DTNA_MOUSE
ID DTNA_MOUSE Reviewed; 746 AA.
AC Q9D2N4; P97319; Q61498; Q61499; Q9QZZ5; Q9WUL9; Q9WUM0;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Dystrobrevin alpha;
DE Short=DTN-A;
DE AltName: Full=Alpha-dystrobrevin;
GN Name=Dtna; Synonyms=Dtn;
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] (ISOFORMS 2 AND 7).
RC TISSUE=Brain;
RX PubMed=8631824; DOI=10.1074/jbc.271.13.7802;
RA Blake D.J., Nawrotzki R., Peters M.F., Froehner S.C., Davies K.E.;
RT "Isoform diversity of dystrobrevin, the murine 87-kDa postsynaptic
RT protein.";
RL J. Biol. Chem. 271:7802-7810(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=129/Sv; TISSUE=Brain;
RX PubMed=9119373; DOI=10.1006/geno.1996.4515;
RA Ambrose H.J., Blake D.J., Nawrotzki R.A., Davies K.E.;
RT "Genomic organization of the mouse dystrobrevin gene: comparative analysis
RT with the dystrophin gene.";
RL Genomics 39:359-369(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
RC TISSUE=Muscle;
RX PubMed=9701558; DOI=10.1242/jcs.111.17.2595;
RA Nawrotzki R., Loh N.Y., Ruegg M.A., Davies K.E., Blake D.J.;
RT "Characterisation of alpha-dystrobrevin in muscle.";
RL J. Cell Sci. 111:2595-2605(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4 AND 6).
RC STRAIN=C3H/HeJ; TISSUE=Muscle;
RX PubMed=10570976; DOI=10.1016/s0378-1119(99)00358-3;
RA Enigk R.E., Maimone M.M.;
RT "Differential expression and developmental regulation of a novel alpha-
RT dystrobrevin isoform in muscle.";
RL Gene 238:479-488(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Skin;
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 [6]
RP INTERACTION WITH SNTA1.
RX PubMed=7547961; DOI=10.1021/bi00038a014;
RA Madhavan R., Jarrett H.W.;
RT "Interactions between dystrophin glycoprotein complex proteins.";
RL Biochemistry 34:12204-12209(1995).
RN [7]
RP INTERACTION WITH SNTB1.
RX PubMed=9214383; DOI=10.1083/jcb.138.1.81;
RA Peters M.F., Adams M.E., Froehner S.C.;
RT "Differential association of syntrophin pairs with the dystrophin
RT complex.";
RL J. Cell Biol. 138:81-93(1997).
RN [8]
RP INTERACTION WITH DYSTROBREVIN BINDING PROTEIN 1.
RX PubMed=11316798; DOI=10.1074/jbc.m010418200;
RA Benson M.A., Newey S.E., Martin-Rendon E., Hawkes R., Blake D.J.;
RT "Dysbindin, a novel coiled-coil-containing protein that interacts with the
RT dystrobrevins in muscle and brain.";
RL J. Biol. Chem. 276:24232-24241(2001).
RN [9]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH MAGEE1.
RX PubMed=14623885; DOI=10.1074/jbc.m312205200;
RA Albrecht D.E., Froehner S.C.;
RT "DAMAGE, a novel alpha-dystrobrevin-associated MAGE protein in dystrophin
RT complexes.";
RL J. Biol. Chem. 279:7014-7023(2004).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Lung, and 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).
CC -!- FUNCTION: Involved in synapse maturation and required for normal muscle
CC function.
CC -!- SUBUNIT: Interacts with dystrophin, utrophin and the syntrophins SNTA1,
CC SNTB1, SNTB2, SNTG1 and SNTG2. Isoforms 5 and 6 do not interact with
CC syntrophin. Isoforms 3 and 4 do not interact with utrophin. Binds
CC dystrobrevin binding protein 1. Interacts with MAGEE1.
CC {ECO:0000269|PubMed:11316798, ECO:0000269|PubMed:14623885,
CC ECO:0000269|PubMed:7547961, ECO:0000269|PubMed:9214383}.
