ID 5HT1A_HUMAN Reviewed; 422 AA. AC P08908; Q6LAE7; DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 3. DT 25-OCT-2017, entry version 174. DE RecName: Full=5-hydroxytryptamine receptor 1A; DE Short=5-HT-1A; DE Short=5-HT1A; DE AltName: Full=G-21; DE AltName: Full=Serotonin receptor 1A; GN Name=HTR1A; Synonyms=ADRB2RL1, ADRBRL1; 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 [GENOMIC DNA], TISSUE SPECIFICITY, AND SUBCELLULAR RP LOCATION. RX PubMed=3041227; DOI=10.1038/329075a0; RA Kobilka B.K., Frielle T., Collins S., Yang-Feng T.L., Kobilka T.S., RA Francke U., Lefkowitz R.J., Caron M.G.; RT "An intronless gene encoding a potential member of the family of RT receptors coupled to guanine nucleotide regulatory proteins."; RL Nature 329:75-79(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Saltzman A.G., Morse B., Felder S.; RT "Nucleotide and deduced amino acid sequence of the human serotonin 5- RT HT1a receptor gene."; RL Submitted (FEB-1991) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Levy F.O., Gudermann T., Birnbaumer M., Kaumann A.J., Birnbaumer L.; RL Submitted (MAY-1992) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=15014171; DOI=10.1093/molbev/msh100; RA Kitano T., Liu Y.-H., Ueda S., Saitou N.; RT "Human-specific amino acid changes found in 103 protein-coding RT genes."; RL Mol. Biol. Evol. 21:936-944(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.; RT "cDNA clones of human proteins involved in signal transduction RT sequenced by the Guthrie cDNA resource center (www.cdna.org)."; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. RN [6] 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9. RX PubMed=1766875; DOI=10.1093/nar/19.25.7155; RA Parks C.L., Chang L.S., Shenk T.; RT "A polymerase chain reaction mediated by a single primer: cloning of RT genomic sequences adjacent to a serotonin receptor protein coding RT region."; RL Nucleic Acids Res. 19:7155-7160(1991). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 200-365, FUNCTION, SUBCELLULAR LOCATION, RP AND TISSUE SPECIFICITY. RX PubMed=8393041; RA Aune T.M., McGrath K.M., Sarr T., Bombara M.P., Kelley K.A.; RT "Expression of 5HT1a receptors on activated human T cells. Regulation RT of cyclic AMP levels and T cell proliferation by 5- RT hydroxytryptamine."; RL J. Immunol. 151:1175-1183(1993). RN [9] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=3138543; DOI=10.1038/335358a0; RA Fargin A., Raymond J.R., Lohse M.L., Kobilka B.K., Caron M.G., RA Lefkowitz R.J.; RT "The genomic clone G-21 which resembles a beta-adrenergic receptor RT sequence encodes the 5-HT1A receptor."; RL Nature 335:358-360(1988). RN [10] RP FUNCTION. RX PubMed=8138923; RA Harrington M.A., Shaw K., Zhong P., Ciaranello R.D.; RT "Agonist-induced desensitization and loss of high-affinity binding RT sites of stably expressed human 5-HT1A receptors."; RL J. Pharmacol. Exp. Ther. 268:1098-1106(1994). RN [11] RP REVIEW. RX PubMed=18476671; DOI=10.1021/cr078224o; RA Nichols D.E., Nichols C.D.; RT "Serotonin receptors."; RL Chem. Rev. 108:1614-1641(2008). RN [12] RP REVIEW. RX PubMed=20363322; DOI=10.1016/j.cellsig.2010.03.019; RA Polter A.M., Li X.; RT "5-HT1A receptor-regulated signal transduction pathways in brain."; RL Cell. Signal. 