KINH_MOUSE
ID KINH_MOUSE Reviewed; 963 AA.
AC Q61768; O08711; Q5BL10; Q61580;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Kinesin-1 heavy chain;
DE AltName: Full=Conventional kinesin heavy chain;
DE AltName: Full=Ubiquitous kinesin heavy chain;
DE Short=UKHC;
GN Name=Kif5b; Synonyms=Khcs, Kns1;
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].
RC TISSUE=Pancreas;
RX PubMed=9112396; DOI=10.1210/endo.138.5.5139;
RA Meng Y.X., Wilson G.W., Avery M.C., Varden C.H., Balczon R.;
RT "Suppression of the expression of a pancreatic beta-cell form of the
RT kinesin heavy chain by antisense oligonucleotides inhibits insulin
RT secretion from primary cultures of mouse beta-cells.";
RL Endocrinology 138:1979-1987(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-881.
RC STRAIN=BALB/cJ;
RX PubMed=8170981; DOI=10.1073/pnas.91.9.3744;
RA Gudkov A.V., Kazarov A.R., Thimmapaya R., Axenovich S.A., Mazo I.A.,
RA Roninson I.B.;
RT "Cloning mammalian genes by expression selection of genetic suppressor
RT elements: association of kinesin with drug resistance and cell
RT immortalization.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:3744-3748(1994).
RN [4]
RP PROTEIN SEQUENCE OF 132-141 AND 490-505, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9657148; DOI=10.1016/s0092-8674(00)81459-2;
RA Tanaka Y., Kanai Y., Okada Y., Nonaka S., Takeda S., Harada A.,
RA Hirokawa N.;
RT "Targeted disruption of mouse conventional kinesin heavy chain, kif5B,
RT results in abnormal perinuclear clustering of mitochondria.";
RL Cell 93:1147-1158(1998).
RN [6]
RP INTERACTION WITH GRIP1.
RX PubMed=11986669; DOI=10.1038/nature743;
RA Setou M., Seog D.-H., Tanaka Y., Kanai Y., Takei Y., Kawagishi M.,
RA Hirokawa N.;
RT "Glutamate-receptor-interacting protein GRIP1 directly steers kinesin to
RT dendrites.";
RL Nature 417:83-87(2002).
RN [7]
RP INTERACTION WITH JAKMIP1.
RX PubMed=17532644; DOI=10.1016/j.mcn.2007.04.008;
RA Vidal R.L., Ramirez O.A., Sandoval L., Koenig-Robert R., Haertel S.,
RA Couve A.;
RT "Marlin-1 and conventional kinesin link GABAB receptors to the cytoskeleton
RT and regulate receptor transport.";
RL Mol. Cell. Neurosci. 35:501-512(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-945, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [9]
RP INTERACTION WITH PPP1R42.
RX PubMed=19886865; DOI=10.1042/bc20090091;
RA Wang R., Kaul A., Sperry A.O.;
RT "TLRR (lrrc67) interacts with PP1 and is associated with a cytoskeletal
RT complex in the testis.";
RL Biol. Cell 102:173-189(2010).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-945, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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 [11]
RP FUNCTION, AND INTERACTION WITH ZFYVE27.
RX PubMed=21976701; DOI=10.1091/mbc.e11-01-0068;
RA Matsuzaki F., Shirane M., Matsumoto M., Nakayama K.I.;
RT "Protrudin serves as an adaptor molecule that connects KIF5 and its cargoes
RT in vesicular transport during process formation.";
RL Mol. Biol. Cell 22:4602-4620(2011).
RN [12]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-956, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE 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: Microtubule-dependent motor required for normal distribution
CC of mitochondria and lysosomes. May be involved in the mechanisms of
CC growth arrest induced by exposure to DNA-damaging drugs or by cellular
CC senescence (PubMed:9657148). Can induce formation of neurite-like
CC membrane protrusions in non-neuronal cells in a ZFYVE27-dependent
CC manner (PubMed:21976701). Regulates centrosome and nuclear positioning
CC during mitotic entry. During the G2 phase of the cell cycle in a BICD2-
CC dependent manner, antagonizes dynein function and drives the separation
CC of nuclei and centrosomes. Required for anterograde axonal
CC transportation of MAPK8IP3/JIP3 which is essential for MAPK8IP3/JIP3
CC function in axon elongation (By similarity). Through binding with
CC PLEKHM2 and ARL8B, directs lysosome movement toward microtubule plus
CC ends. Involved in NK cell-mediated cytotoxicity. Drives the
CC polarization of cytolytic granules and microtubule-organizing centers
CC (MTOCs) toward the immune synapse between effector NK lymphocytes and
CC target cells (By similarity). {ECO:0000250|UniProtKB:P33176,
CC ECO:0000250|UniProtKB:Q2PQA9, ECO:0000269|PubMed:21976701,
CC ECO:0000269|PubMed:9657148}.
