TRPV4_RAT
ID TRPV4_RAT Reviewed; 871 AA.
AC Q9ERZ8;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Transient receptor potential cation channel subfamily V member 4;
DE Short=TrpV4;
DE AltName: Full=Osm-9-like TRP channel 4;
DE Short=OTRPC4;
DE AltName: Full=Vanilloid receptor-related osmotically-activated channel {ECO:0000303|PubMed:11081638};
DE Short=VR-OAC {ECO:0000303|PubMed:11081638};
GN Name=Trpv4; Synonyms=Vroac;
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], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=11081638; DOI=10.1016/s0092-8674(00)00143-4;
RA Liedtke W.B., Choe Y., Marti-Renom M.A., Bell A.M., Denis C.S., Sali A.,
RA Hudspeth A.J., Friedman J.M., Heller S.;
RT "Vanilloid receptor-related osmotically activated channel (VR-OAC), a
RT candidate vertebrate osmoreceptor.";
RL Cell 103:525-535(2000).
RN [2]
RP INTERACTION WITH PACSIN1; PACSIN2 AND PACSIN3.
RX PubMed=16627472; DOI=10.1074/jbc.m602452200;
RA Cuajungco M.P., Grimm C., Oshima K., D'hoedt D., Nilius B.,
RA Mensenkamp A.R., Bindels R.J., Plomann M., Heller S.;
RT "PACSINs bind to the TRPV4 cation channel. PACSIN 3 modulates the
RT subcellular localization of TRPV4.";
RL J. Biol. Chem. 281:18753-18762(2006).
CC -!- FUNCTION: Non-selective calcium permeant cation channel involved in
CC osmotic sensitivity and mechanosensitivity (PubMed:11081638).
CC Activation by exposure to hypotonicity within the physiological range
CC exhibits an outward rectification (PubMed:11081638). Also activated by
CC heat, low pH, citrate and phorbol esters (By similarity). Increase of
CC intracellular Ca(2+) potentiates currents (By similarity). Channel
CC activity seems to be regulated by a calmodulin-dependent mechanism with
CC a negative feedback mechanism (By similarity). Acts as a regulator of
CC intracellular Ca(2+) in synoviocytes (By similarity). Plays an
CC obligatory role as a molecular component in the nonselective cation
CC channel activation induced by 4-alpha-phorbol 12,13-didecanoate and
CC hypotonic stimulation in synoviocytes and also regulates production of
CC IL-8 (By similarity). Together with PKD2, forms mechano- and
CC thermosensitive channels in cilium (By similarity). Promotes cell-cell
CC junction formation in skin keratinocytes and plays an important role in
CC the formation and/or maintenance of functional intercellular barriers
CC (By similarity). Negatively regulates expression of PPARGC1A, UCP1,
CC oxidative metabolism and respiration in adipocytes (By similarity).
CC Regulates expression of chemokines and cytokines related to pro-
CC inflammatory pathway in adipocytes (By similarity). Together with AQP5,
CC controls regulatory volume decrease in salivary epithelial cells (By
CC similarity). Required for normal development and maintenance of bone
CC and cartilage (By similarity). In its inactive state, may sequester
CC DDX3X at the plasma membrane. When activated, the interaction between
CC both proteins is affected and DDX3X relocalizes to the nucleus (By
CC similarity). {ECO:0000250|UniProtKB:Q9EPK8,
CC ECO:0000250|UniProtKB:Q9HBA0, ECO:0000269|PubMed:11081638}.
CC -!- SUBUNIT: Homotetramer. Interacts with calmodulin (By similarity).
CC Interacts with MAP7 and Src family Tyr protein kinases LYN, SRC, FYN,
CC HCK, LCK and YES (By similarity). Interacts with CTNNB1 (By
CC similarity). The TRPV4 and CTNNB1 complex can interact with CDH1 (By
CC similarity). Part of a complex containing MLC1, AQP4, HEPACAM and
CC ATP1B1 (By similarity). Interacts with PACSIN1, PACSIN2 and PACSIN3
CC (via SH3 domain) (PubMed:16627472). Interacts with ITPR3 (By
CC similarity). Interacts with AQP5; the interaction is probably indirect
CC and regulates TRPV4 activation by hypotonicity (By similarity).
CC Interacts with ANO1 (By similarity). Interacts (via C-terminus) with
CC PKD2 (via C-terminus) (By similarity). Interacts with DDX3X; this
CC interaction is decreased when the channel is activated (By similarity).
