BRSK1_MOUSE
ID BRSK1_MOUSE Reviewed; 778 AA.
AC Q5RJI5; A7LH90; A7LH91; B7SRN7; Q699J6;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Serine/threonine-protein kinase BRSK1;
DE EC=2.7.11.1;
DE EC=2.7.11.26;
DE AltName: Full=Brain-specific serine/threonine-protein kinase 1;
DE Short=BR serine/threonine-protein kinase 1;
DE AltName: Full=Serine/threonine-protein kinase SAD-B;
GN Name=Brsk1; Synonyms=Gm1100, Sadb;
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), FUNCTION, TISSUE SPECIFICITY, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=15705853; DOI=10.1126/science.1107403;
RA Kishi M., Pan Y.A., Crump J.G., Sanes J.R.;
RT "Mammalian SAD kinases are required for neuronal polarization.";
RL Science 307:929-932(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 4), FUNCTION, SUBCELLULAR
RP LOCATION, MUTAGENESIS OF LYS-63, AND DEVELOPMENTAL STAGE.
RX PubMed=19648910; DOI=10.1038/ncb1921;
RA Alvarado-Kristensson M., Rodriguez M.J., Silio V., Valpuesta J.M.,
RA Carrera A.C.;
RT "SADB phosphorylation of gamma-tubulin regulates centrosome duplication.";
RL Nat. Cell Biol. 11:1081-1092(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
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, ACTIVITY REGULATION, PHOSPHORYLATION AT THR-189, AND MUTAGENESIS
RP OF THR-189.
RX PubMed=17482548; DOI=10.1016/j.cell.2007.03.025;
RA Barnes A.P., Lilley B.N., Pan Y.A., Plummer L.J., Powell A.W., Raines A.N.,
RA Sanes J.R., Polleux F.;
RT "LKB1 and SAD kinases define a pathway required for the polarization of
RT cortical neurons.";
RL Cell 129:549-563(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-399; SER-443; SER-447;
RP SER-450; THR-529; THR-535 AND THR-583, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, 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).
RN [6]
RP FUNCTION.
RX PubMed=20026642; DOI=10.1242/jcs.058230;
RA Muller M., Lutter D., Puschel A.W.;
RT "Persistence of the cell-cycle checkpoint kinase Wee1 in SadA- and SadB-
RT deficient neurons disrupts neuronal polarity.";
RL J. Cell Sci. 123:286-294(2010).
RN [7]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-466; ARG-481; ARG-484; ARG-498;
RP ARG-525 AND ARG-550, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Serine/threonine-protein kinase that plays a key role in
CC polarization of neurons and centrosome duplication. Phosphorylates
CC CDC25B, CDC25C, MAPT/TAU, RIMS1, TUBG1, TUBG2 and WEE1. Following
CC phosphorylation and activation by STK11/LKB1, acts as a key regulator
CC of polarization of cortical neurons, probably by mediating
CC phosphorylation of microtubule-associated proteins such as MAPT/TAU at
CC 'Thr-504' and 'Ser-554'. Also regulates neuron polarization by
CC mediating phosphorylation of WEE1 at 'Ser-642' in postmitotic neurons,
CC leading to down-regulate WEE1 activity in polarized neurons. In
CC neurons, localizes to synaptic vesicles and plays a role in
CC neurotransmitter release, possibly by phosphorylating RIMS1. Also acts
CC as a positive regulator of centrosome duplication by mediating
CC phosphorylation of gamma-tubulin (TUBG1 and TUBG2) at 'Ser-131',
CC leading to translocation of gamma-tubulin and its associated proteins
CC to the centrosome. Involved in the UV-induced DNA damage checkpoint
CC response, probably by inhibiting CDK1 activity through phosphorylation
CC and activation of WEE1, and inhibition of CDC25B and CDC25C.
