ID SV2A_HUMAN Reviewed; 742 AA. AC Q7L0J3; D3DUZ7; O94841; Q5QNX8; Q7Z3L6; Q8NBJ6; Q9BVZ9; DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 12-OCT-2022, entry version 171. DE RecName: Full=Synaptic vesicle glycoprotein 2A; GN Name=SV2A; Synonyms=KIAA0736; ORFNames=PSEC0174; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=9872452; DOI=10.1093/dnares/5.5.277; RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., RA Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XI. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 5:277-286(1998). RN [2] RP SEQUENCE REVISION. RA Ohara O., Suyama M., Nagase T., Ishikawa K., Kikuno R.; RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Teratocarcinoma; RX PubMed=16303743; DOI=10.1093/dnares/12.2.117; RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y., RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., RA Isogai T.; RT "Signal sequence and keyword trap in silico for selection of full-length RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA RT libraries."; RL DNA Res. 12:117-126(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Retina; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain, and Ovary; 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 [8] RP CHARACTERIZATION AS BINDING-SITE FOR ANTIEPILEPTIC DRUG LEVETIRACETAM. RX PubMed=15210974; DOI=10.1073/pnas.0308208101; RA Lynch B.A., Lambeng N., Nocka K., Kensel-Hammes P., Bajjalieh S.M., RA Matagne A., Fuks B.; RT "The synaptic vesicle protein SV2A is the binding site for the RT antiepileptic drug levetiracetam."; RL Proc. Natl. Acad. Sci. U.S.A. 101:9861-9866(2004). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80; SER-81 AND THR-84, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [10] RP FUNCTION AS C.BOTULINUM NEUROTOXIN TYPE A2 RECEPTOR (MICROBIAL INFECTION), RP AND SUBUNIT (MICROBIAL INFECTION). RX PubMed=29649119; DOI=10.3390/toxins10040153; RA Gustafsson R., Zhang S., Masuyer G., Dong M., Stenmark P.; RT "Crystal structure of botulinum neurotoxin A2 in complex with the human RT protein receptor SV2C reveals plasticity in receptor binding."; RL Toxins 10:0-0(2018). CC -!- FUNCTION: Plays a role in the control of regulated secretion in neural CC and endocrine cells, enhancing selectively low-frequency CC neurotransmission. Positively regulates vesicle fusion by maintaining CC the readily releasable pool of secretory vesicles (By similarity). CC {ECO:0000250}. CC -!- FUNCTION: (Microbial infection) Receptor for the C.botulinum neurotoxin CC type A2 (BoNT/A, botA); glycosylation is not essential but enhances the CC interaction (PubMed:29649119). Probably also serves as a receptor for CC the closely related C.botulinum neurotoxin type A1. CC {ECO:0000269|PubMed:29649119, ECO:0000305|PubMed:29649119}. CC -!- SUBUNIT: Interacts with SYT1/synaptotagmin-1 in a calcium-dependent CC manner. Binds the adapter protein complex AP-2 (By similarity). CC {ECO:0000250}. CC -!- SUBUNIT: (Microbial infection) Interacts with C.botulinum neurotoxin CC type A2 (BoNT/A, botA) (PubMed:29649119). Interaction is improved by CC glycosylation of SV2 (PubMed:29649119). {ECO:0000305|PubMed:29649119}. CC -!- SUBCELLULAR LOCATION: Presynapse {ECO:0000250|UniProtKB:Q9JIS5}. CC Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane CC {ECO:0000250|UniProtKB:Q02563}; Multi-pass membrane protein CC {ECO:0000250|UniProtKB:Q02563}. Note=Enriched in chromaffin granules, CC not present in adrenal microsomes. Associated with both insulin CC granules and synaptic-like microvesicles in insulin-secreting cells of CC the pancreas (By similarity). Colocalizes with ATP2B1 at photoreceptor CC synaptic terminals. {ECO:0000250|UniProtKB:Q02563, CC ECO:0000250|UniProtKB:Q9JIS5}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q7L0J3-1; Sequence=Displayed; CC Name=2; CC IsoId=Q7L0J3-2; Sequence=VSP_019265; CC -!- PTM: Phosphorylation by CK1 of the N-terminal cytoplasmic domain CC regulates interaction with SYT1. {ECO:0000250}. CC -!- PTM: N-glycosylated. {ECO:0000250}. CC -!- MISCELLANEOUS: Identified as the brain binding-site for the CC antiepileptic drug levetiracetam/lev. CC -!- SIMILARITY: Belongs to the major facilitator superfamily. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA34456.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=CAI12573.