KIF1A_MOUSE
ID KIF1A_MOUSE Reviewed; 1695 AA.
AC P33173; Q61770;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Kinesin-like protein KIF1A;
DE AltName: Full=Axonal transporter of synaptic vesicles;
GN Name=Kif1a; Synonyms=Atsv, Kif1;
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], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=7539720; DOI=10.1016/0092-8674(95)90538-3;
RA Okada Y., Yamazaki H., Sekine-Aizawa Y., Hirokawa N.;
RT "The neuron-specific kinesin superfamily protein KIF1A is a unique
RT monomeric motor for anterograde axonal transport of synaptic vesicle
RT precursors.";
RL Cell 81:769-780(1995).
RN [2]
RP PRELIMINARY NUCLEOTIDE SEQUENCE OF 100-247.
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 [3]
RP INTERACTION WITH MADD, AND TISSUE SPECIFICITY.
RX PubMed=18849981; DOI=10.1038/ncb1785;
RA Niwa S., Tanaka Y., Hirokawa N.;
RT "KIF1Bbeta- and KIF1A-mediated axonal transport of presynaptic regulator
RT Rab3 occurs in a GTP-dependent manner through DENN/MADD.";
RL Nat. Cell Biol. 10:1269-1279(2008).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-607; THR-612; SER-932;
RP SER-1342; THR-1524; THR-1528; SER-1533 AND SER-1537, 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 [5]
RP INTERACTION WITH SYT11.
RX PubMed=30808661; DOI=10.1101/gad.320077.118;
RA Shimojo M., Madara J., Pankow S., Liu X., Yates J. III, Suedhof T.C.,
RA Maximov A.;
RT "Synaptotagmin-11 mediates a vesicle trafficking pathway that is essential
RT for development and synaptic plasticity.";
RL Genes Dev. 33:365-376(2019).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-355 IN COMPLEX WITH ADP.
RX PubMed=11373668; DOI=10.1038/35078000;
RA Kikkawa M., Sablin E.P., Okada Y., Yajima H., Fletterick R.J., Hirokawa N.;
RT "Switch-based mechanism of kinesin motors.";
RL Nature 411:439-445(2001).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1-355 IN COMPLEX WITH TRANSITION
RP STATE ANALOGS.
RX PubMed=15286375; DOI=10.1126/science.1096621;
RA Nitta R., Kikkawa M., Okada Y., Hirokawa N.;
RT "KIF1A alternately uses two loops to bind microtubules.";
RL Science 305:678-683(2004).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 1-355 IN COMPLEX WITH ADP.
RX PubMed=18806800; DOI=10.1038/nsmb.1487;
RA Nitta R., Okada Y., Hirokawa N.;
RT "Structural model for strain-dependent microtubule activation of Mg-ADP
RT release from kinesin.";
RL Nat. Struct. Mol. Biol. 15:1067-1075(2008).
CC -!- FUNCTION: Motor for anterograde axonal transport of synaptic vesicle
CC precursors (Probable). Also required for neuronal dense core vesicles
CC (DCVs) transport to the dendritic spines and axons. The interaction
CC calcium-dependent with CALM1 increases vesicle motility and interaction
CC with the scaffolding proteins PPFIA2 and TANC2 recruits DCVs to
CC synaptic sites (By similarity). {ECO:0000250|UniProtKB:F1M4A4,
CC ECO:0000305}.
CC -!- SUBUNIT: Monomer. Interacts with PPFIA1 and PPFIA4 (By similarity).
CC Interacts with CALM1; the interaction is increased in presence of
CC calcium and increases neuronal dense core vesicles motility. Interacts
CC with PPFIA2 and TANC2; both interactions allow the recruitment of
CC neuronal dense core vesicles to dendritic spines and decrease in
CC presence of calcium (By similarity). Interacts with SYT4
CC (unphosphorylated) and SYT11; both interactions increase in presence of
CC calcium (By similarity) (PubMed:30808661). Interacts with MADD
CC (PubMed:18849981). {ECO:0000250|UniProtKB:F1M4A4,
CC ECO:0000269|PubMed:18849981, ECO:0000269|PubMed:30808661}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q12756}. Cell projection, axon
CC {ECO:0000269|PubMed:7539720}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:7539720}. Synapse. Cell projection, neuron
CC projection {ECO:0000250|UniProtKB:Q12756}. Cytoplasmic vesicle,
CC secretory vesicle, neuronal dense core vesicle membrane
CC {ECO:0000250|UniProtKB:F1M4A4}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:F1M4A4}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:F1M4A4}. Note=Within neuronal cells concentrated
CC in the axon, with smaller amounts in the perinuclear and synaptic
CC regions (PubMed:7539720). Expressed in distal regions of neurites.
