DOPR2_CAEEL
ID DOPR2_CAEEL Reviewed; 849 AA.
AC E7EM37; A0A486WWQ7; A0A486WXI1; A0A486WYH7; G5EBI6; G5EEM7; H2L2G2;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Dopamine receptor 2 {ECO:0000312|WormBase:K09G1.4c};
DE AltName: Full=Dopamine D2-like receptor dop-2 {ECO:0000305};
GN Name=dop-2 {ECO:0000312|WormBase:K09G1.4c};
GN Synonyms=dop-2L {ECO:0000312|WormBase:K09G1.4c};
GN ORFNames=K09G1.4 {ECO:0000312|WormBase:K09G1.4c};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=12887685; DOI=10.1046/j.1471-4159.2003.01896.x;
RA Suo S., Sasagawa N., Ishiura S.;
RT "Cloning and characterization of a Caenorhabditis elegans D2-like dopamine
RT receptor.";
RL J. Neurochem. 86:869-878(2003).
RN [2] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3] {ECO:0000305}
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=14568548; DOI=10.1016/s0012-1606(03)00447-0;
RA Tsalik E.L., Niacaris T., Wenick A.S., Pau K., Avery L., Hobert O.;
RT "LIM homeobox gene-dependent expression of biogenic amine receptors in
RT restricted regions of the C. elegans nervous system.";
RL Dev. Biol. 263:81-102(2003).
RN [4] {ECO:0000305}
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=19609300; DOI=10.1038/emboj.2009.194;
RA Suo S., Culotti J.G., Van Tol H.H.;
RT "Dopamine counteracts octopamine signalling in a neural circuit mediating
RT food response in C. elegans.";
RL EMBO J. 28:2437-2448(2009).
RN [5] {ECO:0000305}
RP ROLE IN SWIMMING-INDUCED PARALYSIS.
RX PubMed=20410438; DOI=10.1124/mol.109.062703;
RA Carvelli L., Matthies D.S., Galli A.;
RT "Molecular mechanisms of amphetamine actions in Caenorhabditis elegans.";
RL Mol. Pharmacol. 78:151-156(2010).
RN [6] {ECO:0000305}
RP INTERACTION WITH GPA-14, AND MUTAGENESIS OF 183-PRO--VAL-849.
RX PubMed=22280843; DOI=10.1186/1750-2187-7-3;
RA Pandey P., Harbinder S.;
RT "The Caenorhabditis elegans D2-like dopamine receptor DOP-2 physically
RT interacts with GPA-14, a Galphai subunit.";
RL J. Mol. Signal. 7:3-3(2012).
RN [7] {ECO:0000305}
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=23166505; DOI=10.1371/journal.pgen.1003015;
RA Correa P., LeBoeuf B., Garcia L.R.;
RT "C. elegans dopaminergic D2-like receptors delimit recurrent cholinergic-
RT mediated motor programs during a goal-oriented behavior.";
RL PLoS Genet. 8:E1003015-E1003015(2012).
RN [8] {ECO:0000305}
RP FUNCTION.
RX PubMed=23607404; DOI=10.1186/1744-9081-9-16;
RA Mersha M., Formisano R., McDonald R., Pandey P., Tavernarakis N.,
RA Harbinder S.;
RT "GPA-14, a Galpha(i) subunit mediates dopaminergic behavioral plasticity in
RT C. elegans.";
RL Behav. Brain Funct. 9:16-16(2013).
RN [9] {ECO:0000305}
RP ROLE IN DRUG SENSITIVITY.
RX PubMed=23351035; DOI=10.1111/ejn.12099;
RA Sellings L., Pereira S., Qian C., Dixon-McDougall T., Nowak C., Zhao B.,
RA Tyndale R.F., van der Kooy D.;
RT "Nicotine-motivated behavior in Caenorhabditis elegans requires the
RT nicotinic acetylcholine receptor subunits acr-5 and acr-15.";
RL Eur. J. Neurosci. 37:743-756(2013).
