KIF5A_MOUSE
ID KIF5A_MOUSE Reviewed; 1027 AA.
AC P33175; Q5DTP1; Q6PDY7; Q9Z2F9;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 3.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Kinesin heavy chain isoform 5A;
DE AltName: Full=Kinesin heavy chain neuron-specific 1;
DE AltName: Full=Neuronal kinesin heavy chain;
DE Short=NKHC;
GN Name=Kif5a; Synonyms=Kiaa4086, Kif5, Nkhc1;
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=Brain;
RX PubMed=9782088; DOI=10.1006/geno.1998.5427;
RA Xia C., Rahman A., Yang Z., Goldstein L.S.B.;
RT "Chromosomal localization reveals three kinesin heavy chain genes in
RT mouse.";
RL Genomics 52:209-213(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Fetal brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 89-237.
RC TISSUE=Brain;
RX PubMed=1447303; DOI=10.1083/jcb.119.5.1287;
RA Aizawa H., Sekine Y., Takemura R., Zhang Z., Nangaku M., Hirokawa N.;
RT "Kinesin family in murine central nervous system.";
RL J. Cell Biol. 119:1287-1296(1992).
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 DTNB.
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 [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12682084; DOI=10.1083/jcb.200301026;
RA Xia C.H., Roberts E.A., Her L.S., Liu X., Williams D.S., Cleveland D.W.,
RA Goldstein L.S.;
RT "Abnormal neurofilament transport caused by targeted disruption of neuronal
RT kinesin heavy chain KIF5A.";
RL J. Cell Biol. 161:55-66(2003).
RN [9]
RP INTERACTION WITH FMR1.
RX PubMed=18539120; DOI=10.1016/j.devcel.2008.04.003;
RA Dictenberg J.B., Swanger S.A., Antar L.N., Singer R.H., Bassell G.J.;
RT "A direct role for FMRP in activity-dependent dendritic mRNA transport
RT links filopodial-spine morphogenesis to fragile X syndrome.";
RL Dev. Cell 14:926-939(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-397, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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, MUTAGENESIS OF THR-93, AND INTERACTION WITH ZFYVE27; RAB11A;
RP RAB11B; SURF4; RTN3; VAPA; VAPB AND SURF4.
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 INTERACTION WITH ZFYVE27.
RX PubMed=24251978; DOI=10.1111/gtc.12109;
RA Ohnishi T., Shirane M., Hashimoto Y., Saita S., Nakayama K.I.;
RT "Identification and characterization of a neuron-specific isoform of
RT protrudin.";
RL Genes Cells 19:97-111(2014).
CC -!- FUNCTION: Microtubule-dependent motor required for slow axonal
CC transport of neurofilament proteins (NFH, NFM and NFL)
CC (PubMed:12682084). Can induce formation of neurite-like membrane
CC protrusions in non-neuronal cells in a ZFYVE27-dependent manner. The
CC ZFYVE27-KIF5A complex contributes to the vesicular transport of VAPA,
CC VAPB, SURF4, RAB11A, RAB11B and RTN3 proteins in neurons
CC (PubMed:21976701). Required for anterograde axonal transportation of
CC MAPK8IP3/JIP3 which is essential for MAPK8IP3/JIP3 function in axon
CC elongation (By similarity). {ECO:0000250|UniProtKB:Q6QLM7,
CC ECO:0000269|PubMed:12682084, ECO:0000269|PubMed:21976701}.
CC -!- SUBUNIT: Oligomer composed of two heavy chains and two light chains.
CC Interacts with GRIP1 (PubMed:11986669). Interacts with FMR1 (via C-
CC terminus); this interaction is increased in a mGluR-dependent manner
CC (PubMed:18539120). Interacts with BORCS5 (By similarity). Interacts
CC with ZFYVE27 (PubMed:21976701, PubMed:24251978). Interacts with VAPA,
CC VAPB, SURF4, RAB11A (GDP-bound form), RAB11B (GDP-bound form) and RTN3
CC in a ZFYVE27-dependent manner (PubMed:21976701). Interacts with BICD2
CC (By similarity). Interacts with DTNB (PubMed:14600269).
CC {ECO:0000250|UniProtKB:Q12840, ECO:0000269|PubMed:11986669,
CC ECO:0000269|PubMed:14600269, ECO:0000269|PubMed:18539120,
CC ECO:0000269|PubMed:21976701, ECO:0000269|PubMed:24251978}.
