NSF_MOUSE
ID NSF_MOUSE Reviewed; 744 AA.
AC P46460; A2A646; Q8BQ65; Q8C3R2; Q8CCT9; Q8CEF0; Q923C6;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Vesicle-fusing ATPase;
DE EC=3.6.4.6;
DE AltName: Full=N-ethylmaleimide-sensitive fusion protein;
DE Short=NEM-sensitive fusion protein;
DE AltName: Full=Suppressor of K(+) transport growth defect 2;
DE Short=Protein SKD2;
DE AltName: Full=Vesicular-fusion protein NSF;
GN Name=Nsf; Synonyms=Skd2;
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 STRAIN=BALB/cJ;
RX PubMed=8082782; DOI=10.1016/0014-5793(94)00879-5;
RA Perier F., Coulter K.L., Liang H., Radeke C.M., Gaber R.F.,
RA Vandenberg C.A.;
RT "Identification of a novel mammalian member of the NSF/CDC48p/Pas1p/TBP-1
RT family through heterologous expression in yeast.";
RL FEBS Lett. 351:286-290(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Head, Lung, Medulla oblongata, Spinal ganglion, and Thymus;
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 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Eye, and Mammary tumor;
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 PROTEIN SEQUENCE OF 45-50; 69-87; 106-116; 151-161; 170-198; 218-232;
RP 255-266; 294-303; 305-314; 316-335; 338-357; 404-413; 416-427; 435-446;
RP 517-529; 534-559; 573-581; 595-631; 640-648 AND 710-725, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Kang S.U., Klug S., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [6]
RP FUNCTION, INTERACTION WITH CDK16, SUBUNIT, MUTAGENESIS OF SER-569, AND
RP PHOSPHORYLATION AT SER-569.
RX PubMed=16461345; DOI=10.1074/jbc.m513496200;
RA Liu Y., Cheng K., Gong K., Fu A.K., Ip N.Y.;
RT "Pctaire1 phosphorylates N-ethylmaleimide-sensitive fusion protein:
RT implications in the regulation of its hexamerization and exocytosis.";
RL J. Biol. Chem. 281:9852-9858(2006).
RN [7]
RP INTERACTION WITH MUSK.
RX PubMed=18272689; DOI=10.1523/jneurosci.4130-07.2008;
RA Zhu D., Yang Z., Luo Z., Luo S., Xiong W.C., Mei L.;
RT "Muscle-specific receptor tyrosine kinase endocytosis in acetylcholine
RT receptor clustering in response to agrin.";
RL J. Neurosci. 28:1688-1696(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-259, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, 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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-105, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Required for vesicle-mediated transport. Catalyzes the fusion
CC of transport vesicles within the Golgi cisternae. Is also required for
CC transport from the endoplasmic reticulum to the Golgi stack. Seems to
CC function as a fusion protein required for the delivery of cargo
CC proteins to all compartments of the Golgi stack GRIA2 leads to
CC influence GRIA2 membrane cycling (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:16461345}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.6;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P18708};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P18708};
CC -!- SUBUNIT: Homohexamer. Interacts with GABARAP and GABARAPL2. Interacts
CC with GRIA2. Interacts with PLK2, leading to disrupt the interaction
CC with GRIA2. Interacts with MUSK; may regulate MUSK endocytosis and
CC activity (By similarity). Interacts with CDK16. {ECO:0000250,
CC ECO:0000269|PubMed:16461345, ECO:0000269|PubMed:18272689}.
CC -!- INTERACTION:
CC P46460; Q62108: Dlg4; NbExp=5; IntAct=EBI-398006, EBI-300895;
CC P46460; Q5S006: Lrrk2; NbExp=3; IntAct=EBI-398006, EBI-2693710;
CC P46460; Q61006-3: Musk; NbExp=5; IntAct=EBI-398006, EBI-6308424;
CC P46460; O35239: Ptpn9; NbExp=2; IntAct=EBI-398006, EBI-7297868;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- PTM: Phosphorylation at Ser-569 interferes with homohexamerization.
CC {ECO:0000269|PubMed:16461345}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAM20943.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAM23742.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U10120; AAA50498.1; -; mRNA.
DR EMBL; AK028415; BAC25937.1; -; mRNA.
DR EMBL; AK032120; BAC27713.1; -; mRNA.
DR EMBL; AK049281; BAC33656.1; -; mRNA.
DR EMBL; AK051430; BAC34637.1; -; mRNA.
