DRD4_MOUSE
ID DRD4_MOUSE Reviewed; 387 AA.
AC P51436; O35838; Q7TT80; Q8BXS4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=D(4) dopamine receptor;
DE AltName: Full=D(2C) dopamine receptor;
DE AltName: Full=Dopamine D4 receptor;
GN Name=Drd4;
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], AND TISSUE SPECIFICITY.
RC STRAIN=129/Sv;
RX PubMed=7698326; DOI=10.1016/0014-5793(95)00168-9;
RA Fishburn C.S., Carmon S., Fuchs S.;
RT "Molecular cloning and characterisation of the gene encoding the murine D4
RT dopamine receptor.";
RL FEBS Lett. 361:215-219(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8584230; DOI=10.1016/0304-3940(95)12021-u;
RA Suzuki T., Kobayashi K., Nagatsu T.;
RT "Genomic structure and tissue distribution of the mouse dopamine D4
RT receptor.";
RL Neurosci. Lett. 199:69-72(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Retina;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Retina;
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 [6]
RP IDENTIFICATION.
RX PubMed=18303015; DOI=10.1074/jbc.m708473200;
RA Rondou P., Haegeman G., Vanhoenacker P., Van Craenenbroeck K.;
RT "BTB Protein KLHL12 targets the dopamine D4 receptor for ubiquitination by
RT a Cul3-based E3 ligase.";
RL J. Biol. Chem. 283:11083-11096(2008).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24048828; DOI=10.1523/jneurosci.2039-13.2013;
RA Hwang C.K., Chaurasia S.S., Jackson C.R., Chan G.C., Storm D.R.,
RA Iuvone P.M.;
RT "Circadian rhythm of contrast sensitivity is regulated by a dopamine-
RT neuronal PAS-domain protein 2-adenylyl cyclase 1 signaling pathway in
RT retinal ganglion cells.";
RL J. Neurosci. 33:14989-14997(2013).
CC -!- FUNCTION: Dopamine receptor responsible for neuronal signaling in the
CC mesolimbic system of the brain, an area of the brain that regulates
CC emotion and complex behavior. Activated by dopamine, but also by
CC epinephrine and norepinephrine, and by numerous synthetic agonists and
CC drugs. Agonist binding triggers signaling via G proteins that inhibit
CC adenylyl cyclase (By similarity). Modulates the circadian rhythm of
CC contrast sensitivity by regulating the rhythmic expression of NPAS2 in
CC the retinal ganglion cells (PubMed:24048828).
CC {ECO:0000250|UniProtKB:P21917, ECO:0000269|PubMed:24048828}.
CC -!- SUBUNIT: Forms homo- and heterooligomers with DRD2. D4.7 allele
CC exhibits higher affinity for homodimers compared to DRD2 heterodimers,
CC while alleles D42. and 4.4 have similar affinities for both. The
CC interaction with DRD2 may modulate agonist-induced downstream signaling
CC (By similarity). Interacts with CLIC6 (By similarity). Interacts with
CC GPRASP1. May interact with ADORA2A. Interacts with KLHL12 (By
CC similarity). {ECO:0000250|UniProtKB:P21917,
CC ECO:0000250|UniProtKB:P30729}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P21917};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P21917}.
CC -!- TISSUE SPECIFICITY: Detected in olfactory bulb, hypothalamus, olfactory
CC tubercle, brainstem and striatum. {ECO:0000269|PubMed:7698326}.
CC -!- PTM: Palmitoylated. Palmitoylation of the C-terminal Cys is important
CC for normal expression at the cell membrane.
CC {ECO:0000250|UniProtKB:P21917}.
CC -!- DISRUPTION PHENOTYPE: Mice show a significant reduction in daytime
CC contrast sensitivity. {ECO:0000269|PubMed:24048828}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- CAUTION: In contrast to human protein, does not interact with KLHL12
CC and is not ubiquitinated by the BCR(KLHL12) complex.
CC {ECO:0000305|PubMed:18303015}.
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DR EMBL; U19880; AAC52190.1; -; Genomic_DNA.
DR EMBL; S80929; AAB50730.1; -; Genomic_DNA.
DR EMBL; S80920; AAB50730.1; JOINED; Genomic_DNA.
DR EMBL; S80927; AAB50730.1; JOINED; Genomic_DNA.
DR EMBL; S80928; AAB50730.1; JOINED; Genomic_DNA.
DR EMBL; AK044379; BAC31893.1; -; mRNA.
DR EMBL; CH466531; EDL18041.1; -; Genomic_DNA.
DR EMBL; BC016086; AAH16086.1; -; mRNA.
DR EMBL; BC051421; AAH51421.2; -; mRNA.
DR CCDS; CCDS22007.1; -.
DR PIR; I49246; I49246.
DR RefSeq; NP_031904.1; NM_007878.2.