RN [10] {ECO:0000305}
RP FUNCTION.
RX PubMed=25536037; DOI=10.1371/journal.pone.0115985;
RA Wang D., Yu Y., Li Y., Wang Y., Wang D.;
RT "Dopamine receptors antagonistically regulate behavioral choice between
RT conflicting alternatives in C. elegans.";
RL PLoS ONE 9:E115985-E115985(2014).
RN [11] {ECO:0000305}
RP FUNCTION.
RX PubMed=25474638; DOI=10.1371/journal.pgen.1004767;
RA Masoudi N., Ibanez-Cruceyra P., Offenburger S.L., Holmes A., Gartner A.;
RT "Tetraspanin (TSP-17) protects dopaminergic neurons against 6-OHDA-induced
RT neurodegeneration in C. elegans.";
RL PLoS Genet. 10:E1004767-E1004767(2014).
RN [12] {ECO:0000305}
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=26156999; DOI=10.1523/jneurosci.0940-15.2015;
RA Correa P.A., Gruninger T., Garcia L.R.;
RT "DOP-2 D2-Like Receptor Regulates UNC-7 Innexins to Attenuate Recurrent
RT Sensory Motor Neurons during C. elegans Copulation.";
RL J. Neurosci. 35:9990-10004(2015).
RN [13] {ECO:0000305}
RP FUNCTION.
RX PubMed=31494966; DOI=10.1002/syn.22131;
RA Formisano R., Mersha M.D., Caplan J., Singh A., Rankin C.H.,
RA Tavernarakis N., Dhillon H.S.;
RT "Synaptic vesicle fusion is modulated through feedback inhibition by
RT dopamine auto-receptors.";
RL Synapse 74:E22131-E22131(2020).
CC -!- FUNCTION: G-protein coupled receptor which binds to the
CC neurotransmitter dopamine with high affinity leading to the activation
CC of an associated G-protein and downstream signaling pathways
CC (PubMed:12887685). Couples to G-proteins to inhibit adenylate cyclase
CC (AC) activity and cAMP production (PubMed:12887685). Inhibits synaptic
CC vesicle fusion to negatively regulate the release of dopamine at
CC dopaminergic neuron synapses (PubMed:31494966). Antagonizes octopamine
CC signaling in response to food by promoting the dopamine-mediated
CC suppression of crh-1/CREB1 transcription factor activation in
CC cholinergic SIA neurons (PubMed:19609300). This is most likely in
CC association with the G(o)-alpha G-protein subunit goa-1
CC (PubMed:19609300). In association with the G-alpha protein gpa-14,
CC modulates two types of learning behavior: touch habituation and
CC chemosensory associative conditioning (PubMed:23607404). May act partly
CC via tsp-17 to negatively regulate dopamine reuptake transporter dat-1
CC activity (PubMed:25474638). Plays a role in behavioral plasticity and
CC regulates the decision-making process when conflicting alternatives are
CC present (PubMed:25536037). Promotes male mating behavior by
CC antagonizing acetylcholine signaling to control the protrusions of
CC copulatory spicules from the tail of males during hermaphrodite vulval
CC location (PubMed:23166505, PubMed:26156999). Modulates unc-7 activity
CC at gap junctions to promote inhibitory neuronal signaling transduction
CC between chemosensory and mechanosensory neurons, and thus ensures
CC spicule insertion attempts are confined to the hermaphrodite vulva
CC during copulation (PubMed:26156999). {ECO:0000269|PubMed:12887685,
CC ECO:0000269|PubMed:19609300, ECO:0000269|PubMed:23166505,
CC ECO:0000269|PubMed:23607404, ECO:0000269|PubMed:25474638,
CC ECO:0000269|PubMed:25536037, ECO:0000269|PubMed:26156999,
CC ECO:0000269|PubMed:31494966}.
CC -!- FUNCTION: [Isoform a]: G-protein coupled receptor which binds to the
CC neurotransmitter dopamine with high affinity leading to the activation
CC of an associated G-protein and downstream signaling pathways
CC (PubMed:12887685). Couples to G-proteins to inhibit adenylate cyclase
CC (AC) activity and cAMP production (PubMed:12887685).
