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 05-DEC-2018, entry version 147. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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. RT The complete sequences of 100 new cDNA clones from brain which code RT for large 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- RT length human cDNAs encoding secretion or membrane proteins from oligo- RT capped cDNA 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., RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., RA Ottenwaelder B., Poustka A., 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., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA 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., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA 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., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA 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., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA 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 RT project: 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, RP AND 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 RP INFECTION), 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 RT human 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 CC neural and endocrine cells, enhancing selectively low-frequency CC neurotransmission. Positively regulates vesicle fusion by CC maintaining the readily releasable pool of secretory vesicles (By CC similarity). {ECO:0000250}. CC -!- FUNCTION: (Microbial infection) Receptor for the C.botulinum CC neurotoxin type A2 (BoNT/A, botA); glycosylation is not essential CC but enhances the interaction (PubMed:29649119). Probably also CC serves as a receptor for the closely related C.botulinum CC neurotoxin type A1. {ECO:0000269|PubMed:29649119, CC ECO:0000305|PubMed:29649119}. CC -!- SUBUNIT: Interacts with SYT1/synaptotagmin-1 in a calcium- CC dependent manner. Binds the adapter protein complex AP-2 (By CC similarity). {ECO:0000250}. CC -!- SUBUNIT: (Microbial infection) Interacts with C.botulinum CC neurotoxin type A2 (BoNT/A, botA) (PubMed:29649119). Interaction CC is improved by glycosylation of SV2 (PubMed:29649119). CC {ECO:0000305|PubMed:29649119}. CC -!- SUBCELLULAR LOCATION: Cell junction, synapse CC {ECO:0000250|UniProtKB:Q9JIS5}. Cytoplasmic vesicle, secretory CC vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q02563}; CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q02563}. CC Note=Enriched in chromaffin granules, not present in adrenal CC microsomes. Associated with both insulin granules and synaptic- CC like microvesicles in insulin-secreting cells of the pancreas (By CC similarity). Colocalizes with ATP2B1 at photoreceptor synaptic CC 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 Note=No experimental confirmation available.; 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=Translation N-terminally shortened.; 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 UniGene; Hs.516153; -. DR PDB; 4V11; X-ray; 1.95 A; B=81-90. DR PDBsum; 4V11; -. DR ProteinModelPortal; Q7L0J3; -. DR SMR; Q7L0J3; -. DR BioGrid; 115229; 7. DR IntAct; Q7L0J3; 4. DR STRING; 9606.ENSP00000358142; -. DR ChEMBL; CHEMBL1998; -. DR DrugBank; DB01202; Levetiracetam. DR iPTMnet; Q7L0J3; -. DR PhosphoSitePlus; Q7L0J3; -. DR DMDM; 74749878; -. DR EPD; Q7L0J3; -. DR MaxQB; Q7L0J3; -. DR PaxDb; Q7L0J3; -. DR PeptideAtlas; Q7L0J3; -. DR PRIDE; Q7L0J3; -. DR ProteomicsDB; 68731; -. DR ProteomicsDB; 68732; -. [Q7L0J3-2] DR DNASU; 9900; -. DR Ensembl; ENST00000369145; ENSP00000358141; ENSG00000159164. [Q7L0J3-2] DR Ensembl; ENST00000369146; ENSP00000358142; ENSG00000159164. [Q7L0J3-1] DR GeneID; 9900; -. DR KEGG; hsa:9900; -. DR UCSC; uc001etg.4; human. [Q7L0J3-1] DR CTD; 9900; -. DR DisGeNET; 9900; -. DR EuPathDB; HostDB:ENSG00000159164.9; -. DR GeneCards; SV2A; -. DR HGNC; HGNC:20566; SV2A. DR HPA; CAB002226; -. DR HPA; HPA007863; -. DR