ID   KIF3A_MOUSE             Reviewed;         701 AA.
AC   P28741; Q7TSZ7;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   02-SEP-2026, entry version 199.
DE   RecName: Full=Kinesin-like protein KIF3A;
DE            EC=3.6.4.- {ECO:0000250|UniProtKB:P56536};
DE   AltName: Full=Microtubule plus end-directed kinesin motor 3A;
GN   Name=Kif3a {ECO:0000303|PubMed:23386061}; Synonyms=Kif3;
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=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   [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   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   [4]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=7559760; DOI=10.1083/jcb.130.6.1387;
RA   Yamazaki H., Nakata T., Okada Y., Hirokawa N.;
RT   "KIF3A/B: a heterodimeric kinesin superfamily protein that works as a
RT   microtubule plus end-directed motor for membrane organelle transport.";
RL   J. Cell Biol. 130:1387-1399(1995).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-689, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [6]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=18497258; DOI=10.1126/science.1157983;
RA   Kovacs J.J., Whalen E.J., Liu R., Xiao K., Kim J., Chen M., Wang J.,
RA   Chen W., Lefkowitz R.J.;
RT   "Beta-arrestin-mediated localization of smoothened to the primary cilium.";
RL   Science 320:1777-1781(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-689, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Pancreas, and
RC   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   [8]
RP   INTERACTION WITH CIMAP3.
RX   PubMed=20643351; DOI=10.1016/j.devcel.2010.06.005;
RA   Kinzel D., Boldt K., Davis E.E., Burtscher I., Trumbach D., Diplas B.,
RA   Attie-Bitach T., Wurst W., Katsanis N., Ueffing M., Lickert H.;
RT   "Pitchfork regulates primary cilia disassembly and left-right asymmetry.";
RL   Dev. Cell 19:66-77(2010).
RN   [9]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=21670265; DOI=10.1073/pnas.1016214108;
RA   Choi Y.H., Suzuki A., Hajarnis S., Ma Z., Chapin H.C., Caplan M.J.,
RA   Pontoglio M., Somlo S., Igarashi P.;
RT   "Polycystin-2 and phosphodiesterase 4C are components of a ciliary A-kinase
RT   anchoring protein complex that is disrupted in cystic kidney diseases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:10679-10684(2011).
RN   [10]
RP   FUNCTION, INTERACTION WITH DCTN1, AND SUBCELLULAR LOCATION.
RX   PubMed=23386061; DOI=10.1038/emboj.2013.3;
RA   Kodani A., Salome Sirerol-Piquer M., Seol A., Garcia-Verdugo J.M.,
RA   Reiter J.F.;
RT   "Kif3a interacts with Dynactin subunit p150 Glued to organize centriole
RT   subdistal appendages.";
RL   EMBO J. 32:597-607(2013).
RN   [11]
RP   FUNCTION.
RX   PubMed=39138140; DOI=10.1371/journal.pbio.3002685;
RA   Walker M.F., Zhang J., Steiner W., Ku P.I., Zhu J.F., Michaelson Z.,
RA   Yen Y.C., Lee A., Long A.B., Casey M.J., Poddar A., Nelson I.B.,
RA   Arveseth C.D., Nagel F., Clough R., LaPotin S., Kwan K.M., Schulz S.,
RA   Stewart R.A., Tesmer J.J.G., Caspary T., Subramanian R., Ge X., Myers B.R.;
RT   "GRK2 kinases in the primary cilium initiate SMOOTHENED-PKA signaling in
RT   the Hedgehog cascade.";
RL   PLoS Biol. 22:e3002685-e3002685(2024).
CC   -!- FUNCTION: Microtubule-based anterograde translocator for membranous
CC       organelles, such as primary cilium and centriole (PubMed:18497258,
CC       PubMed:21670265, PubMed:23386061, PubMed:7559760). Shows a plus end-
CC       directed microtubule sliding activity in vitro (PubMed:7559760). Plays
CC       a role in primary cilia formation, probably by mediating transport of
CC       proteins into primary cilia (PubMed:18497258, PubMed:21670265,
CC       PubMed:39138140). Mediates smoothened (SMO) translocation into primary
CC       cilia in response to hedgehog morphogens (PubMed:18497258,
CC       PubMed:39138140). Plays a role in centriole cohesion and subdistal
CC       appendage organization and function (PubMed:23386061). Regulates the
CC       formation of the subdistal appendage via recruitment of DCTN1 to the
CC       centriole (PubMed:23386061). Also required for ciliary basal feet
CC       formation and microtubule anchoring to mother centriole
CC       (PubMed:23386061). {ECO:0000269|PubMed:18497258,
CC       ECO:0000269|PubMed:21670265, ECO:0000269|PubMed:23386061,
CC       ECO:0000269|PubMed:39138140, ECO:0000269|PubMed:7559760}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + phosphate + H(+); Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000250|UniProtKB:P56536};
CC   -!- SUBUNIT: Heterodimer of KIF3A and KIF3B (PubMed:7559760). Interacts
CC       with CIMAP3 (PubMed:20643351). Interacts with CLN3 (By similarity).
