GCY28_CAEEL
ID GCY28_CAEEL Reviewed; 1276 AA.
AC Q86GV3; H2L0J9; Q965F7; Q965F8;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Receptor-type guanylate cyclase gcy-28 {ECO:0000305};
DE EC=4.6.1.2 {ECO:0000269|PubMed:9188508};
DE AltName: Full=GCY-X1 {ECO:0000303|PubMed:9188508};
DE Flags: Precursor;
GN Name=gcy-28 {ECO:0000312|WormBase:T01A4.1c};
GN ORFNames=T01A4.1 {ECO:0000312|WormBase:T01A4.1c};
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 C), FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9188508; DOI=10.1074/jbc.272.25.16035;
RA Baude E.J., Arora V.K., Yu S., Garbers D.L., Wedel B.J.;
RT "The cloning of a Caenorhabditis elegans guanylyl cyclase and the
RT construction of a ligand-sensitive mammalian/nematode chimeric receptor.";
RL J. Biol. Chem. 272:16035-16039(1997).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; C AND D), FUNCTION, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF PHE-1204.
RX PubMed=18817734; DOI=10.1016/j.neuron.2008.07.038;
RA Tsunozaki M., Chalasani S.H., Bargmann C.I.;
RT "A behavioral switch: cGMP and PKC signaling in olfactory neurons reverses
RT odor preference in C. elegans.";
RL Neuron 59:959-971(2008).
RN [3] {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 [4] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=16547101; DOI=10.1534/genetics.106.055749;
RA Ortiz C.O., Etchberger J.F., Posy S.L., Frokjaer-Jensen C., Lockery S.,
RA Honig B., Hobert O.;
RT "Searching for neuronal left/right asymmetry: genomewide analysis of
RT nematode receptor-type guanylyl cyclases.";
RL Genetics 173:131-149(2006).
RN [5] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF PHE-1204.
RX PubMed=21414922; DOI=10.1523/jneurosci.4691-10.2011;
RA Shinkai Y., Yamamoto Y., Fujiwara M., Tabata T., Murayama T., Hirotsu T.,
RA Ikeda D.D., Tsunozaki M., Iino Y., Bargmann C.I., Katsura I., Ishihara T.;
RT "Behavioral choice between conflicting alternatives is regulated by a
RT receptor guanylyl cyclase, GCY-28, and a receptor tyrosine kinase, SCD-2,
RT in AIA interneurons of Caenorhabditis elegans.";
RL J. Neurosci. 31:3007-3015(2011).
CC -!- FUNCTION: Guanylate cyclase involved in the production of the second
CC messenger cGMP (PubMed:9188508). Regulates olfactory perception in AWC
CC sensory neurons although may not be involved in the primary sensory
CC transduction steps (PubMed:18817734). {ECO:0000269|PubMed:18817734,
CC ECO:0000269|PubMed:9188508}.
CC -!- FUNCTION: Isoforms c: Regulates sensory integration of conflicting
CC sensory cues in AIA interneurons (PubMed:21414922).
CC -!- FUNCTION: [Isoform d]: Regulates sensory integration of conflicting
CC sensory cues in AIA interneurons (PubMed:21414922).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP = 3',5'-cyclic GMP + diphosphate; Xref=Rhea:RHEA:13665,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57746; EC=4.6.1.2;
CC Evidence={ECO:0000269|PubMed:9188508};
CC -!- SUBCELLULAR LOCATION: [Isoform c]: Cell membrane {ECO:0000305}; Single-
CC pass type I membrane protein {ECO:0000305}. Cell projection, dendrite
CC {ECO:0000269|PubMed:18817734}. Cell projection, axon
CC {ECO:0000269|PubMed:18817734}. Perikaryon
CC {ECO:0000269|PubMed:18817734}. Note=Excluded from the neuronal sensory
CC cilia. {ECO:0000269|PubMed:18817734}.
CC -!- SUBCELLULAR LOCATION: [Isoform d]: Cell membrane {ECO:0000305}; Single-
CC pass type I membrane protein {ECO:0000305}. Cell projection, dendrite
CC {ECO:0000269|PubMed:18817734}. Cell projection, axon
CC {ECO:0000269|PubMed:18817734}. Perikaryon
CC {ECO:0000269|PubMed:18817734}. Note=Enriched in the axon of AWC sensory
CC neurons. Is excluded from the neuronal sensory cilia.
