ID 5HT2A_MOUSE Reviewed; 471 AA. AC P35363; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 02-SEP-2026, entry version 189. DE RecName: Full=5-hydroxytryptamine receptor 2A; DE Short=5-HT-2; DE Short=5-HT-2A; DE AltName: Full=Serotonin receptor 2A; GN Name=Htr2a; Synonyms=Htr2; 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 TISSUE=Brain; RX PubMed=1333538; DOI=10.1002/jnr.490330203; RA Yang W., Chen K., Lan N.C., Gallaher T.K., Shih J.C.; RT "Gene structure and expression of the mouse 5-HT2 receptor."; RL J. Neurosci. Res. 33:196-204(1992). RN [2] RP DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RX PubMed=11960784; DOI=10.1152/ajpgi.00435.2001; RA Fiorica-Howells E., Hen R., Gingrich J., Li Z., Gershon M.D.; RT "5-HT(2A) receptors: location and functional analysis in intestines of RT wild-type and 5-HT(2A) knockout mice."; RL Am. J. Physiol. 282:G877-G893(2002). RN [3] RP SUBCELLULAR LOCATION. RX PubMed=14988405; DOI=10.1074/jbc.m312106200; RA Becamel C., Gavarini S., Chanrion B., Alonso G., Galeotti N., Dumuis A., RA Bockaert J., Marin P.; RT "The serotonin 5-HT2A and 5-HT2C receptors interact with specific sets of RT PDZ proteins."; RL J. Biol. Chem. 279:20257-20266(2004). RN [4] RP DISRUPTION PHENOTYPE, AND FUNCTION. RX PubMed=16873667; DOI=10.1126/science.1123432; RA Weisstaub N.V., Zhou M., Lira A., Lambe E., Gonzalez-Maeso J., RA Hornung J.P., Sibille E., Underwood M., Itohara S., Dauer W.T., RA Ansorge M.S., Morelli E., Mann J.J., Toth M., Aghajanian G., Sealfon S.C., RA Hen R., Gingrich J.A.; RT "Cortical 5-HT2A receptor signaling modulates anxiety-like behaviors in RT mice."; RL Science 313:536-540(2006). RN [5] RP DISRUPTION PHENOTYPE, AND FUNCTION. RX PubMed=17270739; DOI=10.1016/j.neuron.2007.01.008; RA Gonzalez-Maeso J., Weisstaub N.V., Zhou M., Chan P., Ivic L., Ang R., RA Lira A., Bradley-Moore M., Ge Y., Zhou Q., Sealfon S.C., Gingrich J.A.; RT "Hallucinogens recruit specific cortical 5-HT(2A) receptor-mediated RT signaling pathways to affect behavior."; RL Neuron 53:439-452(2007). RN [6] RP INTERACTION WITH GRM2, FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR RP LOCATION. RX PubMed=18297054; DOI=10.1038/nature06612; RA Gonzalez-Maeso J., Ang R.L., Yuen T., Chan P., Weisstaub N.V., RA Lopez-Gimenez J.F., Zhou M., Okawa Y., Callado L.F., Milligan G., RA Gingrich J.A., Filizola M., Meana J.J., Sealfon S.C.; RT "Identification of a serotonin/glutamate receptor complex implicated in RT psychosis."; RL Nature 452:93-97(2008). RN [7] RP INTERACTION WITH DRD2, FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=21645528; DOI=10.1016/j.neuropharm.2011.05.023; RA Albizu L., Holloway T., Gonzalez-Maeso J., Sealfon S.C.; RT "Functional crosstalk and heteromerization of serotonin 5-HT2A and dopamine RT D2 receptors."; RL Neuropharmacology 61:770-777(2011). RN [8] RP FUNCTION. RX PubMed=23346101; DOI=10.1155/2012/398406; RA Nelson P.M., Harrod J.S., Lamping K.G.; RT "5HT(2A) and 5HT(2B) receptors contribute to serotonin-induced vascular RT dysfunction in diabetes."; RL Exp. Diabetes Res. 2012:398406-398406(2012). RN [9] RP FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION. RX PubMed=23129762; DOI=10.1074/jbc.m112.413161; RA Moreno J.L., Muguruza C., Umali A., Mortillo S., Holloway T., RA Pilar-Cuellar F., Mocci G., Seto J., Callado L.F., Neve R.L., Milligan G., RA Sealfon S.C., Lopez-Gimenez J.F., Meana J.J., Benson D.L., RA Gonzalez-Maeso J.; RT "Identification of three residues essential for 5-hydroxytryptamine 2A- RT metabotropic glutamate 2 (5-HT2A.mGlu2) receptor heteromerization and its RT psychoactive behavioral function."; RL J. Biol. Chem. 287:44301-44319(2012). CC -!