HAP1_MOUSE
ID HAP1_MOUSE Reviewed; 628 AA.
AC O35668; O35636;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Huntingtin-associated protein 1;
DE Short=HAP-1;
GN Name=Hap1;
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 A AND B).
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=9599014; DOI=10.1016/s0014-5793(98)00352-4;
RA Bertaux F., Sharp A.H., Ross C.A., Lehrach H., Bates G.P., Wanker E.;
RT "HAP1-huntingtin interactions do not contribute to the molecular pathology
RT in Huntingtons disease transgenic mice.";
RL FEBS Lett. 426:229-232(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A).
RC STRAIN=129/SvJ;
RX PubMed=9657855; DOI=10.1007/s003359900819;
RA Nasir J., Duan K., Nichol K., Engelender S., Ashworth R., Colomer V.,
RA Thomas S., Disteche C.M., Hayden M.R., Ross C.A.;
RT "Gene structure and map location of the murine homolog of the Huntington-
RT associated protein, Hap1.";
RL Mamm. Genome 9:565-570(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Eye;
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 [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12890790; DOI=10.1523/jneurosci.23-17-06956.2003;
RA Li S.H., Yu Z.X., Li C.L., Nguyen H.P., Zhou Y.X., Deng C., Li X.J.;
RT "Lack of huntingtin-associated protein-1 causes neuronal death resembling
RT hypothalamic degeneration in Huntington's disease.";
RL J. Neurosci. 23:6956-6964(2003).
RN [5]
RP FUNCTION.
RX PubMed=15379999; DOI=10.1111/j.1460-9568.2004.03633.x;
RA Tang T.S., Tu H., Orban P.C., Chan E.Y., Hayden M.R., Bezprozvanny I.;
RT "HAP1 facilitates effects of mutant huntingtin on inositol 1,4,5-
RT trisphosphate-induced Ca release in primary culture of striatal medium
RT spiny neurons.";
RL Eur. J. Neurosci. 20:1779-1787(2004).
RN [6]
RP FUNCTION, AND INTERACTION WITH TBP.
RX PubMed=17868456; DOI=10.1186/1471-2199-8-76;
RA Prigge J.R., Schmidt E.E.;
RT "HAP1 can sequester a subset of TBP in cytoplasmic inclusions via specific
RT interaction with the conserved TBP(CORE).";
RL BMC Mol. Biol. 8:76-76(2007).
RN [7]
RP FUNCTION, AND INTERACTION WITH AHI1.
RX PubMed=18636121; DOI=10.1172/jci35339;
RA Sheng G., Xu X., Lin Y.F., Wang C.E., Rong J., Cheng D., Peng J., Jiang X.,
RA Li S.H., Li X.J.;
RT "Huntingtin-associated protein 1 interacts with Ahi1 to regulate cerebellar
RT and brainstem development in mice.";
RL J. Clin. Invest. 118:2785-2795(2008).
RN [8]
RP FUNCTION.
RX PubMed=21985783; DOI=10.1172/jci57552;
RA Keryer G., Pineda J.R., Liot G., Kim J., Dietrich P., Benstaali C.,
RA Smith K., Cordelieres F.P., Spassky N., Ferrante R.J., Dragatsis I.,
RA Saudou F.;
RT "Ciliogenesis is regulated by a huntingtin-HAP1-PCM1 pathway and is altered
RT in Huntington disease.";
RL J. Clin. Invest. 121:4372-4382(2011).
RN [9]
RP INTERACTION WITH AHI1.
RX PubMed=23532844; DOI=10.1074/jbc.m112.420786;
RA Tuz K., Hsiao Y.C., Juarez O., Shi B., Harmon E.Y., Phelps I.G.,
RA Lennartz M.R., Glass I.A., Doherty D., Ferland R.J.;
RT "The Joubert syndrome-associated missense mutation (V443D) in the Abelson-
RT helper integration site 1 (AHI1) protein alters its localization and
RT protein-protein interactions.";
RL J. Biol. Chem. 288:13676-13694(2013).
RN [10]
RP INTERACTION WITH AHI1.
RX PubMed=23658157; DOI=10.1523/jneurosci.0119-13.2013;
RA Weng L., Lin Y.F., Li A.L., Wang C.E., Yan S., Sun M., Gaertig M.A.,
RA Mitha N., Kosaka J., Wakabayashi T., Xu X., Tang B., Li S., Li X.J.;
RT "Loss of Ahi1 affects early development by impairing BM88/Cend1-mediated
RT neuronal differentiation.";
RL J. Neurosci. 33:8172-8184(2013).