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB018279; BAA34456.2; ALT_INIT; mRNA. DR EMBL; AK075480; BAC11645.1; -; mRNA. DR EMBL; BX537754; CAD97824.1; -; mRNA. DR EMBL; AL591493; CAI12572.1; -; Genomic_DNA. DR EMBL; AL591493; CAI12573.1; ALT_SEQ; Genomic_DNA. DR EMBL; CH471121; EAW53596.1; -; Genomic_DNA. DR EMBL; CH471121; EAW53598.1; -; Genomic_DNA. DR EMBL; BC000776; AAH00776.2; -; mRNA. DR EMBL; BC045111; AAH45111.1; -; mRNA. DR CCDS; CCDS940.1; -. [Q7L0J3-1] DR RefSeq; NP_001265648.1; NM_001278719.1. DR RefSeq; NP_001315603.1; NM_001328674.1. [Q7L0J3-1] DR RefSeq; NP_001315604.1; NM_001328675.1. [Q7L0J3-1] DR RefSeq; NP_055664.3; NM_014849.4. [Q7L0J3-1] DR PDB; 4V11; X-ray; 1.95 A; B=81-90. DR PDBsum; 4V11; -. DR AlphaFoldDB; Q7L0J3; -. DR SMR; Q7L0J3; -. DR BioGRID; 115229; 78. DR IntAct; Q7L0J3; 13. DR MINT; Q7L0J3; -. DR STRING; 9606.ENSP00000358142; -. DR ChEMBL; CHEMBL1998; -. DR DrugBank; DB05541; Brivaracetam. DR DrugBank; DB01202; Levetiracetam. DR DrugBank; DB05885; Seletracetam. DR DrugCentral; Q7L0J3; -. DR GlyGen; Q7L0J3; 3 sites. DR iPTMnet; Q7L0J3; -. DR MetOSite; Q7L0J3; -. DR PhosphoSitePlus; Q7L0J3; -. DR BioMuta; SV2A; -. DR DMDM; 74749878; -. DR EPD; Q7L0J3; -. DR jPOST; Q7L0J3; -. DR MassIVE; Q7L0J3; -. DR MaxQB; Q7L0J3; -. DR PaxDb; Q7L0J3; -. DR PeptideAtlas; Q7L0J3; -. DR PRIDE; Q7L0J3; -. DR ProteomicsDB; 68731; -. [Q7L0J3-1] DR ProteomicsDB; 68732; -. [Q7L0J3-2] DR Antibodypedia; 2184; 184 antibodies from 34 providers. DR DNASU; 9900; -. DR Ensembl; ENST00000369145.1; ENSP00000358141.1; ENSG00000159164.10. [Q7L0J3-2] DR Ensembl; ENST00000369146.8; ENSP00000358142.3; ENSG00000159164.10. [Q7L0J3-1] DR GeneID; 9900; -. DR KEGG; hsa:9900; -. DR MANE-Select; ENST00000369146.8; ENSP00000358142.3; NM_014849.5; NP_055664.3. DR UCSC; uc001etg.4; human. [Q7L0J3-1] DR CTD; 9900; -. DR DisGeNET; 9900; -. DR GeneCards; SV2A; -. DR HGNC; HGNC:20566; SV2A. DR HPA; ENSG00000159164; Tissue enhanced (brain, parathyroid gland). DR MIM; 185860; gene. DR neXtProt; NX_Q7L0J3; -. DR OpenTargets; ENSG00000159164; -. DR PharmGKB; PA128394564; -. DR VEuPathDB; HostDB:ENSG00000159164; -. DR eggNOG; KOG0255; Eukaryota. DR GeneTree; ENSGT00950000182940; -. DR HOGENOM; CLU_001265_46_15_1; -. DR InParanoid; Q7L0J3; -. DR OMA; FNDKSMV; -. DR OrthoDB; 724235at2759; -. DR PhylomeDB; Q7L0J3; -. DR TreeFam; TF324824; -. DR PathwayCommons; Q7L0J3; -. DR Reactome; R-HSA-5250955; Toxicity of botulinum toxin type D (botD). DR Reactome; R-HSA-5250968; Toxicity of botulinum toxin type A (botA). DR Reactome; R-HSA-5250981; Toxicity of botulinum toxin type F (botF). DR Reactome; R-HSA-5250992; Toxicity of botulinum toxin type E (botE). DR SignaLink; Q7L0J3; -. DR SIGNOR; Q7L0J3; -. DR BioGRID-ORCS; 9900; 18 hits in 1071 CRISPR screens. DR ChiTaRS; SV2A; human. DR GeneWiki; SV2A; -. DR GenomeRNAi; 9900; -. DR Pharos; Q7L0J3; Tclin. DR PRO; PR:Q7L0J3; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q7L0J3; protein. DR Bgee; ENSG00000159164; Expressed in Brodmann (1909) area 10 and 152 other tissues. DR Genevisible; Q7L0J3; HS. DR GO; GO:0005911; C:cell-cell junction; IEA:Ensembl. DR GO; GO:0030425; C:dendrite; IEA:Ensembl. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:LIFEdb. DR GO; GO:0098982; C:GABA-ergic synapse; IEA:Ensembl. DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl. DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central. DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; IEA:Ensembl. DR GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl. DR GO; GO:0043005; C:neuron projection; IBA:GO_Central. DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0048786; C:presynaptic active zone; IEA:Ensembl. DR GO; GO:0008021; C:synaptic vesicle; TAS:ParkinsonsUK-UCL. DR GO; GO:0030672; C:synaptic vesicle membrane; IBA:GO_Central. DR GO; GO:0019901; F:protein kinase binding; ISS:ParkinsonsUK-UCL. DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro. DR GO; GO:0006874; P:cellular calcium ion homeostasis; IEA:Ensembl. DR GO; GO:0014052; P:regulation of gamma-aminobutyric acid secretion; IEA:Ensembl. DR GO; GO:0016082; P:synaptic vesicle priming; IEA:Ensembl. DR Gene3D; 1.20.1250.20; -; 2. DR InterPro; IPR011701; MFS. DR InterPro; IPR020846; MFS_dom. DR InterPro; IPR005828; MFS_sugar_transport-like. DR InterPro; IPR036259; MFS_trans_sf. DR InterPro; IPR005829; Sugar_transporter_CS. DR InterPro; IPR022308; SV2. DR Pfam; PF07690; MFS_1; 1. DR Pfam; PF00083; Sugar_tr; 