SV2C_HUMAN
ID SV2C_HUMAN Reviewed; 727 AA.
AC Q496J9; Q496K1; Q9UPU8;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Synaptic vesicle glycoprotein 2C;
GN Name=SV2C; Synonyms=KIAA1054;
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].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 248-727.
RC TISSUE=Brain;
RX PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:197-205(1999).
RN [3]
RP POSSIBLE FUNCTION AS C.BOTULINUM NEUROTOXIN TYPE D RECEPTOR (MICROBIAL
RP INFECTION).
RX PubMed=21483489; DOI=10.1371/journal.ppat.1002008;
RA Peng L., Tepp W.H., Johnson E.A., Dong M.;
RT "Botulinum neurotoxin D uses synaptic vesicle protein SV2 and gangliosides
RT as receptors.";
RL PLoS Pathog. 7:E1002008-E1002008(2011).
RN [4]
RP FUNCTION AS C.BOTULINUM NEUROTOXIN TYPE A RECEPTOR (MICROBIAL INFECTION),
RP SUBUNIT (MICROBIAL INFECTION), TOPOLOGY, GLYCOSYLATION AT ASN-534; ASN-559
RP AND ASN-565, AND MUTAGENESIS OF ASN-559; SER-561 AND ASN-565.
RX PubMed=27313224; DOI=10.1042/bcj20160439;
RA Mahrhold S., Bergstroem T., Stern D., Dorner B.G., Aastot C., Rummel A.;
RT "Only the complex N559-glycan in the synaptic vesicle glycoprotein 2C
RT mediates high affinity binding to botulinum neurotoxin serotype A1.";
RL Biochem. J. 473:2645-2654(2016).
RN [5] {ECO:0007744|PDB:4JRA}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 871-1296 IN COMPLEX WITH
RP C.BOTULINUM NEUROTOXIN TYPE A HEAVY CHAIN C-TERMINUS, SUBUNIT (MICROBIAL
RP INFECTION), AND MUTAGENESIS OF ASN-559 AND PHE-563.
RX PubMed=24240280; DOI=10.1038/nature12732;
RA Benoit R.M., Frey D., Hilbert M., Kevenaar J.T., Wieser M.M.,
RA Stirnimann C.U., McMillan D., Ceska T., Lebon F., Jaussi R.,
RA Steinmetz M.O., Schertler G.F., Hoogenraad C.C., Capitani G.,
RA Kammerer R.A.;
RT "Structural basis for recognition of synaptic vesicle protein 2C by
RT botulinum neurotoxin A.";
RL Nature 505:108-111(2014).
RN [6] {ECO:0007744|PDB:5JLV}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF GLYCOSYLATED 473-567, FUNCTION AS
RP C.BOTULINUM NEUROTOXIN TYPE A RECEPTOR (MICROBIAL INFECTION), SUBUNIT
RP (MICROBIAL INFECTION), AND GLYCOSYLATION AT ASN-534 AND ASN-559.
RX PubMed=27294781; DOI=10.1038/nsmb.3245;
RA Yao G., Zhang S., Mahrhold S., Lam K.H., Stern D., Bagramyan K., Perry K.,
RA Kalkum M., Rummel A., Dong M., Jin R.;
RT "N-linked glycosylation of SV2 is required for binding and uptake of
RT botulinum neurotoxin A.";
RL Nat. Struct. Mol. Biol. 23:656-662(2016).
RN [7] {ECO:0007744|PDB:5MOY}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 456-574 IN COMPLEX WITH
RP C.BOTULINUM NEUROTOXIN TYPE A C-TERMINUS, FUNCTION AS C.BOTULINUM
RP NEUROTOXIN TYPE A RECEPTOR (MICROBIAL INFECTION), SUBUNIT (MICROBIAL
RP INFECTION), AND MUTAGENESIS OF ASN-559 AND PHE-563.
RX PubMed=28252640; DOI=10.1038/srep43588;
RA Benoit R.M., Scharer M.A., Wieser M.M., Li X., Frey D., Kammerer R.A.;
RT "Crystal structure of the BoNT/A2 receptor-binding domain in complex with
RT the luminal domain of its neuronal receptor SV2C.";
RL Sci. Rep. 7:43588-43588(2017).
RN [8] {ECO:0007744|PDB:6ES1}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 474-567 IN COMPLEX WITH
RP C.BOTULINUM NEUROTOXIN TYPE A2 C-TERMINUS, FUNCTION AS C.BOTULINUM
RP NEUROTOXIN TYPE A2 RECEPTOR (MICROBIAL INFECTION), AND SUBUNIT (MICROBIAL
RP 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.