CC {ECO:0000269|PubMed:15705853, ECO:0000269|PubMed:17482548,
CC ECO:0000269|PubMed:19648910, ECO:0000269|PubMed:20026642}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[tau protein] = ADP + H(+) + O-phospho-L-seryl-
CC [tau protein]; Xref=Rhea:RHEA:12801, Rhea:RHEA-COMP:13701, Rhea:RHEA-
CC COMP:13702, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.26;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[tau protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[tau protein]; Xref=Rhea:RHEA:53904, Rhea:RHEA-COMP:13703,
CC Rhea:RHEA-COMP:13704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.26;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Activated by phosphorylation on Thr-189 by
CC STK11/LKB1. {ECO:0000269|PubMed:17482548}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250}. Synapse {ECO:0000250|UniProtKB:B2DD29}. Presynaptic
CC active zone {ECO:0000250|UniProtKB:B2DD29}. Cytoplasmic vesicle,
CC secretory vesicle, synaptic vesicle {ECO:0000250|UniProtKB:B2DD29}.
CC Note=Nuclear in the absence of DNA damage. Translocated to the nucleus
CC in response to UV- or MMS-induced DNA damage (By similarity).
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=SADB-Long, L;
CC IsoId=Q5RJI5-1; Sequence=Displayed;
CC Name=2; Synonyms=SADB-short, S;
CC IsoId=Q5RJI5-2; Sequence=VSP_041745;
CC Name=4; Synonyms=SADB-short 1, S1;
CC IsoId=Q5RJI5-4; Sequence=VSP_041743, VSP_041745;
CC -!- TISSUE SPECIFICITY: Present in the gray matter of the brain and spinal
CC cord (at protein level). Expressed in the nervous system, distributed
CC within the brain and spinal cord of embryonic and postnatal animals.
CC {ECO:0000269|PubMed:15705853}.
CC -!- DEVELOPMENTAL STAGE: Activity is high in G0, decreases after serum
CC addition, and increases transiently in advanced G1, at G1-S, and in S
CC phases. {ECO:0000269|PubMed:19648910}.
CC -!- PTM: Phosphorylated at Thr-189 by STK11/LKB1 in complex with STE20-
CC related adapter-alpha (STRADA) pseudo kinase and CAB39. Not
CC phosphorylated at Thr-189 by CaMKK2. In contrast, it is phosphorylated
CC and activated by CaMKK1. May be inactivated via dephosphorylation of
CC Thr-189 by PP2C. {ECO:0000269|PubMed:17482548}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Mice are fertile and
CC healthy. In contrast, mice lacking both Brsk1 and Brsk2 show little
CC spontaneous movement and are only weakly responsive to tactile
CC stimulation: they die within 2 hours of birth. Defects are due to
CC impaired neuronal differentiation and polarity.
CC {ECO:0000269|PubMed:15705853}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. SNF1 subfamily. {ECO:0000305}.
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DR EMBL; AY533671; AAT08446.1; -; mRNA.
DR EMBL; EU586326; ACE82255.1; -; mRNA.
DR EMBL; EU016556; ABS57358.1; -; mRNA.
DR EMBL; EU016557; ABS57359.1; -; mRNA.
DR EMBL; EU016558; ABS57360.1; -; mRNA.
DR EMBL; BC086636; AAH86636.1; -; mRNA.
DR CCDS; CCDS20741.1; -. [Q5RJI5-1]
DR CCDS; CCDS85205.1; -. [Q5RJI5-2]
DR RefSeq; NP_001003920.2; NM_001003920.3. [Q5RJI5-1]
DR RefSeq; NP_001162044.1; NM_001168572.1. [Q5RJI5-2]
DR PDB; 5IRI; X-ray; 2.80 A; A/B=592-719.
DR PDBsum; 5IRI; -.
DR AlphaFoldDB; Q5RJI5; -.
DR SMR; Q5RJI5; -.
DR BioGRID; 238175; 5.
DR IntAct; Q5RJI5; 4.
DR STRING; 10090.ENSMUSP00000039517; -.
DR iPTMnet; Q5RJI5; -.
DR PhosphoSitePlus; Q5RJI5; -.
DR SwissPalm; Q5RJI5; -.
DR MaxQB; Q5RJI5; -.
DR PaxDb; Q5RJI5; -.
