ID   5HT1A_MOUSE             Reviewed;         421 AA.
AC   Q64264; Q60956; Q61617; Q8BGS4;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   27-MAR-2024, entry version 186.
DE   RecName: Full=5-hydroxytryptamine receptor 1A;
DE            Short=5-HT-1A;
DE            Short=5-HT1A;
DE   AltName: Full=Serotonin receptor 1A;
GN   Name=Htr1a; Synonyms=Gpcr18;
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], FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=NIH Swiss; TISSUE=Brain;
RX   PubMed=8254366; DOI=10.1523/jneurosci.13-12-05164.1993;
RA   Charest A., Wainer B.H., Albert P.R.;
RT   "Cloning and differentiation-induced expression of a murine serotonin 1A
RT   receptor in a septal cell line.";
RL   J. Neurosci. 13:5164-5171(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Brain cortex, Corpora quadrigemina, and Hippocampus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
RC   STRAIN=C3H/An;
RX   PubMed=8626793; DOI=10.1074/jbc.271.8.4417;
RA   Parks C.L., Shenk T.;
RT   "The serotonin 1a receptor gene contains a TATA-less promoter that responds
RT   to MAZ and Sp1.";
RL   J. Biol. Chem. 271:4417-4430(1996).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 136-353.
RC   TISSUE=Testis;
RX   PubMed=8288218; DOI=10.1006/geno.1993.1452;
RA   Wilkie T.M., Chen Y., Gilbert D.J., Moore K.J., Yu L., Simon M.I.,
RA   Copeland N.G., Jenkins N.A.;
RT   "Identification, chromosomal location, and genome organization of mammalian
RT   G-protein-coupled receptors.";
RL   Genomics 18:175-184(1993).
RN   [7]
RP   DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND FUNCTION.
RX   PubMed=9826725; DOI=10.1073/pnas.95.24.14476;
RA   Ramboz S., Oosting R., Amara D.A., Kung H.F., Blier P., Mendelsohn M.,
RA   Mann J.J., Brunner D., Hen R.;
RT   "Serotonin receptor 1A knockout: an animal model of anxiety-related
RT   disorder.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:14476-14481(1998).
RN   [8]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=11080193; DOI=10.1046/j.1471-4159.2000.0752415.x;
RA   Ase A.R., Reader T.A., Hen R., Riad M., Descarries L.;
RT   "Altered serotonin and dopamine metabolism in the CNS of serotonin 5-HT(1A)
RT   or 5-HT(1B) receptor knockout mice.";
RL   J. Neurochem. 75:2415-2426(2000).
RN   [9]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=17543467; DOI=10.1016/j.neuroscience.2007.04.004;
RA   Deng D.R., Djalali S., Holtje M., Grosse G., Stroh T., Voigt I.,
RA   Kusserow H., Theuring F., Ahnert-Hilger G., Hortnagl H.;
RT   "Embryonic and postnatal development of the serotonergic raphe system and
RT   its target regions in 5-HT1A receptor deletion or overexpressing mouse
RT   mutants.";
RL   Neuroscience 147:388-402(2007).
RN   [10]
RP   FUNCTION.
RX   PubMed=18599790; DOI=10.1126/science.1157871;
RA   Audero E., Coppi E., Mlinar B., Rossetti T., Caprioli A.,
RA   Banchaabouchi M.A., Corradetti R., Gross C.;
RT   "Sporadic autonomic dysregulation and death associated with excessive
RT   serotonin autoinhibition.";
RL   Science 321:130-133(2008).
RN   [11]
RP   FUNCTION.
RX   PubMed=21508226; DOI=10.1523/jneurosci.5836-10.2011;
RA   Richardson-Jones J.W., Craige C.P., Nguyen T.H., Kung H.F., Gardier A.M.,
RA   Dranovsky A., David D.J., Guiard B.P., Beck S.G., Hen R., Leonardo E.D.;
RT   "Serotonin-1A autoreceptors are necessary and sufficient for the normal
RT   formation of circuits underlying innate anxiety.";
RL   J. Neurosci. 31:6008-6018(2011).
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 change
CC       that triggers signaling via guanine nucleotide-binding proteins (G
CC       proteins) and modulates the activity of down-stream effectors, such as
CC       adenylate cyclase. Beta-arrestin family members inhibit signaling via G
CC       proteins and mediate activation of alternative signaling pathways.
CC       Signaling inhibits adenylate cyclase activity and activates a
CC       phosphatidylinositol-calcium second messenger system that regulates the
CC       release of Ca(2+) ions from intracellular stores. Plays a role in the
CC       regulation of 5-hydroxytryptamine release and in the regulation of
CC       dopamine and 5-hydroxytryptamine metabolism. Plays a role in the
CC       regulation of dopamine and 5-hydroxytryptamine levels in the brain, and
CC       thereby affects neural activity, mood and behavior. Plays a role in the
CC       response to anxiogenic stimuli. {ECO:0000269|PubMed:11080193,
CC       ECO:0000269|PubMed:17543467, ECO:0000269|PubMed:18599790,
CC       ECO:0000269|PubMed:21508226, ECO:0000269|PubMed:8254366,
CC       ECO:0000269|PubMed:9826725}.
