ID   HRH1_MOUSE              Reviewed;         488 AA.
AC   P70174; Q91V75; Q91XN0; Q91XN1; Q91XN2; Q91XN3;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   09-MAY-2003, sequence version 2.
DT   04-NOV-2026, entry version 195.
DE   RecName: Full=Histamine H1 receptor {ECO:0000303|PubMed:8812432};
DE            Short=H1R {ECO:0000303|PubMed:8917588};
DE            Short=HH1R;
GN   Name=Hrh1 {ECO:0000312|MGI:MGI:107619};
GN   Synonyms=Bphs {ECO:0000303|PubMed:12142541};
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 [GENOMIC DNA].
RC   STRAIN=129/Ola;
RX   PubMed=8812432; DOI=10.1006/geno.1996.0441;
RA   Inoue I., Taniuchi I., Kitamura D., Jenkins N.A., Gilbert D.J.,
RA   Copeland N.G., Watanabe T.;
RT   "Characteristics of the mouse genomic histamine H1 receptor gene.";
RL   Genomics 36:178-181(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE, AND VARIANTS LEU-263; MET-312 AND SER-330.
RC   STRAIN=129/SvJ, A/J, B10.S/DvTe, BALB/cByJ, BALB/cJ, C3H/HeJ,
RC   C57BL/6J, CBA/J, DBA/1, DBA/2J, FVB/NCr, NOD, SJL/J, and SWR;
RC   TISSUE=Spleen;
RX   PubMed=12142541; DOI=10.1126/science.1072810;
RA   Ma R.Z., Gao J., Meeker N.D., Fillmore P.D., Tung K.S.K., Watanabe T.,
RA   Zachary J.F., Offner H., Blankenhorn E.P., Teuscher C.;
RT   "Identification of Bphs, an autoimmune disease locus, as histamine receptor
RT   H1.";
RL   Science 297:620-623(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Adipose tissue, Cerebellum, Hypothalamus, and Mesonephros;
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   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=8917588; DOI=10.1073/pnas.93.23.13316;
RA   Inoue I., Yanai K., Kitamura D., Taniuchi I., Kobayashi T., Niimura K.,
RA   Watanabe T., Watanabe T.;
RT   "Impaired locomotor activity and exploratory behavior in mice lacking
RT   histamine H1 receptors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:13316-13320(1996).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=12595443; DOI=10.1128/iai.71.3.1281-1287.2003;
RA   Gao J.F., Call S.B., Fillmore P.D., Watanabe T., Meeker N.D., Teuscher C.;
RT   "Analysis of the role of Bphs/Hrh1 in the genetic control of responsiveness
RT   to pertussis toxin.";
RL   Infect. Immun. 71:1281-1287(2003).
RN   [6]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=17145090; DOI=10.1016/j.neures.2006.10.020;
RA   Dai H., Kaneko K., Kato H., Fujii S., Jing Y., Xu A., Sakurai E., Kato M.,
RA   Okamura N., Kuramasu A., Yanai K.;
RT   "Selective cognitive dysfunction in mice lacking histamine H1 and H2
RT   receptors.";
RL   Neurosci. Res. 57:306-313(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344; SER-347; SER-381 AND
RP   SER-383, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: G protein-coupled receptor for histamine, a biogenic amine
CC       that functions as an immune modulator and a neurotransmitter (By
CC       similarity). Through the H1 receptor, histamine mediates the
CC       contraction of smooth muscles and increases capillary permeability due
CC       to contraction of terminal venules (PubMed:12595443). Also mediates
CC       neurotransmission in the central nervous system and thereby regulates
CC       circadian rhythms, emotional and locomotor activities as well as
CC       cognitive functions (PubMed:17145090, PubMed:8917588).
CC       {ECO:0000250|UniProtKB:P35367, ECO:0000269|PubMed:12595443,
CC       ECO:0000269|PubMed:17145090, ECO:0000269|PubMed:8917588}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8917588};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:P35367}.
CC   -!- DOMAIN: Histamine activates the receptor by forming hydrogen bonds with
CC       transmembrane domains 3 and 6, squashing the ligand-binding pocket on
CC       the extracellular side and opening the cavity for G protein engagement
CC       on the intracellular side. {ECO:0000250|UniProtKB:P35367}.