CC -!- INTERACTION:
CC Q9D2N4; Q91WZ8: Dtnbp1; NbExp=3; IntAct=EBI-296019, EBI-643186;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14623885}. Synapse
CC {ECO:0000269|PubMed:14623885}. Cell membrane
CC {ECO:0000269|PubMed:14623885}. Note=In peripheral nerves, colocalizes
CC with MAGEE1 in the Schwann cell membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q9D2N4-1; Sequence=Displayed;
CC Name=2; Synonyms=Alpha-dystrobrevin-1, Alpha-DB1;
CC IsoId=Q9D2N4-2; Sequence=VSP_004215, VSP_004220;
CC Name=3; Synonyms=Alpha-dystrobrevin-2B, Alpha-DB2B;
CC IsoId=Q9D2N4-3; Sequence=VSP_004221, VSP_004222;
CC Name=4; Synonyms=Alpha-dystrobrevin-2A, Alpha-DB2A;
CC IsoId=Q9D2N4-4; Sequence=VSP_004218, VSP_004219;
CC Name=5; Synonyms=Alpha-dystrobrevin-3, Alpha-DB3;
CC IsoId=Q9D2N4-5; Sequence=VSP_004214, VSP_004216, VSP_004217;
CC Name=6; Synonyms=Alpha-dystrobrevin-3, Alpha-DB3;
CC IsoId=Q9D2N4-6; Sequence=VSP_004216, VSP_004217;
CC Name=7;
CC IsoId=Q9D2N4-7; Sequence=VSP_004214, VSP_004215, VSP_004218,
CC VSP_004219;
CC -!- TISSUE SPECIFICITY: Expressed in skeletal muscle, heart, lung and
CC brain. Sarcolemma and neuromuscular junction in skeletal muscle.
CC Isoform 2 is restricted to the neuromuscular junction. Isoforms 5 and 6
CC are only expressed in muscle.
CC -!- DEVELOPMENTAL STAGE: Expression of alpha-dystrobrevin is up-regulated
CC during differentiation, with isoforms 2, 5 and 6 expressed earliest and
CC isoform 3 and 4 expressed later.
CC -!- DOMAIN: The coiled coil domain mediates the interaction with dystrophin
CC and utrophin.
CC -!- PTM: Phosphorylation of isoform 2 on tyrosine kinase substrate domain
CC present in the C-terminus.
CC -!- SIMILARITY: Belongs to the dystrophin family. Dystrobrevin subfamily.
CC {ECO:0000305}.
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DR EMBL; X95226; CAA64518.1; -; mRNA.
DR EMBL; X95227; CAA64519.1; -; mRNA.
DR EMBL; Z79787; CAB02145.1; -; Genomic_DNA.
DR EMBL; Z79788; CAB02145.1; JOINED; Genomic_DNA.
DR EMBL; Z79789; CAB02145.1; JOINED; Genomic_DNA.
DR EMBL; Z79790; CAB02145.1; JOINED; Genomic_DNA.
DR EMBL; Z79791; CAB02145.1; JOINED; Genomic_DNA.
DR EMBL; Z79792; CAB02145.1; JOINED; Genomic_DNA.
DR EMBL; Z79793; CAB02145.1; JOINED; Genomic_DNA.
DR EMBL; Z79794; CAB02145.1; JOINED; Genomic_DNA.
DR EMBL; Z79795; CAB02145.1; JOINED; Genomic_DNA.
DR EMBL; Z79796; CAB02145.1; JOINED; Genomic_DNA.
DR EMBL; Z79797; CAB02145.1; JOINED; Genomic_DNA.
DR EMBL; AJ009669; CAA08770.1; -; mRNA.
DR EMBL; AF143544; AAD33915.1; -; mRNA.
DR EMBL; AF143543; AAD33914.1; -; mRNA.
DR EMBL; AF143542; AAD33913.1; -; mRNA.
DR EMBL; AK019477; BAB31746.1; -; mRNA.
DR CCDS; CCDS29094.1; -. [Q9D2N4-6]
DR CCDS; CCDS89200.1; -. [Q9D2N4-1]
DR RefSeq; NP_001272736.1; NM_001285807.1.
DR RefSeq; NP_001272739.1; NM_001285810.1.
DR RefSeq; NP_001272746.1; NM_001285817.1.
