KIF14_MOUSE
ID KIF14_MOUSE Reviewed; 1674 AA.
AC L0N7N1;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2013, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Kinesin-like protein KIF14 {ECO:0000305};
GN Name=Kif14 {ECO:0000303|PubMed:23308235, ECO:0000312|MGI:MGI:1098226};
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 {ECO:0000312|EMBL:BAM74185.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=C57BL/6J;
RX PubMed=23308235; DOI=10.1371/journal.pone.0053490;
RA Fujikura K., Setsu T., Tanigaki K., Abe T., Kiyonari H., Terashima T.,
RA Sakisaka T.;
RT "Kif14 mutation causes severe brain malformation and hypomyelination.";
RL PLoS ONE 8:E53490-E53490(2013).
RN [2]
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 [3]
RP FUNCTION.
RX PubMed=24931760; DOI=10.1016/j.neuroscience.2014.06.011;
RA Yunus J., Setsu T., Kikkawa S., Sakisaka T., Terashima T.;
RT "Cytoarchitecture of the olfactory bulb in the laggard mutant mouse.";
RL Neuroscience 275:259-271(2014).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS) OF 390-738 IN COMPLEX WITH ADP,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND FUNCTION.
RX PubMed=24949858; DOI=10.1016/j.jmb.2014.05.030;
RA Arora K., Talje L., Asenjo A.B., Andersen P., Atchia K., Joshi M., Sosa H.,
RA Allingham J.S., Kwok B.H.;
RT "KIF14 binds tightly to microtubules and adopts a rigor-like
RT conformation.";
RL J. Mol. Biol. 426:2997-3015(2014).
CC -!- FUNCTION: Microtubule motor protein that binds to microtubules with
CC high affinity through each tubulin heterodimer and has an ATPase
CC activity (PubMed:24949858). Plays a role in many processes like cell
CC division, cytokinesis and also in cell proliferation and apoptosis (By
CC similarity). During cytokinesis, targets to central spindle and midbody
CC through its interaction with PRC1 and CIT respectively (By similarity).
CC Regulates cell growth through regulation of cell cycle progression and
CC cytokinesis. During cell cycle progression acts through SCF-dependent
CC proteasomal ubiquitin-dependent protein catabolic process which
CC controls CDKN1B degradation, resulting in positive regulation of
CC cyclins, including CCNE1, CCND1 and CCNB1 (By similarity). During late
CC neurogenesis, regulates the cerebellar and cerebral cortex development
CC and olfactory bulb development through regulation of apoptosis, cell
CC proliferation and cell division (PubMed:23308235, PubMed:24931760).
CC Also is required for chromosome congression and alignment during
CC mitotic cell cycle process (By similarity). Regulates cell spreading,
CC focal adhesion dynamics, and cell migration through its interaction
CC with RADIL resulting in regulation of RAP1A-mediated inside-out
CC integrin activation by tethering RADIL on microtubules (By similarity).
CC {ECO:0000250|UniProtKB:Q15058, ECO:0000269|PubMed:23308235,
CC ECO:0000269|PubMed:24931760, ECO:0000269|PubMed:24949858}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=62 uM for ATP {ECO:0000269|PubMed:24949858};
CC KM=33 uM for ATP (in the presence of microtubule)
CC {ECO:0000269|PubMed:24949858};
CC -!- SUBUNIT: Directly interacts with PRC1 within a complex also containing
CC KIF4A, KIF20A and KIF23; targets to the central spindle. Directly
CC interacts with CIT depending on the activation state of the kinase
CC (stronger interaction with the kinase-dead form); targets to the
CC midbody. Interacts with ARRB2; the interaction is detected in the
CC nucleus upon OR1D2 stimulation (By similarity). Interacts with AKT1;
CC the interaction is detected in the plasma membrane upon INS stimulation
CC and promotes AKT1 phosphorylation. Interacts with SVIL; at midbody
CC during cytokinesis. Interacts with RADIL (via PDZ domain); recruits
CC RADIL to the microtubule network restricting RADIL from interaction
CC with activated RAP1A. {ECO:0000250|UniProtKB:Q15058}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q15058}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q15058}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:Q15058}. Midbody {ECO:0000250|UniProtKB:Q15058}.
CC Note=Nuclear localization observed during interphase. Nuclear
CC localization triggered by entry into mitosis. Cytoplasmic in
CC interphase. Cytoplasmic in metaphase cells. From prophase to metaphase,
CC accumulates at the developing spindle poles and their associated
CC microtubules. During anaphase, accumulates at the spindle midzone.