- FUNCTION: G protein-coupled receptor for 5-hydroxytryptamine CC (serotonin) (PubMed:11960784, PubMed:16873667, PubMed:17270739, CC PubMed:18297054, PubMed:21645528, PubMed:23129762, PubMed:23346101). CC Also functions as a receptor for various drugs and psychoactive CC substances, including mescaline, psilocybin, 1-(2,5-dimethoxy-4- CC iodophenyl)-2-aminopropane (DOI) and lysergic acid diethylamide (LSD) CC (By similarity). Ligand binding causes a conformation change that CC triggers signaling via guanine nucleotide-binding proteins (G proteins) CC and modulates the activity of downstream effectors (By similarity). CC HTR2A is coupled to G(q)/G(11) G alpha proteins and activates CC phospholipase C-beta, releasing diacylglycerol (DAG) and inositol CC 1,4,5-trisphosphate (IP3) second messengers that modulate the activity CC of phosphatidylinositol 3-kinase and promote the release of Ca(2+) ions CC from intracellular stores, respectively (By similarity). Beta-arrestin CC family members inhibit signaling via G proteins and mediate activation CC of alternative signaling pathways (PubMed:18297054). Affects neural CC activity, perception, cognition and mood (PubMed:18297054). Plays a CC role in the regulation of behavior, including responses to anxiogenic CC situations and psychoactive substances (PubMed:16873667, CC PubMed:17270739, PubMed:18297054, PubMed:23129762). Plays a role in CC intestinal smooth muscle contraction, and may play a role in arterial CC vasoconstriction (PubMed:11960784, PubMed:23346101). CC {ECO:0000250|UniProtKB:P28223, ECO:0000269|PubMed:11960784, CC ECO:0000269|PubMed:16873667, ECO:0000269|PubMed:17270739, CC ECO:0000269|PubMed:18297054, ECO:0000269|PubMed:21645528, CC ECO:0000269|PubMed:23129762, ECO:0000269|PubMed:23346101}. CC -!- ACTIVITY REGULATION: G protein-coupled receptor activity is regulated CC by lipids: oleamide increases HTR2A-mediated activity. CC {ECO:0000250|UniProtKB:P28223}. CC -!- SUBUNIT: Interacts (via C-terminus) with MPDZ and PATJ (By similarity). CC May interact (via C-terminus) with MPP3, PRDX6, DLG4, DLG1, CASK, APBA1 CC and MAGI2 (By similarity). Interacts with GRM2 and DRD2; this may CC affect signaling (PubMed:18297054, PubMed:21645528). CC {ECO:0000250|UniProtKB:P28223, ECO:0000269|PubMed:18297054, CC ECO:0000269|PubMed:21645528}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21645528}; CC Multi-pass membrane protein {ECO:0000305}. Cell projection, dendrite CC {ECO:0000269|PubMed:11960784}. Cell projection, axon CC {ECO:0000250|UniProtKB:P14842}. Cytoplasmic vesicle CC {ECO:0000269|PubMed:11960784}. Membrane, caveola CC {ECO:0000250|UniProtKB:P14842}. Presynapse CC {ECO:0000250|UniProtKB:P14842}. CC -!- TISSUE SPECIFICITY: Detected in neurons in brain cortex. Detected in CC adult intestine, especially in mucosal epithelium, longitudinal and CC circular layers of muscularis externa and myenteric plexuses. Highly CC expressed in Paneth cells, and detected at lower levels in enterocytes CC (at protein level). Detected in neurons in the brain cortex. CC {ECO:0000269|PubMed:11960784, ECO:0000269|PubMed:18297054, CC ECO:0000269|PubMed:23129762}. CC -!- DOMAIN: The PDZ domain-binding motif is involved in the interaction CC with PATJ, CASK, APBA1, DLG1 and DLG4. {ECO:0000250|UniProtKB:P28223}. CC -!