DTNB_MOUSE
ID DTNB_MOUSE Reviewed; 659 AA.
AC O70585; E9Q0F2; O70563; Q9CTZ1;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 3.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Dystrobrevin beta {ECO:0000305};
DE Short=DTN-B {ECO:0000303|PubMed:9540997};
DE Short=mDTN-BDTN-B;
DE AltName: Full=Beta-dystrobrevin {ECO:0000303|PubMed:9419360};
GN Name=Dtnb {ECO:0000312|MGI:MGI:1203728};
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).
RX PubMed=9540997; DOI=10.1016/s0014-5793(98)00097-0;
RA Puca A.A., Piluso V.N.G., Belsito A., Sampaolo S., Quaderi N., Rossi E.,
RA Di Iorio G., Ballabio A., Franco B.;
RT "Identification and characterization of a novel member of the dystrobrevin
RT gene family.";
RL FEBS Lett. 425:7-13(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=9419360; DOI=10.1073/pnas.95.1.241;
RA Blake D.J., Nawrotzki R., Loh N.Y., Gorecki D.C., Davies K.E.;
RT "Beta-dystrobrevin, a member of the dystrophin-related protein family.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:241-246(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
RX PubMed=9799833; DOI=10.1007/s003359900883;
RA Loh N.Y., Ambrose H.J., Guay-Woodford L.M., Dasgupta S., Nawrotzki R.A.,
RA Blake D.J., Davies K.E.;
RT "Genomic organization and refined mapping of the mouse beta-dystrobrevin
RT gene.";
RL Mamm. Genome 9:857-862(1998).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 590-608 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Stomach;
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 SNTB2 AND SNTA1.
RX PubMed=10545507; DOI=10.1083/jcb.147.3.645;
RA Blake D.J., Hawkes R., Benson M.A., Beesley P.W.;
RT "Different dystrophin-like complexes are expressed in neurons and glia.";
RL J. Cell Biol. 147:645-658(1999).
RN [7]
RP TISSUE SPECIFICITY, AND INTERACTION WITH UTRN; DMD; SNTB1; SNTB2 AND SNTA1.
RX PubMed=10893187; DOI=10.1242/jcs.113.15.2715;
RA Loh N.Y., Newey S.E., Davies K.E., Blake D.J.;
RT "Assembly of multiple dystrobrevin-containing complexes in the kidney.";
RL J. Cell Sci. 113:2715-2724(2000).
RN [8]
RP INTERACTION WITH DTNBP1.
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 DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=11585924; DOI=10.1128/mcb.21.21.7442-7448.2001;
RA Loh N.Y., Nebenius-Oosthuizen D., Blake D.J., Smith A.J., Davies K.E.;
RT "Role of beta-dystrobrevin in nonmuscle dystrophin-associated protein
RT complex-like complexes in kidney and liver.";
RL Mol. Cell. Biol. 21:7442-7448(2001).
RN [10]
RP INTERACTION WITH KIF5A.
RX PubMed=14600269; DOI=10.1242/jcs.00805;
RA Macioce P., Gambara G., Bernassola M., Gaddini L., Torreri P., Macchia G.,
RA Ramoni C., Ceccarini M., Petrucci T.C.;
RT "Beta-dystrobrevin interacts directly with kinesin heavy chain in brain.";
RL J. Cell Sci. 116:4847-4856(2003).
RN [11]
RP DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=16540561; DOI=10.1523/jneurosci.4823-05.2006;
RA Grady R.M., Wozniak D.F., Ohlemiller K.K., Sanes J.R.;
RT "Cerebellar synaptic defects and abnormal motor behavior in mice lacking
RT alpha- and beta-dystrobrevin.";
RL J. Neurosci. 26:2841-2851(2006).
RN [12]
RP PHOSPHORYLATION, AND INTERACTION WITH PRKAR2B AND PRKAR1A.
RX PubMed=17610895; DOI=10.1016/j.jmb.2007.06.019;
RA Ceccarini M., Grasso M., Veroni C., Gambara G., Artegiani B., Macchia G.,
RA Ramoni C., Torreri P., Mallozzi C., Petrucci T.C., Macioce P.;
RT "Association of dystrobrevin and regulatory subunit of protein kinase A: a
RT new role for dystrobrevin as a scaffold for signaling proteins.";
RL J. Mol. Biol. 371:1174-1187(2007).
RN [13]
RP INTERACTION WITH OLFM1.