CC -!- SUBUNIT: Oligomer composed of two heavy chains and two light chains.
CC Interacts with GRIP1 and PPP1R42 (PubMed:11986669, PubMed:19886865).
CC Interacts with SYBU (By similarity). Interacts with JAKMIP1
CC (PubMed:17532644). Interacts with PLEKHM2. Interacts with ECPAS (By
CC similarity). Interacts with ZFYVE27 (PubMed:21976701). Found in a
CC complex with OGT, RHOT1, RHOT2 and TRAK1 (By similarity). Interacts
CC with APP (via cytoplasmic domain) (By similarity).
CC {ECO:0000250|UniProtKB:P33176, ECO:0000250|UniProtKB:Q2PQA9,
CC ECO:0000269|PubMed:11986669, ECO:0000269|PubMed:17532644,
CC ECO:0000269|PubMed:19886865, ECO:0000269|PubMed:21976701}.
CC -!- INTERACTION:
CC Q61768; O88485: Dync1i1; NbExp=4; IntAct=EBI-776129, EBI-492834;
CC Q61768; O35685: Nudc; NbExp=4; IntAct=EBI-776129, EBI-911192;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q2PQA9}. Cytolytic granule membrane
CC {ECO:0000250|UniProtKB:P33176}. Lysosome membrane
CC {ECO:0000250|UniProtKB:P33176}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P33176}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P33176}. Note=Uniformly distributed between soma
CC and neurites in hippocampal neurons. {ECO:0000250|UniProtKB:Q2PQA9}.
CC -!- DOMAIN: Composed of three structural domains: a large globular N-
CC terminal domain which is responsible for the motor activity of kinesin
CC (it hydrolyzes ATP and binds microtubule), a central alpha-helical
CC coiled coil domain that mediates the heavy chain dimerization; and a
CC small globular C-terminal domain which interacts with other proteins
CC (such as the kinesin light chains), vesicles and membranous organelles.
CC -!- DISRUPTION PHENOTYPE: Mice are embryonic lethal. They show perinuclear
CC clustering of mitochondria and impaired lysosomal dispersion.
CC {ECO:0000269|PubMed:9657148}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. Kinesin subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00283}.
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DR EMBL; U86090; AAB53940.1; -; mRNA.
DR EMBL; BC090841; AAH90841.1; -; mRNA.
DR EMBL; L27153; AAA20133.1; -; mRNA.
DR EMBL; L29223; AAA20132.2; -; mRNA.
DR CCDS; CCDS37724.1; -.
DR PIR; I84737; I84737.
DR RefSeq; NP_032474.2; NM_008448.3.
DR PDB; 6IGN; X-ray; 3.45 A; A=444-566.
DR PDB; 6IGV; X-ray; 3.00 A; A=446-563.
DR PDBsum; 6IGN; -.
DR PDBsum; 6IGV; -.
DR AlphaFoldDB; Q61768; -.
DR SMR; Q61768; -.
DR BioGRID; 200946; 43.
DR CORUM; Q61768; -.
DR DIP; DIP-32053N; -.
DR IntAct; Q61768; 33.
DR MINT; Q61768; -.
DR STRING; 10090.ENSMUSP00000025083; -.
DR iPTMnet; Q61768; -.
DR PhosphoSitePlus; Q61768; -.
DR EPD; Q61768; -.
DR jPOST; Q61768; -.
DR MaxQB; Q61768; -.
DR PaxDb; Q61768; -.
DR PeptideAtlas; Q61768; -.
DR PRIDE; Q61768; -.
DR ProteomicsDB; 264756; -.
DR Antibodypedia; 4077; 476 antibodies from 42 providers.
DR DNASU; 16573; -.
DR Ensembl; ENSMUST00000025083; ENSMUSP00000025083; ENSMUSG00000006740.
DR GeneID; 16573; -.
DR KEGG; mmu:16573; -.