- DISRUPTION PHENOTYPE: Mutant mice display increased exploratory CC behavior in open spaces and reduced anxiety-like behavior CC (PubMed:16873667). Mutant mice fail to show behavorial responses to CC psychoactive substances and hallucinogens, such as mescaline, CC psilocybin, 1-(2,5-dimethoxy-4-iodophenyl)-2-aminopropane (DOI), 1- CC (2,5-dimethoxy-4-bromophenyl)-2-aminopropane and lysergic acid CC diethylamide (LSD) (PubMed:17270739). Besides, the colon from mutant CC mice does not contract in response to 5-hydroxytryptamine CC (PubMed:11960784). {ECO:0000269|PubMed:11960784, CC ECO:0000269|PubMed:16873667, ECO:0000269|PubMed:17270739}. CC -!- SIMILARITY: Belongs to the G protein-coupled receptor 1 family. CC {ECO:0000255|PROSITE-ProRule:PRU00521}. 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; S49542; AAB24369.1; -; mRNA. DR CCDS; CCDS27275.1; -. DR PIR; S40689; S40689. DR RefSeq; NP_766400.1; NM_172812.3. DR AlphaFoldDB; P35363; -. DR SMR; P35363; -. DR BioGRID; 200472; 1. DR CORUM; P35363; -. DR FunCoup; P35363; 785. DR IntAct; P35363; 1. DR STRING; 10090.ENSMUSP00000047774; -. DR BindingDB; P35363; -. DR ChEMBL; CHEMBL5377; -. DR DrugCentral; P35363; -. DR GlyCosmos; P35363; 5 sites, No reported glycans. DR GlyGen; P35363; 5 sites, 1 N-linked glycan (1 site). DR iPTMnet; P35363; -. DR PhosphoSitePlus; P35363; -. DR SwissPalm; P35363; -. DR PaxDb; 10090-ENSMUSP00000047774; -. DR ProteomicsDB; 285689; -. DR Antibodypedia; 2927; 358 antibodies from 35 providers. DR DNASU; 15558; -. DR Ensembl; ENSMUST00000036653.5; ENSMUSP00000047774.4; ENSMUSG00000034997.6. DR GeneID; 15558; -. DR KEGG; mmu:15558; -. DR UCSC; uc007uqc.1; mouse. DR AGR; MGI:109521; -. DR CTD; 3356; -. DR MGI; MGI:109521; Htr2a. DR VEuPathDB; HostDB:ENSMUSG00000034997; -. DR eggNOG; KOG3656; Eukaryota. DR GeneTree; ENSGT01050000244937; -. DR HOGENOM; CLU_009579_11_3_1; -. DR InParanoid; P35363; -. DR OMA; MVTIGIH; -. DR OrthoDB; 420518at2759; -. DR PhylomeDB; P35363; -. DR Reactome; R-MMU-390666; Serotonin receptors. DR Reactome; R-MMU-416476; G alpha (q) signalling events. DR BioGRID-ORCS; 15558; 1 hit in 79 CRISPR screens. DR PRO; PR:P35363; -. DR Proteomes; UP000000589; Chromosome 14. DR RNAct; P35363; protein. DR Bgee; ENSMUSG00000034997; Expressed in superior frontal gyrus and 35 other cell types or tissues. DR ExpressionAtlas; P35363; baseline and differential. DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell. DR GO; GO:0005901; C:caveola; IEA:UniProtKB-SubCell. DR GO; GO:0070852; C:cell body fiber; ISO:GO_Central. DR GO; GO:0031410; C:cytoplasmic vesicle; EXP:UniProtKB. DR GO; GO:0030425; C:dendrite; ISO:GO_Central. DR GO; GO:0043198; C:dendritic shaft; ISO:GO_Central. DR GO; GO:0098666; C:G protein-coupled serotonin receptor complex; ISO:GO_Central. DR GO; GO:0098978; C:glutamatergic synapse; ISO:GO_Central. DR GO; GO:0005883; C:neurofilament; ISO:GO_Central. DR GO; GO:0043025; C:neuronal cell body; ISO:GO_Central. DR GO; GO:0005886; C:plasma membrane; EXP:UniProtKB. DR GO; GO:0045211; C:postsynaptic membrane; ISO:GO_Central. DR GO; GO:0098793; C:presynapse; ISS:UniProtKB. DR GO; GO:0042734; C:presynaptic membrane; ISO:GO_Central. DR GO; GO:0071886; F:1-(4-iodo-2,5-dimethoxyphenyl)propan-2-amine binding; ISO:GO_Central. DR GO; GO:0004993; F:G protein-coupled serotonin receptor activity; ISO:GO_Central. DR GO; GO:0001587; F:Gq/11-coupled serotonin receptor activity; ISO:GO_Central. DR GO; GO:0042802; F:identical protein binding; ISO:GO_Central. DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central. DR GO; GO:0030296; F:protein tyrosine kinase activator activity; IMP:MGI. DR GO; GO:0044877; F:protein-containing complex binding; ISO:GO_Central. DR GO; GO:0051378; F:serotonin