RN [11]
RP FUNCTION.
RX PubMed=24355921; DOI=10.1172/jci69206;
RA Xiang J., Yang H., Zhao T., Sun M., Xu X., Zhou X.F., Li S.H., Li X.J.;
RT "Huntingtin-associated protein 1 regulates postnatal neurogenesis and
RT neurotrophin receptor sorting.";
RL J. Clin. Invest. 124:85-98(2014).
RN [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24453320; DOI=10.1523/jneurosci.1870-13.2014;
RA Wong Y.C., Holzbaur E.L.;
RT "The regulation of autophagosome dynamics by huntingtin and HAP1 is
RT disrupted by expression of mutant huntingtin, leading to defective cargo
RT degradation.";
RL J. Neurosci. 34:1293-1305(2014).
RN [13]
RP FUNCTION.
RX PubMed=24366265; DOI=10.1113/jphysiol.2013.268342;
RA Mackenzie K.D., Duffield M.D., Peiris H., Phillips L., Zanin M.P.,
RA Teo E.H., Zhou X.F., Keating D.J.;
RT "Huntingtin-associated protein 1 regulates exocytosis, vesicle docking,
RT readily releasable pool size and fusion pore stability in mouse chromaffin
RT cells.";
RL J. Physiol. (Lond.) 592:1505-1518(2014).
CC -!- FUNCTION: Originally identified as neuronal protein that specifically
CC associates with HTT/huntingtin and the binding is enhanced by an
CC expanded polyglutamine repeat within HTT possibly affecting HAP1
CC interaction properties. Both HTT and HAP1 are involved in intracellular
CC trafficking and HAP1 is proposed to link HTT to motor proteins and/or
CC transport cargos. Seems to play a role in vesicular transport within
CC neurons and axons such as from early endosomes to late endocytic
CC compartments and to promote neurite outgrowth. The vesicular transport
CC function via association with microtubule-dependent transporters can be
CC attenuated by association with mutant HTT. Involved in the axonal
CC transport of BDNF and its activity-dependent secretion; the function
CC seems to involve HTT, DCTN1 and a complex with SORT1. Involved in APP
CC trafficking and seems to facilitate APP anterograde transport and
CC membrane insertion thereby possibly reducing processing into amyloid
CC beta. Involved in delivery of gamma-aminobutyric acid (GABA(A))
CC receptors to synapses; the function is dependent on kinesin motor
CC protein KIF5 and is disrupted by HTT with expanded polyglutamine
CC repeat. Involved in regulation of autophagosome motility by promoting
CC efficient retrograde axonal transport. Seems to be involved in
CC regulation of membrane receptor recycling and degradation, and
CC respective signal transduction, including GABA(A) receptors, tyrosine
CC kinase receptors, EGFR, IP3 receptor and androgen receptor. Among
CC others suggested to be involved in control of feeding behavior
CC (involving hypothalamic GABA(A) receptors), cerebellar and brainstem
CC development (involving AHI1 and NTRK1/TrkA), postnatal neurogenesis
CC (involving hypothalamic NTRK2/TrkB regulating the number of Npyr1-
CC expressing cells), and ITPR1/InsP3R1-mediated Ca(2+) release (involving
CC HTT and possibly the effect of mutant HTT). Via association with
CC DCTN1/dynactin p150-glued and HTT/huntingtin involved in cytoplasmic
CC retention of REST in neurons. May be involved in ciliogenesiss;
CC however, reports are conflicting: PubMed:21985783 reports that Hap1 is
CC required for ciliogenesis in primary cortical neurons and proposes that
CC HTT interacts with PCM1 through HAP1; PubMed:23532844 reports that mice
CC with disrupted Hap1 display normal cilium formation and function.
CC Involved in regulation of exocytosis. Isoform A but not isoform B seems
CC to be involved in formation of cytoplasmic inclusion bodies (STBs). In
CC case of anomalous expression of TBP, can sequester a subset of TBP into
CC STBs; sequestration is enhanced by an expanded polyglutamine repeat
CC within TBP. {ECO:0000269|PubMed:12890790, ECO:0000269|PubMed:15379999,
CC ECO:0000269|PubMed:17868456, ECO:0000269|PubMed:18636121,
CC ECO:0000269|PubMed:21985783, ECO:0000269|PubMed:24355921,
CC ECO:0000269|PubMed:24366265, ECO:0000269|PubMed:24453320}.