DR PeptideAtlas; Q5RJI5; -.
DR PRIDE; Q5RJI5; -.
DR ProteomicsDB; 265237; -. [Q5RJI5-1]
DR ProteomicsDB; 265238; -. [Q5RJI5-2]
DR ProteomicsDB; 265239; -. [Q5RJI5-4]
DR Antibodypedia; 19545; 476 antibodies from 36 providers.
DR DNASU; 381979; -.
DR Ensembl; ENSMUST00000048248; ENSMUSP00000039517; ENSMUSG00000035390. [Q5RJI5-1]
DR Ensembl; ENSMUST00000205666; ENSMUSP00000145845; ENSMUSG00000035390. [Q5RJI5-4]
DR Ensembl; ENSMUST00000206024; ENSMUSP00000145970; ENSMUSG00000035390. [Q5RJI5-2]
DR GeneID; 381979; -.
DR KEGG; mmu:381979; -.
DR UCSC; uc009eye.2; mouse. [Q5RJI5-2]
DR UCSC; uc009eyf.1; mouse. [Q5RJI5-1]
DR CTD; 84446; -.
DR MGI; MGI:2685946; Brsk1.
DR VEuPathDB; HostDB:ENSMUSG00000035390; -.
DR eggNOG; KOG0588; Eukaryota.
DR GeneTree; ENSGT00940000161254; -.
DR InParanoid; Q5RJI5; -.
DR OMA; LFALLVX; -.
DR OrthoDB; 1127668at2759; -.
DR PhylomeDB; Q5RJI5; -.
DR TreeFam; TF313967; -.
DR BioGRID-ORCS; 381979; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Brsk1; mouse.
DR PRO; PR:Q5RJI5; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q5RJI5; protein.
DR Bgee; ENSMUSG00000035390; Expressed in primary visual cortex and 148 other tissues.
DR ExpressionAtlas; Q5RJI5; baseline and differential.
DR Genevisible; Q5RJI5; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0150034; C:distal axon; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048786; C:presynaptic active zone; IEA:UniProtKB-SubCell.
DR GO; GO:0008021; C:synaptic vesicle; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043015; F:gamma-tubulin binding; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0050321; F:tau-protein kinase activity; IDA:UniProtKB.
DR GO; GO:0008306; P:associative learning; IMP:ARUK-UCL.
DR GO; GO:0007409; P:axonogenesis; IMP:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0042149; P:cellular response to glucose starvation; IBA:GO_Central.
DR GO; GO:0051298; P:centrosome duplication; IMP:UniProtKB.
DR GO; GO:0030010; P:establishment of cell polarity; IMP:UniProtKB.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; ISO:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0090176; P:microtubule cytoskeleton organization involved in establishment of planar polarity; IGI:ARUK-UCL.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; IGI:MGI.
DR GO; GO:0048812; P:neuron projection morphogenesis; IGI:MGI.
DR GO; GO:0007269; P:neurotransmitter secretion; ISS:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0050770; P:regulation of axonogenesis; IGI:ARUK-UCL.
DR GO; GO:0010975; P:regulation of neuron projection development; IGI:ARUK-UCL.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IMP:ARUK-UCL.
DR GO; GO:0009411; P:response to UV; ISS:UniProtKB.
DR GO; GO:0099504; P:synaptic vesicle cycle; IMP:ARUK-UCL.
DR DisProt; DP02423; -.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR015940; UBA.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50030; UBA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Cell cycle;
KW Cell projection; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; DNA damage;
KW Kinase; Magnesium; Metal-binding; Methylation; Neurogenesis;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Synapse; Transferase.
