CASR_RAT
ID CASR_RAT Reviewed; 1079 AA.
AC P48442;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Extracellular calcium-sensing receptor;
DE Short=CaSR;
DE AltName: Full=Parathyroid cell calcium-sensing receptor;
DE Short=PCaR1;
DE Short=RaKCaR {ECO:0000303|PubMed:7816802};
DE Flags: Precursor;
GN Name=Casr; Synonyms=Gprc2a, Pcar1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=Sprague-Dawley; TISSUE=Kidney outer medulla;
RX PubMed=7816802; DOI=10.1073/pnas.92.1.131;
RA Riccardi D., Park J., Lee W., Gamba G., Brown E.M., Hebert S.C.;
RT "Cloning and functional expression of a rat kidney extracellular
RT calcium/polyvalent cation-sensing receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:131-135(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-294.
RC STRAIN=Wistar;
RX PubMed=7724534; DOI=10.1073/pnas.92.8.3161;
RA Ruat M., Snowman A.M., Snyder S.H.;
RT "Calcium sensing receptor: molecular cloning in rat and localization to
RT nerve terminals.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3161-3165(1995).
RN [3]
RP INTERACTION WITH ARRB1.
RX PubMed=17623778; DOI=10.1242/jcs.03469;
RA Bouschet T., Martin S., Kanamarlapudi V., Mundell S., Henley J.M.;
RT "The calcium-sensing receptor changes cell shape via a beta-arrestin-1 ARNO
RT ARF6 ELMO protein network.";
RL J. Cell Sci. 120:2489-2497(2007).
CC -!- FUNCTION: G-protein-coupled receptor that senses changes in the
CC extracellular concentration of calcium ions and plays a key role in
CC maintaining calcium homeostasis (PubMed:7816802). Senses fluctuations
CC in the circulating calcium concentration and modulates the production
CC of parathyroid hormone (PTH) in parathyroid glands (By similarity). The
CC activity of this receptor is mediated by a G-protein that activates a
CC phosphatidylinositol-calcium second messenger system (By similarity).
CC The G-protein-coupled receptor activity is activated by a co-agonist
CC mechanism: aromatic amino acids, such as Trp or Phe, act concertedly
CC with divalent cations, such as calcium or magnesium, to achieve full
CC receptor activation (By similarity). {ECO:0000250|UniProtKB:P41180,
CC ECO:0000250|UniProtKB:Q9QY96}.
CC -!- ACTIVITY REGULATION: In resting state, adopts an open conformation,
CC anion-binding promoting the inactive configuration. Upon aromatic amino
CC acid-binding, the groove in the extracellular venus flytrap module is
CC closed, thereby inducing the formation of a novel homodimer interface
CC between subunits. Calcium ions stabilize the active state by enhancing
CC homodimer interactions between membrane-proximal domains to fully
CC activate the receptor. {ECO:0000250|UniProtKB:P41180}.
CC -!- SUBUNIT: Homodimer; disulfide-linked (By similarity). Interacts with
CC VCP and RNF19A (By similarity). Interacts with ARRB1 (PubMed:17623778).
CC {ECO:0000250|UniProtKB:P41180, ECO:0000269|PubMed:17623778}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P41180};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P41180}.
CC -!- DOMAIN: The extracellular regions of the homodimer interact in a side-
CC by-side fashion while facing opposite directions. Each extracellular
CC region consists of three domains, LB1 (ligand-binding 1), LB2 and CR
CC (cysteine-rich). The two lobe-shaped domains LB1 and LB2 form a venus
CC flytrap module. In the inactive configuration, the venus flytrap
CC modules of both protomers are in the open conformation associated with
CC the resting state (open-open) and the interdomain cleft is empty. In
CC addition, each protomer contains three anions, which reinforce the
CC inactive conformation, and one calcium ion. In the active
CC configuration, both protomers of extracellular regions have the closed
CC conformation associated with agonist-binding (closed-closed). The
CC ligand-binding cleft of each protomer is solely occupied by an aromatic
CC amino-acid. Calcium is bound at four novel sites, including one at the
CC homodimer interface. Agonist-binding induces large conformational
CC changes within the extracellular region homodimer: first, the venus
CC flytrap module of each protomer undergoes domain closure. Second, the
CC LB2 regions of the two protomers approach each other, resulting in an
CC expansion of the homodimer interactions involving LB2 domains. Third,
CC the CR regions of the two subunits interact to form a large homodimer
CC interface that is unique to the active state. The CR regions are
CC brought into close contact by the motion involving LB2 since the two
CC domains are rigidly associated within each subunit.