CC {ECO:0000250|UniProtKB:Q9EPK8, ECO:0000250|UniProtKB:Q9HBA0,
CC ECO:0000269|PubMed:16627472}.
CC -!- INTERACTION:
CC Q9ERZ8; P47863: Aqp4; NbExp=4; IntAct=EBI-10095418, EBI-15907593;
CC Q9ERZ8; P47863-1: Aqp4; NbExp=2; IntAct=EBI-10095418, EBI-15907676;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9HBA0}.
CC Apical cell membrane {ECO:0000305|PubMed:11081638}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:Q9EPK8}. Cell junction, adherens
CC junction {ECO:0000250|UniProtKB:Q9EPK8}. Cell projection, cilium
CC {ECO:0000250|UniProtKB:Q9EPK8}. Note=Assembly of the putative
CC homotetramer occurs primarily in the endoplasmic reticulum.
CC {ECO:0000250|UniProtKB:Q9HBA0}.
CC -!- TISSUE SPECIFICITY: Expressed lung, spleen, kidney, testis, fat, and at
CC very low levels in trigeminal ganglia. {ECO:0000269|PubMed:11081638}.
CC -!- DOMAIN: The ANK repeat region mediates interaction with Ca(2+)-
CC calmodulin and ATP binding. The ANK repeat region mediates interaction
CC with phosphatidylinositol-4,5-bisphosphate and related
CC phosphatidylinositides. {ECO:0000250|UniProtKB:A0A1D5PXA5}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q9EPK8}.
CC -!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family. TrpV
CC subfamily. TRPV4 sub-subfamily. {ECO:0000305}.
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DR EMBL; AF263521; AAG28027.1; -; mRNA.
DR RefSeq; NP_076460.1; NM_023970.1.
DR RefSeq; XP_006249528.1; XM_006249466.2.
DR AlphaFoldDB; Q9ERZ8; -.
DR SMR; Q9ERZ8; -.
DR BioGRID; 249353; 2.
DR DIP; DIP-59600N; -.
DR IntAct; Q9ERZ8; 3.
DR STRING; 10116.ENSRNOP00000001586; -.
DR BindingDB; Q9ERZ8; -.
DR ChEMBL; CHEMBL2775; -.
DR GuidetoPHARMACOLOGY; 510; -.
DR TCDB; 1.A.4.2.5; the transient receptor potential ca(2+) channel (trp-cc) family.
DR iPTMnet; Q9ERZ8; -.
DR PhosphoSitePlus; Q9ERZ8; -.
DR PaxDb; Q9ERZ8; -.
DR PRIDE; Q9ERZ8; -.
DR Ensembl; ENSRNOT00000001586; ENSRNOP00000001586; ENSRNOG00000001195.
DR GeneID; 66026; -.
DR KEGG; rno:66026; -.
DR UCSC; RGD:69337; rat.
DR CTD; 59341; -.
DR RGD; 69337; Trpv4.
DR eggNOG; KOG3676; Eukaryota.
DR GeneTree; ENSGT00940000158615; -.
DR HOGENOM; CLU_012795_1_0_1; -.
DR InParanoid; Q9ERZ8; -.
DR OMA; YPECNLE; -.
DR OrthoDB; 693004at2759; -.
DR PhylomeDB; Q9ERZ8; -.
DR TreeFam; TF314711; -.
DR Reactome; R-RNO-3295583; TRP channels.
DR PRO; PR:Q9ERZ8; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000001195; Expressed in adult mammalian kidney and 15 other tissues.
DR Genevisible; Q9ERZ8; RN.
DR GO; GO:0005912; C:adherens junction; ISS:UniProtKB.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0005929; C:cilium; ISO:RGD.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IDA:BHF-UCL.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:RGD.
DR GO; GO:0030175; C:filopodium; IDA:BHF-UCL.
DR GO; GO:0005925; C:focal adhesion; IDA:BHF-UCL.
DR GO; GO:0030426; C:growth cone; IDA:BHF-UCL.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0030027; C:lamellipodium; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0032587; C:ruffle membrane; IDA:BHF-UCL.
DR GO; GO:0003779; F:actin binding; IDA:BHF-UCL.
DR GO; GO:0051015; F:actin filament binding; IDA:BHF-UCL.
DR GO; GO:0043014; F:alpha-tubulin binding; IDA:BHF-UCL.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0048487; F:beta-tubulin binding; IDA:BHF-UCL.
DR GO; GO:0005262; F:calcium channel activity; IDA:BHF-UCL.