CC   -!- PTM: Phosphorylation at sites in the second and third cytoplasmic loops
CC       independently contribute to agonist-induced receptor down-regulation.
CC       {ECO:0000250|UniProtKB:P35367}.
CC   -!- POLYMORPHISM: Strains C3H/HeJ and CBA/J are resistant to vasoactive
CC       amine sensitization elicited by histamine (VAASH) which is induced by
CC       pertussis toxin. {ECO:0000269|PubMed:12142541}.
CC   -!- DISRUPTION PHENOTYPE: Mice lacking Hrh1 develop normally and are
CC       apparently healthy and fertile. However, they display perturbations in
CC       the control of circadian rhythm and locomotor activities related to
CC       emotion (PubMed:8917588). Learning and memory processes are also
CC       affected in these mice (PubMed:17145090). They also display decreased
CC       sensitivity to the toxic effects of pertussis toxin (PubMed:12595443).
CC       {ECO:0000269|PubMed:12595443, ECO:0000269|PubMed:17145090,
CC       ECO:0000269|PubMed:8917588}.
CC   -!- SIMILARITY: Belongs to the G protein-coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; D50095; BAA08791.1; -; Genomic_DNA.
DR   EMBL; AF387890; AAK71654.1; -; mRNA.
DR   EMBL; AF387891; AAK71655.1; -; mRNA.
DR   EMBL; AF387892; AAK71656.1; -; mRNA.
DR   EMBL; AF387893; AAK71657.1; -; mRNA.
DR   EMBL; AF387894; AAK71658.1; -; mRNA.
DR   EMBL; AF387895; AAK71659.1; -; mRNA.
DR   EMBL; AF387896; AAK71660.1; -; mRNA.
DR   EMBL; AF388052; AAK66774.2; -; mRNA.
DR   EMBL; AF388053; AAK66775.1; -; mRNA.
DR   EMBL; AF388054; AAK66776.1; -; mRNA.
DR   EMBL; AF388055; AAK66777.1; -; mRNA.
DR   EMBL; AF388056; AAK66778.1; -; mRNA.
DR   EMBL; AF388057; AAK66779.1; -; mRNA.
DR   EMBL; AF388058; AAK66780.1; -; mRNA.
DR   EMBL; AK032763; BAC28011.1; -; mRNA.
DR   EMBL; AK038480; BAC30013.1; -; mRNA.
DR   EMBL; AK046607; BAC32805.1; -; mRNA.
DR   EMBL; AK047070; BAC32950.1; -; mRNA.
DR   CCDS; CCDS20435.1; -.
DR   RefSeq; NP_001239571.1; NM_001252642.3.
DR   RefSeq; NP_001239572.1; NM_001252643.3.
DR   RefSeq; NP_001304053.1; NM_001317124.2.
DR   RefSeq; NP_001304054.1; NM_001317125.2.
DR   RefSeq; NP_001304055.1; NM_001317126.2.
DR   RefSeq; NP_001396960.1; NM_001410031.1.
DR   RefSeq; NP_032311.2; NM_008285.5.
DR   AlphaFoldDB; P70174; -.
DR   SMR; P70174; -.
DR   BioGRID; 200419; 1.
DR   FunCoup; P70174; 1028.
DR   STRING; 10090.ENSMUSP00000086383; -.
DR   BindingDB; P70174; -.
DR   ChEMBL; CHEMBL4322; -.
DR   DrugBank; DB11160; Phenyltoloxamine.
DR   DrugBank; DB00512; Vancomycin.
DR   GlyCosmos; P70174; 2 sites, No reported glycans.
DR   GlyGen; P70174; 2 sites, 1 N-linked glycan (1 site).
DR   iPTMnet; P70174; -.
DR   PhosphoSitePlus; P70174; -.
DR   jPOST; P70174; -.
DR   PaxDb; 10090-ENSMUSP00000086383; -.
DR   ProteomicsDB; 273382; -.
DR   Antibodypedia; 10679; 582 antibodies from 39 providers.
DR   DNASU; 15465; -.
DR   Ensembl; ENSMPUT00000020267; ENSMPUP00000019981; ENSMPUG00000020115.
DR   Ensembl; ENSMUST00000088987.3; ENSMUSP00000086383.3; ENSMUSG00000053004.10.