CC {ECO:0000250|UniProtKB:P41180}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P41180}.
CC -!- PTM: Ubiquitinated by RNF19A; which induces proteasomal degradation.
CC {ECO:0000250|UniProtKB:P41180}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
CC {ECO:0000305}.
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DR EMBL; U10354; AAC52149.1; -; mRNA.
DR EMBL; U20289; AAC52195.1; -; mRNA.
DR PIR; I59362; I59362.
DR RefSeq; NP_001296567.1; NM_001309638.1.
DR RefSeq; NP_058692.1; NM_016996.2.
DR RefSeq; XP_017453358.1; XM_017597869.1.
DR RefSeq; XP_017453359.1; XM_017597870.1.
DR RefSeq; XP_017453360.1; XM_017597871.1.
DR RefSeq; XP_017453361.1; XM_017597872.1.
DR AlphaFoldDB; P48442; -.
DR SMR; P48442; -.
DR IntAct; P48442; 1.
DR STRING; 10116.ENSRNOP00000003092; -.
DR BindingDB; P48442; -.
DR ChEMBL; CHEMBL2516; -.
DR DrugCentral; P48442; -.
DR GuidetoPHARMACOLOGY; 54; -.
DR GlyGen; P48442; 10 sites.
DR iPTMnet; P48442; -.
DR PhosphoSitePlus; P48442; -.
DR PaxDb; P48442; -.
DR PRIDE; P48442; -.
DR Ensembl; ENSRNOT00000003092; ENSRNOP00000003092; ENSRNOG00000002265.
DR GeneID; 24247; -.
DR KEGG; rno:24247; -.
DR UCSC; RGD:2277; rat.
DR CTD; 846; -.
DR RGD; 2277; Casr.
DR eggNOG; KOG1056; Eukaryota.
DR GeneTree; ENSGT00940000157596; -.
DR HOGENOM; CLU_005389_1_0_1; -.
DR InParanoid; P48442; -.
DR OMA; CPDDSWS; -.
DR OrthoDB; 327938at2759; -.
DR PhylomeDB; P48442; -.
DR TreeFam; TF331269; -.
DR Reactome; R-RNO-416476; G alpha (q) signalling events.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR Reactome; R-RNO-420499; Class C/3 (Metabotropic glutamate/pheromone receptors).
DR PRO; PR:P48442; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000002265; Expressed in adult mammalian kidney and 2 other tissues.
DR Genevisible; P48442; RN.
DR GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0043679; C:axon terminus; IDA:RGD.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0016597; F:amino acid binding; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISO:RGD.
DR GO; GO:0004930; F:G protein-coupled receptor activity; ISS:UniProtKB.
DR GO; GO:0005178; F:integrin binding; IPI:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:RGD.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:RGD.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IDA:RGD.
DR GO; GO:0006915; P:apoptotic process; IEP:RGD.
DR GO; GO:0032782; P:bile acid secretion; IDA:RGD.
DR GO; GO:0048754; P:branching morphogenesis of an epithelial tube; IMP:RGD.
DR GO; GO:0070509; P:calcium ion import; ISO:RGD.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IDA:RGD.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEP:RGD.
DR GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; IEP:RGD.
DR GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD.
DR GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; IEP:RGD.
DR GO; GO:1901653; P:cellular response to peptide; IEP:RGD.
DR GO; GO:0071305; P:cellular response to vitamin D; IEP:RGD.
