DRD1_MOUSE
ID DRD1_MOUSE Reviewed; 446 AA.
AC Q61616; B2RPW8; Q8C8P8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=D(1A) dopamine receptor;
DE AltName: Full=Dopamine D1 receptor;
GN Name=Drd1; Synonyms=Drd1a, Gpcr15;
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 193-279.
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-441, AND IDENTIFICATION BY
RP 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).
RN [5]
RP INTERACTION WITH DRD2, AND SUBCELLULAR LOCATION.
RX PubMed=25865831; DOI=10.1111/jnc.13119;
RA Jung G., Kim E.J., Cicvaric A., Sase S., Groeger M., Hoeger H.,
RA Sialana F.J., Berger J., Monje F.J., Lubec G.;
RT "Drebrin depletion alters neurotransmitter receptor levels in protein
RT complexes, dendritic spine morphogenesis and memory-related synaptic
RT plasticity in the mouse hippocampus.";
RL J. Neurochem. 134:327-339(2015).
CC -!- FUNCTION: Dopamine receptor whose activity is mediated by G proteins
CC which activate adenylyl cyclase.
CC -!- SUBUNIT: Interacts with DNAJC14 via its C-terminus (By similarity).
CC Interacts with DRD2 (PubMed:25865831). {ECO:0000250|UniProtKB:P18901,
CC ECO:0000269|PubMed:25865831}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P18901};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P18901}. Endoplasmic
CC reticulum membrane {ECO:0000250|UniProtKB:P18901}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:P18901}. Cell projection, dendrite
CC {ECO:0000269|PubMed:25865831}. Cell projection, dendritic spine
CC {ECO:0000269|PubMed:25865831}. Note=Transport from the endoplasmic
CC reticulum to the cell surface is regulated by interaction with DNAJC14.
CC {ECO:0000250|UniProtKB:P18901}.
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; AK044723; BAC32050.1; -; mRNA.
DR EMBL; BC137641; AAI37642.1; -; mRNA.
DR EMBL; BC137655; AAI37656.1; -; mRNA.
DR EMBL; L20336; AAA16848.1; -; mRNA.
DR CCDS; CCDS26524.1; -.
DR RefSeq; NP_001278730.1; NM_001291801.1.
DR RefSeq; NP_034206.1; NM_010076.3.
DR AlphaFoldDB; Q61616; -.
DR SMR; Q61616; -.
DR BioGRID; 199305; 2.
DR STRING; 10090.ENSMUSP00000021932; -.
DR BindingDB; Q61616; -.
DR ChEMBL; CHEMBL3071; -.
DR DrugCentral; Q61616; -.
DR GuidetoPHARMACOLOGY; 214; -.
DR GlyGen; Q61616; 1 site.
DR iPTMnet; Q61616; -.
DR PhosphoSitePlus; Q61616; -.
DR SwissPalm; Q61616; -.
DR PaxDb; Q61616; -.
DR PRIDE; Q61616; -.
DR ProteomicsDB; 277404; -.
DR Antibodypedia; 2811; 666 antibodies from 42 providers.
DR DNASU; 13488; -.
DR Ensembl; ENSMUST00000021932; ENSMUSP00000021932; ENSMUSG00000021478.
DR GeneID; 13488; -.
DR KEGG; mmu:13488; -.
DR UCSC; uc011yzm.3; mouse.
DR CTD; 1812; -.
DR MGI; MGI:99578; Drd1.
DR VEuPathDB; HostDB:ENSMUSG00000021478; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000155857; -.
DR HOGENOM; CLU_009579_11_0_1; -.
DR InParanoid; Q61616; -.
DR OMA; MDCQQPE; -.
DR OrthoDB; 1045889at2759; -.
DR PhylomeDB; Q61616; -.
DR TreeFam; TF325181; -.
DR Reactome; R-MMU-390651; Dopamine receptors.
DR Reactome; R-MMU-418555; G alpha (s) signalling events.
DR BioGRID-ORCS; 13488; 2 hits in 72 CRISPR screens.
DR PRO; PR:Q61616; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q61616; protein.