CC Localization to the central spindle and midbody during anaphase is
CC dependent upon PRC1 and CIT presence. In cells ready to undergo
CC abscission, concentrates at the contractile ring.
CC {ECO:0000250|UniProtKB:Q15058}.
CC -!- DOMAIN: The kinesin motor domain binds to microtubules with high
CC affinity and has a robust ATPase activity but a very slow motility. The
CC kinesin motor domain protects microtubules from cold depolymerization.
CC Binds to each tubulin heterodimer resulting in a microtubule complexes.
CC Binds at the tubulin intradimer interface, at the crest of the
CC protofilament, and orients slightly toward the next protofilament.
CC {ECO:0000269|PubMed:24949858}.
CC -!- DISRUPTION PHENOTYPE: The lag homozygous mutant mice that lack
CC detectable Kif14 expression are indistinguishable from normal
CC littermates at birth. At P10, mutants exhibit an overt ataxic phenotype
CC that increased in severity over time. At P12, lag homozygous mutant
CC mice are unable to stand for 10 s on a narrow platform. Their gait is
CC wide and uncoordinated, and they frequently fell on their backs while
CC walking. These defects in voluntary movement control, posture and
CC balance are accompanied by progressive weakness and failure to gain
CC body weight. By P14, the homozygous mutants in a litter could be
CC identified by their small size and uncontrolled movements. The
CC homozygous mutants all died by P21. The lag homozygous mutant mice also
CC display a flathead, a reduction in brain size, slender optic nerves,
CC and a translucent spinal cord. {ECO:0000269|PubMed:23308235}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000255|PROSITE-ProRule:PRU00283}.
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DR EMBL; AB731728; BAM74185.1; -; mRNA.
DR EMBL; AC122127; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC126606; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS78693.1; -.
DR RefSeq; NP_001274108.1; NM_001287179.2.
DR RefSeq; XP_006529792.1; XM_006529729.3.
DR PDB; 4OZQ; X-ray; 2.71 A; A/B=390-738.
DR PDB; 6WWE; EM; 3.90 A; K=391-772.
DR PDB; 6WWF; EM; 3.30 A; K=391-772.
DR PDB; 6WWG; EM; 2.90 A; K/N=391-772.
DR PDB; 6WWH; EM; 3.80 A; K/N=391-772.
DR PDB; 6WWI; EM; 3.60 A; K=391-755.
DR PDB; 6WWJ; EM; 3.40 A; K=391-755.
DR PDB; 6WWK; EM; 3.00 A; K/N=391-755.
DR PDB; 6WWL; EM; 3.10 A; K/N=391-755.
DR PDB; 6WWM; EM; 2.80 A; K=391-748.
DR PDB; 6WWN; EM; 3.50 A; K=391-748.
DR PDB; 6WWO; EM; 2.80 A; K=391-748.
DR PDB; 6WWP; EM; 3.10 A; K=391-743.
DR PDB; 6WWQ; EM; 3.00 A; K=391-743.
DR PDB; 6WWR; EM; 2.70 A; K=391-743.
DR PDB; 6WWS; EM; 2.70 A; K=391-743.
DR PDB; 6WWT; EM; 3.20 A; K=391-735.
DR PDB; 6WWU; EM; 2.70 A; K=391-735.
DR PDB; 6WWV; EM; 3.10 A; K=391-735.
DR PDB; 7LVQ; EM; 2.90 A; K=391-743.
DR PDB; 7LVR; EM; 2.90 A; K=391-743.
DR PDBsum; 4OZQ; -.
DR PDBsum; 6WWE; -.
DR PDBsum; 6WWF; -.
DR PDBsum; 6WWG; -.
DR PDBsum; 6WWH; -.
DR PDBsum; 6WWI; -.
DR PDBsum; 6WWJ; -.
DR PDBsum; 6WWK; -.
DR PDBsum; 6WWL; -.
DR PDBsum; 6WWM; -.
DR PDBsum; 6WWN; -.
DR PDBsum; 6WWO; -.
DR PDBsum; 6WWP; -.
DR PDBsum; 6WWQ; -.
DR PDBsum; 6WWR; -.
DR PDBsum; 6WWS; -.
DR PDBsum; 6WWT; -.
DR PDBsum; 6WWU; -.