CC {ECO:0000250|UniProtKB:Q12756, ECO:0000269|PubMed:7539720}.
CC -!- TISSUE SPECIFICITY: Expressed almost exclusively in neuronal tissues
CC such as brain and spinal cord (at protein level) (PubMed:7539720,
CC PubMed:18849981). Expressed at lower levels in the adrenal gland (at
CC protein level) (PubMed:7539720). {ECO:0000269|PubMed:18849981,
CC ECO:0000269|PubMed:7539720}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. Unc-104 subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00283}.
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DR EMBL; D29951; BAA06221.1; -; mRNA.
DR PIR; A56921; A56921.
DR PIR; E44259; E44259.
DR PDB; 1I5S; X-ray; 2.20 A; A=1-355.
DR PDB; 1I6I; X-ray; 2.00 A; A=1-355.
DR PDB; 1IA0; EM; 15.00 A; K=1-355.
DR PDB; 1VFV; X-ray; 1.85 A; A=1-355.
DR PDB; 1VFW; X-ray; 2.30 A; A=1-355.
DR PDB; 1VFX; X-ray; 2.55 A; A=1-355.
DR PDB; 1VFZ; X-ray; 2.24 A; A=1-355.
DR PDB; 2HXF; EM; 10.00 A; C=3-355.
DR PDB; 2HXH; EM; 11.00 A; C=3-355.
DR PDB; 2ZFI; X-ray; 1.55 A; A=1-355.
DR PDB; 2ZFJ; X-ray; 3.20 A; A=1-355.
DR PDB; 2ZFK; X-ray; 3.61 A; A=1-355.
DR PDB; 2ZFL; X-ray; 2.70 A; A=1-355.
DR PDB; 2ZFM; X-ray; 2.31 A; A=1-355.
DR PDB; 7EO9; X-ray; 2.57 A; A=1-382.
DR PDB; 7EOB; X-ray; 1.76 A; A=1-382.
DR PDBsum; 1I5S; -.
DR PDBsum; 1I6I; -.
DR PDBsum; 1IA0; -.
DR PDBsum; 1VFV; -.
DR PDBsum; 1VFW; -.
DR PDBsum; 1VFX; -.
DR PDBsum; 1VFZ; -.
DR PDBsum; 2HXF; -.
DR PDBsum; 2HXH; -.
DR PDBsum; 2ZFI; -.
DR PDBsum; 2ZFJ; -.
DR PDBsum; 2ZFK; -.
DR PDBsum; 2ZFL; -.
DR PDBsum; 2ZFM; -.
DR PDBsum; 7EO9; -.
DR PDBsum; 7EOB; -.
DR AlphaFoldDB; P33173; -.
DR SMR; P33173; -.
DR DIP; DIP-46956N; -.
DR IntAct; P33173; 2.
DR MINT; P33173; -.
DR STRING; 10090.ENSMUSP00000108582; -.
DR GlyConnect; 2450; 1 N-Linked glycan (1 site).
DR GlyGen; P33173; 1 site, 1 N-linked glycan (1 site).
DR iPTMnet; P33173; -.
DR PhosphoSitePlus; P33173; -.
DR SwissPalm; P33173; -.
DR jPOST; P33173; -.
DR MaxQB; P33173; -.
DR PaxDb; P33173; -.
DR PeptideAtlas; P33173; -.
DR PRIDE; P33173; -.
DR ProteomicsDB; 269301; -.
DR MGI; MGI:108391; Kif1a.
DR eggNOG; KOG0245; Eukaryota.
DR InParanoid; P33173; -.
DR PhylomeDB; P33173; -.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-MMU-983189; Kinesins.
DR ChiTaRS; Kif1a; mouse.
DR EvolutionaryTrace; P33173; -.
DR PRO; PR:P33173; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P33173; protein.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0098674; C:extrinsic component of neuronal dense core vesicle membrane; ISS:UniProtKB.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
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:0098992; C:neuronal dense core vesicle; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0098794; C:postsynapse; ISO:MGI.
DR GO; GO:0098793; C:presynapse; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
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: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:0008089; P:anterograde axonal transport; ISO:MGI.
DR GO; GO:1990048; P:anterograde neuronal dense core vesicle transport; ISO:MGI.