CC -!- SUBUNIT: Self-associates. Interacts with HTT/huntingtin; enhanced by an
CC expanded polyglutamine repeat within HTT. Isoform A interacts with
CC DCTN1; decreased in presence of HTT with expanded polyglutamine repeat;
CC decreased by phosphorylation of Hap1 isoform A at Thr-598. Isoform A
CC interacts with KLC2; decreased by phosphorylation of Hap1 isoform A at
CC Thr-598. Isoform A interacts with ITPR1 and APP. Isoform A interacts
CC with AR; decreased by an expanded polyglutamine repeat within AR.
CC Isoform A interacts with YWHAZ; enhanced by phosphorylation of Hap1
CC isoform A at Thr-598. Isoform A interacts with BDNF and SORT1; probably
CC forming a complex involved in proBDNF trafficking, degradation and
CC processing. Interacts with TBP, AHI1, HGS and KALRN. Interacts with
CC KIF5A, KIF5B, KIF5C and GABRB3; indicative for an HAP1:KIF5 complex
CC transporting a GABA(A) receptor as cargo. Interacts with ATXN3; in
CC STBs. Interacts with NTRK2; HAP1 stabilizes association of NTRK2 with
CC SORT1 preventing NTRK2 degradation. Interacts with CCDC113.
CC {ECO:0000250|UniProtKB:P54257, ECO:0000269|PubMed:17868456,
CC ECO:0000269|PubMed:18636121, ECO:0000269|PubMed:23532844,
CC ECO:0000269|PubMed:23658157}.
CC -!- INTERACTION:
CC O35668; Q8K3E5: Ahi1; NbExp=3; IntAct=EBI-473704, EBI-4280729;
CC O35668-2; B2GV74: Klc2; Xeno; NbExp=3; IntAct=EBI-473719, EBI-978371;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P54256}.
CC Presynapse {ECO:0000250|UniProtKB:P54256}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P54256}. Cell projection, dendritic spine
CC {ECO:0000250|UniProtKB:P54256}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:P54256}. Cell projection, axon
CC {ECO:0000250|UniProtKB:P54256}. Lysosome
CC {ECO:0000250|UniProtKB:P54256}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P54256}. Mitochondrion
CC {ECO:0000250|UniProtKB:P54256}. Nucleus {ECO:0000250|UniProtKB:P54256}.
CC Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:24453320}. Early
CC endosome {ECO:0000250|UniProtKB:P54256}. Cell projection, growth cone
CC {ECO:0000250|UniProtKB:P54256}. Note=Localizes to large nonmembrane-
CC bound cytoplasmic bodies found in various types of neurons, called
CC stigmoid bodies (STBs); STB formation is regulated by the ratio of
CC isoform A to isoform B. In the nucleus localizes to nuclear rods.
CC {ECO:0000250|UniProtKB:P54256}.
CC -!- SUBCELLULAR LOCATION: [Isoform B]: Cytoplasm
CC {ECO:0000250|UniProtKB:P54256}. Note=In NGF-stimulated PC2 cells
CC isoform A can move anterogradely fom neurite cell body to neurite
CC terminal and is localized to growth cone tips whereas isoform B stays
CC in the cell body. {ECO:0000250|UniProtKB:P54256}.
CC -!- SUBCELLULAR LOCATION: [Isoform A]: Cell projection, growth cone
CC {ECO:0000250|UniProtKB:P54256}. Cell projection, neuron projection
CC {ECO:0000250|UniProtKB:P54256}. Cytoplasmic vesicle, secretory vesicle,
CC synaptic vesicle {ECO:0000250|UniProtKB:P54256}. Presynapse
CC {ECO:0000250|UniProtKB:P54256}. Note=In NGF-stimulated PC2 cells
CC isoform A can move anterogradely fom neurite cell body to neurite
CC terminal and is localized to growth cone tips whereas isoform B stays
CC in the cell body. Localization to neuronal processes and neurite tips
CC is decreased by YWHAZ. {ECO:0000250|UniProtKB:P54256}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B; Synonyms=Long;
CC IsoId=O35668-1; Sequence=Displayed;
CC Name=A; Synonyms=Short;
CC IsoId=O35668-2; Sequence=VSP_004279;
CC -!- PTM: Isoform A is phosphorylated on Thr-598.
CC {ECO:0000250|UniProtKB:P54256}.