DR GO; GO:1902476; P:chloride transmembrane transport; IDA:RGD.
DR GO; GO:0005513; P:detection of calcium ion; IDA:RGD.
DR GO; GO:0060613; P:fat pad development; IEP:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007254; P:JNK cascade; IMP:RGD.
DR GO; GO:0001503; P:ossification; IMP:RGD.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IDA:RGD.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; ISO:RGD.
DR GO; GO:0090280; P:positive regulation of calcium ion import; IMP:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:RGD.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0032024; P:positive regulation of insulin secretion; IMP:RGD.
DR GO; GO:0050927; P:positive regulation of positive chemotaxis; IMP:RGD.
DR GO; GO:0045907; P:positive regulation of vasoconstriction; IMP:RGD.
DR GO; GO:0051924; P:regulation of calcium ion transport; ISO:RGD.
DR GO; GO:0051592; P:response to calcium ion; IEP:RGD.
DR GO; GO:0071774; P:response to fibroblast growth factor; IEP:RGD.
DR GO; GO:0002931; P:response to ischemia; IEP:RGD.
DR GO; GO:0010038; P:response to metal ion; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0042311; P:vasodilation; IMP:RGD.
DR Gene3D; 2.10.50.30; -; 1.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR000337; GPCR_3.
DR InterPro; IPR011500; GPCR_3_9-Cys_dom.
DR InterPro; IPR038550; GPCR_3_9-Cys_sf.
DR InterPro; IPR017978; GPCR_3_C.
DR InterPro; IPR000068; GPCR_3_Ca_sens_rcpt-rel.
DR InterPro; IPR017979; GPCR_3_CS.
DR InterPro; IPR028082; Peripla_BP_I.
DR PANTHER; PTHR24061; PTHR24061; 1.
DR Pfam; PF00003; 7tm_3; 1.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF07562; NCD3G; 1.
DR PRINTS; PR00592; CASENSINGR.
DR PRINTS; PR00248; GPCRMGR.
DR SUPFAM; SSF53822; SSF53822; 1.
DR PROSITE; PS00979; G_PROTEIN_RECEP_F3_1; 1.
DR PROSITE; PS00980; G_PROTEIN_RECEP_F3_2; 1.
DR PROSITE; PS00981; G_PROTEIN_RECEP_F3_3; 1.
DR PROSITE; PS50259; G_PROTEIN_RECEP_F3_4; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell membrane; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Membrane; Metal-binding; Phosphoprotein; Receptor;
KW Reference proteome; Signal; Transducer; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1079
FT /note="Extracellular calcium-sensing receptor"
FT /id="PRO_0000012948"
FT TOPO_DOM 20..612
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 613..635
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 636..649
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 650..670
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 671..681
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 682..700
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 701..724
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 725..745
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 746..769
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 770..792
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 793..805
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 806..828
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 829..836
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 837..862
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 863..1079
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 22..188
FT /note="Ligand-binding 1 (LB1)"
FT /evidence="ECO:0000250|UniProtKB:P41180"
FT REGION 189..324
FT /note="Ligand-binding 2 (LB2)"
FT /evidence="ECO:0000250|UniProtKB:P41180"
FT REGION 542..612
FT /note="Cysteine-rich (CR)"
FT /evidence="ECO:0000250|UniProtKB:P41180"
FT REGION 880..900
FT /note="Interaction with RNF19A"
FT /evidence="ECO:0000250|UniProtKB:P41180"
FT REGION 894..964
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 894..921
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 929..964
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 66..70
