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   24-JAN-2024, entry version 200.
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,
RC   Pancreas, 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; 48.
DR   IntAct; P46460; 25.
DR   MINT; P46460; -.
DR   STRING; 10090.ENSMUSP00000099364; -.
DR   GlyGen; P46460; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P46460; -.
DR   MetOSite; P46460; -.
DR   PhosphoSitePlus; P46460; -.
DR   SwissPalm; P46460; -.
DR   REPRODUCTION-2DPAGE; P46460; -.
DR   EPD; P46460; -.
DR   jPOST; P46460; -.
DR   MaxQB; P46460; -.
DR   PaxDb; 10090-ENSMUSP00000099364; -.
DR   PeptideAtlas; P46460; -.
DR   ProteomicsDB; 295530; -.
DR   Pumba; P46460; -.
DR   Antibodypedia; 1006; 326 antibodies from 37 providers.
DR   DNASU; 18195; -.
DR   Ensembl; ENSMUST00000103075.11; ENSMUSP00000099364.5; ENSMUSG00000034187.19.
DR   GeneID; 18195; -.
DR   KEGG; mmu:18195; -.
DR   UCSC; uc007lvt.1; mouse.
DR   AGR; MGI:104560; -.
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; CFDNEIA; -.
DR   OrthoDB; 553800at2759; -.
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 83 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 261 other cell types or tissues.
DR   ExpressionAtlas; P46460; baseline and differential.
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: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:0019901; F:protein kinase binding; IPI:ParkinsonsUK-UCL.
DR   GO; GO:0120283; F:protein serine/threonine kinase binding; ISO:MGI.
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:0048260; P:positive regulation of receptor-mediated endocytosis; ISO:MGI.
DR   GO; GO:0006813; P:potassium ion transport; IDA: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   CDD; cd19504; RecA-like_NSF-SEC18_r1-like; 1.
DR   Gene3D; 1.10.8.60; -; 2.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.10.330.10; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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:SF3; VESICLE-FUSING ATPASE; 1.
DR   PANTHER; PTHR23078; VESICULAR-FUSION PROTEIN NSF; 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   PRINTS; PR00830; ENDOLAPTASE.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM01072; CDC48_2; 1.
DR   SMART; SM01073; CDC48_N; 1.
DR   SUPFAM; SSF50692; ADC-like; 1.
DR   SUPFAM; SSF54585; Cdc48 domain 2-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00674; AAA; 1.
DR   Genevisible; P46460; MM.
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
//