DR PDBsum; 6WWV; -.
DR PDBsum; 7LVQ; -.
DR PDBsum; 7LVR; -.
DR AlphaFoldDB; L0N7N1; -.
DR SMR; L0N7N1; -.
DR STRING; 10090.ENSMUSP00000139698; -.
DR iPTMnet; L0N7N1; -.
DR PhosphoSitePlus; L0N7N1; -.
DR PaxDb; L0N7N1; -.
DR PRIDE; L0N7N1; -.
DR ProteomicsDB; 269217; -.
DR Antibodypedia; 20633; 158 antibodies from 21 providers.
DR DNASU; 381293; -.
DR Ensembl; ENSMUST00000189413; ENSMUSP00000139698; ENSMUSG00000041498.
DR GeneID; 381293; -.
DR KEGG; mmu:381293; -.
DR UCSC; uc007cuv.2; mouse.
DR CTD; 9928; -.
DR MGI; MGI:1098226; Kif14.
DR VEuPathDB; HostDB:ENSMUSG00000041498; -.
DR eggNOG; KOG0245; Eukaryota.
DR GeneTree; ENSGT00940000156834; -.
DR OMA; VVLIKHW; -.
DR OrthoDB; 76316at2759; -.
DR PhylomeDB; L0N7N1; -.
DR Reactome; R-MMU-5625900; RHO GTPases activate CIT.
DR Reactome; R-MMU-9696270; RND2 GTPase cycle.
DR Reactome; R-MMU-9696273; RND1 GTPase cycle.
DR SABIO-RK; L0N7N1; -.
DR BioGRID-ORCS; 381293; 16 hits in 68 CRISPR screens.
DR ChiTaRS; Kif14; mouse.
DR PRO; PR:L0N7N1; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; L0N7N1; protein.
DR Bgee; ENSMUSG00000041498; Expressed in animal zygote and 51 other tissues.
DR ExpressionAtlas; L0N7N1; baseline and differential.
DR Genevisible; L0N7N1; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0090543; C:Flemming body; ISO:MGI.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0005874; C:microtubule; ISO:MGI.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0051233; C:spindle midzone; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0015631; F:tubulin binding; IDA:UniProtKB.
DR GO; GO:0032147; P:activation of protein kinase activity; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IMP:UniProtKB.
DR GO; GO:0021846; P:cell proliferation in forebrain; IMP:UniProtKB.
DR GO; GO:0021695; P:cerebellar cortex development; IMP:UniProtKB.
DR GO; GO:0021685; P:cerebellar granular layer structural organization; IMP:UniProtKB.
DR GO; GO:0021693; P:cerebellar Purkinje cell layer structural organization; IMP:UniProtKB.
DR GO; GO:0021987; P:cerebral cortex development; IMP:UniProtKB.
DR GO; GO:0045184; P:establishment of protein localization; ISO:MGI.
DR GO; GO:0021766; P:hippocampus development; IMP:UniProtKB.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0007080; P:mitotic metaphase plate congression; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0033624; P:negative regulation of integrin activation; ISO:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:UniProtKB.
DR GO; GO:0021772; P:olfactory bulb development; IMP:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0032467; P:positive regulation of cytokinesis; ISS:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0030155; P:regulation of cell adhesion; ISO:MGI.
DR GO; GO:0001558; P:regulation of cell growth; ISS:UniProtKB.
DR GO; GO:1903429; P:regulation of cell maturation; IMP:UniProtKB.
DR GO; GO:0030334; P:regulation of cell migration; ISO:MGI.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0031641; P:regulation of myelination; IMP:UniProtKB.
DR GO; GO:0043523; P:regulation of neuron apoptotic process; IMP:UniProtKB.
DR GO; GO:0032487; P:regulation of Rap protein signal transduction; ISO:MGI.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISO:MGI.
DR CDD; cd00060; FHA; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR027640; Kinesin-like_fam.
DR InterPro; IPR032405; Kinesin_assoc.