DR GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
DR GO; GO:0005261; F:cation channel activity; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0005216; F:ion channel activity; IBA:GO_Central.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IDA:BHF-UCL.
DR GO; GO:0005034; F:osmosensor activity; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0005080; F:protein kinase C binding; IDA:BHF-UCL.
DR GO; GO:0042169; F:SH2 domain binding; ISO:RGD.
DR GO; GO:0015275; F:stretch-activated, cation-selective, calcium channel activity; ISO:RGD.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; IDA:BHF-UCL.
DR GO; GO:0007015; P:actin filament organization; IDA:BHF-UCL.
DR GO; GO:0097497; P:blood vessel endothelial cell delamination; ISO:RGD.
DR GO; GO:0070509; P:calcium ion import; IDA:BHF-UCL.
DR GO; GO:0098703; P:calcium ion import across plasma membrane; IBA:GO_Central.
DR GO; GO:1902656; P:calcium ion import into cytosol; ISS:UniProtKB.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IMP:UniProtKB.
DR GO; GO:0006816; P:calcium ion transport; ISO:RGD.
DR GO; GO:0060351; P:cartilage development involved in endochondral bone morphogenesis; ISO:RGD.
DR GO; GO:0007043; P:cell-cell junction assembly; ISS:UniProtKB.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; ISS:UniProtKB.
DR GO; GO:0071476; P:cellular hypotonic response; ISO:RGD.
DR GO; GO:0071477; P:cellular hypotonic salinity response; ISO:RGD.
DR GO; GO:0034605; P:cellular response to heat; ISS:UniProtKB.
DR GO; GO:0071470; P:cellular response to osmotic stress; ISS:UniProtKB.
DR GO; GO:0043622; P:cortical microtubule organization; IDA:BHF-UCL.
DR GO; GO:0002024; P:diet induced thermogenesis; ISO:RGD.
DR GO; GO:0097009; P:energy homeostasis; ISO:RGD.
DR GO; GO:0042593; P:glucose homeostasis; ISO:RGD.
DR GO; GO:0042538; P:hyperosmotic salinity response; ISO:RGD.
DR GO; GO:0006971; P:hypotonic response; IDA:RGD.
DR GO; GO:0046785; P:microtubule polymerization; IDA:BHF-UCL.
DR GO; GO:0050891; P:multicellular organismal water homeostasis; IMP:UniProtKB.
DR GO; GO:1903444; P:negative regulation of brown fat cell differentiation; ISO:RGD.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IDA:BHF-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0007231; P:osmosensory signaling pathway; ISO:RGD.
DR GO; GO:0071651; P:positive regulation of chemokine (C-C motif) ligand 5 production; ISO:RGD.
DR GO; GO:2000340; P:positive regulation of chemokine (C-X-C motif) ligand 1 production; ISO:RGD.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:RGD.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0050729; P:positive regulation of inflammatory response; ISO:RGD.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; ISO:RGD.
DR GO; GO:0046330; P:positive regulation of JNK cascade; ISO:RGD.
DR GO; GO:0010759; P:positive regulation of macrophage chemotaxis; ISO:RGD.
DR GO; GO:0071642; P:positive regulation of macrophage inflammatory protein 1 alpha production; ISO:RGD.
DR GO; GO:0031117; P:positive regulation of microtubule depolymerization; IDA:BHF-UCL.
DR GO; GO:0071639; P:positive regulation of monocyte chemotactic protein-1 production; ISO:RGD.
DR GO; GO:0045989; P:positive regulation of striated muscle contraction; IMP:RGD.
DR GO; GO:0043117; P:positive regulation of vascular permeability; IMP:UniProtKB.
DR GO; GO:1903715; P:regulation of aerobic respiration; ISO:RGD.
DR GO; GO:0047484; P:regulation of response to osmotic stress; ISO:RGD.
DR GO; GO:0032868; P:response to insulin; ISO:RGD.
DR GO; GO:0006970; P:response to osmotic stress; ISO:RGD.
DR GO; GO:0030103; P:vasopressin secretion; ISO:RGD.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR024862; TRPV.
DR InterPro; IPR008347; TrpV1-4.
DR InterPro; IPR008348; TrpV4.
DR PANTHER; PTHR10582; PTHR10582; 1.
DR PANTHER; PTHR10582:SF4; PTHR10582:SF4; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR PRINTS; PR01768; TRPVRECEPTOR.
DR PRINTS; PR01769; VRL2RECEPTOR.