CC   -!- SUBUNIT: Heterodimer; heterodimerizes with GPER1. Interacts with YIF1B
CC       (By similarity). Interacts with GPR39 and GALR1 (By similarity).
CC       {ECO:0000250|UniProtKB:P08908, ECO:0000250|UniProtKB:P19327}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8254366};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:8254366}. Cell
CC       projection, dendrite {ECO:0000250|UniProtKB:P19327}.
CC   -!- TISSUE SPECIFICITY: Most abundantly expressed in midbrain, in dorsal
CC       raphe and hippocampus. Detected at lower levels in amygdala and brain
CC       cortex. {ECO:0000269|PubMed:9826725}.
CC   -!- DISRUPTION PHENOTYPE: Mutant mice display decreased exploratory
CC       behavior and increased fear-related behavior in anxiogenic
CC       environments. Mutant mice display altered monoamine metabolism in
CC       specific parts of the brain, especially in dorsal and medial raphe
CC       nuclei, thalamus and hypothalamus, leading to altered levels of 5-
CC       hydroxytryptamine, dopamine and their metabolites, as well as altered
CC       noradrenaline levels. {ECO:0000269|PubMed:11080193,
CC       ECO:0000269|PubMed:17543467, ECO:0000269|PubMed:9826725}.
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}.
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DR   EMBL; U39391; AAA81519.1; -; mRNA.
DR   EMBL; AK043668; BAC31611.1; -; mRNA.
DR   EMBL; AK049814; BAC33931.1; -; mRNA.
DR   EMBL; AK049884; BAC33970.1; -; mRNA.
DR   EMBL; AK140194; BAE24273.1; -; mRNA.
DR   EMBL; CH466568; EDL18479.1; -; Genomic_DNA.
DR   EMBL; BC138669; AAI38670.1; -; mRNA.
DR   EMBL; BC138681; AAI38682.1; -; mRNA.
DR   EMBL; U33820; AAC52572.1; -; Genomic_DNA.
DR   EMBL; L20339; AAA16850.1; -; mRNA.
DR   CCDS; CCDS26756.1; -.
DR   PIR; I49375; I49375.
DR   RefSeq; NP_032334.2; NM_008308.4.
DR   AlphaFoldDB; Q64264; -.
DR   SMR; Q64264; -.
DR   STRING; 10090.ENSMUSP00000022235; -.
DR   BindingDB; Q64264; -.
DR   ChEMBL; CHEMBL3737; -.
DR   DrugCentral; Q64264; -.
DR   GlyCosmos; Q64264; 4 sites, No reported glycans.
DR   GlyGen; Q64264; 4 sites.
DR   iPTMnet; Q64264; -.
DR   PhosphoSitePlus; Q64264; -.
DR   SwissPalm; Q64264; -.
DR   MaxQB; Q64264; -.
DR   PaxDb; 10090-ENSMUSP00000022235; -.
DR   ProteomicsDB; 285688; -.
DR   Antibodypedia; 2959; 367 antibodies from 39 providers.
DR   DNASU; 15550; -.
DR   Ensembl; ENSMUST00000022235.6; ENSMUSP00000022235.5; ENSMUSG00000021721.6.
DR   GeneID; 15550; -.
DR   KEGG; mmu:15550; -.
DR   UCSC; uc007rtu.2; mouse.
DR   AGR; MGI:96273; -.
DR   CTD; 3350; -.
DR   MGI; MGI:96273; Htr1a.
DR   VEuPathDB; HostDB:ENSMUSG00000021721; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT00940000154484; -.
DR   HOGENOM; CLU_009579_11_1_1; -.
DR   InParanoid; Q64264; -.
DR   OMA; CAESCYM; -.
DR   OrthoDB; 2999405at2759; -.
DR   PhylomeDB; Q64264; -.
DR   TreeFam; TF316350; -.
DR   Reactome; R-MMU-390666; Serotonin receptors.
DR   BioGRID-ORCS; 15550; 2 hits in 77 CRISPR screens.
DR   PRO; PR:Q64264; -.
DR   Proteomes; UP000000589; Chromosome 13.
DR   RNAct; Q64264; Protein.
DR   Bgee; ENSMUSG00000021721; Expressed in ventral nuclear group and 73 other cell types or tissues.
DR   GO; GO:0043203; C:axon hillock; ISO:MGI.
DR   GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR   GO; GO:0098982; C:GABA-ergic synapse; ISO:MGI.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0042734; C:presynaptic membrane; ISO:MGI.
DR   GO; GO:0004993; F:G protein-coupled serotonin receptor activity; IDA:MGI.
DR   GO; GO:0001965; F:G-protein alpha-subunit binding; ISO:MGI.
DR   GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR   GO; GO:0090722; F:receptor-receptor interaction; ISO:MGI.
DR   GO; GO:0051378; F:serotonin binding; ISO:MGI.
DR   GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR   GO; GO:0007198; P:adenylate cyclase-inhibiting serotonin receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0001662; P:behavioral fear response; IMP:UniProtKB.