DR Bgee; ENSMUSG00000021478; Expressed in nucleus accumbens and 82 other tissues.
DR ExpressionAtlas; Q61616; baseline and differential.
DR Genevisible; Q61616; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0043679; C:axon terminus; ISO:MGI.
DR GO; GO:0005901; C:caveola; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0060170; C:ciliary membrane; ISO:MGI.
DR GO; GO:0005929; C:cilium; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0043198; C:dendritic shaft; ISO:MGI.
DR GO; GO:0043197; C:dendritic spine; IDA:UniProtKB.
DR GO; GO:0044327; C:dendritic spine head; ISO:MGI.
DR GO; GO:0044326; C:dendritic spine neck; ISO:MGI.
DR GO; GO:0012505; C:endomembrane system; IDA:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IDA:SynGO.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0097730; C:non-motile cilium; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0031701; F:angiotensin receptor binding; ISO:MGI.
DR GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR GO; GO:0031750; F:D3 dopamine receptor binding; ISO:MGI.
DR GO; GO:0035240; F:dopamine binding; ISO:MGI.
DR GO; GO:0004952; F:dopamine neurotransmitter receptor activity; IDA:MGI.
DR GO; GO:0001588; F:dopamine neurotransmitter receptor activity, coupled via Gs; IDA:MGI.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IDA:MGI.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; ISO:MGI.
DR GO; GO:1901363; F:heterocyclic compound binding; ISO:MGI.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0007190; P:activation of adenylate cyclase activity; IDA:MGI.
DR GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007191; P:adenylate cyclase-activating dopamine receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0007628; P:adult walking behavior; IMP:MGI.
DR GO; GO:0008306; P:associative learning; IMP:MGI.
DR GO; GO:0014002; P:astrocyte development; IMP:MGI.
DR GO; GO:0001662; P:behavioral fear response; IMP:MGI.
DR GO; GO:0048148; P:behavioral response to cocaine; IMP:MGI.
DR GO; GO:0019722; P:calcium-mediated signaling; ISO:MGI.
DR GO; GO:0016477; P:cell migration; IMP:MGI.
DR GO; GO:0071870; P:cellular response to catecholamine stimulus; ISO:MGI.
DR GO; GO:1903351; P:cellular response to dopamine; ISO:MGI.
DR GO; GO:0021853; P:cerebral cortex GABAergic interneuron migration; IMP:MGI.
DR GO; GO:0001661; P:conditioned taste aversion; IMP:MGI.
DR GO; GO:0021542; P:dentate gyrus development; IMP:MGI.
DR GO; GO:0007212; P:dopamine receptor signaling pathway; IMP:MGI.
DR GO; GO:0015872; P:dopamine transport; IMP:MGI.
DR GO; GO:0042755; P:eating behavior; ISO:MGI.
DR GO; GO:0007631; P:feeding behavior; IGI:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:MGI.
DR GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; ISO:MGI.
DR GO; GO:0046323; P:glucose import; IMP:MGI.
DR GO; GO:0007625; P:grooming behavior; IMP:MGI.
DR GO; GO:0046959; P:habituation; IMP:MGI.
DR GO; GO:0021766; P:hippocampus development; IMP:MGI.
DR GO; GO:0006886; P:intracellular protein transport; ISO:MGI.
DR GO; GO:0007612; P:learning; IMP:MGI.
DR GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR GO; GO:0060292; P:long-term synaptic depression; IMP:MGI.
DR GO; GO:0060291; P:long-term synaptic potentiation; IMP:MGI.
DR GO; GO:0042711; P:maternal behavior; IMP:MGI.
DR GO; GO:0007617; P:mating behavior; IDA:MGI.
DR GO; GO:0007613; P:memory; IMP:MGI.
DR GO; GO:0099010; P:modification of postsynaptic structure; EXP:SynGO.
DR GO; GO:0006936; P:muscle contraction; IMP:MGI.
DR GO; GO:0060548; P:negative regulation of cell death; ISO:MGI.
DR GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI.
DR GO; GO:0042321; P:negative regulation of circadian sleep/wake cycle, sleep; ISO:MGI.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; ISO:MGI.
