TBB4A_HUMAN
ID TBB4A_HUMAN Reviewed; 444 AA.
AC P04350; B3KQP4; Q969E5;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 223.
DE RecName: Full=Tubulin beta-4A chain;
DE AltName: Full=Tubulin 5 beta;
DE AltName: Full=Tubulin beta-4 chain;
GN Name=TUBB4A; Synonyms=TUBB4, TUBB5;
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 [GENOMIC DNA], AND VARIANTS MET-155 AND VAL-365.
RX PubMed=6462917; DOI=10.1093/nar/12.14.5823;
RA Lee M.G.-S., Loomis C., Cowan N.J.;
RT "Sequence of an expressed human beta-tubulin gene containing ten Alu family
RT members.";
RL Nucleic Acids Res. 12:5823-5836(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Uterus;
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 PROTEIN SEQUENCE OF 283-289 AND 310-318.
RC TISSUE=Brain;
RX PubMed=8619814; DOI=10.1006/bbrc.1996.0211;
RA Baumann M.H., Wisniewski T., Levy E., Plant G.T., Ghiso J.;
RT "C-terminal fragments of alpha- and beta-tubulin form amyloid fibrils in
RT vitro and associate with amyloid deposits of familial cerebral amyloid
RT angiopathy, British type.";
RL Biochem. Biophys. Res. Commun. 219:238-242(1996).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [7]
RP PHOSPHORYLATION AT SER-172.
RX PubMed=16371510; DOI=10.1091/mbc.e05-07-0621;
RA Fourest-Lieuvin A., Peris L., Gache V., Garcia-Saez I., Juillan-Binard C.,
RA Lantez V., Job D.;
RT "Microtubule regulation in mitosis: tubulin phosphorylation by the cyclin-
RT dependent kinase Cdk1.";
RL Mol. Biol. Cell 17:1041-1050(2006).
RN [8]
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 [9]
RP TISSUE SPECIFICITY.
RX PubMed=20191564; DOI=10.1002/cm.20436;
RA Leandro-Garcia L.J., Leskela S., Landa I., Montero-Conde C.,
RA Lopez-Jimenez E., Leton R., Cascon A., Robledo M., Rodriguez-Antona C.;
RT "Tumoral and tissue-specific expression of the major human beta-tubulin
RT isotypes.";
RL Cytoskeleton 67:214-223(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP GLUTAMYLATION.
RX PubMed=26875866; DOI=10.1016/j.cell.2016.01.019;
RA Valenstein M.L., Roll-Mecak A.;
RT "Graded control of microtubule severing by tubulin glutamylation.";
RL Cell 164:911-921(2016).
RN [12]
RP VARIANT HLD ASN-249.
RX PubMed=23582646; DOI=10.1016/j.ajhg.2013.03.018;
RA Simons C., Wolf N.I., McNeil N., Caldovic L., Devaney J.M., Takanohashi A.,
RA Crawford J., Ru K., Grimmond S.M., Miller D., Tonduti D., Schmidt J.L.,
RA Chudnow R.S., van Coster R., Lagae L., Kisler J., Sperner J.,
RA van der Knaap M.S., Schiffmann R., Taft R.J., Vanderver A.;
RT "A de novo mutation in the beta-tubulin gene TUBB4A results in the
RT leukoencephalopathy hypomyelination with atrophy of the basal ganglia and
RT cerebellum.";
RL Am. J. Hum. Genet. 92:767-773(2013).
RN [13]
RP VARIANT DYT4 GLY-2, AND TISSUE SPECIFICITY.
RX PubMed=23424103; DOI=10.1002/ana.23832;
RA Hersheson J., Mencacci N.E., Davis M., Macdonald N., Trabzuni D., Ryten M.,
RA Pittman A., Paudel R., Kara E., Fawcett K., Plagnol V., Bhatia K.P.,
RA Medlar A.J., Stanescu H.C., Hardy J., Kleta R., Wood N.W., Houlden H.;
RT "Mutations in the autoregulatory domain of beta-tubulin 4a cause hereditary
RT dystonia.";
RL Ann. Neurol. 73:546-553(2013).
CC -!- FUNCTION: Tubulin is the major constituent of microtubules. It binds
CC two moles of GTP, one at an exchangeable site on the beta chain and one
CC at a non-exchangeable site on the alpha chain.