CC {ECO:0000269|PubMed:18817734}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=c {ECO:0000312|WormBase:T01A4.1c}; Synonyms=GCY-X1
CC {ECO:0000305|PubMed:9188508};
CC IsoId=Q86GV3-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:T01A4.1a};
CC IsoId=Q86GV3-2; Sequence=VSP_057712, VSP_057713, VSP_057714,
CC VSP_057715;
CC Name=b {ECO:0000312|WormBase:T01A4.1b};
CC IsoId=Q86GV3-3; Sequence=VSP_057710, VSP_057716, VSP_057717;
CC Name=d {ECO:0000312|WormBase:T01A4.1d};
CC IsoId=Q86GV3-4; Sequence=VSP_057711, VSP_057714, VSP_057715;
CC -!- TISSUE SPECIFICITY: Expressed in head neurons, ventral cord and tail
CC neurons, body wall muscle, hypodermis, somatic gonad and intestine
CC (PubMed:16547101). Isoform d is expressed specifically in AIA
CC interneurons (PubMed:21414922). {ECO:0000269|PubMed:16547101,
CC ECO:0000269|PubMed:21414922}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
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DR EMBL; FO081694; CCD73355.1; -; Genomic_DNA.
DR EMBL; FO081694; CCD73353.1; -; Genomic_DNA.
DR EMBL; FO081694; CCD73354.1; -; Genomic_DNA.
DR EMBL; FO081694; CCD73356.1; -; Genomic_DNA.
DR RefSeq; NP_001021600.1; NM_001026429.2. [Q86GV3-1]
DR RefSeq; NP_001249628.1; NM_001262699.1. [Q86GV3-4]
DR RefSeq; NP_491379.3; NM_058978.3.
DR RefSeq; NP_491380.1; NM_058979.1.
DR AlphaFoldDB; Q86GV3; -.
DR SMR; Q86GV3; -.
DR STRING; 6239.T01A4.1c; -.
DR EPD; Q86GV3; -.
DR PaxDb; Q86GV3; -.
DR PeptideAtlas; Q86GV3; -.
DR EnsemblMetazoa; T01A4.1a.1; T01A4.1a.1; WBGene00020131. [Q86GV3-2]
DR EnsemblMetazoa; T01A4.1b.1; T01A4.1b.1; WBGene00020131. [Q86GV3-3]
DR EnsemblMetazoa; T01A4.1c.1; T01A4.1c.1; WBGene00020131. [Q86GV3-1]
DR EnsemblMetazoa; T01A4.1d.1; T01A4.1d.1; WBGene00020131. [Q86GV3-4]
DR GeneID; 172051; -.
DR KEGG; cel:CELE_T01A4.1; -.
DR UCSC; T01A4.1c; c. elegans.
DR CTD; 172051; -.
DR WormBase; T01A4.1a; CE33582; WBGene00020131; gcy-28. [Q86GV3-2]
DR WormBase; T01A4.1b; CE25977; WBGene00020131; gcy-28. [Q86GV3-3]
DR WormBase; T01A4.1c; CE33583; WBGene00020131; gcy-28. [Q86GV3-1]
DR WormBase; T01A4.1d; CE43478; WBGene00020131; gcy-28. [Q86GV3-4]
DR eggNOG; KOG1023; Eukaryota.
DR GeneTree; ENSGT00940000156223; -.
DR InParanoid; Q86GV3; -.
DR OMA; KCLTRTI; -.
DR OrthoDB; 229634at2759; -.
DR PhylomeDB; Q86GV3; -.
DR PRO; PR:Q86GV3; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00020131; Expressed in larva and 4 other tissues.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0044297; C:cell body; IDA:WormBase.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; IDA:WormBase.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004383; F:guanylate cyclase activity; IDA:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001653; F:peptide receptor activity; IBA:GO_Central.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0006182; P:cGMP biosynthetic process; IBA:GO_Central.
