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 27-MAR-2024, entry version 159. 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, TRANSPORTER ACTIVITY, SUBCELLULAR RP LOCATION, AND TISSUE 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). In neurons of the central nervous system, could play a CC role in triggering voluntary water intake in response to increased CC sodium concentration in body fluid (By similarity). CC {ECO:0000250|UniProtKB:Q9EPK8, ECO:0000250|UniProtKB:Q9HBA0, CC ECO:0000269|PubMed:11081638}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Ca(2+)(in) = Ca(2+)(out); Xref=Rhea:RHEA:29671, CC ChEBI:CHEBI:29108; Evidence={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:Q9HBA0}. Cell junction, adherens CC junction {ECO:0000250|UniProtKB:Q9EPK8}. Cell projection, cilium CC {ECO:0000250|UniProtKB:Q9HBA0}. Note=Assembly of the putative CC homotetramer occurs primarily in the endoplasmic reticulum. CC Localization to the cell membrane is inhibited by WNK kinases (WNK1, CC WNK2, WNK3 or WNK4) in a kinase-independent mechanism. 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}. 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; AF263521; AAG28027.1; -; mRNA. DR RefSeq; NP_076460.1; NM_023970.1. DR RefSeq; XP_006249528.1; XM_006249466.2. DR AlphaFoldDB; Q9ERZ8; -. DR EMDB; EMD-23477; -. 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 ca2+/cation channel (trp-cc) family. DR iPTMnet; Q9ERZ8; -. DR PhosphoSitePlus; Q9ERZ8; -. DR PaxDb; 10116-ENSRNOP00000001586; -. DR Ensembl; ENSRNOT00000001586.3; ENSRNOP00000001586.1; ENSRNOG00000001195.3. DR Ensembl; ENSRNOT00055003153; ENSRNOP00055002364; ENSRNOG00055001978. DR Ensembl; ENSRNOT00060007995; ENSRNOP00060005981; ENSRNOG00060004776. DR Ensembl; ENSRNOT00065011080; ENSRNOP00065008117; ENSRNOG00065007095. DR GeneID; 66026; -. DR KEGG; rno:66026; -. DR UCSC; RGD:69337; rat. DR AGR; RGD:69337; -. 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; KVCNQDQ; -. DR OrthoDB; 1003028at2759; -. 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 cell types or tissues. 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: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: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:0042802; F:identical protein binding; ISO:RGD. 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:0005261; F:monoatomic cation channel activity; IDA:RGD. 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, monoatomic cation-selective, calcium channel activity; ISO:RGD. DR GO; GO:0030036; P:actin cytoskeleton organization; 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: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: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:0006874; P:intracellular calcium ion homeostasis; ISS:UniProtKB. DR GO; GO:0046785; P:microtubule polymerization; IDA:BHF-UCL. DR GO; GO:0050891; P:multicellular organismal-level 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:0001666; P:response to hypoxia; IEP: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 CDD; cd22195; TRPV4; 1. DR Gene3D; 1.10.287.70; -; 1. DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 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 NCBIfam; TIGR00870; trp; 1. DR PANTHER; PTHR10582:SF4; TRANSIENT RECEPTOR POTENTIAL CATION CHANNEL SUBFAMILY V MEMBER 4; 1. DR PANTHER; PTHR10582; TRANSIENT RECEPTOR POTENTIAL ION CHANNEL PROTEIN; 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; Ankyrin repeat; 1. DR PROSITE; PS50297; ANK_REP_REGION; 1. DR PROSITE; PS50088; ANK_REPEAT; 1. DR Genevisible; Q9ERZ8; RN. 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 //