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 -!- INTERACTION:
CC P04350; Q5S007: LRRK2; NbExp=6; IntAct=EBI-355007, EBI-5323863;
CC P04350; P22736: NR4A1; NbExp=2; IntAct=EBI-355007, EBI-721550;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- TISSUE SPECIFICITY: Major isotype in brain, where it represents 46% of
CC all beta-tubulins. In the brain, highest expression levels in the
CC cerebellum, followed by putamen and white matter. Moderate levels in
CC testis. Very low levels, if any, in other tissues.
CC {ECO:0000269|PubMed:20191564, ECO:0000269|PubMed:23424103}.
CC -!- DOMAIN: The highly acidic C-terminal region may bind cations such as
CC calcium.
CC -!- DOMAIN: The MREI motif is common among all beta-tubulin isoforms and
CC may be critical for tubulin autoregulation.
CC {ECO:0000250|UniProtKB:P07437}.
CC -!- PTM: Some glutamate residues at the C-terminus are polyglutamylated,
CC resulting in polyglutamate chains on the gamma-carboxyl group
CC (PubMed:26875866). 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 (PubMed:26875866). Glutamylation is also involved in cilia
CC motility (By similarity). {ECO:0000250|UniProtKB:P99024,
CC ECO:0000269|PubMed:26875866}.
CC -!- PTM: Some glutamate residues at the C-terminus are monoglycylated but
CC not polyglycylated due to the absence of functional TTLL10 in human.
CC Monoglycylation is mainly limited to tubulin incorporated into cilia
CC and flagella axonemes, which is required for their stability and
CC maintenance. Flagella glycylation controls sperm motility. Both
CC polyglutamylation and monoglycylation can coexist on the same protein
CC on adjacent residues, and lowering glycylation levels increases
CC polyglutamylation, and reciprocally. {ECO:0000250|UniProtKB:P07437,
CC ECO:0000305|PubMed:19524510}.
CC -!- PTM: Phosphorylated on Ser-172 by CDK1 during the cell cycle, from
CC metaphase to telophase, but not in interphase. This phosphorylation
CC inhibits tubulin incorporation into microtubules.
CC {ECO:0000269|PubMed:16371510}.
CC -!- DISEASE: Dystonia 4, torsion, autosomal dominant (DYT4) [MIM:128101]: A
CC form of torsion dystonia, a disease defined by the presence of
CC sustained involuntary muscle contractions, often leading to abnormal
CC postures. 'Torsion' refers to the twisting nature of body movements,
CC often affecting the trunk. DYT4 is characterized by onset in the second
CC to third decade of progressive laryngeal dysphonia followed by the
CC involvement of other muscles, such as the neck or limbs. Some patients
CC develop an ataxic gait. {ECO:0000269|PubMed:23424103}. Note=The disease
CC is caused by variants affecting the gene represented in this entry.
CC -!- DISEASE: Leukodystrophy, hypomyelinating, 6 (HLD) [MIM:612438]: A
CC neurologic disorder characterized by onset in infancy or early
CC childhood of delayed motor development and gait instability, followed
CC by extrapyramidal movement disorders, such as dystonia,
CC choreoathetosis, rigidity, opisthotonus, and oculogyric crises,
CC progressive spastic tetraplegia, ataxia, and, more rarely, seizures.
CC Most patients have cognitive decline and speech delay, but some can
CC function normally. Brain MRI shows a combination of hypomyelination,
CC cerebellar atrophy, and atrophy or disappearance of the putamen.
CC {ECO:0000269|PubMed:23582646}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; X00734; CAA25318.1; -; Genomic_DNA.
DR EMBL; AK075307; BAG52106.1; -; mRNA.
DR EMBL; CH471139; EAW69078.1; -; Genomic_DNA.
DR EMBL; BC006570; AAH06570.1; -; mRNA.
DR EMBL; BC013683; AAH13683.1; -; mRNA.
DR CCDS; CCDS12168.1; -.
DR PIR; A02972; UBHU5B.
DR RefSeq; NP_001276052.1; NM_001289123.1.
DR RefSeq; NP_001276056.1; NM_001289127.1.
DR RefSeq; NP_001276058.1; NM_001289129.1.
DR RefSeq; NP_001276059.1; NM_001289130.1.
DR RefSeq; NP_001276060.1; NM_001289131.1.
DR RefSeq; NP_006078.2; NM_006087.3.
DR AlphaFoldDB; P04350; -.
DR SMR; P04350; -.