DR EMBL; AK085086; BAC39361.1; -; mRNA.
DR EMBL; AK153905; BAE32247.1; -; mRNA.
DR EMBL; AL596108; CAM20943.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL603829; CAM20943.1; JOINED; Genomic_DNA.
DR EMBL; AL596108; CAM20945.1; -; Genomic_DNA.
DR EMBL; AL603829; CAM20945.1; JOINED; Genomic_DNA.
DR EMBL; AL603829; CAM23742.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL596108; CAM23742.1; JOINED; Genomic_DNA.
DR EMBL; AL603829; CAM23743.1; -; Genomic_DNA.
DR EMBL; AL596108; CAM23743.1; JOINED; Genomic_DNA.
DR EMBL; BC006627; AAH06627.1; -; mRNA.
DR EMBL; BC019167; AAH19167.1; -; mRNA.
DR CCDS; CCDS25524.1; -.
DR RefSeq; NP_032766.2; NM_008740.4.
DR AlphaFoldDB; P46460; -.
DR SMR; P46460; -.
DR BioGRID; 201857; 45.
DR IntAct; P46460; 25.
DR MINT; P46460; -.
DR STRING; 10090.ENSMUSP00000099364; -.
DR iPTMnet; P46460; -.
DR PhosphoSitePlus; P46460; -.
DR SwissPalm; P46460; -.
DR REPRODUCTION-2DPAGE; P46460; -.
DR EPD; P46460; -.
DR jPOST; P46460; -.
DR MaxQB; P46460; -.
DR PaxDb; P46460; -.
DR PeptideAtlas; P46460; -.
DR PRIDE; P46460; -.
DR ProteomicsDB; 295530; -.
DR Antibodypedia; 1006; 289 antibodies from 37 providers.
DR DNASU; 18195; -.
DR Ensembl; ENSMUST00000103075; ENSMUSP00000099364; ENSMUSG00000034187.
DR GeneID; 18195; -.
DR KEGG; mmu:18195; -.
DR UCSC; uc007lvt.1; mouse.
DR CTD; 4905; -.
DR MGI; MGI:104560; Nsf.
DR VEuPathDB; HostDB:ENSMUSG00000034187; -.
DR eggNOG; KOG0741; Eukaryota.
DR GeneTree; ENSGT00530000064085; -.
DR HOGENOM; CLU_008037_2_0_1; -.
DR InParanoid; P46460; -.
DR OMA; IQHVKGM; -.
DR OrthoDB; 197562at2759; -.
DR PhylomeDB; P46460; -.
DR TreeFam; TF300371; -.
DR Reactome; R-MMU-204005; COPII-mediated vesicle transport.
DR Reactome; R-MMU-416993; Trafficking of GluR2-containing AMPA receptors.
DR Reactome; R-MMU-6807878; COPI-mediated anterograde transport.
DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-MMU-6811438; Intra-Golgi traffic.
DR Reactome; R-MMU-6811440; Retrograde transport at the Trans-Golgi-Network.
DR BioGRID-ORCS; 18195; 29 hits in 78 CRISPR screens.
DR ChiTaRS; Nsf; mouse.
DR PRO; PR:P46460; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P46460; protein.
DR Bgee; ENSMUSG00000034187; Expressed in dentate gyrus of hippocampal formation granule cell and 258 other tissues.
DR ExpressionAtlas; P46460; baseline and differential.
DR Genevisible; P46460; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043198; C:dendritic shaft; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005795; C:Golgi stack; ISO:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IMP:MGI.
DR GO; GO:0043008; F:ATP-dependent protein binding; ISO:MGI.
DR GO; GO:0140545; F:ATP-dependent protein disaggregase activity; ISS:ParkinsonsUK-UCL.
DR GO; GO:0031748; F:D1 dopamine receptor binding; ISO:MGI.
DR GO; GO:0035255; F:ionotropic glutamate receptor binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0044877; F:protein-containing complex binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0000149; F:SNARE binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0019905; F:syntaxin binding; IDA:MGI.
DR GO; GO:0017075; F:syntaxin-1 binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IBA:GO_Central.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; ISO:MGI.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; ISO:MGI.
DR GO; GO:0001921; P:positive regulation of receptor recycling; ISO:MGI.
DR GO; GO:0006813; P:potassium ion transport; IDA:MGI.
DR GO; GO:0015031; P:protein transport; ISO:MGI.