CC -!- DISRUPTION PHENOTYPE: Depressed postnatal feeding behavior leading to
CC premature death latest at P9. Degeneration in hypothalamic regions that
CC control feeding behavior. {ECO:0000269|PubMed:12890790}.
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DR EMBL; AJ000262; CAA03978.1; -; mRNA.
DR EMBL; AJ002271; CAA05286.1; -; mRNA.
DR EMBL; AJ003128; CAA05883.1; -; Genomic_DNA.
DR EMBL; BC034089; AAH34089.1; -; mRNA.
DR EMBL; BC053043; AAH53043.1; -; mRNA.
DR CCDS; CCDS25419.1; -. [O35668-2]
DR CCDS; CCDS56806.1; -. [O35668-1]
DR RefSeq; NP_034534.1; NM_010404.3. [O35668-2]
DR RefSeq; NP_817090.1; NM_177981.2. [O35668-1]
DR AlphaFoldDB; O35668; -.
DR SMR; O35668; -.
DR BioGRID; 200207; 5.
DR CORUM; O35668; -.
DR DIP; DIP-32510N; -.
DR IntAct; O35668; 18.
DR MINT; O35668; -.
DR STRING; 10090.ENSMUSP00000099413; -.
DR iPTMnet; O35668; -.
DR PhosphoSitePlus; O35668; -.
DR MaxQB; O35668; -.
DR PaxDb; O35668; -.
DR PRIDE; O35668; -.
DR ProteomicsDB; 269713; -. [O35668-1]
DR ProteomicsDB; 269714; -. [O35668-2]
DR Antibodypedia; 80380; 250 antibodies from 35 providers.
DR DNASU; 15114; -.
DR Ensembl; ENSMUST00000103124; ENSMUSP00000099413; ENSMUSG00000006930. [O35668-2]
DR Ensembl; ENSMUST00000138603; ENSMUSP00000133356; ENSMUSG00000006930. [O35668-1]
DR GeneID; 15114; -.
DR KEGG; mmu:15114; -.
DR UCSC; uc007lkx.2; mouse. [O35668-2]
DR UCSC; uc007lky.2; mouse. [O35668-1]
DR CTD; 9001; -.
DR MGI; MGI:1261831; Hap1.
DR VEuPathDB; HostDB:ENSMUSG00000006930; -.
DR eggNOG; KOG4360; Eukaryota.
DR GeneTree; ENSGT00940000162183; -.
DR HOGENOM; CLU_036493_0_0_1; -.
DR InParanoid; O35668; -.
DR OMA; MERNYEV; -.
DR OrthoDB; 592923at2759; -.
DR PhylomeDB; O35668; -.
DR TreeFam; TF323495; -.
DR BioGRID-ORCS; 15114; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Hap1; mouse.
DR PRO; PR:O35668; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; O35668; protein.
DR Bgee; ENSMUSG00000006930; Expressed in dorsomedial nucleus of hypothalamus and 187 other tissues.
DR ExpressionAtlas; O35668; baseline and differential.
DR Genevisible; O35668; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005776; C:autophagosome; IDA:UniProtKB.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0043679; C:axon terminus; ISO:MGI.
DR GO; GO:0005814; C:centriole; IDA:MGI.
DR GO; GO:0005813; C:centrosome; IDA:CACAO.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0098982; C:GABA-ergic synapse; ISO:MGI.
DR GO; GO:0030426; C:growth cone; ISO:MGI.
DR GO; GO:0016234; C:inclusion body; ISO:MGI.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0099524; C:postsynaptic cytosol; ISO:MGI.
DR GO; GO:0099523; C:presynaptic cytosol; ISO:MGI.
DR GO; GO:0008021; C:synaptic vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0048403; F:brain-derived neurotrophic factor binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0017022; F:myosin binding; IBA:GO_Central.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0044325; F:transmembrane transporter binding; ISS:UniProtKB.
DR GO; GO:0008089; P:anterograde axonal transport; IMP:UniProtKB.
DR GO; GO:0098957; P:anterograde axonal transport of mitochondrion; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0021549; P:cerebellum development; IMP:UniProtKB.
DR GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR GO; GO:0021979; P:hypothalamus cell differentiation; IMP:UniProtKB.
DR GO; GO:0048311; P:mitochondrion distribution; IBA:GO_Central.
DR GO; GO:1902430; P:negative regulation of amyloid-beta formation; ISS:UniProtKB.
DR GO; GO:0022008; P:neurogenesis; IMP:CACAO.
DR GO; GO:0031175; P:neuron projection development; ISO:MGI.
