SSR3_HUMAN
ID SSR3_HUMAN Reviewed; 418 AA.
AC P32745; A8K550; Q53ZR7;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Somatostatin receptor type 3;
DE Short=SS-3-R;
DE Short=SS3-R;
DE Short=SS3R;
DE Short=SST3;
DE AltName: Full=SSR-28;
GN Name=SSTR3;
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 [GENOMIC DNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=1337145; DOI=10.1210/mend.6.12.1337145;
RA Yamada Y., Reisine T., Law S.F., Ihara Y., Kubota A., Kagimoto S.,
RA Seino M., Seino Y., Bell G.I., Seino S.;
RT "Somatostatin receptors, an expanding gene family: cloning and functional
RT characterization of human SSTR3, a protein coupled to adenylyl cyclase.";
RL Mol. Endocrinol. 6:2136-2142(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8097479; DOI=10.1016/0014-5793(93)80124-d;
RA Corness J.D., Demchyshyn L.L., Seeman P., van Tol H.H.M., Srikant C.B.,
RA Kent G., Patel Y.C., Niznik H.B.;
RT "A human somatostatin receptor (SSTR3), located on chromosome 22, displays
RT preferential affinity for somatostatin-14 like peptides.";
RL FEBS Lett. 321:279-284(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Rasch A.C., Boehnke C., Petersenn S.;
RT "The human somatostatin receptor subtype 3 contains an upstream exon in the
RT 5'-untranslated region: functional promoter studies.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Kopatz S.A., Aronstam R.S., Sharma S.V.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [8]
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).
CC -!- FUNCTION: Receptor for somatostatin-14 and -28. This receptor is
CC coupled via pertussis toxin sensitive G proteins to inhibition of
CC adenylyl cyclase. {ECO:0000269|PubMed:1337145}.
CC -!- SUBUNIT: Homodimer and heterodimer with SSTR2. Heterodimerization with
CC SSTR2 inactivates SSTR3 receptor function (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC P32745; P05067: APP; NbExp=3; IntAct=EBI-6266935, EBI-77613;
CC P32745; O75970: MPDZ; NbExp=5; IntAct=EBI-6266935, EBI-821405;
CC P32745; P30874: SSTR2; NbExp=3; IntAct=EBI-6266935, EBI-6266898;
CC P32745; O55164: Mpdz; Xeno; NbExp=2; IntAct=EBI-6266935, EBI-7401093;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Note=Internalized into endoplasmic vesicles upon
CC somatostatin-stimulation. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Brain, pituitary and pancreas.
CC {ECO:0000269|PubMed:1337145}.
CC -!- PTM: Phosphorylated. Phosphorylation increases upon somatostatin
CC binding (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; M96738; AAA60592.1; -; Genomic_DNA.
DR EMBL; AY277678; AAP32288.1; -; Genomic_DNA.
DR EMBL; AY322541; AAP84354.1; -; Genomic_DNA.
DR EMBL; CR456585; CAG30471.1; -; mRNA.
DR EMBL; AK291165; BAF83854.1; -; mRNA.
DR EMBL; Z82188; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC096829; AAH96829.1; -; mRNA.
DR CCDS; CCDS13944.1; -.
DR PIR; A46226; A46226.
DR RefSeq; NP_001042.1; NM_001051.4.
DR RefSeq; NP_001265616.1; NM_001278687.2.
DR RefSeq; XP_005261778.1; XM_005261721.4.
DR RefSeq; XP_006724374.1; XM_006724311.2.
DR RefSeq; XP_011528651.1; XM_011530349.2.
DR RefSeq; XP_016884412.1; XM_017028923.1.
DR RefSeq; XP_016884413.1; XM_017028924.1.
DR AlphaFoldDB; P32745; -.
DR SMR; P32745; -.
DR BioGRID; 112631; 13.
DR CORUM; P32745; -.
DR IntAct; P32745; 12.
DR MINT; P32745; -.
DR STRING; 9606.ENSP00000480971; -.
DR BindingDB; P32745; -.
DR ChEMBL; CHEMBL2028; -.
DR DrugBank; DB15494; Edotreotide gallium Ga-68.
DR DrugBank; DB13985; Lutetium Lu 177 dotatate.
DR DrugBank; DB06663; Pasireotide.
DR DrugBank; DB09099; Somatostatin.
DR DrugCentral; P32745; -.
DR GuidetoPHARMACOLOGY; 357; -.
DR TCDB; 9.A.14.13.23; the g-protein-coupled receptor (gpcr) family.
DR GlyGen; P32745; 2 sites.
DR iPTMnet; P32745; -.
DR PhosphoSitePlus; P32745; -.
DR BioMuta; SSTR3; -.
DR DMDM; 417815; -.
DR MassIVE; P32745; -.
DR PaxDb; P32745; -.
DR PeptideAtlas; P32745; -.
DR PRIDE; P32745; -.
DR ProteomicsDB; 54880; -.
DR Antibodypedia; 74216; 182 antibodies from 32 providers.
DR DNASU; 6753; -.
DR Ensembl; ENST00000610913.2; ENSP00000480971.1; ENSG00000278195.2.
DR Ensembl; ENST00000617123.1; ENSP00000481325.1; ENSG00000278195.2.