DR GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; IBA:GO_Central.
DR GO; GO:0099519; P:dense core granule cytoskeletal transport; ISS:UniProtKB.
DR GO; GO:0022027; P:interkinetic nuclear migration; ISO:MGI.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0098840; P:protein transport along microtubule; ISO:MGI.
DR GO; GO:0060998; P:regulation of dendritic spine development; ISS:UniProtKB.
DR GO; GO:0061001; P:regulation of dendritic spine morphogenesis; ISS:UniProtKB.
DR GO; GO:1990049; P:retrograde neuronal dense core vesicle transport; ISO:MGI.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR CDD; cd00060; FHA; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR022164; Kinesin-like.
DR InterPro; IPR027640; Kinesin-like_fam.
DR InterPro; IPR022140; Kinesin-like_KIF1-typ.
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; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR24115; PTHR24115; 2.
DR Pfam; PF12473; DUF3694; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF12423; KIF1B; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF16183; Kinesin_assoc; 1.
DR Pfam; PF00169; PH; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00240; FHA; 1.
DR SMART; SM00129; KISc; 1.
DR SMART; SM00233; PH; 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.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell projection; Coiled coil; Cytoplasm;
KW Cytoplasmic vesicle; Cytoskeleton; Membrane; Microtubule; Motor protein;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Synapse.
FT CHAIN 1..1695
FT /note="Kinesin-like protein KIF1A"
FT /id="PRO_0000125406"
FT DOMAIN 5..354
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT DOMAIN 516..572
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT DOMAIN 1580..1678
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 1410..1451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1524..1564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 366..383
FT /evidence="ECO:0000255"
FT COILED 429..462
FT /evidence="ECO:0000255"
FT COILED 622..681
FT /evidence="ECO:0000255"
FT COILED 801..822
FT /evidence="ECO:0000255"
FT COMPBIAS 1414..1441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 97..104
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MOD_RES 416
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12756"
FT MOD_RES 418
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12756"
FT MOD_RES 419
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12756"
FT MOD_RES 607
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 612
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 932
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 937
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12756"
FT MOD_RES 1315
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12756"
FT MOD_RES 1342
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1524
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1528
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1533
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1537
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1553
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12756"
FT STRAND 6..12
FT /evidence="ECO:0007829|PDB:2ZFI"
FT HELIX 17..21
FT /evidence="ECO:0007829|PDB:2ZFI"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:2ZFI"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:2ZFI"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:7EOB"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:2ZFI"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:2ZFI"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:2ZFI"