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 InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR24115; PTHR24115; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF16183; Kinesin_assoc; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00240; FHA; 1.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton;
KW Microtubule; Motor protein; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1674
FT /note="Kinesin-like protein KIF14"
FT /id="PRO_0000431706"
FT DOMAIN 393..736
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT DOMAIN 860..911
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT REGION 1..391
FT /note="Required for PRC1-binding"
FT /evidence="ECO:0000250|UniProtKB:Q15058"
FT REGION 132..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..772
FT /note="Required for microtubule-binding with high affinity"
FT /evidence="ECO:0000269|PubMed:24949858"
FT REGION 936..1674
FT /note="Required for CIT-binding"
FT /evidence="ECO:0000250|UniProtKB:Q15058"
FT REGION 1618..1674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 743..826
FT /evidence="ECO:0000255"
FT COILED 961..1110
FT /evidence="ECO:0000255"
FT COMPBIAS 138..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1631..1651
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 482..489
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283,
FT ECO:0007744|PDB:4OZQ"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15058"
FT MOD_RES 262
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15058"
FT MOD_RES 973
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15058"
FT MOD_RES 1326
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15058"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:6WWO"
FT STRAND 394..400
FT /evidence="ECO:0007829|PDB:6WWR"
FT HELIX 405..410
FT /evidence="ECO:0007829|PDB:6WWR"
FT STRAND 416..418
FT /evidence="ECO:0007829|PDB:6WWR"
FT STRAND 419..421
FT /evidence="ECO:0007829|PDB:6WWN"
FT STRAND 423..426
FT /evidence="ECO:0007829|PDB:6WWR"
FT STRAND 428..431
FT /evidence="ECO:0007829|PDB:6WWM"
FT STRAND 433..436
FT /evidence="ECO:0007829|PDB:6WWR"
FT STRAND 439..443
FT /evidence="ECO:0007829|PDB:6WWR"
FT STRAND 445..449
FT /evidence="ECO:0007829|PDB:6WWU"
FT HELIX 456..459
FT /evidence="ECO:0007829|PDB:6WWR"
FT TURN 460..463
FT /evidence="ECO:0007829|PDB:6WWR"
FT HELIX 464..471
FT /evidence="ECO:0007829|PDB:6WWR"
FT STRAND 475..482
FT /evidence="ECO:0007829|PDB:6WWR"
FT STRAND 484..487
FT /evidence="ECO:0007829|PDB:6WWG"
FT HELIX 488..491
FT /evidence="ECO:0007829|PDB:6WWR"
FT STRAND 492..494
FT /evidence="ECO:0007829|PDB:6WWO"
FT STRAND 496..499
FT /evidence="ECO:0007829|PDB:6WWR"
FT HELIX 501..516
FT /evidence="ECO:0007829|PDB:6WWR"
FT STRAND 519..533
FT /evidence="ECO:0007829|PDB:6WWR"
FT STRAND 536..539
FT /evidence="ECO:0007829|PDB:6WWR"
FT STRAND 546..548
FT /evidence="ECO:0007829|PDB:6WWR"
FT STRAND 556..559
FT /evidence="ECO:0007829|PDB:6WWR"
FT TURN 560..562
FT /evidence="ECO:0007829|PDB:6WWR"
