ID GPR39_HUMAN Reviewed; 453 AA.
AC O43194; B2RC12; B6V9G4; Q08AS2; Q53R01;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 27-MAR-2024, entry version 179.
DE RecName: Full=G-protein coupled receptor 39;
GN Name=GPR39;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9441746; DOI=10.1006/geno.1997.5069;
RA McKee K.K., Tan C.P., Palyha O.C., Liu J., Feighner S.D., Hreniuk D.L.,
RA Smith R.G., Howard A.D., van der Ploeg L.H.T.;
RT "Cloning and characterization of two human G protein-coupled receptor genes
RT (GPR38 and GPR39) related to the growth hormone secretagogue and
RT neurotensin receptors.";
RL Genomics 46:426-434(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Kaighin V.A., Martin A.L., Aronstam R.S.;
RT "Isolation of cDNA coding for Homo sapiens G protein-coupled receptor 39
RT (GPR39).";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-50.
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 DISULFIDE BONDS.
RX PubMed=18693759; DOI=10.1021/bi8005016;
RA Storjohann L., Holst B., Schwartz T.W.;
RT "A second disulfide bridge from the N-terminal domain to extracellular loop
RT 2 dampens receptor activity in GPR39.";
RL Biochemistry 47:9198-9207(2008).
RN [7]
RP ZINC-BINDING SITES, AND MUTAGENESIS OF HIS-17; HIS-19; HIS-312 AND ASP-313.
RX PubMed=18588883; DOI=10.1016/j.febslet.2008.06.030;
RA Storjohann L., Holst B., Schwartz T.W.;
RT "Molecular mechanism of Zn2+ agonism in the extracellular domain of
RT GPR39.";
RL FEBS Lett. 582:2583-2588(2008).
RN [8]
RP FUNCTION.
RX PubMed=18180304; DOI=10.1074/jbc.m704323200;
RA Dittmer S., Sahin M., Pantlen A., Saxena A., Toutzaris D., Pina A.L.,
RA Geerts A., Golz S., Methner A.;
RT "The constitutively active orphan G-protein-coupled receptor GPR39 protects
RT from cell death by increasing secretion of pigment epithelium-derived
RT growth factor.";
RL J. Biol. Chem. 283:7074-7081(2008).
RN [9]
RP FUNCTION.
RX PubMed=20522546; DOI=10.1074/jbc.m110.107490;
RA Sharir H., Zinger A., Nevo A., Sekler I., Hershfinkel M.;
RT "Zinc released from injured cells is acting via the Zn2+-sensing receptor,
RT ZnR, to trigger signaling leading to epithelial repair.";
RL J. Biol. Chem. 285:26097-26106(2010).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-396, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH HTR1A AND GALR1.
RX PubMed=26365466; DOI=10.1016/j.bbadis.2015.09.003;
RA Tena-Campos M., Ramon E., Borroto-Escuela D.O., Fuxe K., Garriga P.;
RT "The zinc binding receptor GPR39 interacts with 5-HT1A and GalR1 to form
RT dynamic heteroreceptor complexes with signaling diversity.";
RL Biochim. Biophys. Acta 1852:2585-2592(2015).
CC -!- FUNCTION: Zinc-sensing receptor that can sense changes in extracellular
CC Zn(2+), mediate Zn(2+) signal transmission, and participates in the
CC regulation of numerous physiological processes including glucose
CC homeostasis regulation, gastrointestinal mobility, hormone secretion
CC and cell death (PubMed:18180304). Activation by Zn(2+) in keratinocytes
CC increases the intracellular concentration of Ca(2+) and activates the
CC ERK/MAPK and PI3K/AKT signaling pathways leading to epithelial repair
CC (PubMed:20522546). Plays an essential role in normal wound healing by
CC inducing the production of cytokines including the major inflammatory
CC cytokine IL6 via the PKC/MAPK/CEBPB pathway (By similarity). Regulates
CC adipose tissue metabolism, especially lipolysis, and regulates the
CC function of lipases, such as hormone-sensitive lipase and adipose
CC triglyceride lipase (By similarity). Plays a role in the inhibition of
CC cell death and protects against oxidative, endoplasmic reticulum and
CC mitochondrial stress by inducing secretion of the cytoprotective
CC pigment epithelium-derived growth factor (PEDF) and probably other
CC protective transcripts in a GNA13/RHOA/SRE-dependent manner
CC (PubMed:18180304). Forms dynamic heteroreceptor complexes with HTR1A
CC and GALR1 depending on cell type or specific physiological states,
CC resulting in signaling diversity: HTR1A-GPR39 shows additive increase
CC in signaling along the serum response element (SRE) and NF-kappa-B
CC pathways while GALR1 acts as an antagonist blocking SRE
CC (PubMed:26365466). {ECO:0000250|UniProtKB:Q5U431,
CC ECO:0000269|PubMed:18180304, ECO:0000269|PubMed:20522546,
CC ECO:0000269|PubMed:26365466}.