DR PDB; 6IQL; X-ray; 3.50 A; A/B=23-219, A/B=304-387.
DR PDBsum; 6IQL; -.
DR AlphaFoldDB; P51436; -.
DR SMR; P51436; -.
DR DIP; DIP-61454N; -.
DR IntAct; P51436; 3.
DR STRING; 10090.ENSMUSP00000026569; -.
DR BindingDB; P51436; -.
DR ChEMBL; CHEMBL2574; -.
DR DrugCentral; P51436; -.
DR GlyGen; P51436; 1 site.
DR iPTMnet; P51436; -.
DR PhosphoSitePlus; P51436; -.
DR PaxDb; P51436; -.
DR PRIDE; P51436; -.
DR ProteomicsDB; 279579; -.
DR Antibodypedia; 22579; 461 antibodies from 35 providers.
DR DNASU; 13491; -.
DR Ensembl; ENSMUST00000026569; ENSMUSP00000026569; ENSMUSG00000025496.
DR GeneID; 13491; -.
DR KEGG; mmu:13491; -.
DR UCSC; uc009kkm.1; mouse.
DR CTD; 1815; -.
DR MGI; MGI:94926; Drd4.
DR VEuPathDB; HostDB:ENSMUSG00000025496; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000160974; -.
DR HOGENOM; CLU_009579_11_1_1; -.
DR InParanoid; P51436; -.
DR OMA; VVHITQA; -.
DR OrthoDB; 1215361at2759; -.
DR PhylomeDB; P51436; -.
DR TreeFam; TF334382; -.
DR Reactome; R-MMU-390651; Dopamine receptors.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR BioGRID-ORCS; 13491; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Drd4; mouse.
DR PRO; PR:P51436; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P51436; protein.
DR Bgee; ENSMUSG00000025496; Expressed in retinal neural layer and 48 other tissues.
DR Genevisible; P51436; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0043679; C:axon terminus; ISO:MGI.
DR GO; GO:0005938; C:cell cortex; ISO:MGI.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0098982; C:GABA-ergic synapse; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; ISO:MGI.
DR GO; GO:0099056; C:integral component of presynaptic membrane; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0043195; C:terminal bouton; ISO:MGI.
DR GO; GO:0012506; C:vesicle membrane; ISO:MGI.
DR GO; GO:0035240; F:dopamine binding; ISS:UniProtKB.
DR GO; GO:0004952; F:dopamine neurotransmitter receptor activity; ISO:MGI.
DR GO; GO:0001591; F:dopamine neurotransmitter receptor activity, coupled via Gi/Go; IMP:MGI.
DR GO; GO:0051379; F:epinephrine binding; ISO:MGI.
DR GO; GO:0004993; F:G protein-coupled serotonin receptor activity; IBA:GO_Central.
DR GO; GO:1901363; F:heterocyclic compound binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0051380; F:norepinephrine binding; ISO:MGI.
DR GO; GO:0017124; F:SH3 domain binding; ISO:MGI.
DR GO; GO:0007195; P:adenylate cyclase-inhibiting dopamine receptor signaling pathway; IMP:MGI.
DR GO; GO:0008344; P:adult locomotory behavior; IMP:MGI.
DR GO; GO:0050482; P:arachidonic acid secretion; ISO:MGI.
DR GO; GO:0008306; P:associative learning; ISO:MGI.
DR GO; GO:0001662; P:behavioral fear response; ISO:MGI.
DR GO; GO:0048148; P:behavioral response to cocaine; IMP:MGI.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0007212; P:dopamine receptor signaling pathway; ISO:MGI.
DR GO; GO:0042596; P:fear response; IMP:MGI.
DR GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; IBA:GO_Central.
DR GO; GO:0060080; P:inhibitory postsynaptic potential; IMP:MGI.
DR GO; GO:0050709; P:negative regulation of protein secretion; ISO:MGI.
DR GO; GO:0050805; P:negative regulation of synaptic transmission; ISO:MGI.
DR GO; GO:1904753; P:negative regulation of vascular associated smooth muscle cell migration; ISO:MGI.
DR GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:1901386; P:negative regulation of voltage-gated calcium channel activity; ISO:MGI.
DR GO; GO:0008355; P:olfactory learning; ISO:MGI.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; ISO:MGI.
DR GO; GO:0033674; P:positive regulation of kinase activity; ISO:MGI.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; ISO:MGI.
DR GO; GO:0060406; P:positive regulation of penile erection; ISO:MGI.
DR GO; GO:0032417; P:positive regulation of sodium:proton antiporter activity; ISO:MGI.
DR GO; GO:0050848; P:regulation of calcium-mediated signaling; ISO:MGI.
DR GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
DR GO; GO:0042053; P:regulation of dopamine metabolic process; IMP:MGI.
DR GO; GO:0046928; P:regulation of neurotransmitter secretion; ISO:MGI.
