal body; IDA:MGI. DR GO; GO:0005929; C:cilium; IDA:MGI. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005874; C:microtubule; IDA:MGI. DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI. DR GO; GO:0005525; F:GTP binding; IBA:GO_Central. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central. DR GO; GO:0036098; P:male germ-line stem cell population maintenance; IMP:MGI. DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central. DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central. DR CDD; cd02186; alpha_tubulin; 1. DR Gene3D; 1.10.287.600; Helix hairpin bin; 1. DR Gene3D; 3.30.1330.20; Tubulin/FtsZ, C-terminal domain; 1. DR Gene3D; 3.40.50.1440; Tubulin/FtsZ, GTPase domain; 1. DR InterPro; IPR002452; Alpha_tubulin. DR InterPro; IPR008280; Tub_FtsZ_C. DR InterPro; IPR000217; Tubulin. DR InterPro; IPR037103; Tubulin/FtsZ-like_C. DR InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom. DR InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf. DR InterPro; IPR023123; Tubulin_C. DR InterPro; IPR017975; Tubulin_CS. DR InterPro; IPR003008; Tubulin_FtsZ_GTPase. DR PANTHER; PTHR11588; TUBULIN; 1. DR PANTHER; PTHR11588:SF113; TUBULIN ALPHA-3D CHAIN; 1. DR Pfam; PF00091; Tubulin; 1. DR Pfam; PF03953; Tubulin_C; 1. DR PRINTS; PR01162; ALPHATUBULIN. DR PRINTS; PR01161; TUBULIN. DR SMART; SM00864; Tubulin; 1. DR SMART; SM00865; Tubulin_C; 1. DR SUPFAM; SSF55307; Tubulin C-terminal domain-like; 1. DR SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1. DR PROSITE; PS00227; TUBULIN; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cytoplasm; Cytoskeleton; KW Direct protein sequencing; GTP-binding; Hydrolase; Magnesium; KW Metal-binding; Methylation; Microtubule; Nitration; Nucleotide-binding; KW Phosphoprotein; Reference proteome. FT CHAIN 1..450 FT /note="Tubulin alpha-3 chain" FT /id="PRO_0000048122" FT CHAIN 1..449 FT /note="Detyrosinated tubulin alpha-3 chain" FT /evidence="ECO:0000305|PubMed:26446751, FT ECO:0000305|PubMed:27102488, ECO:0000305|PubMed:29146868" FT /id="PRO_0000437401" FT MOTIF 1..4 FT /note="MREC motif" FT /evidence="ECO:0000250|UniProtKB:P68363" FT ACT_SITE 254 FT /evidence="ECO:0000250|UniProtKB:P68363" FT BINDING 11 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P68363" FT BINDING 71 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P68363" FT BINDING 71 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P68363" FT BINDING 140 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P68363" FT BINDING 144 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P68363" FT BINDING 145 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P68363" FT BINDING 179 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P68363" FT BINDING 206 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P68363" FT BINDING 228 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P68363" FT SITE 450 FT /note="Involved in polymerization" FT /evidence="ECO:0000250" FT MOD_RES 40 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9BQE3" FT MOD_RES 48 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P68366" FT MOD_RES 83 FT /note="3'-nitrotyrosine" FT /evidence="ECO:0000250|UniProtKB:P68368" FT MOD_RES 432 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q9BQE3" FT MOD_RES 439 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9BQE3" FT MOD_RES 450 FT /note="3'-nitrotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q71U36" SQ SEQUENCE 450 AA; 49960 MW; 2A78714CBA782D55 CRC64; MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN TFFSETGAGK HVPRAVFVDL EPTVVDEVRT GTYRQLFHPE QLITGKEDAA NNYARGHYTI GKEIVDLVLD RIRKLADLCT GLQGFLIFHS FGGGTGSGFA SLLMERLSVD YGKKSKLEFA IYPAPQVSTA VVEPYNSILT THTTLEHSDC AFMVDNEAIY DICRRNLDIE RPTYTNLNRL IGQIVSSITA SLRFDGALNV DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLSVAE ITNACFEPAN QMVKCDPRHG KYMACCMLYR GDVVPKDVNA AIATIKTKRT IQFVDWCPTG FKVGINYQPP TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE AREDLAALEK DYEEVGVDSV EAEAEEGEEY //