DR GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0090261; P:positive regulation of inclusion body assembly; ISO:MGI.
DR GO; GO:0031587; P:positive regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity; IMP:UniProtKB.
DR GO; GO:0050769; P:positive regulation of neurogenesis; IMP:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR GO; GO:0032901; P:positive regulation of neurotrophin production; ISS:UniProtKB.
DR GO; GO:1902857; P:positive regulation of non-motile cilium assembly; IMP:UniProtKB.
DR GO; GO:0032230; P:positive regulation of synaptic transmission, GABAergic; ISS:UniProtKB.
DR GO; GO:0008104; P:protein localization; ISO:MGI.
DR GO; GO:0006605; P:protein targeting; IBA:GO_Central.
DR GO; GO:0017157; P:regulation of exocytosis; IMP:UniProtKB.
DR GO; GO:1902513; P:regulation of organelle transport along microtubule; IMP:UniProtKB.
DR GO; GO:0099149; P:regulation of postsynaptic neurotransmitter receptor internalization; ISO:MGI.
DR GO; GO:0008090; P:retrograde axonal transport; ISS:UniProtKB.
DR GO; GO:0047496; P:vesicle transport along microtubule; IMP:MGI.
DR InterPro; IPR006933; HAP1_N.
DR Pfam; PF04849; HAP1_N; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Autophagy; Cell projection;
KW Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoplasmic vesicle;
KW Cytoskeleton; Endoplasmic reticulum; Endosome; Exocytosis; Lysosome;
KW Mitochondrion; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Synapse; Transport.
FT CHAIN 1..628
FT /note="Huntingtin-associated protein 1"
FT /id="PRO_0000083895"
FT DOMAIN 79..403
FT /note="HAP1 N-terminal"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..319
FT /note="Sufficient for interaction with KIF5B"
FT /evidence="ECO:0000250"
FT REGION 157..261
FT /note="Interaction with TBP"
FT /evidence="ECO:0000269|PubMed:17868456"
FT REGION 212..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..444
FT /note="Sufficient for self-association and interaction with
FT HD"
FT /evidence="ECO:0000250"
FT REGION 372..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..582
FT /note="Interaction with TBP"
FT /evidence="ECO:0000269|PubMed:17868456"
FT REGION 562..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 168..301
FT /evidence="ECO:0000255"
FT COILED 327..367
FT /evidence="ECO:0000255"
FT COMPBIAS 48..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..236
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..466
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..524
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..602
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..618
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 578..628
FT /note="DSPTPQQQTNMGGGILEQQPRVPTQDSQRLEEDRATHSPSAREEEGPSGAT
FT -> GECSRRGHPPASGTSFRSSTI (in isoform A)"
FT /evidence="ECO:0000303|PubMed:9599014"
FT /id="VSP_004279"
FT MOD_RES O35668-2:598
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P54256"
SQ SEQUENCE 628 AA; 70116 MW; AF516F61D6AB7CCB CRC64;
MRPKEQVQSG AGDGTGSGDP AAGTPTTQPA VGPAPEPSAE PKPAPAQGTG SGQKSGSRTK
TGSFCRSMII GDSDAPWTRY VFQGPYGPRA TGLGTGKAEG IWKTPAAYIG RRPGVSGPER
AAFIRELQEA LCPNPPPTKK ITEDDVKVML YLLEEKERDL NTAARIGQSL VKQNSVLMEE
NNKLETMLGS AREEILHLRK QVNLRDDLLQ LYSDSDDDDD EEDEEDEEEG EEEEREGQRD
QDQQHDHPYG APKPHPKAET AHRCPQLETL QQKLRLLEEE NDHLREEASH LDNLEDEEQM
LILECVEQFS EASQQMAELS EVLVLRLEGY ERQQKEITQL QAEITKLQQR CQSYGAQTEK
LQQMLASEKG IHSESLRAGS YMQDYGSRPR DRQEDGKSHR QRSSMPAGSV THYGYSVPLD
ALPSFPETLA EELRTSLRKF ITDPAYFMER RDTHCREGRK KEQRAMPPPP AQDLKPPEDF
EAPEELVPEE ELGAIEEVGT AEDGQAEENE QASEETEAWE EVEPEVDETT RMNVVVSALE
ASGLGPSHLD MKYVLQQLSN WQDAHSKRQQ KQKVVPKDSP TPQQQTNMGG GILEQQPRVP
TQDSQRLEED RATHSPSARE EEGPSGAT