DR UCSC; uc008dzf.2; mouse.
DR CTD; 3799; -.
DR MGI; MGI:1098268; Kif5b.
DR VEuPathDB; HostDB:ENSMUSG00000006740; -.
DR eggNOG; KOG0240; Eukaryota.
DR GeneTree; ENSGT00940000154801; -.
DR HOGENOM; CLU_001485_11_1_1; -.
DR InParanoid; Q61768; -.
DR OMA; RMAKMMA; -.
DR OrthoDB; 1334528at2759; -.
DR PhylomeDB; Q61768; -.
DR TreeFam; TF105225; -.
DR BRENDA; 5.6.1.3; 3474.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-5625970; RHO GTPases activate KTN1.
DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-MMU-983189; Kinesins.
DR BioGRID-ORCS; 16573; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Kif5b; mouse.
DR PRO; PR:Q61768; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q61768; protein.
DR Bgee; ENSMUSG00000006740; Expressed in globus pallidus and 277 other tissues.
DR ExpressionAtlas; Q61768; baseline and differential.
DR Genevisible; Q61768; MM.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0044295; C:axonal growth cone; ISO:MGI.
DR GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR GO; GO:0035253; C:ciliary rootlet; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0032839; C:dendrite cytoplasm; IEA:GOC.
DR GO; GO:0030139; C:endocytic vesicle; IDA:MGI.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043227; C:membrane-bounded organelle; IDA:MGI.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:HGNC-UCL.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:MGI.
DR GO; GO:0031982; C:vesicle; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008432; F:JUN kinase binding; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; ISS:HGNC-UCL.
DR GO; GO:0099609; F:microtubule lateral binding; ISO:MGI.
DR GO; GO:0003777; F:microtubule motor activity; ISS:HGNC-UCL.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:MGI.
DR GO; GO:0099641; P:anterograde axonal protein transport; ISS:UniProtKB.
DR GO; GO:0098971; P:anterograde dendritic transport of neurotransmitter receptor complex; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IDA:MGI.
DR GO; GO:0051642; P:centrosome localization; ISS:UniProtKB.
DR GO; GO:0007028; P:cytoplasm organization; IMP:MGI.
DR GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; IBA:GO_Central.
DR GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
DR GO; GO:0032418; P:lysosome localization; ISS:UniProtKB.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0007017; P:microtubule-based process; TAS:MGI.
DR GO; GO:0006839; P:mitochondrial transport; TAS:MGI.
DR GO; GO:0042267; P:natural killer cell mediated cytotoxicity; ISS:UniProtKB.
DR GO; GO:0072383; P:plus-end-directed vesicle transport along microtubule; IMP:MGI.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; ISO:MGI.
DR GO; GO:0090316; P:positive regulation of intracellular protein transport; ISO:MGI.
DR GO; GO:0043268; P:positive regulation of potassium ion transport; ISO:MGI.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISO:MGI.
DR GO; GO:0032230; P:positive regulation of synaptic transmission, GABAergic; IDA:UniProtKB.
DR GO; GO:0031340; P:positive regulation of vesicle fusion; ISO:MGI.
DR GO; GO:1905152; P:positive regulation of voltage-gated sodium channel activity; ISO:MGI.
DR GO; GO:0042391; P:regulation of membrane potential; ISO:MGI.
DR GO; GO:1990049; P:retrograde neuronal dense core vesicle transport; ISO:MGI.
DR GO; GO:0035617; P:stress granule disassembly; IMP:BHF-UCL.
DR GO; GO:0048489; P:synaptic vesicle transport; IBA:GO_Central.
DR GO; GO:0047496; P:vesicle transport along microtubule; IGI:MGI.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR027640; Kinesin-like_fam.