DR RefSeq; NP_034217.2; NM_010087.4. [Q9D2N4-6]
DR RefSeq; XP_017173306.1; XM_017317817.1.
DR RefSeq; XP_017173308.1; XM_017317819.1.
DR RefSeq; XP_017173310.1; XM_017317821.1.
DR RefSeq; XP_017173311.1; XM_017317822.1.
DR RefSeq; XP_017173312.1; XM_017317823.1.
DR RefSeq; XP_017173313.1; XM_017317824.1.
DR RefSeq; XP_017173315.1; XM_017317826.1.
DR AlphaFoldDB; Q9D2N4; -.
DR SMR; Q9D2N4; -.
DR BioGRID; 199334; 9.
DR CORUM; Q9D2N4; -.
DR IntAct; Q9D2N4; 18.
DR MINT; Q9D2N4; -.
DR STRING; 10090.ENSMUSP00000111498; -.
DR iPTMnet; Q9D2N4; -.
DR PhosphoSitePlus; Q9D2N4; -.
DR SwissPalm; Q9D2N4; -.
DR MaxQB; Q9D2N4; -.
DR PeptideAtlas; Q9D2N4; -.
DR PRIDE; Q9D2N4; -.
DR ProteomicsDB; 277515; -. [Q9D2N4-1]
DR ProteomicsDB; 277516; -. [Q9D2N4-2]
DR ProteomicsDB; 277517; -. [Q9D2N4-3]
DR ProteomicsDB; 277518; -. [Q9D2N4-4]
DR ProteomicsDB; 277519; -. [Q9D2N4-5]
DR ProteomicsDB; 277520; -. [Q9D2N4-6]
DR ProteomicsDB; 277521; -. [Q9D2N4-7]
DR Antibodypedia; 22242; 262 antibodies from 26 providers.
DR DNASU; 13527; -.
DR Ensembl; ENSMUST00000047954; ENSMUSP00000037475; ENSMUSG00000024302. [Q9D2N4-6]
DR GeneID; 13527; -.
DR KEGG; mmu:13527; -.
DR UCSC; uc008efs.2; mouse. [Q9D2N4-7]
DR UCSC; uc008efv.2; mouse. [Q9D2N4-4]
DR UCSC; uc008efw.2; mouse. [Q9D2N4-3]
DR UCSC; uc008efx.2; mouse. [Q9D2N4-1]
DR CTD; 1837; -.
DR MGI; MGI:106039; Dtna.
DR VEuPathDB; HostDB:ENSMUSG00000024302; -.
DR eggNOG; KOG4301; Eukaryota.
DR GeneTree; ENSGT00940000153897; -.
DR HOGENOM; CLU_001187_2_0_1; -.
DR InParanoid; Q9D2N4; -.
DR OrthoDB; 699158at2759; -.
DR PhylomeDB; Q9D2N4; -.
DR BioGRID-ORCS; 13527; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Dtna; mouse.
DR PRO; PR:Q9D2N4; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q9D2N4; protein.
DR Bgee; ENSMUSG00000024302; Expressed in saccule of membranous labyrinth and 234 other tissues.
DR ExpressionAtlas; Q9D2N4; baseline and differential.
DR Genevisible; Q9D2N4; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016014; C:dystrobrevin complex; NAS:UniProtKB.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0042383; C:sarcolemma; TAS:MGI.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0099536; P:synaptic signaling; IBA:GO_Central.
DR Gene3D; 3.30.60.90; -; 1.
DR InterPro; IPR017432; Distrobrevin.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR015153; EF-hand_dom_typ1.
DR InterPro; IPR015154; EF-hand_dom_typ2.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR Pfam; PF09068; EF-hand_2; 1.
DR Pfam; PF09069; EF-hand_3; 1.
DR Pfam; PF00569; ZZ; 1.
DR PIRSF; PIRSF038204; Distrobrevin; 1.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF47473; SSF47473; 2.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Coiled coil; Cytoplasm; Membrane;
KW Metal-binding; Phosphoprotein; Reference proteome; Synapse; Zinc;
KW Zinc-finger.