DR GeneID; 6753; -.
DR KEGG; hsa:6753; -.
DR MANE-Select; ENST00000610913.2; ENSP00000480971.1; NM_001051.5; NP_001042.1.
DR UCSC; uc021wos.3; human.
DR CTD; 6753; -.
DR DisGeNET; 6753; -.
DR GeneCards; SSTR3; -.
DR HGNC; HGNC:11332; SSTR3.
DR HPA; ENSG00000278195; Tissue enhanced (brain, lymphoid tissue, testis).
DR MIM; 182453; gene.
DR neXtProt; NX_P32745; -.
DR OpenTargets; ENSG00000278195; -.
DR PharmGKB; PA36156; -.
DR VEuPathDB; HostDB:ENSG00000278195; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000162038; -.
DR HOGENOM; CLU_009579_8_1_1; -.
DR InParanoid; P32745; -.
DR OMA; VCSQEPT; -.
DR OrthoDB; 1011272at2759; -.
DR PhylomeDB; P32745; -.
DR TreeFam; TF315737; -.
DR PathwayCommons; P32745; -.
DR Reactome; R-HSA-375276; Peptide ligand-binding receptors.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR Reactome; R-HSA-5620922; BBSome-mediated cargo-targeting to cilium.
DR SignaLink; P32745; -.
DR SIGNOR; P32745; -.
DR BioGRID-ORCS; 6753; 11 hits in 1068 CRISPR screens.
DR GeneWiki; Somatostatin_receptor_3; -.
DR GenomeRNAi; 6753; -.
DR Pharos; P32745; Tclin.
DR PRO; PR:P32745; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; P32745; protein.
DR Bgee; ENSG00000278195; Expressed in buccal mucosa cell and 76 other tissues.
DR Genevisible; P32745; HS.
DR GO; GO:0060170; C:ciliary membrane; TAS:Reactome.
DR GO; GO:0005929; C:cilium; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0097730; C:non-motile cilium; ISS:BHF-UCL.
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:0042923; F:neuropeptide binding; IBA:GO_Central.
DR GO; GO:0042277; F:peptide binding; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
DR GO; GO:0004994; F:somatostatin receptor activity; TAS:ProtInc.
DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; IEA:Ensembl.
DR GO; GO:0071385; P:cellular response to glucocorticoid stimulus; IEA:Ensembl.
DR GO; GO:0021549; P:cerebellum development; IEA:Ensembl.
DR GO; GO:0030900; P:forebrain development; IEA:Ensembl.
DR GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; TAS:ProtInc.
DR GO; GO:0008628; P:hormone-mediated apoptotic signaling pathway; TAS:ProtInc.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:ProtInc.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR GO; GO:0042594; P:response to starvation; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR000586; Somatstn_rcpt.
DR InterPro; IPR001856; Somatstn_rcpt_3.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00246; SOMATOSTATNR.
DR PRINTS; PR00589; SOMATOSTTN3R.
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; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Phosphoprotein; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..418
FT /note="Somatostatin receptor type 3"
FT /id="PRO_0000070124"
FT TOPO_DOM 1..43
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..69
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..79
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..101
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 102..116
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..138
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 139..161
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..181
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 182..205
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..231
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 232..257
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..279
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 280..293
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..316
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 317..418
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..360
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30936"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30936"
FT MOD_RES 348
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P30936"
FT CARBOHYD 17
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 116..191
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VARIANT 33
FT /note="A -> V (in dbSNP:rs4988466)"
FT /id="VAR_029219"
FT VARIANT 37
FT /note="P -> L (in dbSNP:rs34943557)"
FT /id="VAR_049440"
FT VARIANT 251
FT /note="S -> F (in dbSNP:rs6413537)"
FT /id="VAR_020072"
FT VARIANT 336
FT /note="R -> C (in dbSNP:rs4988469)"
FT /id="VAR_029220"
FT VARIANT 411
FT /note="S -> T (in dbSNP:rs229568)"
FT /id="VAR_011853"
FT VARIANT 414
FT /note="R -> H (in dbSNP:rs4988471)"
FT /id="VAR_029221"
SQ SEQUENCE 418 AA; 45847 MW; 1227095F801190C4 CRC64;
MDMLHPSSVS TTSEPENASS AWPPDATLGN VSAGPSPAGL AVSGVLIPLV YLVVCVVGLL
GNSLVIYVVL RHTASPSVTN VYILNLALAD ELFMLGLPFL AAQNALSYWP FGSLMCRLVM
AVDGINQFTS IFCLTVMSVD RYLAVVHPTR SARWRTAPVA RTVSAAVWVA SAVVVLPVVV
FSGVPRGMST CHMQWPEPAA AWRAGFIIYT AALGFFGPLL VICLCYLLIV VKVRSAGRRV
WAPSCQRRRR SERRVTRMVV AVVALFVLCW MPFYVLNIVN VVCPLPEEPA FFGLYFLVVA
LPYANSCANP ILYGFLSYRF KQGFRRVLLR PSRRVRSQEP TVGPPEKTEE EDEEEEDGEE
SREGGKGKEM NGRVSQITQP GTSGQERPPS RVASKEQQLL PQEASTGEKS STMRISYL