RX PubMed=17265465; DOI=10.1002/jnr.21186;
RA Veroni C., Grasso M., Macchia G., Ramoni C., Ceccarini M., Petrucci T.C.,
RA Macioce P.;
RT "beta-dystrobrevin, a kinesin-binding receptor, interacts with the
RT extracellular matrix components pancortins.";
RL J. Neurosci. Res. 85:2631-2639(2007).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, and Pancreas;
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 [15]
RP INTERACTION WITH HMG20A AND HMG20B, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=20530487; DOI=10.1074/jbc.m109.090654;
RA Artegiani B., Labbaye C., Sferra A., Quaranta M.T., Torreri P., Macchia G.,
RA Ceccarini M., Petrucci T.C., Macioce P.;
RT "The interaction with HMG20a/b proteins suggests a potential role for beta-
RT dystrobrevin in neuronal differentiation.";
RL J. Biol. Chem. 285:24740-24750(2010).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT THR-11; THR-69;
RP THR-179; THR-212 AND THR-424, MUTAGENESIS OF THR-11, AND INTERACTION WITH
RP KIF5A.
RX PubMed=22978324; DOI=10.1111/febs.12006;
RA Fratini F., Macchia G., Torreri P., Matteucci A., Salzano A.M.,
RA Crescenzi M., Macioce P., Petrucci T.C., Ceccarini M.;
RT "Phosphorylation on threonine 11 of beta-dystrobrevin alters its
RT interaction with kinesin heavy chain.";
RL FEBS J. 279:4131-4144(2012).
CC -!- FUNCTION: Scaffolding protein that assembles DMD and SNTA1 molecules to
CC the basal membrane of kidney cells and liver sinusoids
CC (PubMed:11585924). May function as a repressor of the SYN1 promoter
CC through the binding of repressor element-1 (RE-1), in turn regulates
CC SYN1 expression and may be involved in cell proliferation regulation
CC during the early phase of neural differentiation (PubMed:20530487). May
CC be required for proper maturation and function of a subset of
CC inhibitory synapses (PubMed:16540561). {ECO:0000269|PubMed:11585924,
CC ECO:0000269|PubMed:16540561, ECO:0000269|PubMed:20530487}.
CC -!- SUBUNIT: Interacts with dystrophin short form DP71 and syntrophins
CC SNTG1 and SNTG2 (By similarity). Binds DTNBP1 (PubMed:11316798). Forms
CC a specific complex composed of DMD, SNTB2 and SNTA1 in neuron; the
CC interaction with SNTB2 and SNTA1 is DMD independent (PubMed:10545507).
CC Interacts with UTRN and dystrophin short form DP71 in the kidney and
CC liver (PubMed:10893187). Interacts with SNTB1, SNTB2 and SNTA1 in
CC kidney and liver (PubMed:10893187). Interacts with KIF5A
CC (PubMed:14600269, PubMed:22978324). Interacts with HMG20A and HMG20B
CC (PubMed:20530487). Interacts with OLFM1 (PubMed:17265465). Interacts
CC with PRKAR2B and PRKAR1A (PubMed:17610895).
CC {ECO:0000250|UniProtKB:O60941, ECO:0000269|PubMed:10545507,
CC ECO:0000269|PubMed:10893187, ECO:0000269|PubMed:11316798,
CC ECO:0000269|PubMed:14600269, ECO:0000269|PubMed:17265465,
CC ECO:0000269|PubMed:17610895, ECO:0000269|PubMed:20530487,
CC ECO:0000269|PubMed:22978324}.
CC -!- INTERACTION:
CC O70585; P33175: Kif5a; NbExp=4; IntAct=EBI-349714, EBI-349710;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20530487}.
CC Postsynaptic density {ECO:0000250|UniProtKB:P84060}. Cell projection,
CC dendrite {ECO:0000269|PubMed:11585924, ECO:0000269|PubMed:16540561}.
CC Basal cell membrane {ECO:0000269|PubMed:10893187}. Postsynapse
CC {ECO:0000269|PubMed:16540561}. Nucleus {ECO:0000269|PubMed:20530487}.
CC Note=Localized at inhibitory synapses on the dendrites of cerebellar
CC Purkinje cells. {ECO:0000269|PubMed:16540561}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=O70585-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O70585-2; Sequence=VSP_004227, VSP_004228, VSP_004229;
CC -!- TISSUE SPECIFICITY: Expressed mainly in liver and lung. Expressed in
CC brain, namely in neurons of the cortex and hippocampus and in the
CC dendrites, soma, and nuclei of pyramidal neurons of the hippocampus
CC region CA1 (PubMed:11585924). Expressed in kidney, namely in epithelial
CC cells of renal tubules, collecting ducts, Bowman's capsules and
CC glomeruli (PubMed:10893187). Expressed in blood vessels and pia
CC (PubMed:16540561). {ECO:0000269|PubMed:10893187,
CC ECO:0000269|PubMed:11585924, ECO:0000269|PubMed:16540561}.