DR   GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR   GO; GO:0035640; P:exploration behavior; IMP:UniProtKB.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:MGI.
DR   GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; IBA:GO_Central.
DR   GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IMP:MGI.
DR   GO; GO:0014053; P:negative regulation of gamma-aminobutyric acid secretion; ISO:MGI.
DR   GO; GO:0097114; P:NMDA glutamate receptor clustering; ISO:MGI.
DR   GO; GO:0031117; P:positive regulation of microtubule depolymerization; ISO:MGI.
DR   GO; GO:0099171; P:presynaptic modulation of chemical synaptic transmission; ISO:MGI.
DR   GO; GO:0042053; P:regulation of dopamine metabolic process; IMP:UniProtKB.
DR   GO; GO:0060259; P:regulation of feeding behavior; ISO:MGI.
DR   GO; GO:0046883; P:regulation of hormone secretion; IEA:InterPro.
DR   GO; GO:0014062; P:regulation of serotonin secretion; IMP:UniProtKB.
DR   GO; GO:0019229; P:regulation of vasoconstriction; IEA:InterPro.
DR   GO; GO:0042428; P:serotonin metabolic process; IMP:UniProtKB.
DR   GO; GO:0007210; P:serotonin receptor signaling pathway; IMP:UniProtKB.
DR   CDD; cd15330; 7tmA_5-HT1A_vertebrates; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR000610; 5HT1A_rcpt.
DR   InterPro; IPR002231; 5HT_rcpt.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   PANTHER; PTHR24248; ADRENERGIC RECEPTOR-RELATED G-PROTEIN COUPLED RECEPTOR; 1.
DR   PANTHER; PTHR24248:SF191; G-PROTEIN COUPLED RECEPTORS FAMILY 1 PROFILE DOMAIN-CONTAINING PROTEIN; 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   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.
DR   Genevisible; Q64264; MM.
PE   2: Evidence at transcript level;
KW   Behavior; Cell membrane; Cell projection; Disulfide bond;
KW   G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW   Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN           1..421
FT                   /note="5-hydroxytryptamine receptor 1A"
FT                   /id="PRO_0000068904"
FT   TOPO_DOM        1..36
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        37..62
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        63..73
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        74..98
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        99..110
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        111..132
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        133..152
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        153..178
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        179..191
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        192..217
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        218..345
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        346..367
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        368..378
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        379..403
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        404..421
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   REGION          237..268
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           133..135
FT                   /note="DRY motif; important for ligand-induced conformation
FT                   changes"
FT                   /evidence="ECO:0000250"
FT   MOTIF           396..400
FT                   /note="NPxxY motif; important for ligand-induced
FT                   conformation changes and signaling"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        239..253
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         116
FT                   /ligand="ergotamine"
FT                   /ligand_id="ChEBI:CHEBI:190463"
FT                   /ligand_note="agonist"
FT                   /evidence="ECO:0000250|UniProtKB:P28222"
FT   BINDING         121
FT                   /ligand="ergotamine"
FT                   /ligand_id="ChEBI:CHEBI:190463"
FT                   /ligand_note="agonist"
FT                   /evidence="ECO:0000250|UniProtKB:P28222"
FT   BINDING         189
FT                   /ligand="ergotamine"
FT                   /ligand_id="ChEBI:CHEBI:190463"
FT                   /ligand_note="agonist"
FT                   /evidence="ECO:0000250|UniProtKB:P28222"
FT   CARBOHYD        10
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        11
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        24
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        30
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        109..187
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   VARIANT         17..19
FT                   /note="EPF -> DHL (in strain: C3H/An)"
FT   CONFLICT        177
FT                   /note="T -> A (in Ref. 1; AAA81519)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        242
FT                   /note="F -> L (in Ref. 6; AAA16850)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        247
FT                   /note="A -> V (in Ref. 6; AAA16850)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        263
FT                   /note="C -> W (in Ref. 6; AAA16850)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        304
FT                   /note="H -> D (in Ref. 1; AAA81519)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   421 AA;  46176 MW;  74F519DF7CC0C7AA CRC64;
     MDMFSLGQGN NTTTSLEPFG TGGNDTGLSN VTFSYQVITS LLLGTLIFCA VLGNACVVAA
     IALERSLQNV ANYLIGSLAV TDLMVSVLVL PMAALYQVLN KWTLGQVTCD LFIALDVLCC
     TSSILHLCAI ALDRYWAITD PIDYVNKRTP RRAAALISLT WLIGFLISIP PMLGWRTPED
     RSNPNECTIS KDHGYTIYST FGAFYIPLLL MLVLYGRIFR AARFRIRKTV KKVEKKGAGT
     SFGTSSAPPP KKSLNGQPGS GDCRRSAENR AVGTPCANGA VRQGEDDATL EVIEVHRVGN
     SKGHLPLPSE SGATSYVPAC LERKNERTAE AKRKMALARE RKTVKTLGII MGTFILCWLP
     FFIVALVLPF CESSCHMPEL LGAIINWLGY SNSLLNPVIY AYFNKDFQNA FKKIIKCKFC
     R
//