DR SMART; SM00248; ANK; 3.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
PE 1: Evidence at protein level;
KW ANK repeat; ATP-binding; Calcium; Calcium channel; Calcium transport;
KW Calmodulin-binding; Cell junction; Cell membrane; Cell projection; Cilium;
KW Glycoprotein; Ion channel; Ion transport; Lipid-binding; Membrane;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..871
FT /note="Transient receptor potential cation channel
FT subfamily V member 4"
FT /id="PRO_0000215349"
FT TOPO_DOM 1..469
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT TRANSMEM 470..490
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT TOPO_DOM 491..507
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT TRANSMEM 508..534
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT TOPO_DOM 535..547
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT TRANSMEM 548..568
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT TOPO_DOM 569..572
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT TRANSMEM 573..593
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT TOPO_DOM 594..608
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT TRANSMEM 609..636
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT TOPO_DOM 637..665
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT INTRAMEM 666..685
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT TOPO_DOM 686..693
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT TRANSMEM 694..722
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT TOPO_DOM 723..871
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT REPEAT 237..266
FT /note="ANK 1"
FT REPEAT 284..313
FT /note="ANK 2"
FT REPEAT 369..398
FT /note="ANK 3"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 110..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 812..831
FT /note="Interaction with calmodulin and ITPR3"
FT /evidence="ECO:0000250|UniProtKB:Q9HBA0"
FT MOTIF 679..682
FT /note="Selectivity filter"
FT /evidence="ECO:0000250|UniProtKB:O35433"
FT COMPBIAS 112..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 192
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9HBA0"
FT BINDING 197
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9HBA0"
FT BINDING 201
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9HBA0"
FT BINDING 236..239
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9HBA0"
FT BINDING 248
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9HBA0"
FT BINDING 249..251
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000250|UniProtKB:A0A1D5PXA5"
FT BINDING 296..299
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000250|UniProtKB:A0A1D5PXA5"
FT BINDING 344
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000250|UniProtKB:A0A1D5PXA5"
FT BINDING 682
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000250|UniProtKB:Q9R186"
FT MOD_RES 110
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9EPK8"
FT MOD_RES 253
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9EPK8"
FT MOD_RES 805
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9EPK8"
FT MOD_RES 824
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9EPK8"
SQ SEQUENCE 871 AA; 98010 MW; 5D50684DA08C354B CRC64;
MADPGDGPRA APGDVAEPPG DESGTSGGEA FPLSSLANLF EGEEGSSSLS PVDASRPAGP
GDGRPNLRMK FQGAFRKGVP NPIDLLESTL YESSVVPGPK KAPMDSLFDY GTYRHHPSDN
KRWRRKVVEK QPQSPKAPAP QPPPILKVFN RPILFDIVSR GSTADLDGLL SYLLTHKKRL
TDEEFREPST GKTCLPKALL NLSNGRNDTI PVLLDIAERT GNMREFINSP FRDIYYRGQT
ALHIAIERRC KHYVELLVAQ GADVHAQARG RFFQPKDEGG YFYFGELPLS LAACTNQPHI
VNYLTENPHK KADMRRQDSR GNTVLHALVA IADNTRENTK FVTKMYDLLL LKCSRLFPDS
NLETVLNNDG LSPLMMAAKT GKIGVFQHII RREVTDEDTR HLSRKFKDWA YGPVYSSLYD
LSSLDTCGEE VSVLEILVYN SKIENRHEML AVEPINELLR DKWRKFGAVS FYINVVSYLC
AMVIFTLTAY YQPLEGTPPY PYRTTVDYLR LAGEVITLLT GVLFFFTSIK DLFMKKCPGV
NSLFVDGSFQ LLYFIYSVLV VVSAALYLAG IEAYLAVMVF ALVLGWMNAL YFTRGLKLTG
TYSIMIQKIL FKDLFRFLLV YLLFMIGYAS ALVTLLNPCT NMKVCNEDQS NCTVPSYPAC
RDSETFSAFL LDLFKLTIGM GDLEMLSSAK YPVVFILLLV TYIILTFVLL LNMLIALMGE
TVGQVSKESK HIWKLQWATT ILDIERSFPV FLRKAFRSGE MVTVGKSSDG TPDRRWCFRV
DEVNWSHWNQ NLGIINEDPG KSEIYQYYGF SHTMGRLRRD RWSSVVPRVV ELNKNSGTDE
VVVPLDNLGN PNCDGHQQGY APKWRAEDAP L