CC {ECO:0000269|PubMed:12887685}.
CC -!- SUBUNIT: Interacts (via C-terminus) with the G-alpha protein gpa-14;
CC the interaction is direct. {ECO:0000269|PubMed:22280843}.
CC -!- INTERACTION:
CC E7EM37; Q9BIG2: gpa-14; NbExp=4; IntAct=EBI-6082999, EBI-2923711;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:12887685};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=c {ECO:0000312|WormBase:K09G1.4c}; Synonyms=CeDOP-2XL
CC {ECO:0000303|PubMed:22280843};
CC IsoId=E7EM37-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:K09G1.4a}; Synonyms=CeDOP2S
CC {ECO:0000303|PubMed:12887685};
CC IsoId=E7EM37-2; Sequence=VSP_060562;
CC Name=d {ECO:0000312|WormBase:K09G1.4d};
CC IsoId=E7EM37-3; Sequence=VSP_060563;
CC Name=e {ECO:0000312|WormBase:K09G1.4e};
CC IsoId=E7EM37-4; Sequence=VSP_060563, VSP_060564;
CC Name=f {ECO:0000312|WormBase:K09G1.4f};
CC IsoId=E7EM37-5; Sequence=VSP_060564;
CC Name=g {ECO:0000312|WormBase:K09G1.4g};
CC IsoId=E7EM37-6; Sequence=VSP_060562, VSP_060564;
CC -!- TISSUE SPECIFICITY: Expressed in all dopaminergic neurons
CC (PubMed:12887685). Expressed in neurons around the nerve ring and the
CC posterior side of the body including PDE neurons (PubMed:12887685). In
CC hermaphrodites, expressed in the head and tail ganglia including in the
CC RIA interneuron pair, and in a subset of sublateral interneurons and
CC the PDA neuron in the tail (PubMed:14568548). Expressed in cholinergic
CC SIA neurons (PubMed:19609300). Also expressed in the male tail
CC (PubMed:12887685, PubMed:23166505, PubMed:26156999). In males,
CC expressed in the dorsal spicule protractor, ventral spicule protractor,
CC dorsal spicule retractor and ventral spicule retractor muscles and the
CC sensory post-cloacal sensilla B (PCB) neuron (PubMed:23166505). In
CC males, expressed in the sensory hook neurons HOA (PubMed:26156999).
CC {ECO:0000269|PubMed:12887685, ECO:0000269|PubMed:14568548,
CC ECO:0000269|PubMed:19609300, ECO:0000269|PubMed:23166505,
CC ECO:0000269|PubMed:26156999}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the head and tail ganglia of larval
CC hermaphrodites. {ECO:0000269|PubMed:14568548}.
CC -!- MISCELLANEOUS: Modulates drug-mediated behavior, such as the response
CC to nicotine and amphetamine (PubMed:20410438, PubMed:23351035). Plays a
CC role in the sensitivity to the drug nicotine and promotes movement
CC towards nicotine sources (PubMed:23351035). Plays a role in promoting
CC amphetamine-induced loss of motility in water, termed swimming-induced
CC paralysis (PubMed:20410438). {ECO:0000269|PubMed:20410438,
CC ECO:0000269|PubMed:23351035}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AB125701; BAD01495.1; -; mRNA.
DR EMBL; AB125702; BAD01496.1; -; mRNA.
DR EMBL; BX284605; CAB03199.3; -; Genomic_DNA.
DR EMBL; BX284605; CBY85347.1; -; Genomic_DNA.
DR EMBL; BX284605; CCE72138.1; -; Genomic_DNA.
DR EMBL; BX284605; VGM69570.1; -; Genomic_DNA.
DR EMBL; BX284605; VGM69571.1; -; Genomic_DNA.
DR EMBL; BX284605; VGM69572.1; -; Genomic_DNA.
DR PIR; T23551; T23551.