1. DR SUPFAM; SSF103473; SSF103473; 2. DR TIGRFAMs; TIGR01299; synapt_SV2; 1. DR PROSITE; PS50850; MFS; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell projection; Cytoplasmic vesicle; KW Glycoprotein; Membrane; Neurotransmitter transport; Phosphoprotein; KW Reference proteome; Synapse; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..742 FT /note="Synaptic vesicle glycoprotein 2A" FT /id="PRO_0000239764" FT TOPO_DOM 1..169 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 170..190 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 191..205 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 206..226 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 227..233 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 234..254 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 255..262 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 263..283 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 284..294 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 295..315 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 316..334 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 335..355 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 356..447 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 448..468 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 469..598 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 599..619 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 620..626 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 627..647 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 648..651 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 652..672 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 673..685 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 686..708 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 709..712 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 713..731 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 732..742 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REGION 1..57 FT /note="Interaction with SYT1" FT /evidence="ECO:0000250" FT REGION 33..144 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 33..50 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 68..84 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 80 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 81 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 84 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 127 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9JIS5" FT MOD_RES 393 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q02563" FT MOD_RES 480 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q9JIS5" FT CARBOHYD 498 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 548 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 573 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 683..742 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:16303743" FT /id="VSP_019265" FT CONFLICT 100 FT /note="G -> D (in Ref. 4; CAD97824)" FT /evidence="ECO:0000305" FT CONFLICT 404 FT /note="D -> G (in Ref. 3; BAC11645)" FT /evidence="ECO:0000305" FT CONFLICT 493 FT /note="E -> G (in Ref. 4; CAD97824)" FT /evidence="ECO:0000305" FT CONFLICT 524 FT /note="V -> A (in Ref. 3; BAC11645)" FT /evidence="ECO:0000305" FT CONFLICT 544 FT /note="T -> A (in Ref. 3; BAC11645)" FT /evidence="ECO:0000305" FT CONFLICT 582 FT /note="G -> D (in Ref. 3; BAC11645)" FT /evidence="ECO:0000305" FT CONFLICT 611 FT /note="G -> R (in Ref. 3; BAC11645)" FT /evidence="ECO:0000305" SQ SEQUENCE 742 AA; 82695 MW; 913E216D5CFC2FB2 CRC64; MEEGFRDRAA FIRGAKDIAK EVKKHAAKKV VKGLDRVQDE YSRRSYSRFE EEDDDDDFPA PSDGYYRGEG TQDEEEGGAS SDATEGHDED DEIYEGEYQG IPRAESGGKG ERMADGAPLA GVRGGLSDGE GPPGGRGEAQ RRKEREELAQ QYEAILRECG HGRFQWTLYF VLGLALMADG VEVFVVGFVL PSAEKDMCLS DSNKGMLGLI VYLGMMVGAF LWGGLADRLG RRQCLLISLS VNSVFAFFSS FVQGYGTFLF CRLLSGVGIG GSIPIVFSYF SEFLAQEKRG EHLSWLCMFW MIGGVYAAAM AWAIIPHYGW SFQMGSAYQF HSWRVFVLVC AFPSVFAIGA LTTQPESPRF FLENGKHDEA WMVLKQVHDT NMRAKGHPER VFSVTHIKTI HQEDELIEIQ SDTGTWYQRW GVRALSLGGQ VWGNFLSCFG PEYRRITLMM MGVWFTMSFS YYGLTVWFPD MIRHLQAVDY ASRTKVFPGE RVEHVTFNFT LENQIHRGGQ YFNDKFIGLR LKSVSFEDSL FEECYFEDVT SSNTFFRNCT FINTVFYNTD LFEYKFVNSR LINSTFLHNK EGCPLDVTGT GEGAYMVYFV SFLGTLAVLP GNIVSALLMD KIGRLRMLAG SSVMSCVSCF FLSFGNSESA MIALLCLFGG VSIASWNALD VLTVELYPSD KRTTAFGFLN ALCKLAAVLG ISIFTSFVGI TKAAPILFAS AALALGSSLA LKLPETRGQV LQ //