CC       Interacts with DCTN1 (PubMed:23386061). Interacts with FLCN (By
CC       similarity). Interacts with AP3B1 (By similarity).
CC       {ECO:0000250|UniProtKB:Q9Y496, ECO:0000269|PubMed:20643351,
CC       ECO:0000269|PubMed:23386061, ECO:0000269|PubMed:7559760}.
CC   -!- INTERACTION:
CC       P28741; Q6A078: Cep290; NbExp=3; IntAct=EBI-6169413, EBI-1811999;
CC       P28741; O08788: Dctn1; NbExp=4; IntAct=EBI-6169413, EBI-776180;
CC       P28741; Q61771: Kif3b; NbExp=6; IntAct=EBI-6169413, EBI-6395332;
CC       P28741; P70188: Kifap3; NbExp=4; IntAct=EBI-6169413, EBI-6169443;
CC       P28741; Q8VI40: Trim60; NbExp=5; IntAct=EBI-6169413, EBI-6395249;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000305|PubMed:21670265}. Cell projection, cilium
CC       {ECO:0000269|PubMed:18497258, ECO:0000269|PubMed:21670265}. Cytoplasm,
CC       cytoskeleton, microtubule organizing center, centrosome, centriole
CC       {ECO:0000269|PubMed:23386061}. Note=Localizes to the subdistal
CC       appendage region of the centriole. {ECO:0000269|PubMed:23386061}.
CC   -!- TISSUE SPECIFICITY: Expressed almost exclusively in adult brain tissue
CC       (mainly in the cerebellar granular layer) within a single type of
CC       neuronal cell.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. Kinesin II subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00283}.
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DR   EMBL; D12645; BAA02166.1; -; mRNA.
DR   EMBL; AL596095; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC052707; AAH52707.1; -; mRNA.
DR   CCDS; CCDS48795.1; -.
DR   PIR; B44259; B44259.
DR   RefSeq; NP_001277734.1; NM_001290805.1.
DR   RefSeq; NP_001277735.1; NM_001290806.1.
DR   RefSeq; NP_032469.2; NM_008443.4.
DR   PDB; 5JVR; X-ray; 2.10 A; A/B/C/D/E/F/G/H=352-359.
DR   PDB; 5JX1; X-ray; 1.67 A; A=352-376.
DR   PDB; 9W9H; EM; 2.83 A; A=481-701.
DR   PDB; 9W9I; EM; 2.90 A; A=536-701.
DR   AlphaFoldDB; P28741; -.
DR   EMDB; EMD-65777; -.
DR   EMDB; EMD-65778; -.
DR   MDRepo; P28741; -.
DR   SASBDB; P28741; -.
DR   SMR; P28741; -.
DR   BioGRID; 200941; 13.
DR   ComplexPortal; CPX-3202; KIF3 complex variant AC.
DR   ComplexPortal; CPX-3203; KIF3 complex variant AB.
DR   ComplexPortal; CPX-3204; KIF3 complex variant AB-KAP3.
DR   ComplexPortal; CPX-3205; KIF3 complex variant AC-KAP3.
DR   CORUM; P28741; -.
DR   DIP; DIP-46318N; -.
DR   FunCoup; P28741; 1513.
DR   IntAct; P28741; 17.
DR   MINT; P28741; -.
DR   STRING; 10090.ENSMUSP00000112782; -.
DR   MoonProt; P28741; -.
DR   GlyGen; P28741; 2 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site).
DR   iPTMnet; P28741; -.
DR   PhosphoSitePlus; P28741; -.
DR   jPOST; P28741; -.
DR   PaxDb; 10090-ENSMUSP00000112782; -.
DR   ProteomicsDB; 263605; -.
DR   Pumba; P28741; -.
DR   Antibodypedia; 14507; 234 antibodies from 35 providers.
DR   DNASU; 16568; -.
DR   Ensembl; ENSMUST00000120613.9; ENSMUSP00000112782.3; ENSMUSG00000018395.20.
DR   GeneID; 16568; -.