DR   Ensembl; ENSMUST00000160780.2; ENSMUSP00000124320.2; ENSMUSG00000053004.10.
DR   Ensembl; ENSMUST00000161220.2; ENSMUSP00000124037.2; ENSMUSG00000053004.10.
DR   Ensembl; ENSMUST00000161650.3; ENSMUSP00000124460.2; ENSMUSG00000053004.10.
DR   GeneID; 15465; -.
DR   KEGG; mmu:15465; -.
DR   UCSC; uc009dhw.1; mouse.
DR   AGR; MGI:107619; -.
DR   CTD; 3269; -.
DR   MGI; MGI:107619; Hrh1.
DR   VEuPathDB; HostDB:ENSMUSG00000053004; -.
DR   eggNOG; KOG4220; Eukaryota.
DR   GeneTree; ENSGT00940000160690; -.
DR   HOGENOM; CLU_009579_11_2_1; -.
DR   InParanoid; P70174; -.
DR   OMA; ACAYETL; -.
DR   OrthoDB; 10071887at2759; -.
DR   PhylomeDB; P70174; -.
DR   Reactome; R-MMU-390650; Histamine receptors.
DR   Reactome; R-MMU-416476; G alpha (q) signalling events.
DR   BioGRID-ORCS; 15465; 2 hits in 78 CRISPR screens.
DR   PRO; PR:P70174; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; P70174; protein.
DR   Bgee; ENSMUSG00000053004; Expressed in subparaventricular zone and 78 other cell types or tissues.
DR   ExpressionAtlas; P70174; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISO:GO_Central.
DR   GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; EXP:UniProtKB.
DR   GO; GO:0045202; C:synapse; IEA:GOC.
DR   GO; GO:0015085; F:calcium ion transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0051381; F:histamine binding; ISO:GO_Central.
DR   GO; GO:0004969; F:histamine receptor activity; ISS:UniProtKB.
DR   GO; GO:0070509; P:calcium ion import; ISO:MGI.
DR   GO; GO:0071420; P:cellular response to histamine; ISS:UniProtKB.
DR   GO; GO:0007268; P:chemical synaptic transmission; ISO:GO_Central.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; IBA:GO_Central.
DR   GO; GO:0071421; P:manganese ion transmembrane transport; ISO:MGI.
DR   GO; GO:0007613; P:memory; IMP:MGI.
DR   GO; GO:0010894; P:negative regulation of steroid biosynthetic process; ISO:GO_Central.
DR   GO; GO:0007208; P:phospholipase C-activating serotonin receptor signaling pathway; ISO:GO_Central.
DR   GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISO:GO_Central.
DR   GO; GO:0045907; P:positive regulation of vasoconstriction; ISO:GO_Central.
DR   GO; GO:0048167; P:regulation of synaptic plasticity; IMP:MGI.
DR   GO; GO:0043114; P:regulation of vascular permeability; IEA:InterPro.
DR   GO; GO:0008542; P:visual learning; IMP:MGI.
DR   CDD; cd15050; 7tmA_Histamine_H1R; 1.
DR   FunFam; 1.20.1070.10:FF:000147; Histamine H1 receptor; 1.
DR   FunFam; 1.20.1070.10:FF:000189; Histamine H1 receptor; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 2.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR000921; Histamine_H1_rcpt.
DR   PANTHER; PTHR24248; ADRENERGIC RECEPTOR-RELATED G-PROTEIN COUPLED RECEPTOR; 1.
DR   PANTHER; PTHR24248:SF204; HISTAMINE H1 RECEPTOR; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00530; HISTAMINEH1R.