22:1406-1412(2010). RN [13] RP REVIEW. RX PubMed=20945968; RA Pytliak M., Vargova V., Mechirova V., Felsoci M.; RT "Serotonin receptors - from molecular biology to clinical RT applications."; RL Physiol. Res. 60:15-25(2011). RN [14] RP INVOLVEMENT IN PFMC. RX PubMed=21990073; DOI=10.1002/humu.21622; RA Jiang Y.C., Wu H.M., Cheng K.H., Sunny Sun H.; RT "Menstrual cycle-dependent febrile episode mediated by sequence- RT specific repression of poly(ADP-ribose) polymerase-1 on the RT transcription of the human serotonin receptor 1A gene."; RL Hum. Mutat. 33:209-217(2012). RN [15] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=22957663; DOI=10.1111/jnc.12008; RA Singh P., Paila Y.D., Chattopadhyay A.; RT "Role of glycosphingolipids in the function of human serotonin(1)A RT receptors."; RL J. Neurochem. 123:716-724(2012). RN [16] RP SUBUNIT. RX PubMed=23300088; DOI=10.1074/jbc.M112.412478; RA Akama K.T., Thompson L.I., Milner T.A., McEwen B.S.; RT "Post-synaptic density-95 (PSD-95) binding capacity of G-protein- RT coupled receptor 30 (GPR30), an estrogen receptor that can be RT identified in hippocampal dendritic spines."; RL J. Biol. Chem. 288:6438-6450(2013). RN [17] RP VARIANTS SER-22 AND VAL-28. RX PubMed=7755630; DOI=10.1006/bbrc.1995.1692; RA Nakhai B., Nielsen D.A., Linnoila M., Goldman D.; RT "Two naturally occurring amino acid substitutions in the human 5-HT1A RT receptor: glycine 22 to serine 22 and isoleucine 28 to valine 28."; RL Biochem. Biophys. Res. Commun. 210:530-536(1995). RN [18] RP VARIANTS LEU-16 AND ASP-273. RX PubMed=9754630; RX DOI=10.1002/(SICI)1096-8628(19980907)81:5<434::AID-AJMG13>3.0.CO;2-D; RA Kawanishi Y., Harada S., Tachikawa H., Okubo T., Shiraishi H.; RT "Novel mutations in the promoter and coding region of the human 5-HT1A RT receptor gene and association analysis in schizophrenia."; RL Am. J. Med. Genet. 81:434-439(1998). CC -!- FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine CC (serotonin). Also functions as a receptor for various drugs and CC psychoactive substances. Ligand binding causes a conformation CC change that triggers signaling via guanine nucleotide-binding CC proteins (G proteins) and modulates the activity of down-stream CC effectors, such as adenylate cyclase. Beta-arrestin family members CC inhibit signaling via G proteins and mediate activation of CC alternative signaling pathways. Signaling inhibits adenylate CC cyclase activity and activates a phosphatidylinositol-calcium CC second messenger system that regulates the release of Ca(2+) ions CC from intracellular stores. Plays a role in the regulation of 5- CC hydroxytryptamine release and in the regulation of dopamine and 5- CC hydroxytryptamine metabolism. Plays a role in the regulation of CC dopamine and 5-hydroxytryptamine levels in the brain, and thereby CC affects neural activity, mood and behavior. Plays a role in the CC response to anxiogenic stimuli. {ECO:0000269|PubMed:22957663, CC ECO:0000269|PubMed:3138543, ECO:0000269|PubMed:8138923, CC ECO:0000269|PubMed:8393041}. CC -!- SUBUNIT: Heterodimer; heterodimerizes with GPER1. CC {ECO:0000269|PubMed:23300088}. CC -!- INTERACTION: CC P11362:FGFR1; NbExp=11; IntAct=EBI-6570214, EBI-1028277; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22957663, CC ECO:0000269|PubMed:3041227, ECO:0000269|PubMed:3138543, CC ECO:0000269|PubMed:8393041}; Multi-pass membrane protein CC {ECO:0000269|PubMed:22957663, ECO:0000269|PubMed:3041227, CC ECO:0000269|PubMed:3138543, ECO:0000269|PubMed:8393041}. CC -!