DR   KEGG; mmu:16568; -.
DR   UCSC; uc007iwl.2; mouse.
DR   AGR; MGI:107689; -.
DR   CTD; 11127; -.
DR   MGI; MGI:107689; Kif3a.
DR   VEuPathDB; HostDB:ENSMUSG00000018395; -.
DR   eggNOG; KOG4280; Eukaryota.
DR   GeneTree; ENSGT00940000156386; -.
DR   InParanoid; P28741; -.
DR   OMA; NMRKHIE; -.
DR   OrthoDB; 3176171at2759; -.
DR   BRENDA; 5.6.1.3; 3474.
DR   Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR   Reactome; R-MMU-5610787; Hedgehog 'off' state.
DR   Reactome; R-MMU-5620924; Intraflagellar transport.
DR   Reactome; R-MMU-5635838; Activation of SMO.
DR   Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR   Reactome; R-MMU-983189; Kinesins.
DR   BioGRID-ORCS; 16568; 6 hits in 79 CRISPR screens.
DR   CD-CODE; CE726F99; Postsynaptic density.
DR   PRO; PR:P28741; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; P28741; protein.
DR   Bgee; ENSMUSG00000018395; Expressed in ventromedial nucleus of hypothalamus and 234 other cell types or tissues.
DR   ExpressionAtlas; P28741; baseline and differential.
DR   GO; GO:1904115; C:axon cytoplasm; ISO:GO_Central.
DR   GO; GO:0005930; C:axoneme; ISO:GO_Central.
DR   GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR   GO; GO:0005813; C:centrosome; ISO:GO_Central.
DR   GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0032839; C:dendrite cytoplasm; IEA:GOC.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR   GO; GO:0016939; C:kinesin II complex; IDA:MGI.
DR   GO; GO:0015630; C:microtubule cytoskeleton; ISO:GO_Central.
DR   GO; GO:0031514; C:motile cilium; IDA:MGI.
DR   GO; GO:0043005; C:neuron projection; IDA:MGI.
DR   GO; GO:0043025; C:neuronal cell body; ISO:GO_Central.
DR   GO; GO:0097730; C:non-motile cilium; IDA:UniProtKB.
DR   GO; GO:0032391; C:photoreceptor connecting cilium; IDA:UniProtKB.
DR   GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR   GO; GO:0097470; C:ribbon synapse; ISO:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0120170; F:intraciliary transport particle B binding; IDA:MGI.
DR   GO; GO:0019894; F:kinesin binding; ISO:GO_Central.
DR   GO; GO:0008017; F:microtubule binding; IDA:MGI.
DR   GO; GO:0003777; F:microtubule motor activity; IDA:UniProtKB.
DR   GO; GO:0019903; F:protein phosphatase binding; ISO:GO_Central.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:GO_Central.
DR   GO; GO:0031267; F:small GTPase binding; ISO:GO_Central.
DR   GO; GO:0030507; F:spectrin binding; ISO:MGI.
DR   GO; GO:0071929; P:alpha-tubulin acetylation; IMP:MGI.
DR   GO; GO:0009952; P:anterior/posterior pattern specification; IMP:MGI.
DR   GO; GO:0008089; P:anterograde axonal transport; IBA:GO_Central.
DR   GO; GO:0098937; P:anterograde dendritic transport; IDA:SynGO.
DR   GO; GO:0098971; P:anterograde dendritic transport of neurotransmitter receptor complex; IDA:SynGO.
DR   GO; GO:0010457; P:centriole-centriole cohesion; IMP:UniProtKB.
DR   GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR   GO; GO:0003341; P:cilium movement; IMP:MGI.
DR   GO; GO:0021542; P:dentate gyrus development; IMP:MGI.
DR   GO; GO:0007368; P:determination of left/right symmetry; IMP:MGI.
DR   GO; GO:0021904; P:dorsal/ventral neural tube patterning; IMP:BHF-UCL.
DR   GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:MGI.
DR   GO; GO:0036334; P:epidermal stem cell homeostasis; IMP:MGI.
DR   GO; GO:0008544; P:epidermis development; IMP:MGI.
DR   GO; GO:0030900; P:forebrain development; IMP:MGI.
DR   GO; GO:0007507; P:heart development; IMP:MGI.
DR   GO; GO:0001947; P:heart looping; IMP:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IGI:MGI.
DR   GO; GO:0060122; P:inner ear receptor cell stereocilium organization; IMP:MGI.
DR   GO; GO:0001822; P:kidney development; IMP:MGI.
DR   GO; GO:0034454; P:microtubule anchoring at centrosome; IMP:UniProtKB.