FT CHAIN 1..778
FT /note="Serine/threonine-protein kinase BRSK1"
FT /id="PRO_0000260829"
FT DOMAIN 34..285
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 314..356
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..510
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 156
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 40..48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 63
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT MOD_RES 189
FT /note="Phosphothreonine; by LKB1"
FT /evidence="ECO:0000269|PubMed:17482548"
FT MOD_RES 399
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 447
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 466
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 481
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 484
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 498
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 508
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TDC3"
FT MOD_RES 525
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 529
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 535
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 550
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 583
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 586
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B2DD29"
FT MOD_RES 587
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B2DD29"
FT MOD_RES 601
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B2DD29"
FT VAR_SEQ 1..45
FT /note="MSSGSKEGGGGSPAYHLPHPHPHPPQHAQYVGPYRLEKTLGKGQT -> MQK
FT FGIEEM (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:19648910"
FT /id="VSP_041743"
FT VAR_SEQ 344..778
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:19648910"
FT /id="VSP_041745"
FT MUTAGEN 63
FT /note="K->R: Abolishes kinase activity and ability to
FT regulate centrosome duplication."
FT /evidence="ECO:0000269|PubMed:19648910"
FT MUTAGEN 189
FT /note="T->A: Abolishes activation by STK11/LKB1."
FT /evidence="ECO:0000269|PubMed:17482548"
FT CONFLICT 18..19
FT /note="Missing (in Ref. 2; ABS57359/ABS57360)"
FT /evidence="ECO:0000305"
FT CONFLICT 23..24
FT /note="Missing (in Ref. 1; AAT08446)"
FT /evidence="ECO:0000305"
FT STRAND 598..602
FT /evidence="ECO:0007829|PDB:5IRI"
FT STRAND 605..614
FT /evidence="ECO:0007829|PDB:5IRI"
FT HELIX 617..630
FT /evidence="ECO:0007829|PDB:5IRI"
FT STRAND 634..640
FT /evidence="ECO:0007829|PDB:5IRI"
FT STRAND 643..648
FT /evidence="ECO:0007829|PDB:5IRI"
FT HELIX 649..651
FT /evidence="ECO:0007829|PDB:5IRI"
FT STRAND 654..658
FT /evidence="ECO:0007829|PDB:5IRI"
FT STRAND 661..669
FT /evidence="ECO:0007829|PDB:5IRI"
FT STRAND 688..697
FT /evidence="ECO:0007829|PDB:5IRI"
FT HELIX 699..714
FT /evidence="ECO:0007829|PDB:5IRI"
SQ SEQUENCE 778 AA; 85155 MW; A35C86293A958D99 CRC64;
MSSGSKEGGG GSPAYHLPHP HPHPPQHAQY VGPYRLEKTL GKGQTGLVKL GVHCITGQKV
AVKIVNREKL SESVLMKVER EIAILKLIEH PHVLKLHDVY ENKKYLYLVL EHVSGGELFD
YLVKKGRLTP KEARKFFRQI VSALDFCHSY SICHRDLKPE NLLLDEKNNI RIADFGMASL
QVGDSLLETS CGSPHYACPE VIKGEKYDGR RADMWSCGVI LFALLVGALP FDDDNLRQLL
EKVKRGVFHM PHFIPPDCQS LLRGMIEVEP EKRLSLEQIQ KHPWYLGGKH EPDPCLEPAP
GRRVAMRSLP SNGELDPDVL ESMASLGCFR DRERLHRELR SEEENQEKMI YYLLLDRKER
YPSCEDQDLP PRNDVDPPRK RVDSPMLSRH GKRRPERKSM EVLSITDAGS GGSPVPTRRA
LEMAQHSQRS RSVSGASTGL SSSPLSSPRS PVFSFSPEPG AGDEARGGGS PTSKTQTLPS
RGPRGGGAGE QPPPPSARST PLPGPPGSPR SSGGTPLHSP LHTPRASPTG TPGTTPPPSP
GGGVGGAAWR SRLNSIRNSF LGSPRFHRRK MQVPTAEEMS SLTPESSPEL AKRSWFGNFI
SLDKEEQIFL VLKDKPLSSI KADIVHAFLS IPSLSHSVLS QTSFRAEYKA SGGPSVFQKP
VRFQVDISSS EGPEPSPRRD GSSGGGIYSV TFTLISGPSR RFKRVVETIQ AQLLSTHDQP
SVQALADEKN GAQTRPAGTP PRSLQPPPGR SDPDLSSSPR RGPPKDKKLL ATNGTPLP