- TISSUE SPECIFICITY: Detected in lymph nodes, thymus and spleen. CC Detected in activated T-cells, but not in resting T-cells. CC {ECO:0000269|PubMed:3041227, ECO:0000269|PubMed:8393041}. CC -!- DISEASE: Periodic fever, menstrual cycle-dependent (PFMC) CC [MIM:614674]: A condition characterized by recurrent fevers up to CC 40 degrees Celsius associated with the luteal phase of the CC menstrual cycle. Women show menstrual cycle-dependent physiologic CC changes in relation to sex hormone levels. Because ovulation CC triggers a significant change in the hormonal milieu that is CC similar to local inflammation, a 0.5 to 1.0 degree Celsius CC increase in basal body temperature after ovulation is commonly CC associated with progesterone secretion and is believed to be CC triggered by the induction of several inflammatory cytokines. CC {ECO:0000269|PubMed:21990073}. Note=The disease is caused by CC mutations affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. 5- CC hydroxytryptamine receptor subfamily. HTR1A sub-subfamily. 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; M28269; AAA36440.1; -; Genomic_DNA. DR EMBL; X13556; CAA31908.1; -; Genomic_DNA. DR EMBL; X57829; CAA40962.1; -; Genomic_DNA. DR EMBL; M83181; AAA66493.1; -; Genomic_DNA. DR EMBL; AB041403; BAA94488.1; -; Genomic_DNA. DR EMBL; AF498978; AAM21125.1; -; mRNA. DR EMBL; BC069159; AAH69159.1; -; mRNA. DR EMBL; Z11168; CAA77560.1; -; Genomic_DNA. DR CCDS; CCDS34168.1; -. DR PIR; I38209; I38209. DR RefSeq; NP_000515.2; NM_000524.3. DR UniGene; Hs.247940; -. DR ProteinModelPortal; P08908; -. DR BioGrid; 109582; 6. DR CORUM; P08908; -. DR IntAct; P08908; 4. DR STRING; 9606.ENSP00000316244; -. DR BindingDB; P08908; -. DR ChEMBL; CHEMBL214; -. DR DrugBank; DB01614; Acepromazine. DR DrugBank; DB00866; Alprenolol. DR DrugBank; DB01616; Alverine. DR DrugBank; DB00321; Amitriptyline. DR DrugBank; DB00543; Amoxapine. DR DrugBank; DB00714; Apomorphine. DR DrugBank; DB01238; Aripiprazole. DR DrugBank; DB06216; Asenapine. DR DrugBank; DB04888; Bifeprunox. DR DrugBank; DB08807; Bopindolol. DR DrugBank; DB09128; Brexpiprazole. DR DrugBank; DB01200; Bromocriptine. DR DrugBank; DB00490; Buspirone. DR DrugBank; DB00248; Cabergoline. DR DrugBank; DB06016; Cariprazine. DR DrugBank; DB00477; Chlorpromazine. DR DrugBank; DB08810; Cinitapride. DR DrugBank; DB00363; Clozapine. DR DrugBank; DB04884; Dapoxetine. DR DrugBank; DB01151; Desipramine. DR DrugBank; DB00988; Dopamine. DR DrugBank; DB01142; Doxepin. DR DrugBank; DB00216; Eletriptan. DR DrugBank; DB01049; Ergoloid mesylate. DR DrugBank; DB00696; Ergotamine. DR DrugBank; DB04908; Flibanserin. DR DrugBank; DB04946; Iloperidone. DR DrugBank; DB00458; Imipramine. DR DrugBank; DB01221; Ketamine. DR DrugBank; DB04970; Lesopitron. DR DrugBank; DB05509; LI-301. DR DrugBank; DB00589; Lisuride. DR DrugBank; DB00408; Loxapine. DR DrugBank; DB08815; Lurasidone. DR DrugBank; DB04829; Lysergic Acid Diethylamide. DR DrugBank; DB00247; Methysergide. DR DrugBank; DB06148; Mianserin. DR DrugBank; DB05339; MN-305. DR DrugBank; DB01618; Molindone. DR DrugBank; DB00952; Naratriptan. DR DrugBank; DB01149; Nefazodone. DR DrugBank; DB00540; Nortriptyline. DR DrugBank; DB00334; Olanzapine. DR DrugBank; DB00904; Ondansetron. DR DrugBank; DB01267; Paliperidone. DR DrugBank; DB01359; Penbutolol. DR DrugBank; DB01186; Pergolide. DR DrugBank; DB00960; Pindolol. DR