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /ligand_note="required for structural stability of the
FT receptor"
FT /evidence="ECO:0000250|UniProtKB:P41180"
FT BINDING 81
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P41180"
FT BINDING 84
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P41180"
FT BINDING 87
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P41180"
FT BINDING 88
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P41180"
FT BINDING 100
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P41180"
FT BINDING 145
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P41180"
FT BINDING 147
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:P41180"
FT BINDING 168
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:P41180"
FT BINDING 170
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:P41180"
FT BINDING 231
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P41180"
FT BINDING 234
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P41180"
FT BINDING 297
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:P41180"
FT BINDING 415..417
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /ligand_note="required for structural stability of the
FT receptor"
FT /evidence="ECO:0000250|UniProtKB:P41180"
FT BINDING 557
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P41180"
FT MOD_RES 920
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QY96"
FT MOD_RES 1062
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QY96"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 386
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 446
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 468
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 488
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 541
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 594
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 60..101
FT /evidence="ECO:0000250|UniProtKB:P41180"
FT DISULFID 129
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:P41180"
FT DISULFID 131
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:P41180"
FT DISULFID 236..561
FT /evidence="ECO:0000250|UniProtKB:P41180"
FT DISULFID 358..395
FT /evidence="ECO:0000250|UniProtKB:P41180"
FT DISULFID 437..449
FT /evidence="ECO:0000250|UniProtKB:P41180"
FT DISULFID 542..562
FT /evidence="ECO:0000250|UniProtKB:P41180"
FT DISULFID 546..565
FT /evidence="ECO:0000250|UniProtKB:P41180"
FT DISULFID 568..582
FT /evidence="ECO:0000250|UniProtKB:P41180"
FT DISULFID 585..598
FT /evidence="ECO:0000250|UniProtKB:P41180"
SQ SEQUENCE 1079 AA; 120868 MW; D7664550361F9736 CRC64;
MASYSCCLAL LALAWHSSAY GPDQRAQKKG DIILGGLFPI HFGVAAKDQD LKSRPESVEC
IRYNFRGFRW LQAMIFAIEE INSSPSLLPN MTLGYRIFDT CNTVSKALEA TLSFVAQNKI
DSLNLDEFCN CSEHIPSTIA VVGATGSGVS TAVANLLGLF YIPQVSYASS SRLLSNKNQY
KSFLRTIPND EHQATAMADI IEYFRWNWVG TIAADDDYGR PGIEKFREEA EERDICIDFS
ELISQYSDEE EIQQVVEVIQ NSTAKVIVVF SSGPDLEPLI KEIVRRNITG RIWLASEAWA
SSSLIAMPEY FHVVGGTIGF GLKAGQIPGF REFLQKVHPR KSVHNGFAKE FWEETFNCHL
QEGAKGPLPV DTFVRSHEEG GNRLLNSSTA FRPLCTGDEN INSVETPYMD YEHLRISYNV
YLAVYSIAHA LQDIYTCLPG RGLFTNGSCA DIKKVEAWQV LKHLRHLNFT NNMGEQVTFD
ECGDLVGNYS IINWHLSPED GSIVFKEVGY YNVYAKKGER LFINEEKILW SGFSREVPFS
NCSRDCQAGT RKGIIEGEPT CCFECVECPD GEYSGETDAS ACDKCPDDFW SNENHTSCIA
KEIEFLAWTE PFGIALTLFA VLGIFLTAFV LGVFIKFRNT PIVKATNREL SYLLLFSLLC
CFSSSLFFIG EPQDWTCRLR QPAFGISFVL CISCILVKTN RVLLVFEAKI PTSFHRKWWG
LNLQFLLVFL CTFMQILICI IWLYTAPPSS YRNHELEDEI IFITCHEGSL MALGSLIGYT
CLLAAICFFF AFKSRKLPEN FNEAKFITFS MLIFFIVWIS FIPAYASTYG KFVSAVEVIA
ILAASFGLLA CIFFNKVYII LFKPSRNTIE EVRSSTAAHA FKVAARATLR RPNISRKRSS
SLGGSTGSIP SSSISSKSNS EDRFPQPERQ KQQQPLSLTQ QEQQQQPLTL HPQQQQQPQQ
PRCKQKVIFG SGTVTFSLSF DEPQKNAMAH RNSMRQNSLE AQRSNDTLGR HQALLPLQCA
DADSEMTIQE TGLQGPMVGD HQPEMESSDE MSPALVMSTS RSFVISGGGS SVTENVLHS