CC -!- SUBUNIT: Interacts with HTR1A. Interacts with GALR1.
CC {ECO:0000269|PubMed:26365466}.
CC -!- INTERACTION:
CC O43194; P08908: HTR1A; NbExp=4; IntAct=EBI-7165599, EBI-6570214;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26365466};
CC Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in many tissues, including the stomach,
CC intestine and hypothalamus. {ECO:0000269|PubMed:9441746}.
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; AF034633; AAC26082.1; -; mRNA.
DR EMBL; FJ348258; ACI96302.1; -; mRNA.
DR EMBL; AK314895; BAG37409.1; -; mRNA.
DR EMBL; AC098800; AAY24154.1; -; Genomic_DNA.
DR EMBL; AC079773; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC125046; AAI25047.1; -; mRNA.
DR CCDS; CCDS2170.1; -.
DR RefSeq; NP_001499.1; NM_001508.2.
DR AlphaFoldDB; O43194; -.
DR SMR; O43194; -.
DR BioGRID; 109121; 4.
DR IntAct; O43194; 4.
DR MINT; O43194; -.
DR STRING; 9606.ENSP00000327417; -.
DR BindingDB; O43194; -.
DR ChEMBL; CHEMBL3091266; -.
DR DrugCentral; O43194; -.
DR GuidetoPHARMACOLOGY; 105; -.
DR TCDB; 9.A.14.1.15; the g-protein-coupled receptor (gpcr) family.
DR GlyCosmos; O43194; 3 sites, No reported glycans.
DR GlyGen; O43194; 3 sites.
DR iPTMnet; O43194; -.
DR PhosphoSitePlus; O43194; -.
DR SwissPalm; O43194; -.
DR BioMuta; GPR39; -.
DR EPD; O43194; -.
DR jPOST; O43194; -.
DR MassIVE; O43194; -.
DR MaxQB; O43194; -.
DR PaxDb; 9606-ENSP00000327417; -.
DR PeptideAtlas; O43194; -.
DR ProteomicsDB; 48809; -.
DR Antibodypedia; 18657; 388 antibodies from 34 providers.
DR DNASU; 2863; -.
DR Ensembl; ENST00000329321.4; ENSP00000327417.3; ENSG00000183840.8.
DR GeneID; 2863; -.
DR KEGG; hsa:2863; -.
DR MANE-Select; ENST00000329321.4; ENSP00000327417.3; NM_001508.3; NP_001499.1.
DR UCSC; uc002ttl.4; human.
DR AGR; HGNC:4496; -.
DR CTD; 2863; -.
DR DisGeNET; 2863; -.
DR GeneCards; GPR39; -.
DR HGNC; HGNC:4496; GPR39.
DR HPA; ENSG00000183840; Tissue enhanced (intestine).
DR MIM; 602886; gene.
DR neXtProt; NX_O43194; -.
DR OpenTargets; ENSG00000183840; -.
DR PharmGKB; PA28885; -.
DR VEuPathDB; HostDB:ENSG00000183840; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01100000263518; -.
DR HOGENOM; CLU_009579_6_5_1; -.
DR InParanoid; O43194; -.
DR OMA; HNMTICT; -.
DR OrthoDB; 3471593at2759; -.
DR PhylomeDB; O43194; -.
DR TreeFam; TF331140; -.
DR PathwayCommons; O43194; -.
DR Reactome; R-HSA-373076; Class A/1 (Rhodopsin-like receptors).