CC -!- DOMAIN: The coiled coil domain may mediate the interaction with
CC dystrophin.
CC -!- PTM: Phosphorylated by PKA (PubMed:17610895). Phosphorylation at Thr-11
CC alters the interaction with KIF5A (PubMed:22978324).
CC {ECO:0000269|PubMed:17610895, ECO:0000269|PubMed:22978324}.
CC -!- DISRUPTION PHENOTYPE: Homozygous knockout mice for Dtnb are viable and
CC fertile, and are normal in appearance (PubMed:11585924,
CC PubMed:16540561). Double knockout mice for DTNA and DTNB genes have a
CC mild myopathy plus synaptic defects and abnormal motor behavior
CC (PubMed:16540561). {ECO:0000269|PubMed:11585924,
CC ECO:0000269|PubMed:16540561}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the dystrophin family. Dystrobrevin subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA75752.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA75752.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Y15742; CAA75752.1; ALT_SEQ; mRNA.
DR EMBL; AJ003007; CAA05796.1; -; mRNA.
DR EMBL; AJ010204; CAA09038.1; -; Genomic_DNA.
DR EMBL; AJ010205; CAA09038.1; JOINED; Genomic_DNA.
DR EMBL; AJ010206; CAA09038.1; JOINED; Genomic_DNA.
DR EMBL; AJ010207; CAA09038.1; JOINED; Genomic_DNA.
DR EMBL; AJ010208; CAA09038.1; JOINED; Genomic_DNA.
DR EMBL; AJ010209; CAA09038.1; JOINED; Genomic_DNA.
DR EMBL; AJ010210; CAA09038.1; JOINED; Genomic_DNA.
DR EMBL; AJ010211; CAA09038.1; JOINED; Genomic_DNA.
DR EMBL; AJ010212; CAA09038.1; JOINED; Genomic_DNA.
DR EMBL; AJ010213; CAA09038.1; JOINED; Genomic_DNA.
DR EMBL; AJ010214; CAA09038.1; JOINED; Genomic_DNA.
DR EMBL; AJ010215; CAA09038.1; JOINED; Genomic_DNA.
DR EMBL; AJ010216; CAA09038.1; JOINED; Genomic_DNA.
DR EMBL; AJ010217; CAA09038.1; JOINED; Genomic_DNA.
DR EMBL; AJ010218; CAA09038.1; JOINED; Genomic_DNA.
DR EMBL; AJ010219; CAA09038.1; JOINED; Genomic_DNA.
DR EMBL; AJ010220; CAA09038.1; JOINED; Genomic_DNA.
DR EMBL; AJ010221; CAA09038.1; JOINED; Genomic_DNA.
DR EMBL; AC155273; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR974568; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK019068; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS49015.1; -. [O70585-1]
DR RefSeq; NP_001155937.1; NM_001162465.1. [O70585-1]
DR AlphaFoldDB; O70585; -.
DR SMR; O70585; -.
DR BioGRID; 199335; 9.
DR CORUM; O70585; -.
DR IntAct; O70585; 7.
DR MINT; O70585; -.
DR STRING; 10090.ENSMUSP00000126194; -.
DR iPTMnet; O70585; -.
DR PhosphoSitePlus; O70585; -.
DR SwissPalm; O70585; -.
DR jPOST; O70585; -.
DR MaxQB; O70585; -.
DR PaxDb; O70585; -.
DR PRIDE; O70585; -.
DR ProteomicsDB; 277522; -. [O70585-1]
DR ProteomicsDB; 277523; -. [O70585-2]
DR DNASU; 13528; -.
DR Ensembl; ENSMUST00000101637; ENSMUSP00000099161; ENSMUSG00000071454. [O70585-2]
DR Ensembl; ENSMUST00000164578; ENSMUSP00000126194; ENSMUSG00000071454. [O70585-1]
DR GeneID; 13528; -.
DR KEGG; mmu:13528; -.
DR UCSC; uc007mww.2; mouse. [O70585-2]
DR UCSC; uc007mwy.2; mouse. [O70585-1]
DR CTD; 1838; -.
DR MGI; MGI:1203728; Dtnb.
DR VEuPathDB; HostDB:ENSMUSG00000071454; -.
DR eggNOG; KOG4301; Eukaryota.
DR GeneTree; ENSGT00940000153897; -.