DR InterPro; IPR019821; Kinesin_motor_CS.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR24115; PTHR24115; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Coiled coil; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Isopeptide bond; Lysosome;
KW Membrane; Methylation; Microtubule; Motor protein; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P33176"
FT CHAIN 2..963
FT /note="Kinesin-1 heavy chain"
FT /id="PRO_0000125352"
FT DOMAIN 8..325
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 908..963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 915..963
FT /note="Globular"
FT COILED 329..914
FT COMPBIAS 942..957
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 85..92
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P33176"
FT MOD_RES 933
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P33176"
FT MOD_RES 945
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 956
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CROSSLNK 213
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P33176"
FT CONFLICT 20..21
FT /note="ES -> AT (in Ref. 3; AAA20133)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="M -> V (in Ref. 1; AAB53940)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="E -> G (in Ref. 3; AAA20133)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="H -> D (in Ref. 3; AAA20133)"
FT /evidence="ECO:0000305"
FT CONFLICT 255
FT /note="N -> K (in Ref. 3; AAA20133)"
FT /evidence="ECO:0000305"
FT CONFLICT 396
FT /note="I -> T (in Ref. 3; AAA20133)"
FT /evidence="ECO:0000305"
FT CONFLICT 403
FT /note="P -> G (in Ref. 1; AAB53940)"
FT /evidence="ECO:0000305"
FT CONFLICT 451
FT /note="T -> I (in Ref. 3; AAA20132)"
FT /evidence="ECO:0000305"
FT CONFLICT 520
FT /note="S -> T (in Ref. 1; AAB53940)"
FT /evidence="ECO:0000305"
FT CONFLICT 523
FT /note="L -> F (in Ref. 1; AAB53940)"
FT /evidence="ECO:0000305"
FT CONFLICT 653
FT /note="V -> D (in Ref. 1; AAB53940)"
FT /evidence="ECO:0000305"
FT CONFLICT 664
FT /note="V -> L (in Ref. 1; AAB53940)"
FT /evidence="ECO:0000305"
FT CONFLICT 744
FT /note="Q -> T (in Ref. 1; AAB53940)"
FT /evidence="ECO:0000305"
FT CONFLICT 814
FT /note="S -> R (in Ref. 3; AAA20133)"
FT /evidence="ECO:0000305"
FT CONFLICT 865
FT /note="K -> F (in Ref. 1; AAB53940)"
FT /evidence="ECO:0000305"
FT CONFLICT 881
FT /note="L -> R (in Ref. 3; AAA20133)"
FT /evidence="ECO:0000305"
FT HELIX 447..558
FT /evidence="ECO:0007829|PDB:6IGV"
SQ SEQUENCE 963 AA; 109551 MW; C3D3461A0C314901 CRC64;
MADPAECNIK VMCRFRPLNE SEVNRGDKYV AKFQGEDTVM IASKPYAFDR VFQSSTSQEQ
VYNDCAKKIV KDVLEGYNGT IFAYGQTSSG KTHTMEGKLH DPEGMGIIPR IVQDIFNYIY
SMDENLEFHI KVSYFEIYLD KIRDLLDVSK TNLSVHEDKN RVPYVKGCTE RFVCSPDEVM
DTIDEGKSNR HVAVTNMNEH SSRSHSIFLI NVKQENTQTE QKLSGKLYLV DLAGSEKVSK
TGAEGAVLDE AKNINKSLSA LGNVISALAE GSTYVPYRDS KMTRILQDSL GGNCRTTIVI
CCSPSSYNES ETKSTLLFGQ RAKTIKNTVC VNVELTAEQW KKKYEKEKEK NKTLRNTIQW
LENELNRWRN GETVPIDEQF DKEKANLEAF TADKDIAITS DKPAAAVGMA GSFTDAERRK
CEEELAKLYK QLDDKDEEIN QQSQLVEKLK TQMLDQEELL ASTRRDQDNM QAELNRLQAE
NDASKEEVKE VLQALEELAV NYDQKSQEVE DKTKEYELLS DELNQKSATL ASIDAELQKL
KEMTNHQKKR AAEMMASLLK DLAEIGIAVG NNDVKQPEGT GMIDEEFTVA RLYISKMKSE
VKTMVKRCKQ LESTQTESNK KMEENEKELA ACQLRISQHE AKIKSLTEYL QNVEQKKRQL
EESVDSLGEE LVQLRAQEKV HEMEKEHLNK VQTANEVKQA VEQQIQSHRE THQKQISSLR
DEVEAKEKLI TDLQDQNQKM VLEQERLRVE HERLKATDQE KSRKLHELTV MQDRREQARQ
DLKGLEETVA KELQTLHNLR KLFVQDLATR VKKSAEVDSD DTGGSAAQKQ KISFLENNLE
QLTKVHKQLV RDNADLRCEL PKLEKRLRAT AERVKALESA LKEAKENASR DRKRYQQEVD
RIKEAVRSKN MARRGHSAQI AKPIRPGQHP AASPTHPGTV RGGGSFVQNN QPVGLRGGGG
KQS