CC {ECO:0000250|UniProtKB:Q9Z2I6}.
CC -!- FUNCTION: (Microbial infection) Receptor for C.botulinum neurotoxin
CC type A (BoNT/A, botA); the toxin probably binds via extracellular loop
CC 4 (PubMed:27313224). Recognition by BoNT/A relies on both protein-
CC protein and protein-N-glycosylation; glycosylation of Asn-559 increases
CC its affinity for BoNT/A (PubMed:27313224). Also serves as a receptor
CC for the closely related C.botulinum neurotoxin type A2; glycosylation
CC is not essential but enhances the interaction (PubMed:29649119).
CC {ECO:0000269|PubMed:24240280, ECO:0000269|PubMed:27294781,
CC ECO:0000269|PubMed:27313224, ECO:0000269|PubMed:28252640,
CC ECO:0000269|PubMed:29649119}.
CC -!- FUNCTION: (Microbial infection) Possible receptor for C.botulinum
CC neurotoxin type D (BoNT/D, botD); note that type D does not usually
CC infect humans. {ECO:0000269|PubMed:21483489}.
CC -!- SUBUNIT: Interacts with SYT1 in a calcium-dependent manner.
CC {ECO:0000250|UniProtKB:Q9Z2I6}.
CC -!- SUBUNIT: (Microbial infection) Interacts with C.botulinum neurotoxin
CC type A1 and type A2 (BoNT/A, botA) (PubMed:29649119). Interaction is
CC improved by glycosylation of SV2 (PubMed:29649119).
CC {ECO:0000269|PubMed:24240280, ECO:0000269|PubMed:27294781,
CC ECO:0000269|PubMed:28252640, ECO:0000269|PubMed:29649119}.
CC -!- INTERACTION:
CC Q496J9; P0DPI0: botA; Xeno; NbExp=4; IntAct=EBI-16081469, EBI-8178893;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000250|UniProtKB:Q9Z2I6}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:Q9Z2I6}. Note=Enriched in small synaptic
CC vesicles and adrenal microsomes, not present in chromaffin granules.
CC Associated with both insulin granules and synaptic-like microvesicles
CC in insulin-secreting cells of the pancreas.
CC {ECO:0000250|UniProtKB:Q9Z2I6}.
CC -!- PTM: N-glycosylated. Upon expression in a kidney cell line the most
CC abundant glycan on Asn-534 is GlcNAc(3)Hex(5), while on Asn-559 and
CC Asn-565 the most abundant glycan is GlcNAc2Fuc1Man3GlcNAc3Gal3. Both
CC Asn-559 and Asn-565 have a high degree of glycan heterogeneity
CC (PubMed:27313224). {ECO:0000269|PubMed:27294781,
CC ECO:0000269|PubMed:27313224, ECO:0000269|PubMed:28252640}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000305}.
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DR EMBL; BC100824; AAI00825.1; -; mRNA.
DR EMBL; BC100825; AAI00826.1; -; mRNA.
DR EMBL; BC100826; AAI00827.1; -; mRNA.
DR EMBL; BC100827; AAI00828.1; -; mRNA.
DR EMBL; AB028977; BAA83006.1; -; mRNA.
DR CCDS; CCDS43331.1; -.
DR RefSeq; NP_055794.3; NM_014979.3.
DR RefSeq; XP_011541583.1; XM_011543281.2.
DR RefSeq; XP_011541584.2; XM_011543282.2.
DR PDB; 4JRA; X-ray; 2.30 A; C/D=456-574.
DR PDB; 5JLV; X-ray; 2.00 A; C/D=473-567.
DR PDB; 5MOY; X-ray; 2.30 A; B=456-574.
DR PDB; 6ES1; X-ray; 2.00 A; B=474-567.
DR PDBsum; 4JRA; -.
DR PDBsum; 5JLV; -.
DR PDBsum; 5MOY; -.
DR PDBsum; 6ES1; -.
DR AlphaFoldDB; Q496J9; -.
DR SMR; Q496J9; -.
DR BioGRID; 116636; 9.
DR DIP; DIP-60687N; -.
DR IntAct; Q496J9; 8.
DR STRING; 9606.ENSP00000423541; -.
DR ChEMBL; CHEMBL4665594; -.
DR TCDB; 2.A.1.22.6; the major facilitator superfamily (mfs).