DR GO; GO:0099072; P:regulation of postsynaptic membrane neurotransmitter receptor levels; ISO:MGI.
DR GO; GO:0099149; P:regulation of postsynaptic neurotransmitter receptor internalization; IDA:SynGO.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; ISO:MGI.
DR GO; GO:0001975; P:response to amphetamine; IMP:MGI.
DR GO; GO:0034776; P:response to histamine; ISO:MGI.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0007614; P:short-term memory; ISO:MGI.
DR GO; GO:0001963; P:synaptic transmission, dopaminergic; ISO:MGI.
DR InterPro; IPR002185; Dopamine_D4_rcpt.
DR InterPro; IPR000929; Dopamine_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR24248:SF143; PTHR24248:SF143; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00569; DOPAMINED4R.
DR PRINTS; PR00242; DOPAMINER.
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 3D-structure; Biological rhythms; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane;
KW Metal-binding; Palmitate; Receptor; Reference proteome; Sodium; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..387
FT /note="D(4) dopamine receptor"
FT /id="PRO_0000069402"
FT TOPO_DOM 1..34
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P21917"
FT TRANSMEM 35..57
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P21917"
FT TOPO_DOM 58..67
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P21917"
FT TRANSMEM 68..90
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P21917"
FT TOPO_DOM 91..106
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P21917"
FT TRANSMEM 107..128
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P21917"
FT TOPO_DOM 129..146
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P21917"
FT TRANSMEM 147..170
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P21917"
FT TOPO_DOM 171..186
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P21917"
FT TRANSMEM 187..208
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P21917"
FT TOPO_DOM 209..314
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P21917"
FT TRANSMEM 315..337
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P21917"
FT TOPO_DOM 338..346
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P21917"
FT TRANSMEM 347..369
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P21917"
FT TOPO_DOM 370..387
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P21917"
FT REGION 224..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..247
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 77
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250|UniProtKB:P21917"
FT BINDING 119
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250|UniProtKB:P21917"
FT LIPID 387
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P21917"
FT CARBOHYD 3
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 105..180
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 340..343
FT /evidence="ECO:0000250|UniProtKB:P21917"
FT CONFLICT 1
FT /note="M -> L (in Ref. 3; BAC31893)"
FT /evidence="ECO:0000305"
FT CONFLICT 19
FT /note="E -> K (in Ref. 3; BAC31893)"
FT /evidence="ECO:0000305"
FT CONFLICT 47
FT /note="A -> T (in Ref. 2; AAB50730)"
FT /evidence="ECO:0000305"
FT HELIX 33..46
FT /evidence="ECO:0007829|PDB:6IQL"
FT HELIX 48..56
FT /evidence="ECO:0007829|PDB:6IQL"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:6IQL"
FT HELIX 65..83
FT /evidence="ECO:0007829|PDB:6IQL"
FT HELIX 85..93
FT /evidence="ECO:0007829|PDB:6IQL"
FT HELIX 102..129
FT /evidence="ECO:0007829|PDB:6IQL"
FT HELIX 148..155
FT /evidence="ECO:0007829|PDB:6IQL"
FT HELIX 159..162
FT /evidence="ECO:0007829|PDB:6IQL"
FT HELIX 166..171
FT /evidence="ECO:0007829|PDB:6IQL"
FT TURN 185..187
FT /evidence="ECO:0007829|PDB:6IQL"
FT HELIX 188..193
FT /evidence="ECO:0007829|PDB:6IQL"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:6IQL"
FT HELIX 197..219
FT /evidence="ECO:0007829|PDB:6IQL"
FT HELIX 304..339
FT /evidence="ECO:0007829|PDB:6IQL"
FT HELIX 347..367
FT /evidence="ECO:0007829|PDB:6IQL"
FT TURN 368..371
FT /evidence="ECO:0007829|PDB:6IQL"
SQ SEQUENCE 387 AA; 41487 MW; BEA306D5E8AA02E9 CRC64;
MGNSSATEDG GLLAGRGPES LGTGAGLGGA GAAALVGGVL LIGLVLAGNS LVCVSVASER
TLQTPTNYFI VSLAAADLLL AVLVLPLFVY SEVQGGVWLL SPRLCDTLMA MDVMLCTASI
FNLCAISVDR FVAVTVPLRY NQQGQCQLLL IAATWLLSAA VASPVVCGLN DVPGRDPAVC
CLENRDYVVY SSVCSFFLPC PLMLLLYWAT FRGLRRWEAA RHTKLHSRAP RRPSGPGPPV
SDPTQGPFFP DCPPPLPSLR TSPSDSSRPE SELSQRPCSP GCLLADAALP QPPEPSSRRR
RGAKITGRER KAMRVLPVVV GAFLVCWTPF FVVHITRALC PACFVSPRLV SAVTWLGYVN
SALNPIIYTI FNAEFRSVFR KTLRLRC