FT CHAIN 1..746
FT /note="Dystrobrevin alpha"
FT /id="PRO_0000080037"
FT ZN_FING 238..294
FT /note="ZZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT REGION 1..288
FT /note="Interaction with MAGEE1"
FT /evidence="ECO:0000269|PubMed:14623885"
FT REGION 397..447
FT /note="Syntrophin-binding region"
FT REGION 555..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 646..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 684..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 458..557
FT /evidence="ECO:0000255"
FT COMPBIAS 557..574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 243
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 246
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 258
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 261
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 267
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 270
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 280
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 284
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT MOD_RES 666
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 334
FT /note="V -> VDTW (in isoform 5 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:8631824,
FT ECO:0000303|PubMed:9701558"
FT /id="VSP_004214"
FT VAR_SEQ 363..419
FT /note="Missing (in isoform 2 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:8631824"
FT /id="VSP_004215"
FT VAR_SEQ 364..371
FT /note="PPKDSEVE -> DGAHGGCV (in isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:10570976,
FT ECO:0000303|PubMed:9701558"
FT /id="VSP_004216"
FT VAR_SEQ 372..746
FT /note="Missing (in isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:10570976,
FT ECO:0000303|PubMed:9701558"
FT /id="VSP_004217"
FT VAR_SEQ 559..570
FT /note="TQGASSPRSSPS -> VMHEIIPLEERT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10570976"
FT /id="VSP_004221"
FT VAR_SEQ 559..567
FT /note="TQGASSPRS -> VSYVPYCRS (in isoform 4 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:10570976,
FT ECO:0000303|PubMed:8631824"
FT /id="VSP_004218"
FT VAR_SEQ 560..561
FT /note="QG -> R (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8631824"
FT /id="VSP_004220"
FT VAR_SEQ 568..746
FT /note="Missing (in isoform 4 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:10570976,
FT ECO:0000303|PubMed:8631824"
FT /id="VSP_004219"
FT VAR_SEQ 571..746
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10570976"
FT /id="VSP_004222"
FT CONFLICT 241
FT /note="V -> L (in Ref. 1; CAA64519)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="M -> I (in Ref. 5; BAB31746)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="Q -> P (in Ref. 4; AAD33915)"
FT /evidence="ECO:0000305"
FT CONFLICT 416
FT /note="D -> N (in Ref. 4; AAD33915/AAD33914)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 746 AA; 84067 MW; 6AB7EF3B69250A09 CRC64;
MIEDSGKRGN TMAERRQLFA EMRAQDLDRI RLSTYRTACK LRFVQKKCNL HLVDIWNVIE
ALRENALNNL DPNIELNVAR LEAVLSTIFY QLNKRMPTTH QIHVEQSISL LLNFLLAAFD
PEGHGKISVF AVKMALATLC GGKIMDKLRY IFSMISDSSG VMVYGRYDQF LREVLKLPTA
VFEGPSFGYT EQSARSCFSQ QKKVTLNGFL DTLMSDPPPQ CLVWLPLLHR LANVENVFHP
VECSYCHSES MMGFRYRCQQ CHNYQLCQDC FWRGHAGGSH SNQHQMKEYT SWKSPAKKLT
NALSKSLSCA SSREPLHPMF PDQPEKPLNL AHIVPPRPVT SMNDTLFSHS VPSSGSPFIT
RSSPPKDSEV EQNKMLARAA PAFLKGRGIQ YSLNVADRLA DEHVLIGLYV NMLRNDPPCM
LESSNRLDEE HRLIARYAAR LAAESSSSQP TQQRSAPDIS FTIDANKQQR QLIAELENKN
REILQEIQRL RVEHEQASQP TPEKAQQNPT LLAELRLLRQ RKDELEQRMS ALQESRRELM
VQLEGLMKLL KEEELKQGTQ GASSPRSSPS HTISRPIPMP IRSASACPTP THTPQDSLTG
VGGDVQEAFA QSSRRNLRSD LLVAADSITN TMSSLVKELN SEVASETEST VDSEFSRPQF
EDLAPSPTSE KAFLAQIHSR KPGYIHGGAA STTHGDMVPE DGDPYTQPED GNYENESVRQ
LENELQLEEY LKQKLQDEAY QVSLQG