DR GlyGen; Q496J9; 5 sites.
DR iPTMnet; Q496J9; -.
DR PhosphoSitePlus; Q496J9; -.
DR BioMuta; SV2C; -.
DR DMDM; 108860965; -.
DR MassIVE; Q496J9; -.
DR PaxDb; Q496J9; -.
DR PeptideAtlas; Q496J9; -.
DR PRIDE; Q496J9; -.
DR ProteomicsDB; 61995; -.
DR Antibodypedia; 24435; 133 antibodies from 25 providers.
DR DNASU; 22987; -.
DR Ensembl; ENST00000502798.7; ENSP00000423541.2; ENSG00000122012.14.
DR GeneID; 22987; -.
DR KEGG; hsa:22987; -.
DR MANE-Select; ENST00000502798.7; ENSP00000423541.2; NM_014979.4; NP_055794.3.
DR UCSC; uc003kei.2; human.
DR CTD; 22987; -.
DR DisGeNET; 22987; -.
DR GeneCards; SV2C; -.
DR HGNC; HGNC:30670; SV2C.
DR HPA; ENSG00000122012; Tissue enriched (brain).
DR MIM; 610291; gene.
DR neXtProt; NX_Q496J9; -.
DR OpenTargets; ENSG00000122012; -.
DR PharmGKB; PA25005; -.
DR VEuPathDB; HostDB:ENSG00000122012; -.
DR eggNOG; KOG0255; Eukaryota.
DR GeneTree; ENSGT00950000182940; -.
DR HOGENOM; CLU_001265_46_15_1; -.
DR InParanoid; Q496J9; -.
DR OMA; HDEYKDR; -.
DR OrthoDB; 724235at2759; -.
DR PhylomeDB; Q496J9; -.
DR TreeFam; TF324824; -.
DR PathwayCommons; Q496J9; -.
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 SignaLink; Q496J9; -.
DR BioGRID-ORCS; 22987; 14 hits in 1068 CRISPR screens.
DR ChiTaRS; SV2C; human.
DR GenomeRNAi; 22987; -.
DR Pharos; Q496J9; Tbio.
DR PRO; PR:Q496J9; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q496J9; protein.
DR Bgee; ENSG00000122012; Expressed in substantia nigra pars reticulata and 120 other tissues.
DR ExpressionAtlas; Q496J9; baseline and differential.
DR Genevisible; Q496J9; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0008021; C:synaptic vesicle; TAS:ParkinsonsUK-UCL.
DR GO; GO:0030672; C:synaptic vesicle membrane; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0007268; P:chemical synaptic transmission; IEA:InterPro.
DR GO; GO:0006836; P:neurotransmitter transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1250.20; -; 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; Cytoplasmic vesicle; Glycoprotein; Membrane;
KW Neurotransmitter transport; Phosphoprotein; Reference proteome; Synapse;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..727
FT /note="Synaptic vesicle glycoprotein 2C"
FT /id="PRO_0000239771"
FT TOPO_DOM 1..154
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 176..191
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 213..226
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 248
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 270..280
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 302..320
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 342..437
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 438..458
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 459..578
FT /note="Extracellular"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:27313224"
FT TRANSMEM 579..599
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 600..609
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 610..630
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 631..636
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 637..657
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 658..669
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 670..690
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 691..698
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 699..719
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 720..727
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..57
FT /note="Interaction with SYT1"
FT /evidence="ECO:0000250"
FT REGION 24..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 109..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..563
FT /note="(Microbial infection) C.botulinum neurotoxin type A-
FT binding"
FT /evidence="ECO:0000269|PubMed:27294781"
FT COMPBIAS 24..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7L0J3"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7L0J3"
FT MOD_RES 79
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7L0J3"
FT MOD_RES 466
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIS5"
FT CARBOHYD 480
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 484
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 534
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:27313224,
FT ECO:0007744|PDB:5JLV"
FT CARBOHYD 559
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:27313224,
FT ECO:0000269|PubMed:28252640, ECO:0007744|PDB:5JLV"
FT CARBOHYD 565
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:27313224"
FT VARIANT 482
FT /note="T -> S (in dbSNP:rs2270927)"
FT /id="VAR_050303"
FT VARIANT 543
FT /note="D -> N (in dbSNP:rs31244)"
FT /id="VAR_050304"
FT MUTAGEN 559
FT /note="N->A: No change in interaction with C.botulinum
FT neurotoxin type A heavy chain (botA, BoNT/A HC). Decreased
FT molecular weight probably due to glycosylation loss,
FT decreased interaction with BoNT/A HC."