FT STRAND 563..566
FT /evidence="ECO:0007829|PDB:6WWR"
FT STRAND 572..576
FT /evidence="ECO:0007829|PDB:6WWR"
FT HELIX 577..579
FT /evidence="ECO:0007829|PDB:6WWR"
FT HELIX 580..588
FT /evidence="ECO:0007829|PDB:6WWR"
FT STRAND 596..598
FT /evidence="ECO:0007829|PDB:6WWM"
FT STRAND 600..603
FT /evidence="ECO:0007829|PDB:6WWR"
FT STRAND 605..617
FT /evidence="ECO:0007829|PDB:6WWR"
FT STRAND 621..623
FT /evidence="ECO:0007829|PDB:6WWR"
FT STRAND 629..637
FT /evidence="ECO:0007829|PDB:6WWR"
FT TURN 645..647
FT /evidence="ECO:0007829|PDB:6WWR"
FT HELIX 653..679
FT /evidence="ECO:0007829|PDB:6WWR"
FT HELIX 688..690
FT /evidence="ECO:0007829|PDB:6WWM"
FT HELIX 692..696
FT /evidence="ECO:0007829|PDB:6WWR"
FT HELIX 698..700
FT /evidence="ECO:0007829|PDB:6WWR"
FT STRAND 701..713
FT /evidence="ECO:0007829|PDB:6WWR"
FT HELIX 717..719
FT /evidence="ECO:0007829|PDB:6WWR"
FT HELIX 720..731
FT /evidence="ECO:0007829|PDB:6WWR"
FT STRAND 737..740
FT /evidence="ECO:0007829|PDB:6WWO"
FT TURN 747..749
FT /evidence="ECO:0007829|PDB:6WWG"
FT HELIX 751..754
FT /evidence="ECO:0007829|PDB:6WWG"
SQ SEQUENCE 1674 AA; 186445 MW; 7A2616CA801C4183 CRC64;
MSVHTSHSRH NIGSLEVSSS QKISASSGLV HSSRLELHLK ADMSECENHD PFVNAGSKTI
DINSTYVISA CKKTRETPVT SDPRRLSLQR RATCGDRESS LLGSELGNRR TADTSLRLQR
RHGRADYVGK WETLNPVGGN PGSDSASQAS RTEAKGVNND TRVLSSVVSV KDSNDTGLTR
CKDPGPPVGA SNEKVTVKDT NSRAPVGSQR QTEAMRSGHL VVQLTESKSD TPVSGGRNSH
RGNAGKDTAK QVGTFGSSDT RTPVKCVLEH RWTPRHDPPP PKSPALSTPK NNGKDIPKHG
STFRSASSES RTPVKCVPEH RWTPRHDLPP PKSPALSTLK NRIASPRVKP RPKSSLFANK
RESSRESTLP PEENSLVQKT FTEPDSLKVE NSQVTVAVRV RPFSKREKTE KASQVVFTNG
EEITVEHPDM KQVYSFIYDV SFWSFDECHP GYASQTTVYE TLAAPLLDRA FEGYNTCLFA
YGQTGSGKSY TMMGLNEEPG IIPRFCEDLF AQIAKKQTSE VSYHLEMSFF EVYNEKIHDL
LVCKGENGQR KQPLRAREHP VSGPYVEGLS MNVVSSYSDI QSWLELGNKQ RATAATGMND
KSSRSHSVFT LVMTQTKTEV VEGEEHDHRI TSRINLVDLA GSERCSTAHS SGQRLKEGVS
INKSLLTLGK VISALSEQAN GKRVFIPYRE STLTWLLKES LGGNSKTAMI ATVSPAASNI
EETLSTLRYA TQARLIVNIA KVNEDMNAKL IRELKAEIEK LKAAQRSNRN IDPERYRLCR
QEITSLRMKL HQQERDMAEI QRVWKEKFEQ AEKRKLQETK ELQKAGVTFQ MDNHLPNLVN
LNEDPQLSEM LLYMVKEGVT TVGKHTPSSS HDIQLSGVLI ADDHCTIRNF GGTVSIVPAG
EAKTYVNGTH ISEPTVLHHG DRVVLGGDHY FRFNHPVEVQ KGKKLSSRNN LTTSEGPKDF
EFAKNELLTA QRSRLEAEIK DAQLKAKEEM MQGIQIAKEM AQQELSSQKA VYERKIQALE
AELREESQRK RLEELNNQKA SHKIEELERA KQHLEQEVYV NKRRLEMETL ATKQALEDHR
IRHARILEAL EIEKQKIAEE VQMLQENRGN RDKTFTIQPN WNSMKLSTMI QEANAISDKF
KKCYIFGRHD ASDKGRSDTS VRVRNLQLGI STFWSLEKFE SKLAAMKELY ESNGGDRDED
VFCDPADEWE PDITSTPVSS LSRRRSRSLM KNRRVSGCLH DIHPIQSMQS SHSSGLMEKP
STIYSNSSES FLPGICKELI GSSIDFLGQS FDEEKTIADS LINNLLRLHN GVIAISKAHE
EQDEESQDNL FSDRAAQALT IQVACAFEQL VVLFKHWLGD FLPCTGSARL EDELRQDIKK
LGGYLQLFLQ GCCSDISSMV KEAQNKVMKI IQQAVQCVGQ LAVLKGSKLC VLENSSKVSS
TQEFMAALQD GVTSGMKSLL DSGLETAQDL RQDLSRQSAR EEVTKQMKAS TVEWVGSLEN
AVAEWRTKSF RTQAQEGSRQ QVSKLLSLAS EFLKLKSCLQ QTVEMIVSAL RGCPSDLHCL
RSCTETICSL ARKLHSDFSA HSASAGSCGN ELPRADCEEL ESLAKSLLLC FECGESPGLS
KPWESCSSNS KEEQCKSDRA DCGKSGPRRA CEPHGDATPA VSSGDCTPNR IQWV