MIM; 185860; gene. DR neXtProt; NX_Q7L0J3; -. DR OpenTargets; ENSG00000159164; -. DR PharmGKB; PA128394564; -. DR eggNOG; ENOG410IRID; Eukaryota. DR eggNOG; ENOG410YQME; LUCA. DR GeneTree; ENSGT00940000153537; -. DR HOVERGEN; HBG053967; -. DR InParanoid; Q7L0J3; -. DR KO; K06258; -. DR OMA; MMMAVWF; -. DR OrthoDB; EOG091G02NC; -. DR PhylomeDB; Q7L0J3; -. DR TreeFam; TF324824; -. DR Reactome; R-HSA-5250955; Toxicity of botulinum toxin type D (BoNT/D). DR Reactome; R-HSA-5250968; Toxicity of botulinum toxin type A (BoNT/A). DR Reactome; R-HSA-5250981; Toxicity of botulinum toxin type F (BoNT/F). DR Reactome; R-HSA-5250992; Toxicity of botulinum toxin type E (BoNT/E). DR ChiTaRS; SV2A; human. DR GeneWiki; SV2A; -. DR GenomeRNAi; 9900; -. DR PRO; PR:Q7L0J3; -. DR Proteomes; UP000005640; Chromosome 1. DR Bgee; ENSG00000159164; Expressed in 176 organ(s), highest expression level in Brodmann (1909) area 10. DR CleanEx; HS_SV2A; -. 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 CDD; cd06174; MFS; 2. DR InterPro; IPR001646; 5peptide_repeat. 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; PF13599; Pentapeptide_4; 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 junction; Complete proteome; KW Cytoplasmic vesicle; Glycoprotein; Membrane; KW Neurotransmitter transport; Phosphoprotein; Reference proteome; KW Synapse; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 742 Synaptic vesicle glycoprotein 2A. FT /FTId=PRO_0000239764. FT TOPO_DOM 1 169 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 170 190 Helical. {ECO:0000255}. FT TOPO_DOM 191 205 Extracellular. {ECO:0000255}. FT TRANSMEM 206 226 Helical. {ECO:0000255}. FT TOPO_DOM 227 233 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 234 254 Helical. {ECO:0000255}. FT TOPO_DOM 255 262 Extracellular. {ECO:0000255}. FT TRANSMEM 263 283 Helical. {ECO:0000255}. FT TOPO_DOM 284 294 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 295 315 Helical. {ECO:0000255}. FT TOPO_DOM 316 334 Extracellular. {ECO:0000255}. FT TRANSMEM 335 355 Helical. {ECO:0000255}. FT TOPO_DOM 356 447 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 448 468 Helical. {ECO:0000255}. FT TOPO_DOM 469 598 Extracellular. {ECO:0000255}. FT TRANSMEM 599 619 Helical. {ECO:0000255}. FT TOPO_DOM 620 626 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 627 647 Helical. {ECO:0000255}. FT TOPO_DOM 648 651 Extracellular. {ECO:0000255}. FT TRANSMEM 652 672 Helical. {ECO:0000255}. FT TOPO_DOM 673 685 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 686 708 Helical. {ECO:0000255}. FT TOPO_DOM 709 712 Extracellular. {ECO:0000255}. FT TRANSMEM 713 731 Helical. {ECO:0000255}. FT TOPO_DOM 732 742 Cytoplasmic. {ECO:0000255}. FT REGION 1 57 Interaction with SYT1. {ECO:0000250}. FT MOD_RES 80 80 Phosphoserine. FT {ECO:0000244|PubMed:19690332}. FT MOD_RES 81 81 Phosphoserine. FT {ECO:0000244|PubMed:19690332}. FT MOD_RES 84 84 Phosphothreonine. FT {ECO:0000244|PubMed:19690332}. FT MOD_RES 127 127 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9JIS5}. FT MOD_RES 393 393 Phosphoserine. FT {ECO:0000250|UniProtKB:Q02563}. FT MOD_RES 480 480 Phosphotyrosine. FT {ECO:0000250|UniProtKB:Q9JIS5}. FT CARBOHYD 498 498 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 548 548 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 573 573 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT VAR_SEQ 683 742 Missing (in isoform 2). FT {ECO:0000303|PubMed:16303743}. FT /FTId=VSP_019265. FT CONFLICT 100 100 G -> D (in Ref. 4; CAD97824). FT {ECO:0000305}. FT CONFLICT 404 404 D -> G (in Ref. 3; BAC11645). FT {ECO:0000305}. FT CONFLICT 493 493 E -> G (in Ref. 4; CAD97824). FT {ECO:0000305}. FT CONFLICT 524 524 V -> A (in Ref. 3; BAC11645). FT {ECO:0000305}. FT CONFLICT 544 544 T -> A (in Ref. 3; BAC11645). FT {ECO:0000305}. FT CONFLICT 582 582 G -> D (in Ref. 3; BAC11645). FT {ECO:0000305}. FT CONFLICT 611 611 G -> R (in Ref. 3; BAC11645). FT {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 //