DrugBank; DB01621; Pipotiazine. DR DrugBank; DB00413; Pramipexole. DR DrugBank; DB00571; Propranolol. DR DrugBank; DB01224; Quetiapine. DR DrugBank; DB00734; Risperidone. DR DrugBank; DB00268; Ropinirole. DR DrugBank; DB05271; Rotigotine. DR DrugBank; DB05280; SLV 308. DR DrugBank; DB00669; Sumatriptan. DR DrugBank; DB01622; Thioproperazine. DR DrugBank; DB13025; Tiapride. DR DrugBank; DB00656; Trazodone. DR DrugBank; DB00726; Trimipramine. DR DrugBank; DB06684; Vilazodone. DR DrugBank; DB09068; Vortioxetine. DR DrugBank; DB01392; Yohimbine. DR DrugBank; DB00246; Ziprasidone. DR DrugBank; DB00315; Zolmitriptan. DR GuidetoPHARMACOLOGY; 1; -. DR iPTMnet; P08908; -. DR PhosphoSitePlus; P08908; -. DR BioMuta; HTR1A; -. DR DMDM; 231454; -. DR PaxDb; P08908; -. DR PeptideAtlas; P08908; -. DR PRIDE; P08908; -. DR DNASU; 3350; -. DR Ensembl; ENST00000323865; ENSP00000316244; ENSG00000178394. DR GeneID; 3350; -. DR KEGG; hsa:3350; -. DR CTD; 3350; -. DR DisGeNET; 3350; -. DR EuPathDB; HostDB:ENSG00000178394.4; -. DR GeneCards; HTR1A; -. DR HGNC; HGNC:5286; HTR1A. DR HPA; HPA018073; -. DR MalaCards; HTR1A; -. DR MIM; 109760; gene. DR MIM; 614674; phenotype. DR neXtProt; NX_P08908; -. DR OpenTargets; ENSG00000178394; -. DR PharmGKB; PA192; -. DR eggNOG; KOG3656; Eukaryota. DR eggNOG; ENOG410XRW9; LUCA. DR GeneTree; ENSGT00760000118795; -. DR HOGENOM; HOG000239242; -. DR HOVERGEN; HBG106962; -. DR InParanoid; P08908; -. DR KO; K04153; -. DR OMA; YQVLNKW; -. DR OrthoDB; EOG091G06VI; -. DR PhylomeDB; P08908; -. DR TreeFam; TF316350; -. DR Reactome; R-HSA-390666; Serotonin receptors. DR Reactome; R-HSA-418594; G alpha (i) signalling events. DR SIGNOR; P08908; -. DR GenomeRNAi; 3350; -. DR PRO; PR:P08908; -. DR Proteomes; UP000005640; Chromosome 5. DR Bgee; ENSG00000178394; -. DR CleanEx; HS_HTR1A; -. DR ExpressionAtlas; P08908; baseline and differential. DR Genevisible; P08908; HS. DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0004993; F:G-protein coupled serotonin receptor activity; IDA:UniProtKB. DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central. DR GO; GO:0090722; F:receptor-receptor interaction; IDA:ParkinsonsUK-UCL. DR GO; GO:0051378; F:serotonin binding; IBA:GO_Central. DR GO; GO:0007198; P:adenylate cyclase-inhibiting serotonin receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0001662; P:behavioral fear response; ISS:UniProtKB. DR GO; GO:0008283; P:cell proliferation; IEA:InterPro. DR GO; GO:0035640; P:exploration behavior; ISS:UniProtKB. DR GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IMP:UniProtKB. DR GO; GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc. DR GO; GO:0050795; P:regulation of behavior; IEA:InterPro. DR GO; GO:0042053; P:regulation of dopamine metabolic process; ISS:UniProtKB. DR GO; GO:0046883; P:regulation of hormone secretion; IEA:InterPro. DR GO; GO:0014062; P:regulation of serotonin secretion; ISS:UniProtKB. DR GO; GO:0042428; P:serotonin metabolic process; ISS:UniProtKB. DR GO; GO:0007210; P:serotonin receptor signaling pathway; ISS:UniProtKB. DR GO; GO:0042310; P:vasoconstriction; IEA:InterPro. DR CDD; cd15330; 7tmA_5-HT1A_vertebrates; 1. DR InterPro; IPR000610; 5HT1A_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR017452; GPCR_Rhodpsn_7TM. DR PANTHER; PTHR24247:SF20; PTHR24247:SF20; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00512; 