CC -!- INTERACTION:
CC P33175; O08788: Dctn1; NbExp=2; IntAct=EBI-349710, EBI-776180;
CC P33175; O70585: Dtnb; NbExp=4; IntAct=EBI-349710, EBI-349714;
CC P33175; Q96NW4: ANKRD27; Xeno; NbExp=2; IntAct=EBI-349710, EBI-6125599;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q6QLM7}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q6QLM7}. Perikaryon
CC {ECO:0000250|UniProtKB:Q6QLM7}. Note=Concentrated in the cell body of
CC the neurons, particularly in the perinuclear region.
CC {ECO:0000250|UniProtKB:Q6QLM7}.
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: Death shortly after birth. Neuron-specific
CC deletion within the first 3 weeks after birth is lethal in 75% of
CC animals. Surviving animals show accumulation of neurofilament proteins
CC in neuronal soma, age-dependent sensory neuron degeneration, loss of
CC large caliber axons, and hind limb paralysis with a stronger effect on
CC sensory neurons compared with motor neurons.
CC {ECO:0000269|PubMed:12682084}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. Kinesin subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00283}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD90503.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF067179; AAC79803.1; -; mRNA.
DR EMBL; AK147352; BAE27862.1; -; mRNA.
DR EMBL; AK147660; BAE28054.1; -; mRNA.
DR EMBL; AK147707; BAE28087.1; -; mRNA.
DR EMBL; AK220479; BAD90503.1; ALT_INIT; mRNA.
DR EMBL; BC058396; AAH58396.1; -; mRNA.
DR CCDS; CCDS24233.1; -.
DR PIR; C44259; C44259.
DR RefSeq; NP_001034089.1; NM_001039000.4.
DR RefSeq; NP_032473.2; NM_008447.4.
DR AlphaFoldDB; P33175; -.
DR SMR; P33175; -.
DR BioGRID; 200945; 22.
DR CORUM; P33175; -.
DR IntAct; P33175; 12.
DR MINT; P33175; -.
DR STRING; 10090.ENSMUSP00000096775; -.
DR iPTMnet; P33175; -.
DR PhosphoSitePlus; P33175; -.
DR jPOST; P33175; -.
DR MaxQB; P33175; -.
DR PaxDb; P33175; -.
DR PeptideAtlas; P33175; -.
DR PRIDE; P33175; -.
DR ProteomicsDB; 263539; -.
DR Antibodypedia; 1390; 270 antibodies from 36 providers.
DR DNASU; 16572; -.
DR Ensembl; ENSMUST00000099172; ENSMUSP00000096775; ENSMUSG00000074657.
DR Ensembl; ENSMUST00000217895; ENSMUSP00000151402; ENSMUSG00000074657.
DR GeneID; 16572; -.
DR KEGG; mmu:16572; -.
DR UCSC; uc007his.2; mouse.
DR CTD; 3798; -.
DR MGI; MGI:109564; Kif5a.
DR VEuPathDB; HostDB:ENSMUSG00000074657; -.
DR eggNOG; KOG0240; Eukaryota.
DR GeneTree; ENSGT00940000159439; -.
DR HOGENOM; CLU_001485_11_1_1; -.
DR InParanoid; P33175; -.
DR OMA; NHMRIGV; -.
DR OrthoDB; 1334528at2759; -.
DR PhylomeDB; P33175; -.
DR TreeFam; TF105225; -.
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; 16572; 8 hits in 72 CRISPR screens.
DR ChiTaRS; Kif5a; mouse.
DR PRO; PR:P33175; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P33175; protein.
DR Bgee; ENSMUSG00000074657; Expressed in globus pallidus and 166 other tissues.
DR ExpressionAtlas; P33175; baseline and differential.
DR Genevisible; P33175; MM.
DR GO; GO:0097440; C:apical dendrite; ISO:MGI.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0090724; C:central region of growth cone; 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:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0032839; C:dendrite cytoplasm; IEA:GOC.
DR GO; GO:0005871; C:kinesin complex; ISO:MGI.
DR GO; GO:0005874; C:microtubule; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0000932; C:P-body; ISO:MGI.
DR GO; GO:0043204; C:perikaryon; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0019894; F:kinesin binding; IPI:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IDA:MGI.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
DR GO; GO:0099641; P:anterograde axonal protein transport; ISS:UniProtKB.