binding; ISO:GO_Central. DR GO; GO:0099589; F:serotonin receptor activity; ISO:GO_Central. DR GO; GO:0014824; P:artery smooth muscle contraction; ISO:GO_Central. DR GO; GO:0048148; P:behavioral response to cocaine; ISO:GO_Central. DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central. DR GO; GO:0050966; P:detection of mechanical stimulus involved in sensory perception of pain; ISO:GO_Central. DR GO; GO:0050965; P:detection of temperature stimulus involved in sensory perception of pain; ISO:GO_Central. DR GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; IBA:GO_Central. DR GO; GO:0098664; P:G protein-coupled serotonin receptor signaling pathway; ISO:GO_Central. DR GO; GO:0006874; P:intracellular calcium ion homeostasis; ISO:GO_Central. DR GO; GO:0007613; P:memory; ISO:GO_Central. DR GO; GO:0043267; P:negative regulation of potassium ion transport; ISO:GO_Central. DR GO; GO:0051967; P:negative regulation of synaptic transmission, glutamatergic; ISO:GO_Central. DR GO; GO:0007208; P:phospholipase C-activating serotonin receptor signaling pathway; ISO:GO_Central. DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:GO_Central. DR GO; GO:0002720; P:positive regulation of cytokine production involved in immune response; ISO:GO_Central. DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:GO_Central. DR GO; GO:2000573; P:positive regulation of DNA biosynthetic process; ISO:GO_Central. DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:GO_Central. DR GO; GO:1900119; P:positive regulation of execution phase of apoptosis; ISO:GO_Central. DR GO; GO:0045600; P:positive regulation of fat cell differentiation; IMP:MGI. DR GO; GO:0045821; P:positive regulation of glycolytic process; IMP:MGI. DR GO; GO:0031652; P:positive regulation of heat generation; ISO:GO_Central. DR GO; GO:0050729; P:positive regulation of inflammatory response; ISO:GO_Central. DR GO; GO:0043406; P:positive regulation of MAP kinase activity; ISO:GO_Central. DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISO:GO_Central. DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IMP:MGI. DR GO; GO:0010513; P:positive regulation of phosphatidylinositol biosynthetic process; ISO:GO_Central. DR GO; GO:1901731; P:positive regulation of platelet aggregation; ISO:GO_Central. DR GO; GO:0045907; P:positive regulation of vasoconstriction; ISO:GO_Central. DR GO; GO:0099171; P:presynaptic modulation of chemical synaptic transmission; ISO:GO_Central. DR GO; GO:0044380; P:protein localization to cytoskeleton; IDA:MGI. DR GO; GO:0014059; P:regulation of dopamine secretion; ISO:GO_Central. DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; ISO:GO_Central. DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:GO_Central. DR GO; GO:0046960; P:sensitization; ISO:GO_Central. DR GO; GO:0050951; P:sensory perception of temperature stimulus; ISO:GO_Central. DR GO; GO:0007210; P:serotonin receptor signaling pathway; IBA:GO_Central. DR GO; GO:0001659; P:temperature homeostasis; ISO:GO_Central. DR GO; GO:0014832; P:urinary bladder smooth muscle contraction; ISO:GO_Central. DR CDD; cd15304; 7tmA_5-HT2A; 1. DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1. DR InterPro; IPR000455; 5HT2A_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR017452; GPCR_Rhodpsn_7TM. DR PANTHER; PTHR24247; 5-HYDROXYTRYPTAMINE RECEPTOR; 1. DR PANTHER; PTHR24247:SF30; 5-HYDROXYTRYPTAMINE RECEPTOR 2A; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00516; 5HT2ARECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR SMART; SM01381; 7TM_GPCR_Srsx; 1. DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. PE 1: Evidence at protein level; KW Behavior; Cell membrane; Cell projection; Cytoplasmic vesicle; KW Disulfide bond; G protein-coupled receptor; Glycoprotein; Membrane; KW Phosphoprotein; Receptor; Reference proteome; Synapse; Transducer; KW Transmembrane; Transmembrane helix. FT CHAIN 1..471 FT /note="5-hydroxytryptamine receptor 2A" FT /id="PRO_0000068948" FT TOPO_DOM 1..80 FT /note="Extracellular" FT /evidence="ECO:0000250|UniProtKB:P28223" FT TRANSMEM 81..97 FT /note="Helical; Name=1" FT /evidence="ECO:0000250|UniProtKB:P28223" FT TOPO_DOM 98..111 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:P28223" FT TRANSMEM 112..137 FT /note="Helical; Name=2" FT /evidence="ECO:0000250|UniProtKB:P28223" FT TOPO_DOM 138..146 FT /note="Extracellular" FT /evidence="ECO:0000250|UniProtKB:P28223" FT TRANSMEM 147..171 FT /note="Helical; Name=3" FT /evidence="ECO:0000250|UniProtKB:P28223" FT TOPO_DOM 172..191 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:P28223" FT TRANSMEM 192..215 FT /note="Helical; Name=4" FT /evidence="ECO:0000250|UniProtKB:P28223" FT TOPO_DOM 216..232 FT /note="Extracellular" FT /evidence="ECO:0000250|UniProtKB:P28223" FT TRANSMEM 233..258 FT /note="Helical; Name=5" FT /evidence="ECO:0000250|UniProtKB:P28223" FT TOPO_DOM 259..322 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:P28223" FT TRANSMEM 323..348 FT /note="Helical; Name=6" FT /evidence="ECO:0000250|UniProtKB:P28223" FT TOPO_DOM 349..356 FT /note="Extracellular" FT /evidence="ECO:0000250|UniProtKB:P28223" FT TRANSMEM 357..382 FT /note="Helical; Name=7" FT /evidence="ECO:0000250|UniProtKB:P28223" FT TOPO_DOM 383..471 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:P28223" FT MOTIF 172..174 FT /note="DRY motif; important for ligand-induced conformation FT changes" FT /evidence="ECO:0000250|UniProtKB:P41595" FT MOTIF 376..380 FT /note="NPxxY motif; important for ligand-induced FT conformation changes and signaling" FT /evidence="ECO:0000250|UniProtKB:P41595" FT MOTIF 469..471 FT /note="PDZ-binding" FT /evidence="ECO:0000250|UniProtKB:P28223" FT BINDING 155 FT /ligand="serotonin" FT /ligand_id="ChEBI:CHEBI:350546" FT /evidence="ECO:0000250|UniProtKB:P28223" FT BINDING 343 FT /ligand="serotonin" FT /ligand_id="ChEBI:CHEBI:350546" FT /evidence="ECO:0000250|UniProtKB:P28223" FT SITE 229 FT /note="Hydrophobic barrier that decreases the speed of FT ligand binding and dissociation" FT /evidence="ECO:0000250|UniProtKB:P28223" FT MOD_RES 280 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P28223" FT CARBOHYD 8 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 38 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 44 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 51 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 54 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 148..227 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521" FT DISULFID 349..353 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521" SQ SEQUENCE 471 AA; 52842 MW; DE763E5617EE8435 CRC64; MEILCEDNIS LSSIPNSLMQ LGDDSRLYPN DFNSRDANTS EASNWTIDAE NRTNLSCEGY LPPTCLSILH LQEKNWSALL TTVVIILTIA GNILVIMAVS LEKKLQNATN YFLMSLAIAD MLLGFLVMPV SMLTILYGYR WPLPSKLCAV WIYLDVLFST ASIMHLCAIS LDRYVAIQNP IHHSRFNSRT KAFLKIIAVW TISVGISMPI PVFGLQDDSK VFKEGSCLLA DDNFVLIGSF VAFFIPLTIM VITYFLTIKS LQKEATLCVS DLSTRAKLSS FSFLPQSSLS SEKLFQRSIH REPGSYAGRR TMQSISNEQK ACKVLGIVFF LFVVMWCPFF ITNIMAVICK ESCNENVIGA LLNVFVWIGY LSSAVNPLVY TLFNKTYRSA FSRYIQCQYK ENRKPLQLIL VNTIPTLAYK SSQLQVGQKK NSQEDAEPTA NDCSMVTLGN QHSEEMCTDN IETVNEKVSC V //