5HT1ARECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR SMART; SM01381; 7TM_GPCR_Srsx; 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; Complete proteome; Disulfide bond; KW G-protein coupled receptor; Glycoprotein; Membrane; Polymorphism; KW Receptor; Reference proteome; Transducer; Transmembrane; KW Transmembrane helix. FT CHAIN 1 422 5-hydroxytryptamine receptor 1A. FT /FTId=PRO_0000068903. FT TOPO_DOM 1 36 Extracellular. {ECO:0000250}. FT TRANSMEM 37 62 Helical; Name=1. {ECO:0000250}. FT TOPO_DOM 63 73 Cytoplasmic. {ECO:0000250}. FT TRANSMEM 74 98 Helical; Name=2. {ECO:0000250}. FT TOPO_DOM 99 110 Extracellular. {ECO:0000250}. FT TRANSMEM 111 132 Helical; Name=3. {ECO:0000250}. FT TOPO_DOM 133 152 Cytoplasmic. {ECO:0000250}. FT TRANSMEM 153 178 Helical; Name=4. {ECO:0000250}. FT TOPO_DOM 179 191 Extracellular. {ECO:0000250}. FT TRANSMEM 192 217 Helical; Name=5. {ECO:0000250}. FT TOPO_DOM 218 345 Cytoplasmic. {ECO:0000250}. FT TRANSMEM 346 367 Helical; Name=6. {ECO:0000250}. FT TOPO_DOM 368 378 Extracellular. {ECO:0000250}. FT TRANSMEM 379 403 Helical; Name=7. {ECO:0000250}. FT TOPO_DOM 404 422 Cytoplasmic. {ECO:0000250}. FT REGION 112 121 Agonist binding. {ECO:0000250}. FT REGION 358 362 Agonist binding. {ECO:0000250}. FT MOTIF 133 135 DRY motif; important for ligand-induced FT conformation changes. {ECO:0000250}. FT MOTIF 396 400 NPxxY motif; important for ligand-induced FT conformation changes and signaling. FT {ECO:0000250}. FT CARBOHYD 10 10 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 11 11 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 24 24 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 109 187 {ECO:0000255|PROSITE-ProRule:PRU00521}. FT VARIANT 16 16 P -> L (in dbSNP:rs1800041). FT {ECO:0000269|PubMed:9754630}. FT /FTId=VAR_003446. FT VARIANT 22 22 G -> S (in dbSNP:rs1799920). FT {ECO:0000269|PubMed:7755630}. FT /FTId=VAR_011826. FT VARIANT 28 28 I -> V (in dbSNP:rs1799921). FT {ECO:0000269|PubMed:7755630}. FT /FTId=VAR_011827. FT VARIANT 184 184 P -> L (in dbSNP:rs1800043). FT /FTId=VAR_011828. FT VARIANT 220 220 R -> L (in dbSNP:rs1800044). FT /FTId=VAR_011829. FT VARIANT 273 273 G -> D (in dbSNP:rs1800042). FT {ECO:0000269|PubMed:9754630}. FT /FTId=VAR_011830. FT CONFLICT 152 154 RAA -> PR (in Ref. 1; AAA36440/CAA31908). FT {ECO:0000305}. FT CONFLICT 172 172 M -> I (in Ref. 1; AAA36440/CAA31908). FT {ECO:0000305}. FT CONFLICT 200 202 TFG -> RPR (in Ref. 8; no nucleotide FT entry). {ECO:0000305}. FT CONFLICT 228 228 K -> R (in Ref. 8; no nucleotide entry). FT {ECO:0000305}. FT CONFLICT 244 244 A -> AA (in Ref. 8; no nucleotide entry). FT {ECO:0000305}. FT CONFLICT 355 355 I -> T (in Ref. 8; no nucleotide entry). FT {ECO:0000305}. FT CONFLICT 363 365 IVA -> MRP (in Ref. 8; no nucleotide FT entry). {ECO:0000305}. FT CONFLICT 418 418 K -> N (in Ref. 1; AAA36440/CAA31908). FT {ECO:0000305}. SQ SEQUENCE 422 AA; 46107 MW; 762664FCF62CFD8F CRC64; MDVLSPGQGN NTTSPPAPFE TGGNTTGISD VTVSYQVITS LLLGTLIFCA VLGNACVVAA IALERSLQNV ANYLIGSLAV TDLMVSVLVL PMAALYQVLN KWTLGQVTCD LFIALDVLCC TSSILHLCAI ALDRYWAITD PIDYVNKRTP RRAAALISLT WLIGFLISIP PMLGWRTPED RSDPDACTIS KDHGYTIYST FGAFYIPLLL MLVLYGRIFR AARFRIRKTV KKVEKTGADT RHGASPAPQP KKSVNGESGS RNWRLGVESK AGGALCANGA VRQGDDGAAL EVIEVHRVGN SKEHLPLPSE AGPTPCAPAS FERKNERNAE AKRKMALARE RKTVKTLGII MGTFILCWLP FFIVALVLPF CESSCHMPTL LGAIINWLGY SNSLLNPVIY AYFNKDFQNA FKKIIKCKFC RQ //