DR BioGRID; 115655; 212.
DR IntAct; P04350; 89.
DR MINT; P04350; -.
DR STRING; 9606.ENSP00000264071; -.
DR ChEMBL; CHEMBL3838; -.
DR DrugBank; DB11638; Artenimol.
DR DrugBank; DB05147; CYT997.
DR DrugBank; DB01873; Epothilone D.
DR DrugBank; DB03010; Patupilone.
DR DrugBank; DB06042; ZEN-012.
DR DrugCentral; P04350; -.
DR GlyGen; P04350; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P04350; -.
DR MetOSite; P04350; -.
DR PhosphoSitePlus; P04350; -.
DR SwissPalm; P04350; -.
DR BioMuta; TUBB4A; -.
DR DMDM; 93141323; -.
DR OGP; P04350; -.
DR REPRODUCTION-2DPAGE; IPI00023598; -.
DR EPD; P04350; -.
DR jPOST; P04350; -.
DR MassIVE; P04350; -.
DR MaxQB; P04350; -.
DR PaxDb; P04350; -.
DR PeptideAtlas; P04350; -.
DR PRIDE; P04350; -.
DR ProteomicsDB; 51702; -.
DR TopDownProteomics; P04350; -.
DR Antibodypedia; 4387; 216 antibodies from 21 providers.
DR DNASU; 10382; -.
DR Ensembl; ENST00000264071.7; ENSP00000264071.1; ENSG00000104833.12.
DR GeneID; 10382; -.
DR KEGG; hsa:10382; -.
DR MANE-Select; ENST00000264071.7; ENSP00000264071.1; NM_006087.4; NP_006078.2.
DR UCSC; uc002mfg.2; human.
DR CTD; 10382; -.
DR DisGeNET; 10382; -.
DR GeneCards; TUBB4A; -.
DR GeneReviews; TUBB4A; -.
DR HGNC; HGNC:20774; TUBB4A.
DR HPA; ENSG00000104833; Group enriched (adrenal gland, brain).
DR MalaCards; TUBB4A; -.
DR MIM; 128101; phenotype.
DR MIM; 602662; gene.
DR MIM; 612438; phenotype.
DR neXtProt; NX_P04350; -.
DR OpenTargets; ENSG00000104833; -.
DR Orphanet; 139441; Hypomyelination with atrophy of basal ganglia and cerebellum.
DR Orphanet; 98805; Primary dystonia, DYT4 type.
DR PharmGKB; PA134949465; -.
DR VEuPathDB; HostDB:ENSG00000104833; -.
DR eggNOG; KOG1375; Eukaryota.
DR GeneTree; ENSGT00940000161972; -.
DR HOGENOM; CLU_015718_1_1_1; -.
DR InParanoid; P04350; -.
DR OMA; MQLERIN; -.
DR OrthoDB; 962471at2759; -.
DR PhylomeDB; P04350; -.
DR TreeFam; TF300298; -.
DR PathwayCommons; P04350; -.
DR Reactome; R-HSA-1445148; Translocation of SLC2A4 (GLUT4) to the plasma membrane.
DR Reactome; R-HSA-190840; Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
DR Reactome; R-HSA-190861; Gap junction assembly.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-HSA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-HSA-389957; Prefoldin mediated transfer of substrate to CCT/TriC.
DR Reactome; R-HSA-389960; Formation of tubulin folding intermediates by CCT/TriC.
DR Reactome; R-HSA-389977; Post-chaperonin tubulin folding pathway.
DR Reactome; R-HSA-437239; Recycling pathway of L1.
DR Reactome; R-HSA-5610787; Hedgehog 'off' state.
DR Reactome; R-HSA-5617833; Cilium Assembly.
DR Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-HSA-5620924; Intraflagellar transport.
DR Reactome; R-HSA-5626467; RHO GTPases activate IQGAPs.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-HSA-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-HSA-68877; Mitotic Prometaphase.
DR Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-HSA-8854518; AURKA Activation by TPX2.
DR Reactome; R-HSA-8955332; Carboxyterminal post-translational modifications of tubulin.
DR Reactome; R-HSA-9609690; HCMV Early Events.
DR Reactome; R-HSA-9609736; Assembly and cell surface presentation of NMDA receptors.
DR Reactome; R-HSA-9619483; Activation of AMPK downstream of NMDARs.
DR Reactome; R-HSA-9646399; Aggrephagy.
DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR Reactome; R-HSA-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III.
DR Reactome; R-HSA-983189; Kinesins.
DR SignaLink; P04350; -.
DR SIGNOR; P04350; -.
DR BioGRID-ORCS; 10382; 29 hits in 1068 CRISPR screens.
DR ChiTaRS; TUBB4A; human.
DR GeneWiki; TUBB4; -.
DR GenomeRNAi; 10382; -.
DR Pharos; P04350; Tclin.
DR PRO; PR:P04350; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P04350; protein.
DR Bgee; ENSG00000104833; Expressed in right hemisphere of cerebellum and 129 other tissues.
DR ExpressionAtlas; P04350; baseline and differential.
DR Genevisible; P04350; HS.
DR GO; GO:0005930; C:axoneme; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0045171; C:intercellular bridge; IDA:HPA.
DR GO; GO:0033269; C:internode region of axon; IEA:Ensembl.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
DR GO; GO:0072686; C:mitotic spindle; IDA:HPA.
DR GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IMP:CAFA.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0031115; P:negative regulation of microtubule polymerization; IMP:CAFA.
DR Gene3D; 1.10.287.600; -; 1.
DR Gene3D; 3.30.1330.20; -; 1.
DR Gene3D; 3.40.50.1440; -; 1.
DR InterPro; IPR013838; Beta-tubulin_BS.
DR InterPro; IPR002453; Beta_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; PTHR11588; 1.
DR Pfam; PF00091; Tubulin; 1.
DR Pfam; PF03953; Tubulin_C; 1.
DR PRINTS; PR01163; BETATUBULIN.
DR PRINTS; PR01161; TUBULIN.
DR SMART; SM00864; Tubulin; 1.
DR SMART; SM00865; Tubulin_C; 1.
DR SUPFAM; SSF52490; SSF52490; 1.
DR SUPFAM; SSF55307; SSF55307; 1.
DR PROSITE; PS00227; TUBULIN; 1.
DR PROSITE; PS00228; TUBULIN_B_AUTOREG; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; Direct protein sequencing; Disease variant;
KW Dystonia; GTP-binding; Isopeptide bond; Leukodystrophy; Microtubule;
KW Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..444
FT /note="Tubulin beta-4A chain"
FT /id="PRO_0000048252"
FT MOTIF 1..4
FT /note="MREI motif"
FT /evidence="ECO:0000250|UniProtKB:P07437"
FT BINDING 140..146
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT MOD_RES 172
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000269|PubMed:16371510"
FT MOD_RES 436
FT /note="5-glutamyl polyglutamate"
FT /evidence="ECO:0000250|UniProtKB:Q2T9S0"
FT VARIANT 2
FT /note="R -> G (in DYT4; dbSNP:rs587776983)"
FT /evidence="ECO:0000269|PubMed:23424103"
FT /id="VAR_069798"
FT VARIANT 155
FT /note="I -> M (in dbSNP:rs1053262)"
FT /evidence="ECO:0000269|PubMed:6462917"
FT /id="VAR_052673"
FT VARIANT 249
FT /note="D -> N (in HLD; dbSNP:rs483352809)"
FT /evidence="ECO:0000269|PubMed:23582646"
FT /id="VAR_069799"
FT VARIANT 365
FT /note="A -> V (in dbSNP:rs1053267)"
FT /evidence="ECO:0000269|PubMed:6462917"
FT /id="VAR_026044"
FT CONFLICT 269
FT /note="G -> A (in Ref. 1; CAA25318)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="A -> G (in Ref. 1; CAA25318)"
FT /evidence="ECO:0000305"
FT CONFLICT 432
FT /note="E -> Q (in Ref. 1; CAA25318)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 444 AA; 49586 MW; F7429D057C11A3F5 CRC64;
MREIVHLQAG QCGNQIGAKF WEVISDEHGI DPTGTYHGDS DLQLERINVY YNEATGGNYV
PRAVLVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDAVLDVV
RKEAESCDCL QGFQLTHSLG GGTGSGMGTL LISKIREEFP DRIMNTFSVV PSPKVSDTVV
EPYNATLSVH QLVENTDETY CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL
RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQMFDAKNMM
AACDPRHGRY LTVAAVFRGR MSMKEVDEQM LSVQSKNSSY FVEWIPNNVK TAVCDIPPRG
LKMAATFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
EYQQYQDATA EEGEFEEEAE EEVA