DR GO; GO:0098971; P:anterograde dendritic transport of neurotransmitter receptor complex; IDA:SynGO.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:1990049; P:retrograde neuronal dense core vesicle transport; ISO:MGI.
DR GO; GO:0048489; P:synaptic vesicle transport; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; IDA:UniProtKB.
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 Acetylation; ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton;
KW Microtubule; Motor protein; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q12840"
FT CHAIN 2..1027
FT /note="Kinesin heavy chain isoform 5A"
FT /id="PRO_0000125354"
FT DOMAIN 9..327
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 174..315
FT /note="Microtubule-binding"
FT REGION 271..361
FT /note="Necessary for interaction with ZFYVE27"
FT /evidence="ECO:0000269|PubMed:21976701"
FT REGION 353..1027
FT /note="Interaction with BICD2"
FT /evidence="ECO:0000250|UniProtKB:Q12840"
FT REGION 906..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 907..1027
FT /note="Globular"
FT COILED 331..906
FT BINDING 86..93
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:Q12840"
FT MOD_RES 397
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MUTAGEN 93
FT /note="T->N: Loss of ability to induce formation of
FT neurite-like membrane protrusions in non-neuronal cells."
FT /evidence="ECO:0000269|PubMed:21976701"
FT CONFLICT 146
FT /note="L -> P (in Ref. 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="S -> T (in Ref. 1; AAC79803)"
FT /evidence="ECO:0000305"
FT CONFLICT 362..363
FT /note="KL -> NV (in Ref. 1; AAC79803)"
FT /evidence="ECO:0000305"
FT CONFLICT 727
FT /note="T -> I (in Ref. 3; BAD90503)"
FT /evidence="ECO:0000305"
FT CONFLICT 976
FT /note="A -> R (in Ref. 1; AAC79803)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1027 AA; 117019 MW; 419AD8C2D747DA0A CRC64;
MAETNNECSI KVLCRFRPLN QAEILRGDKF IPIFQGDDSV IIGGKPYVFD RVFPPNTTQE
QVYHACAMQI VKDVLAGYNG TIFAYGQTSS GKTHTMEGKL HDPQLMGIIP RIARDIFNHI
YSMDENLEFH IKVSYFEIYL DKIRDLLDVT KTNLSVHEDK NRVPFVKGCT ERFVSSPEEI
LDVIDEGKSN RHVAVTNMNE HSSRSHSIFL INIKQENVET EQKLSGKLYL VDLAGSEKVS
KTGAEGAVLD EAKNINKSLS ALGNVISALA EGTKSYVPYR DSKMTRILQD SLGGNCRTTM
FICCSPSSYN DAETKSTLMF GQRAKTIKNT ASVNLELTAE QWKKKYEKEK EKTKAQKETI
AKLEAELSRW RNGENVPETE RLAGEDSALG AELCEETPVN DNSSIVVRIA PEERQKYEEE
IRRLYKQLDD KDDEINQQSQ LIEKLKQQML DQEELLVSTR GDNEKVQREL SHLQSENDAA
KDEVKEVLQA LEELAVNYDQ KSQEVEEKSQ QNQLLVDELS QKVATMLSLE SELQRLQEVS
GHQRKRIAEV LNGLMRDLSE FSVIVGNGEI KLPVEISGAI EEEFTVARLY ISKIKSEVKS
VVKRCRQLEN LQVECHRKME VTGRELSSCQ LLISQHEAKI RSLTEYMQTV ELKKRHLEES
YDSLSDELAR LQAHETVHEV ALKDKEPDTQ DAEEVKKALE LQMENHREAH HRQLARLRDE
INEKQKTIDE LKDLNQKLQL ELEKLQADYE RLKNEENEKS AKLQELTFLY ERHEQSKQDL
KGLEETVARE LQTLHNLRKL FVQDVTTRVK KSAEMEPEDS GGIHSQKQKI SFLENNLEQL
TKVHKQLVRD NADLRCELPK LEKRLRATAE RVKALEGALK EAKEGAMKDK RRYQQEVDRI
KEAVRYKSSG KRGHSAQIAK PVRPGHYPAS SPTNPYGTRS PECISYTNNL FQNYQNLHLQ
AAPSSTSDMY FASSGATSVA PLASYQKANM DNGNATDIND NRSDLPCGYE AEDQAKLFPL
HQETAAS