DR GO; GO:0006935; P:chemotaxis; IMP:WormBase.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0042048; P:olfactory behavior; IMP:WormBase.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0007168; P:receptor guanylyl cyclase signaling pathway; IBA:GO_Central.
DR GO; GO:0007606; P:sensory perception of chemical stimulus; IMP:UniProtKB.
DR GO; GO:0050893; P:sensory processing; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd07302; CHD; 1.
DR Gene3D; 3.30.70.1230; -; 1.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR018297; A/G_cyclase_CS.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR001170; ANPR/GUC.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR028082; Peripla_BP_I.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00255; NATPEPTIDER.
DR SMART; SM00044; CYCc; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
DR SUPFAM; SSF55073; SSF55073; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell membrane; Cell projection;
KW cGMP biosynthesis; Chemotaxis; Coiled coil; Glycoprotein; GTP-binding;
KW Lyase; Magnesium; Membrane; Metal-binding; Nucleotide-binding; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..1276
FT /note="Receptor-type guanylate cyclase gcy-28"
FT /evidence="ECO:0000255"
FT /id="PRO_0000433295"
FT TOPO_DOM 19..515
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 516..536
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 537..1276
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 717..1013
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 1086..1215
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT REGION 562..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1017..1063
FT /evidence="ECO:0000255"
FT COMPBIAS 638..666
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..709
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 723..731
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 756
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1091
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 1091
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 1092
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 1135
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 1135
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 384
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 414
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 428
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 1..627
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_057710"
FT VAR_SEQ 1..287
FT /note="MLRWLTLLSCILLTALHGNIVEDVGAAQQASYPPPPPPFPFNVIVILPKRES
FT TYDNFGMTLQKAMPVIDIAVQEVIKAKKLPPGWINLTYWDSRLYEDILLAERHATVGVI
FT QAYCEHRLDAILGFADNYGLATVTKVTAGLNGGIPILTTSGMPSLLNSKKEYPFLTRMQ
FT GSYRLLADSMYQLIAYHDEDSVSKSNSSLNYLNLIFFYHDKRRAVNRVIAQDESQETGA
FT TSSHCYFSLYAIKRYFTEKSKTFKREWALNTPQFPFDEDLVIERETFKQWLREISLQS
FT -> MWINSTRTLIFNHFVRIVLVLLLSHEVVTKSNRKFEEISVKHPIHLVIPLPDDDDF
FT SDGKNPFLFSSHKVKPLADLALERVYREGILPNNSVNLIYRDSKLSDAIGPNVAVEQLL
FT RKQIDCIIGYAYGYALAPVARMSPYWKNGIPIITPIGLTMSLDDKREYQLMTRINSPYK
FT VVSSAVSTLFNTYKWKRHIFMFHHAKAPSVAVGECFLLMASLQHPLRKVMEMQHNFFTF
FT NEDHGANISKAERHNQFRNYLRASSNMA (in isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_057711"
FT VAR_SEQ 1..233
FT /note="MLRWLTLLSCILLTALHGNIVEDVGAAQQASYPPPPPPFPFNVIVILPKRES
FT TYDNFGMTLQKAMPVIDIAVQEVIKAKKLPPGWINLTYWDSRLYEDILLAERHATVGVI
FT QAYCEHRLDAILGFADNYGLATVTKVTAGLNGGIPILTTSGMPSLLNSKKEYPFLTRMQ
FT GSYRLLADSMYQLIAYHDEDSVSKSNSSLNYLNLIFFYHDKRRAVNRVIAQDESQETGA
FT TSSH -> MILSDVLLLSLVISSSSSSSHQHSLLPIDIVVGLPIEEGDRGKNPFLLTLA
FT KSKPVFDVALQDVYHLRILPYGSLKVTFENSALSDAVGPQKMIEHYCNKTVDAIMGLPY
FT VYALAPVARISKFWGQGVPVFTTTALVDELGDRNEFPLLTRMMGSYKSLGKLVTRIAER
FT FEWQHYFFMFNDEVARGPRNKGRSE (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_057712"
FT VAR_SEQ 239..289
FT /note="YAIKRYFTEKSKTFKREWALNTPQFPFDEDLVIERETFKQWLREISLQSNV
FT -> SAIKNLIMNNKTSTWNVKMFSEFEADRLQYRALLSEASVMSNL (in isoform
FT a)"
FT /evidence="ECO:0000305"
FT /id="VSP_057713"
FT VAR_SEQ 510
FT /note="P -> PQ (in isoform a and isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_057714"
FT VAR_SEQ 602..614
FT /note="Missing (in isoform a and isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_057715"
FT VAR_SEQ 1220..1264
FT /note="PLKIHVSQQTYDILMQEAGFKLELRGSVEMKGKGMQTTYWLRGYK -> RMF
FT WNFSLYKIYKFKVFKNKIELDFLKNEKESIEFEGKKMVTEFN (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_057716"
FT VAR_SEQ 1265..1276
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_057717"
FT MUTAGEN 1204
FT /note="F->L: In ky713; loss of chemotaxis response to
FT butanone. Defect in sensory integration when confronted to
FT two opposing environmental chemicals."