DR InParanoid; O70585; -.
DR OrthoDB; 699158at2759; -.
DR PhylomeDB; O70585; -.
DR TreeFam; TF343849; -.
DR BioGRID-ORCS; 13528; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Dtnb; mouse.
DR PRO; PR:O70585; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; O70585; protein.
DR Bgee; ENSMUSG00000071454; Expressed in superior frontal gyrus and 207 other tissues.
DR ExpressionAtlas; O70585; baseline and differential.
DR Genevisible; O70585; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0009925; C:basal plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0060077; C:inhibitory synapse; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0019902; F:phosphatase binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030182; P:neuron differentiation; ISO:MGI.
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 Acetylation; Alternative splicing; Cell membrane; Cell projection;
KW Coiled coil; Cytoplasm; Membrane; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Synapse; Zinc; Zinc-finger.
FT CHAIN 1..659
FT /note="Dystrobrevin beta"
FT /id="PRO_0000086879"
FT ZN_FING 238..294
FT /note="ZZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT REGION 369..418
FT /note="Syntrophin-binding region"
FT REGION 520..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 429..519
FT /evidence="ECO:0000255"
FT COMPBIAS 542..556
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..614
FT /note="Basic and acidic 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 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O60941"
FT MOD_RES 11
FT /note="Phosphothreonine; by PKA and PKC"
FT /evidence="ECO:0000269|PubMed:22978324"
FT MOD_RES 69
FT /note="Phosphothreonine; by PKC"
FT /evidence="ECO:0000269|PubMed:22978324"
FT MOD_RES 179
FT /note="Phosphothreonine; by PKC"
FT /evidence="ECO:0000269|PubMed:22978324"
FT MOD_RES 212
FT /note="Phosphothreonine; by PKC"
FT /evidence="ECO:0000269|PubMed:22978324"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60941"
FT MOD_RES 424
FT /note="Phosphothreonine; by PKA"
FT /evidence="ECO:0000269|PubMed:22978324"
FT VAR_SEQ 518
FT /note="K -> KEEEQKQA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:9419360"
FT /id="VSP_004227"
FT VAR_SEQ 603..608
FT /note="AEAEEQ -> EVTPVS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:9419360"
FT /id="VSP_004228"
FT VAR_SEQ 609..659
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:9419360"
FT /id="VSP_004229"
FT MUTAGEN 11
FT /note="T->A: Does not affect interaction with Kif5A."
FT /evidence="ECO:0000269|PubMed:22978324"
FT MUTAGEN 11
FT /note="T->D: Reduces interaction with Kif5A."
FT /evidence="ECO:0000269|PubMed:22978324"
FT CONFLICT 412
FT /note="L -> P (in Ref. 1; CAA75752)"
FT /evidence="ECO:0000305"
FT CONFLICT 465
FT /note="S -> F (in Ref. 2; CAA05796 and 3; CAA09038)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 659 AA; 74399 MW; 27AB3141A65797A8 CRC64;
MIEEGGNKRK TMAEKRQLFI EMRAQNFDVI RLSTYRTACK LRFVQKRCNL HLVDIWNMIE
AFRDNGLNTL DHSTEISVSR LETVISSIYY QLNKRLPSTH QISVEQSISL LLNFMVAAYD
SEGRGKLTVF SVKAMLATMC GGKMLDKLRY IFSQMSDSNG LMMFGKLDQF LKEALKLPTA
VFEGPSFGYT EHAVRTCFPQ QKKIMLNMFL DTMMADPPPQ CLVWLPLMHR LAHVENVFHP
VECSYCHCES MMGFRYRCQQ CHNYQLCQNC FWRGHASGAH SNQHQMKEHS SWKSPAKKLS
HAISKSLGCV PSREPPHPVF PEQPEKPLDL AHLVPPRPLT NMNDTVVSHM SSGVPTPTKR
LQYSQDMPNL LADEHALIAS YVARLQHCTR VLDSPSRLDE EHRLIARYAA RLAAEAGNMT
RPPTDASFNF DANKQQRQLI AELENKNREI LQEIQRLRLE HEQASQPTPE KAQQNPMLLA
ELRLLRQRKD ELEQRMSALQ ESRRELMVQL EGLMKLLKAQ ATGSPHTSPT HGGGRPMPMP
VRSTSAGSTP THGPQDSLSG VGGDVQEAFA QGTRRNLRND LLVAADSITN TMSSLVKELH
SGAEAEEQAG TEKTREGLPP RGTFLSVFLL HTWTKLAGCQ THSTSRERSQ AYGKWGGTA