DR RefSeq; NP_001024047.1; NM_001028876.2. [E7EM37-2]
DR RefSeq; NP_001024048.1; NM_001028877.3.
DR RefSeq; NP_001256126.1; NM_001269197.1. [E7EM37-1]
DR RefSeq; NP_001256127.1; NM_001269198.1. [E7EM37-3]
DR AlphaFoldDB; E7EM37; -.
DR SMR; E7EM37; -.
DR IntAct; E7EM37; 1.
DR STRING; 6239.K09G1.4c; -.
DR PaxDb; E7EM37; -.
DR EnsemblMetazoa; K09G1.4a.1; K09G1.4a.1; WBGene00001053. [E7EM37-2]
DR EnsemblMetazoa; K09G1.4c.1; K09G1.4c.1; WBGene00001053. [E7EM37-1]
DR EnsemblMetazoa; K09G1.4d.1; K09G1.4d.1; WBGene00001053. [E7EM37-3]
DR EnsemblMetazoa; K09G1.4e.1; K09G1.4e.1; WBGene00001053. [E7EM37-4]
DR EnsemblMetazoa; K09G1.4f.1; K09G1.4f.1; WBGene00001053. [E7EM37-5]
DR EnsemblMetazoa; K09G1.4g.1; K09G1.4g.1; WBGene00001053. [E7EM37-6]
DR GeneID; 179347; -.
DR KEGG; cel:CELE_K09G1.4; -.
DR CTD; 179347; -.
DR WormBase; K09G1.4a; CE35993; WBGene00001053; dop-2. [E7EM37-2]
DR WormBase; K09G1.4c; CE45633; WBGene00001053; dop-2. [E7EM37-1]
DR WormBase; K09G1.4d; CE46806; WBGene00001053; dop-2. [E7EM37-3]
DR WormBase; K09G1.4e; CE53007; WBGene00001053; dop-2. [E7EM37-4]
DR WormBase; K09G1.4f; CE53034; WBGene00001053; dop-2. [E7EM37-5]
DR WormBase; K09G1.4g; CE52992; WBGene00001053; dop-2. [E7EM37-6]
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000164988; -.
DR HOGENOM; CLU_009579_11_1_1; -.
DR InParanoid; E7EM37; -.
DR OMA; MEAGETW; -.
DR OrthoDB; 1215361at2759; -.
DR Reactome; R-CEL-390651; Dopamine receptors.
DR Reactome; R-CEL-418594; G alpha (i) signalling events.
DR PRO; PR:E7EM37; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00001053; Expressed in larva and 3 other tissues.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0001591; F:dopamine neurotransmitter receptor activity, coupled via Gi/Go; IMP:WormBase.
DR GO; GO:0004993; F:G protein-coupled serotonin receptor activity; IBA:GO_Central.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0071419; P:cellular response to amphetamine; IMP:UniProtKB.
DR GO; GO:0071316; P:cellular response to nicotine; IMP:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0007212; P:dopamine receptor signaling pathway; IMP:WormBase.
DR GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; IBA:GO_Central.
DR GO; GO:0033602; P:negative regulation of dopamine secretion; IMP:UniProtKB.
DR GO; GO:0090327; P:negative regulation of locomotion involved in locomotory behavior; IMP:UniProtKB.
DR GO; GO:0090326; P:positive regulation of locomotion involved in locomotory behavior; IMP:UniProtKB.
DR GO; GO:1902437; P:positive regulation of male mating behavior; IMP:UniProtKB.
DR GO; GO:1902435; P:regulation of male mating behavior; IMP:UniProtKB.
DR GO; GO:1902847; P:regulation of neuronal signal transduction; IMP:UniProtKB.
DR GO; GO:0032094; P:response to food; IMP:WormBase.
DR GO; GO:0034609; P:spicule insertion; IMP:UniProtKB.