FT /evidence="ECO:0000269|PubMed:18817734,
FT ECO:0000269|PubMed:21414922"
SQ SEQUENCE 1276 AA; 144989 MW; 4941A68DD206E547 CRC64;
MLRWLTLLSC ILLTALHGNI VEDVGAAQQA SYPPPPPPFP FNVIVILPKR ESTYDNFGMT
LQKAMPVIDI AVQEVIKAKK LPPGWINLTY WDSRLYEDIL LAERHATVGV IQAYCEHRLD
AILGFADNYG LATVTKVTAG LNGGIPILTT SGMPSLLNSK KEYPFLTRMQ GSYRLLADSM
YQLIAYHDED SVSKSNSSLN YLNLIFFYHD KRRAVNRVIA QDESQETGAT SSHCYFSLYA
IKRYFTEKSK TFKREWALNT PQFPFDEDLV IERETFKQWL REISLQSNVI ILCASPDTVR
EIMLAAHDLG MATSGEYVFI NIDVSTGSHA EQPWIRANDT NNEENEKAKE AYRALKTISL
RRSDLDEYKN FELRVKERAD QKYNYTNITG KDYEMNNFIS AFYDAVLLYA IALNETIQSG
LDPRNGHNIT SRMWGRTFVG ITGNVSIDHN GDRYSDYSLL DLDPVQNRFV EVAYYSGASN
QLKTVGQLHW VGGKPPTDLP ICGYDKSKCP GYPLHVYLLM GSFLLILVLV GLFIFFWRRY
KLEQELAAMS WKIRWEELDG EESQKKNEKK KAKKRKNHND YLPESDPLLR STSRSSVNSD
KFDEDSLIPI RFRLRSSSSG TTRKISAMID RKLSIFTRKK STPPSESQKN GGLTPNSLQK
AENGDCSPIN EVQFRLPLND RRVSSPSSEA TRKKNSNEED PENGAKKSLS LKNRKLSFGM
VSFKSGSGGS VETIAQNNTQ IYTKTAIFKG VVVAIKKLNI DPKKYPRLDL SRAQLMELKK
MKDLQHDHIT RFTGACIDFP HYCVVTEYCP KGSLEDILEN EKIELDKLMK YSLLHDLVKG
LFFLHNSEIR SHGRLKSSNC VVDSRFVLKV TDFGLHRLHC LEEINLEEIG EHAYYKKMLW
TAPELLRDSN APPMGTQKGD IYSFAIILHE MMFRKGVFAL ENEDLSPNEI VQRVRKPVSE
DQEPLRPWVS ETGEGEGDDA LNDTLLSLMV ACWSEDPHER PEVSSVRKAV RSLNRDNETS
NLVDNLLKRM EQYANNLEGL VEERTQEYLA EKKKVEELLH QLLPPAIADT LIAGRAVQAE
SYDCVTIYFS DIVGFTSLSS QSTPMQVVTL LNDLYLAFDG VVDNFKVYKV ETIGDAYMVV
SGLPERRDDH ANQIAQMSLS LLHKVKNFVI RHRPHEQLKL RIGMHSGSVV AGVVGSKMPR
YCLFGDTVNT SSRMESNGLP LKIHVSQQTY DILMQEAGFK LELRGSVEMK GKGMQTTYWL
RGYKDVEIPD FGEEFA