DR GO; GO:0050805; P:negative regulation of synaptic transmission; ISO:MGI.
DR GO; GO:0001764; P:neuron migration; IMP:MGI.
DR GO; GO:0019228; P:neuronal action potential; IMP:MGI.
DR GO; GO:0035106; P:operant conditioning; IMP:MGI.
DR GO; GO:0030432; P:peristalsis; IGI:MGI.
DR GO; GO:0060158; P:phospholipase C-activating dopamine receptor signaling pathway; IDA:MGI.
DR GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway; ISO:MGI.
DR GO; GO:2000253; P:positive regulation of feeding behavior; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; ISO:MGI.
DR GO; GO:0045838; P:positive regulation of membrane potential; ISO:MGI.
DR GO; GO:2001224; P:positive regulation of neuron migration; IMP:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; ISO:MGI.
DR GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IMP:MGI.
DR GO; GO:0099170; P:postsynaptic modulation of chemical synaptic transmission; ISO:MGI.
DR GO; GO:0006606; P:protein import into nucleus; IMP:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR GO; GO:0042053; P:regulation of dopamine metabolic process; IMP:MGI.
DR GO; GO:0043269; P:regulation of ion transport; ISO:MGI.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IMP:MGI.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IDA:SynGO.
DR GO; GO:0019229; P:regulation of vasoconstriction; ISO:MGI.
DR GO; GO:0001975; P:response to amphetamine; IMP:MGI.
DR GO; GO:0042220; P:response to cocaine; IMP:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IDA:MGI.
DR GO; GO:0046960; P:sensitization; IGI:MGI.
DR GO; GO:0035176; P:social behavior; ISO:MGI.
DR GO; GO:0021756; P:striatum development; IMP:MGI.
DR GO; GO:0001963; P:synaptic transmission, dopaminergic; IMP:MGI.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IMP:MGI.
DR GO; GO:0001659; P:temperature homeostasis; IMP:MGI.
DR GO; GO:0019226; P:transmission of nerve impulse; IMP:MGI.
DR GO; GO:0042311; P:vasodilation; IEA:InterPro.
DR GO; GO:0008542; P:visual learning; IMP:MGI.
DR InterPro; IPR001413; Dopamine_D1_rcpt.
DR InterPro; IPR000929; Dopamine_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00565; DOPAMINED1AR.
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 Cell membrane; Cell projection; Disulfide bond; Endoplasmic reticulum;
KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; Palmitate;
KW Phosphoprotein; Receptor; Reference proteome; Synapse; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..446
FT /note="D(1A) dopamine receptor"
FT /id="PRO_0000069375"
FT TOPO_DOM 1..22
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 23..48
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 49..59
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..86
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 87..95
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..118
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..137
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..162
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..192
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..218
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 219..272
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..299
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 300..312
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..337
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 338..446
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 441
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT LIPID 347
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 351
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 4
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 95..186
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 193..196
FT /note="TYAI -> DIRH (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="N -> S (in Ref. 3; AAA16848)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 446 AA; 49612 MW; 509BA66F9DF82A74 CRC64;
MAPNTSTMDE TGLPVERDFS FRILTACFLS LLILSTLLGN TLVCAAVIRF RHLRSKVTNF
FVISLAVSDL LVAVLVMPWK AVAEIAGFWP FGSFCNIWVA FDIMCSTASI LNLCVISVDR
YWAISSPFQY ERKMTPKAAF ILISVAWTLS VLISFIPVQL SWHKAKPTWP LDGNFTSLED
AEDDNCDTRL SRTYAISSSL ISFYIPVAIM IVTYTSIYRI AQKQIRRISA LERAAVHAKN
CQTTTGNGNP VECSQSESSF KMSFKRETKV LKTLSVIMGV FVCCWLPFFI SNCMVPFCGS
EETQPFCIDS ITFDVFVWFG WANSSLNPII YAFNADFQKA FSTLLGCYRL CPTTNNAIET
VSINNNGAVM FSSHHEPRGS ISKDCNLVYL IPHAVGSSED LKREEAGGIP KPLEKLSPAL
SVILDYDTDV SLEKIQPVTH SGQHST