DR GO; GO:0034608; P:vulval location; IMP:UniProtKB.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
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 Alternative splicing; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..849
FT /note="Dopamine receptor 2"
FT /id="PRO_0000449488"
FT TOPO_DOM 1..39
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 40..60
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 61..70
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 71..91
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 92..112
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 113..133
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 134..155
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 156..176
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 177..203
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 204..224
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 225..759
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 760..780
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 781..798
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 799..819
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 820..849
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 183..849
FT /note="Required for the interaction with gpa-14"
FT /evidence="ECO:0000269|PubMed:22280843"
FT REGION 450..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..500
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 8
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 111..190
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VAR_SEQ 268..412
FT /note="VVNVMMAALPSMTRRMRQFERHRRAIELAGDEEWEEDELDVMDECCGGDDAG
FT DDDDDYHADNGQGVVEASAPRTTSMLRRIINAASVGTANSTAQSVASASGMPAFFAQNI
FT STTSPSSSSCARTTTTTSAIPKASGDLPLPMLLN -> D (in isoform a and
FT isoform g)"
FT /evidence="ECO:0000305"
FT /id="VSP_060562"
FT VAR_SEQ 297..412
FT /note="GDEEWEEDELDVMDECCGGDDAGDDDDDYHADNGQGVVEASAPRTTSMLRRI
FT INAASVGTANSTAQSVASASGMPAFFAQNISTTSPSSSSCARTTTTTSAIPKASGDLPL
FT PMLLN -> D (in isoform d and isoform e)"
FT /evidence="ECO:0000305"
FT /id="VSP_060563"
FT VAR_SEQ 598..602
FT /note="Missing (in isoform e, isoform f and isoform g)"
FT /evidence="ECO:0000305"
FT /id="VSP_060564"
FT MUTAGEN 183..849
FT /note="Missing: In Isoform c; abolishes interaction with
FT gpa-14."
FT /evidence="ECO:0000269|PubMed:22280843"
FT CONFLICT 403..412
FT /note="GDLPLPMLLN -> D (in Ref. 1; BAD01495)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 849 AA; 94160 MW; 3B7B22704CE67BCC CRC64;
MEAGETWNVS LEWPPPSLDL STITQTPSTI VGSGIPLNYA GLSLIVIPLI TLLGNLLVII
SVLRYRALQS AINFLILGLA VADLLVAIIV MPYAVYVYVT NGDWYLGNLM CDIYMASDVC
CSTASILLLA VISFDRYRAV SLPIQYSRQS QNVKRVWTLI AVIWLVSLTL ASPMVFGVNV
RPPDANPYEC RFYNAEFSIL SSMISFVIPC FLVLFVYIRI IIALKKREKA AKMRREKNTI
AHGLTMRPDT GEEQVDEEAA GRIVAGPVVN VMMAALPSMT RRMRQFERHR RAIELAGDEE
WEEDELDVMD ECCGGDDAGD DDDDYHADNG QGVVEASAPR TTSMLRRIIN AASVGTANST
AQSVASASGM PAFFAQNIST TSPSSSSCAR TTTTTSAIPK ASGDLPLPML LNEREFGNSS
TPRSSLESLS ENVNVITNDF VSENCTTFSR RSSYADDSQP TSSQTSSGDG RSYSIKGQKR
FRNLSRNYST KHHRKVVKVN RGNSRNNSRT ASITNQSDDA LIPAIIRTIS RKSPRLFRRD
KTDIKKHSMI LANPITEPPK EYRRVSMPIH PTNSQTETET ISASRDIENL PTTTISRSTT
ANSAELLGSP DDFEKFPALI TETVLEDVLA ETREGCFMQP TVSFALTVRE MEGNALNNLK
GCSVESSRRV SQVDPPLAIQ ILTRPSLPHL DLQRMDSIGT TCSSKTRADS LRSVDSKGSK
KSNRNGIAVK LVKRAIKHEH SLKRKVSKAQ RKEKRATKTL GVVVGVFLVC WVPFFVINIL
NAVCILLNKD SCQVGYDLFF YCTWIGYMNS FMNPIIYTIF NTEFRRAFKS IIFGRNSTRH
HFSNKQAHV