DR   GO; GO:0044458; P:motile cilium assembly; IMP:MGI.
DR   GO; GO:0061351; P:neural precursor cell proliferation; IMP:MGI.
DR   GO; GO:0021915; P:neural tube development; IMP:MGI.
DR   GO; GO:1905515; P:non-motile cilium assembly; IMP:MGI.
DR   GO; GO:1905128; P:positive regulation of axo-dendritic protein transport; ISO:GO_Central.
DR   GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IMP:MGI.
DR   GO; GO:2000771; P:positive regulation of establishment or maintenance of cell polarity regulating cell shape; ISO:GO_Central.
DR   GO; GO:0090316; P:positive regulation of intracellular protein transport; ISO:GO_Central.
DR   GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; ISO:GO_Central.
DR   GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IDA:UniProtKB.
DR   GO; GO:1902414; P:protein localization to cell junction; ISO:GO_Central.
DR   GO; GO:0097499; P:protein localization to non-motile cilium; IDA:UniProtKB.
DR   GO; GO:0015031; P:protein transport; ISO:GO_Central.
DR   GO; GO:0007224; P:smoothened signaling pathway; IMP:MGI.
DR   CDD; cd01371; KISc_KIF3; 1.
DR   FunFam; 3.40.850.10:FF:000028; Kinesin-like protein; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 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; PTHR47969; CHROMOSOME-ASSOCIATED KINESIN KIF4A-RELATED; 1.
DR   PANTHER; PTHR47969:SF21; KINESIN-LIKE PROTEIN; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR   PDBsum; 5JVR; -.
DR   PDBsum; 5JX1; -.
DR   PDBsum; 9W9H; -.
DR   PDBsum; 9W9I; -.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cell projection; Cilium;
KW   Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Hydrolase; Microtubule; Motor protein; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..701
FT                   /note="Kinesin-like protein KIF3A"
FT                   /id="PRO_0000125394"
FT   DOMAIN          14..345
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   REGION          365..701
FT                   /note="Interaction with DCTN1"
FT                   /evidence="ECO:0000269|PubMed:23386061"
FT   REGION          373..423
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          599..701
FT                   /note="Globular"
FT   REGION          665..701
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          355..592
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        376..399
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        409..423
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        674..689
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         100..107
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   MOD_RES         689
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:15345747,
FT                   ECO:0007744|PubMed:21183079"
FT   CONFLICT        404
FT                   /note="K -> R (in Ref. 1; BAA02166)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        683
FT                   /note="M -> T (in Ref. 1; BAA02166)"
FT                   /evidence="ECO:0000305"
FT   HELIX           355..376
FT                   /evidence="ECO:0007829|PDB:5JX1"
SQ   SEQUENCE   701 AA;  80170 MW;  15EB43A6F6CC08A3 CRC64;
     MPINKSEKPE SCDNVKVVVR CRPLNEREKS MCYRQAVSVD EMRGTITVHK TDSSNEPPKT
     FTFDTVFGPE SKQLDVYNLT ARPIIDSVLE GYNGTIFAYG QTGTGKTFTM EGVRAVPGLR
     GVIPNSFAHI FGHIAKAEGD TRFLVRVSYL EIYNEEVRDL LGKDQTQRLE VKERPDVGVY
     IKDLSAYVVN NADDMDRIMT LGHKNRSVGA TNMNEHSSRS HAIFTITIEC SEKGVDGNMH
     VRMGKLHLVD LAGSERQAKT GATGQRLKEA TKINLSLSTL GNVISALVDG KSTHVPYRNS
     KLTRLLQDSL GGNSKTMMCA NIGPADYNYD ETISTLRYAN RAKNIKNKAR INEDPKDALL
     RQFQKEIEEL KKKLEEGEEV SGSDISGSEE DDEEGELGED GEKKKKRRDQ AGKKKVSPDK
     MVEMQAKIDE ERKALETKLD MEEEERNKAR AELERREKDL LKAQQEHQSL LEKLSALEKK
     VIVGGVDLLA KAEEQEKLLE ESNMELEERR RRAEQLRKEL EEKEQERLDI EEKYTSLQEE
     AQGKTKKLKK VWTMLMAAKS EMADLQQEHQ REIEGLLENI RQLSRELRLQ MLIIDNFIPQ
     DYQEMIENYV HWNEDIGEWQ LKCVAYTGNN MRKQTPVPDK KERDPFEVDL SHVYLAYTEE
     SLRQSLMKLE RPRTSKGKAR PKMGRRKRSA KPETVIDSLL Q
//