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR Reactome; R-HSA-418555; G alpha (s) signalling events.
DR SignaLink; O43194; -.
DR BioGRID-ORCS; 2863; 10 hits in 1144 CRISPR screens.
DR ChiTaRS; GPR39; human.
DR GeneWiki; GPR39; -.
DR GenomeRNAi; 2863; -.
DR Pharos; O43194; Tchem.
DR PRO; PR:O43194; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; O43194; Protein.
DR Bgee; ENSG00000183840; Expressed in oocyte and 135 other cell types or tissues.
DR ExpressionAtlas; O43194; baseline and differential.
DR Genevisible; O43194; HS.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR CDD; cd15135; 7tmA_GPR39; 1.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR46752; G-PROTEIN COUPLED RECEPTOR 39; 1.
DR PANTHER; PTHR46752:SF1; G-PROTEIN COUPLED RECEPTOR 39; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
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 Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Metal-binding; Phosphoprotein; Receptor; Reference proteome;
KW Transducer; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..453
FT /note="G-protein coupled receptor 39"
FT /id="PRO_0000069565"
FT TOPO_DOM 1..34
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TRANSMEM 35..55
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TOPO_DOM 56..69
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TRANSMEM 70..89
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TOPO_DOM 90..109
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TRANSMEM 110..131
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TOPO_DOM 132..151
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TRANSMEM 152..172
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TOPO_DOM 173..217
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TRANSMEM 218..242
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TOPO_DOM 243..283
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TRANSMEM 284..305
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TOPO_DOM 306..323
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TRANSMEM 324..344
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TOPO_DOM 345..453
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT REGION 255..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..442
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 17
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:18588883"
FT BINDING 19
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:18588883"
FT MOD_RES 396
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 11..191
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521,
FT ECO:0000269|PubMed:18693759"
FT DISULFID 108..210
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521,
FT ECO:0000269|PubMed:18693759"
FT VARIANT 50
FT /note="A -> V (in dbSNP:rs2241764)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_022067"
FT VARIANT 390
FT /note="R -> C (in dbSNP:rs16838944)"
FT /id="VAR_049393"
FT MUTAGEN 17
FT /note="H->A: Decreases activation by Zn(2+). Abolishes
FT activation by Zn(2+); when associated with A-19."
FT /evidence="ECO:0000269|PubMed:18588883"
FT MUTAGEN 19
FT /note="H->A: Decreases activation by Zn(2+). Abolishes
FT activation by Zn(2+); when associated with A-17."
FT /evidence="ECO:0000269|PubMed:18588883"
FT MUTAGEN 312
FT /note="H->A: Not affect constitutive or Zn(2+)-induced
FT activation."
FT /evidence="ECO:0000269|PubMed:18588883"
FT MUTAGEN 313
FT /note="D->A: Induces very high constitutive activity and
FT eliminates Zn(2+)-induced activation."
FT /evidence="ECO:0000269|PubMed:18588883"
SQ SEQUENCE 453 AA; 51329 MW; 8E3A233420D9021E CRC64;
MASPSLPGSD CSQIIDHSHV PEFEVATWIK ITLILVYLII FVMGLLGNSA TIRVTQVLQK
KGYLQKEVTD HMVSLACSDI LVFLIGMPME FYSIIWNPLT TSSYTLSCKL HTFLFEACSY
ATLLHVLTLS FERYIAICHP FRYKAVSGPC QVKLLIGFVW VTSALVALPL LFAMGTEYPL
VNVPSHRGLT CNRSSTRHHE QPETSNMSIC TNLSSRWTVF QSSIFGAFVV YLVVLLSVAF
MCWNMMQVLM KSQKGSLAGG TRPPQLRKSE SEESRTARRQ TIIFLRLIVV TLAVCWMPNQ
IRRIMAAAKP KHDWTRSYFR AYMILLPFSE TFFYLSSVIN PLLYTVSSQQ FRRVFVQVLC
CRLSLQHANH EKRLRVHAHS TTDSARFVQR PLLFASRRQS SARRTEKIFL STFQSEAEPQ
SKSQSLSLES LEPNSGAKPA NSAAENGFQE HEV
//