DR GO; GO:0032984; P:protein-containing complex disassembly; ISO:MGI.
DR GO; GO:0017157; P:regulation of exocytosis; ISO:MGI.
DR GO; GO:0002090; P:regulation of receptor internalization; ISO:MGI.
DR GO; GO:0035494; P:SNARE complex disassembly; ISS:ParkinsonsUK-UCL.
DR GO; GO:0016192; P:vesicle-mediated transport; ISO:MGI.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR004201; Cdc48_dom2.
DR InterPro; IPR029067; CDC48_domain_2-like_sf.
DR InterPro; IPR003338; CDC4_N-term_subdom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039812; Vesicle-fus_ATPase.
DR PANTHER; PTHR23078; PTHR23078; 1.
DR Pfam; PF00004; AAA; 2.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF02933; CDC48_2; 1.
DR Pfam; PF02359; CDC48_N; 1.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01072; CDC48_2; 1.
DR SMART; SM01073; CDC48_N; 1.
DR SUPFAM; SSF50692; SSF50692; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF54585; SSF54585; 1.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cytoplasm; Direct protein sequencing; Hydrolase;
KW Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Transport.
FT CHAIN 1..744
FT /note="Vesicle-fusing ATPase"
FT /id="PRO_0000084564"
FT BINDING 505..510
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P18708"
FT BINDING 545..552
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P18708"
FT BINDING 550
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P18708"
FT MOD_RES 105
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 259
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 569
FT /note="Phosphoserine; by CDK16"
FT /evidence="ECO:0000269|PubMed:16461345"
FT MUTAGEN 569
FT /note="S->A: Abolishes phosphorylation by CDK16."
FT /evidence="ECO:0000269|PubMed:16461345"
FT MUTAGEN 569
FT /note="S->E: Interferes with oligomerization."
FT /evidence="ECO:0000269|PubMed:16461345"
FT CONFLICT 300
FT /note="A -> G (in Ref. 2; BAC39361)"
FT /evidence="ECO:0000305"
FT CONFLICT 316..326
FT /note="LGANSGLHIII -> VCGHKTNLLKM (in Ref. 2; BAC34637)"
FT /evidence="ECO:0000305"
FT CONFLICT 492
FT /note="F -> I (in Ref. 1; AAA50498)"
FT /evidence="ECO:0000305"
FT CONFLICT 552
FT /note="L -> V (in Ref. 1; AAA50498)"
FT /evidence="ECO:0000305"
FT CONFLICT 657
FT /note="M -> I (in Ref. 2; BAC25937)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 744 AA; 82613 MW; BE55AD0056AD5585 CRC64;
MAGRTMQAAR CPTDELSLSN CAVVNEKDFQ SGQHVMVRTS PNHKYIFTLR THPSVVPGCI
AFSLPQRKWA GLSIGQDIEV ALYSFDKAKQ CIGTMTIEID FLQKKNIDSN PYDTDKMAAE
FIQQFNNQAF SVGQQLVFSF NDKLFGLLVK DIEAMDPSIL KGEPASGKRQ KIEVGLVVGN
SQVAFEKAEN SSLNLIGKAK TKENRQSIIN PDWNFEKMGI GGLDKEFSDI FRRAFASRVF
PPEIVEQMGC KHVKGILLYG PPGCGKTLLA RQIGKMLNAR EPKVVNGPEI LNKYVGESEA
NIRKLFADAE EEQRRLGANS GLHIIIFDEI DAICKQRGSM AGSTGVHDTV VNQLLSKIDG
VEQLNNILVI GMTNRPDLID EALLRPGRLE VKMEIGLPDE KGRLQILHIH TARMRGHQLL
SADVDIKELA VETKNFSGAE LEGLVRAAQS TAMNRHIKAS TKVEVDMEKA ESLQVTRGDF
LASLENDIKP AFGTNQEDYA SYIMNGIIKW GDPVTRVLDD GELLVQQTKN SDRTPLVSVL
LEGPPHSGKT ALAAKIAEES NFPFIKICSP DKMIGFSETA KCQAMKKIFD DAYKSQLSCV
VVDDIERLLD YVPIGPRFSN LVLQALLVLL KKAPPQGRKL LIIGTTSRKD VLQEMEMLNA
FSTTIHVPNI ATGEQLLEAL ELLGNFKDKE RTTIAQQVKG KKVWIGIKKL LMLIEMSLQM
DPEYRVRKFL ALMREEGASP LDFD