FT /evidence="ECO:0000269|PubMed:24240280,
FT ECO:0000269|PubMed:27313224, ECO:0000269|PubMed:28252640"
FT MUTAGEN 559
FT /note="N->Q: Decreased molecular weight probably due to
FT glycosylation loss, decreased binding to BoNT/A HC. Greater
FT reduction in weight; when associated with Q-565."
FT /evidence="ECO:0000269|PubMed:27313224"
FT MUTAGEN 561
FT /note="S->A: Decreased molecular weight probably due to
FT glycosylation loss, decreased binding to BoNT/A HC."
FT /evidence="ECO:0000269|PubMed:27313224"
FT MUTAGEN 563
FT /note="F->A: No longer interacts with BoNT/A HC."
FT /evidence="ECO:0000269|PubMed:24240280,
FT ECO:0000269|PubMed:28252640"
FT MUTAGEN 565
FT /note="N->Q: Decreased molecular weight probably due to
FT glycosylation loss, no change in binding to BoNT/A heavy
FT chain. Greater reduction in weight; when associated with Q-
FT 559."
FT /evidence="ECO:0000269|PubMed:27313224"
FT CONFLICT 346
FT /note="F -> S (in Ref. 1; AAI00825)"
FT /evidence="ECO:0000305"
FT STRAND 477..483
FT /evidence="ECO:0007829|PDB:5JLV"
FT STRAND 487..494
FT /evidence="ECO:0007829|PDB:5JLV"
FT STRAND 496..504
FT /evidence="ECO:0007829|PDB:5JLV"
FT STRAND 506..514
FT /evidence="ECO:0007829|PDB:5JLV"
FT STRAND 516..519
FT /evidence="ECO:0007829|PDB:5JLV"
FT STRAND 521..524
FT /evidence="ECO:0007829|PDB:5JLV"
FT STRAND 526..529
FT /evidence="ECO:0007829|PDB:5JLV"
FT STRAND 531..534
FT /evidence="ECO:0007829|PDB:5JLV"
FT STRAND 536..539
FT /evidence="ECO:0007829|PDB:5JLV"
FT STRAND 541..544
FT /evidence="ECO:0007829|PDB:5JLV"
FT HELIX 549..551
FT /evidence="ECO:0007829|PDB:5JLV"
FT STRAND 552..554
FT /evidence="ECO:0007829|PDB:5JLV"
FT STRAND 556..563
FT /evidence="ECO:0007829|PDB:5JLV"
SQ SEQUENCE 727 AA; 82342 MW; 0411B47057B3279C CRC64;
MEDSYKDRTS LMKGAKDIAR EVKKQTVKKV NQAVDRAQDE YTQRSYSRFQ DEEDDDDYYP
AGETYNGEAN DDEGSSEATE GHDEDDEIYE GEYQGIPSMN QAKDSIVSVG QPKGDEYKDR
RELESERRAD EEELAQQYEL IIQECGHGRF QWALFFVLGM ALMADGVEVF VVGFVLPSAE
TDLCIPNSGS GWLGSIVYLG MMVGAFFWGG LADKVGRKQS LLICMSVNGF FAFLSSFVQG
YGFFLFCRLL SGFGIGGAIP TVFSYFAEVL AREKRGEHLS WLCMFWMIGG IYASAMAWAI
IPHYGWSFSM GSAYQFHSWR VFVIVCALPC VSSVVALTFM PESPRFLLEV GKHDEAWMIL
KLIHDTNMRA RGQPEKVFTV NKIKTPKQID ELIEIESDTG TWYRRCFVRI RTELYGIWLT
FMRCFNYPVR DNTIKLTIVW FTLSFGYYGL SVWFPDVIKP LQSDEYALLT RNVERDKYAN
FTINFTMENQ IHTGMEYDNG RFIGVKFKSV TFKDSVFKSC TFEDVTSVNT YFKNCTFIDT
VFDNTDFEPY KFIDSEFKNC SFFHNKTGCQ ITFDDDYSAY WIYFVNFLGT LAVLPGNIVS
ALLMDRIGRL TMLGGSMVLS GISCFFLWFG TSESMMIGML CLYNGLTISA WNSLDVVTVE
LYPTDRRATG FGFLNALCKA AAVLGNLIFG SLVSITKSIP ILLASTVLVC GGLVGLCLPD
TRTQVLM