FT HELIX 70..76
FT /evidence="ECO:0007829|PDB:2ZFI"
FT HELIX 78..86
FT /evidence="ECO:0007829|PDB:2ZFI"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:2ZFI"
FT HELIX 103..107
FT /evidence="ECO:0007829|PDB:2ZFI"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:2ZFI"
FT HELIX 118..131
FT /evidence="ECO:0007829|PDB:2ZFI"
FT STRAND 138..150
FT /evidence="ECO:0007829|PDB:2ZFI"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:2ZFI"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:2ZFI"
FT STRAND 168..171
FT /evidence="ECO:0007829|PDB:2ZFI"
FT TURN 172..174
FT /evidence="ECO:0007829|PDB:2ZFI"
FT STRAND 175..178
FT /evidence="ECO:0007829|PDB:2ZFI"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:1I5S"
FT HELIX 189..203
FT /evidence="ECO:0007829|PDB:2ZFI"
FT HELIX 206..209
FT /evidence="ECO:0007829|PDB:2ZFI"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:2ZFI"
FT HELIX 213..216
FT /evidence="ECO:0007829|PDB:2ZFI"
FT STRAND 217..230
FT /evidence="ECO:0007829|PDB:2ZFI"
FT TURN 232..235
FT /evidence="ECO:0007829|PDB:2ZFI"
FT STRAND 237..248
FT /evidence="ECO:0007829|PDB:2ZFI"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:2ZFI"
FT HELIX 265..288
FT /evidence="ECO:0007829|PDB:2ZFI"
FT HELIX 306..308
FT /evidence="ECO:0007829|PDB:2ZFI"
FT HELIX 310..314
FT /evidence="ECO:0007829|PDB:2ZFI"
FT HELIX 316..318
FT /evidence="ECO:0007829|PDB:2ZFI"
FT STRAND 320..322
FT /evidence="ECO:0007829|PDB:1I5S"
FT STRAND 324..331
FT /evidence="ECO:0007829|PDB:2ZFI"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:2ZFI"
FT HELIX 338..350
FT /evidence="ECO:0007829|PDB:2ZFI"
FT HELIX 365..380
FT /evidence="ECO:0007829|PDB:7EOB"
SQ SEQUENCE 1695 AA; 191725 MW; D6EC3B88CBC9CCC6 CRC64;
MAGASVKVAV RVRPFNSREM SRDSKCIIQM SGSTTTIVNP KQPKETPKSF SFDYSYWSHT
SPEDINYASQ KQVYRDIGEE MLQHAFEGYN VCIFAYGQTG AGKSYTMMGK QEKDQQGIIP
QLCEDLFSRI NDTTNDNMSY SVEVSYMEIY CERVRDLLNP KNKGNLRVRE HPLLGPYVED
LSKLAVTSYN DIQDLMDSGN KPRTVAATNM NETSSRSHAV FNIIFTQKRH DAETNITTEK
VSKISLVDLA GSERADSTGA KGTRLKEGAN INKSLTTLGK VISALAEMDS GPNKNKKKKK
TDFIPYRDSV LTWLLRENLG GNSRTAMVAA LSPADINYDE TLSTLRYADR AKQIRCNAII
NEDPNNKLIR ELKDEVTRLR DLLYAQGLGD ITDMTNALVG MSPSSSLSAL SSRAASVSSL
HERILFAPGS EEAIERLKET EKIIAELNET WEEKLRRTEA IRMEREALLA EMGVAMREDG
GTLGVFSPKK TPHLVNLNED PLMSECLLYY IKDGVTRVGR EDAERRQDIV LSGHFIKEEH
CIFRSDSRGG GEAVVTLEPC EGADTYVNGK KVTEPSILRS GNRIIMGKSH VFRFNHPEQA
RQERERTPCA ETPAEPVDWA FAQRELLEKQ GIDMKQEMEQ RLQELEDQYR REREEATYLL
EQQRLDYESK LEALQKQMDS RYYPEVNEEE EEPEDEVQWT ERECELALWA FRKWKWYQFT
SLRDLLWGNA IFLKEANAIS VELKKKVQFQ FVLLTDTLYS PLPPDLLPPE AAKDRETRPF
PRTIVAVEVQ DQKNGATHYW TLEKLRQRLD LMREMYDRAA EVPSSVVEDC DNVVTGGDPF
YDRFPWFRLV GRAFVYLSNL LYPVPLVHRV AIVSEKGEVK GFLRVAVQAI SADEEAPDYG
SGVRQSGTAK ISFDDQHFEK FQSESCPVVG MSRSGTSQEE LRIVEGQGQG ADAGPSADEV
NNNTCSAVPP EGLMDSPEKA ALDGPLDTAL DHLRLGSTFT FRVTVLQASS ISAEYADIFC
QFNFIHRHDE AFSTEPLKNT GRGPPLGFYH VQNIAVEVTK SFIEYIKSQP IVFEVFGHYQ
QHPFPPLCKD VLSPLRPSRR HFPRVMPLSK PVPATKLSTM TRPSPGPCHC KYDLLVYFEI
CELEANGDYI PAVVDHRGAC MGTFLLHQGI QRRITVTLLH ETGSHIRWKE VRELVVGRIR
NTPETDEALI DPNILSLNIL SSGYVHPAQD DRVFFGNDTR TFYQFEAAWD SSMHNSLLLN
RVTPYREKIY MTLSAYIEME NCTQPAVITK DFCMVFYSRD AKLPASRSIR NLFGSGSLRA
TEGNRVTGVY ELSLCHVADA GSPGMQRRRR RVLDTSVAYV RGEENLAGWR PRSDSLILDH
QWELEKLSLL QEVEKTRHYL LLREKLETTQ RPGPEVLSPA SSEDSESRSS SGASSPLSAE
GQPSPLEAPN ERQRELAVKC LRLLMHTFNR EYTHSHVCIS ASESKLSEMS VTLMRDPSMS
PLGAATLTPS STCPSLIEGR YGATDVRTPQ PCSRPASPEP ELLPELDSKK TPSPVRATET
EKEPQRLLVP DIQEIRVSPI VSKKGYLHFL EPHTAGWAKR FVVVRRPYAY MYNSDKDTVE
RFVLNLSTAQ VEYSEDQQAM LKTPNTFAVC TEHRGILLQA NSDKDMHDWL YAFNPLLAGT
IRSKLSRRRS AQMRV