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   Biological rhythms; Cell membrane; Disulfide bond;
KW   G protein-coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
KW   Receptor; Reference proteome; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..488
FT                   /note="Histamine H1 receptor"
FT                   /id="PRO_0000069677"
FT   TOPO_DOM        1..29
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        30..50
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250|UniProtKB:P35367"
FT   TOPO_DOM        51..64
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        65..89
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250|UniProtKB:P35367"
FT   TOPO_DOM        90..97
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        98..123
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000250|UniProtKB:P35367"
FT   TOPO_DOM        124..144
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        145..164
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250|UniProtKB:P35367"
FT   TOPO_DOM        165..188
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        189..211
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250|UniProtKB:P35367"
FT   TOPO_DOM        212..417
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        418..441
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250|UniProtKB:P35367"
FT   TOPO_DOM        442..447
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        448..470
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000250|UniProtKB:P35367"
FT   TOPO_DOM        471..488
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   REGION          107..112
FT                   /note="Important for agonist binding"
FT                   /evidence="ECO:0000250|UniProtKB:P35367"
FT   REGION          245..337
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          425..429
FT                   /note="Important for agonist binding"
FT                   /evidence="ECO:0000250|UniProtKB:P35367"
FT   COMPBIAS        322..337
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         107
FT                   /ligand="histamine"
FT                   /ligand_id="ChEBI:CHEBI:58432"
FT                   /evidence="ECO:0000250|UniProtKB:P35367"
FT   BINDING         112
FT                   /ligand="histamine"
FT                   /ligand_id="ChEBI:CHEBI:58432"
FT                   /evidence="ECO:0000250|UniProtKB:P35367"
FT   BINDING         198
FT                   /ligand="histamine"
FT                   /ligand_id="ChEBI:CHEBI:58432"
FT                   /evidence="ECO:0000250|UniProtKB:P35367"
FT   BINDING         432
FT                   /ligand="histamine"
FT                   /ligand_id="ChEBI:CHEBI:58432"
FT                   /evidence="ECO:0000250|UniProtKB:P35367"
FT   MOD_RES         140
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P35367"
FT   MOD_RES         142
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P35367"
FT   MOD_RES         230
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P35367"
FT   MOD_RES         344
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         347
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         381
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         383
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         397
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P35367"
FT   MOD_RES         399
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P35367"
FT   CARBOHYD        5
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        18
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        100..180
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   DISULFID        442..445
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   VARIANT         263
FT                   /note="P -> L (in strain: C3H/HeJ and CBA/J)"
FT                   /evidence="ECO:0000269|PubMed:12142541"
FT   VARIANT         312
FT                   /note="V -> M (in strain: C3H/HeJ and CBA/J)"
FT                   /evidence="ECO:0000269|PubMed:12142541"
FT   VARIANT         330
FT                   /note="P -> S (in strain: C3H/HeJ and CBA/J)"
FT                   /evidence="ECO:0000269|PubMed:12142541"
FT   CONFLICT        2
FT                   /note="S -> R (in Ref. 1; BAA08791)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        47
FT                   /note="L -> G (in Ref. 1; BAA08791)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        79
FT                   /note="V -> I (in Ref. 1; BAA08791)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        215..216
FT                   /note="KA -> NG (in Ref. 1; BAA08791)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        224
FT                   /note="R -> P (in Ref. 1; BAA08791)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        242
FT                   /note="E -> D (in Ref. 2; AAK66778)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        244
FT                   /note="A -> S (in Ref. 1; BAA08791)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        261
FT                   /note="K -> T (in Ref. 1; BAA08791)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        278
FT                   /note="E -> A (in Ref. 1; BAA08791)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        379
FT                   /note="S -> R (in Ref. 1; BAA08791)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   488 AA;  55682 MW;  82612DF712998B41 CRC64;
     MSLPNTSSAS EDKMCEGNRT AMASPQLLPL VVVLSSISLV TVGLNLLVLY AVRSERKLHT
     VGNLYIVSLS VADLIVGAVV MPMNILYLIM TKWSLGRPLC LFWLSMDYVA STASIFSVFI
     LCIDRYRSVQ QPLRYLRYRT KTRASATILG AWFLSFLWVI PILGWHHFTP LAPELREDKC
     ETDFYNVTWF KIMTAIINFY LPTLLMLWFY VKIYKAVRRH CQHRQLTNGS LPTFLEIKLR
     SEDAKEGAKK PGKESPWGVQ KRPSRDPTGG LDQKSTSEDP KVTSPTVFSQ EGERETVTRP
     CFRLDVMQTQ PVPEGDARGS KANDQTLSQP KMDEQSLSTC RRISETSEDQ TLVDRQSFSR
     TTDSDTSIEP GLGKVKARSR SNSGLDYIKV TWKRLRSHSR QYVSGLHLNR ERKAAKQLGC
     IMAAFILCWI PYFIFFMVIA FCNSCCSEPV HMFTIWLGYI NSTLNPLIYP LCNENFKKTF
     KKILHIRS
//