ID   TRPV4_CHICK             Reviewed;         852 AA.
AC   A0A1D5PXA5; Q9DFS3;
DT   28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=Transient receptor potential cation channel subfamily V member 4;
DE            Short=TrpV4;
DE   AltName: Full=Vanilloid receptor-related osmotically activated channel {ECO:0000303|PubMed:11081638};
DE            Short=VR-OAC {ECO:0000303|PubMed:11081638};
GN   Name=TRPV4;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031 {ECO:0000312|Proteomes:UP000000539};
RN   [1] {ECO:0000312|EMBL:AAG28026.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TRANSPORTER ACTIVITY, AND SUBCELLULAR
RP   LOCATION.
RC   TISSUE=Cochlea {ECO:0000312|EMBL:AAG28026.1};
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   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Red jungle fowl;
RX   PubMed=15592404; DOI=10.1038/nature03154;
RA   Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA   Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA   Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA   Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA   McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA   Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA   Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA   Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA   Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA   Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA   Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA   Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA   Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA   Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA   Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA   Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA   Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA   Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA   Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA   Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA   Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA   Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA   Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA   Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA   Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA   Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA   Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA   Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA   Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA   Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA   Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA   Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA   Wilson R.K.;
RT   "Sequence and comparative analysis of the chicken genome provide unique
RT   perspectives on vertebrate evolution.";
RL   Nature 432:695-716(2004).
RN   [3]
RP   FUNCTION, TRANSPORTER ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH
RP   CALMODULIN, ATP-BINDING, DOMAIN, ACTIVITY REGULATION, AND MUTAGENESIS OF
RP   LYS-178; LYS-183 AND LYS-205.
RX   PubMed=19864432; DOI=10.1074/jbc.m109.052548;
RA   Phelps C.B., Wang R.R., Choo S.S., Gaudet R.;
RT   "Differential regulation of TRPV1, TRPV3, and TRPV4 sensitivity through a
RT   conserved binding site on the ankyrin repeat domain.";
RL   J. Biol. Chem. 285:731-740(2010).
RN   [4] {ECO:0007744|PDB:3JXI, ECO:0007744|PDB:3JXJ}
RP   X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 133-382.
RX   PubMed=20037586; DOI=10.1038/ng.512;
RA   Landoure G., Zdebik A.A., Martinez T.L., Burnett B.G., Stanescu H.C.,
RA   Inada H., Shi Y., Taye A.A., Kong L., Munns C.H., Choo S.S., Phelps C.B.,
RA   Paudel R., Houlden H., Ludlow C.L., Caterina M.J., Gaudet R., Kleta R.,
RA   Fischbeck K.H., Sumner C.J.;
RT   "Mutations in TRPV4 cause Charcot-Marie-Tooth disease type 2C.";
RL   Nat. Genet. 42:170-174(2010).
RN   [5] {ECO:0007744|PDB:3W9F, ECO:0007744|PDB:3W9G}
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 133-382 IN COMPLEX WITH
RP   MYO-INOSITOL-1,4,5-TRISPHOSPHATE, LIPID-BINDING, AND DOMAIN.
RX   PubMed=25256292; DOI=10.1038/ncomms5994;
RA   Takahashi N., Hamada-Nakahara S., Itoh Y., Takemura K., Shimada A.,
RA   Ueda Y., Kitamata M., Matsuoka R., Hanawa-Suetsugu K., Senju Y., Mori M.X.,
RA   Kiyonaka S., Kohda D., Kitao A., Mori Y., Suetsugu S.;
RT   "TRPV4 channel activity is modulated by direct interaction of the ankyrin
RT   domain to PI(4,5)P.";
RL   Nat. Commun. 5:4994-4994(2014).
CC   -!- FUNCTION: Non-selective calcium permeant cation channel involved in
CC       osmotic sensitivity and mechanosensitivity (PubMed:11081638,
CC       PubMed:19864432). Activation by exposure to hypotonicity within the
CC       physiological range exhibits an outward rectification
CC       (PubMed:11081638). Also activated by phorbol esters (PubMed:19864432).
CC       Channel activity seems to be regulated by a calmodulin-dependent
CC       mechanism (By similarity). {ECO:0000250|UniProtKB:Q9HBA0,
CC       ECO:0000269|PubMed:11081638, ECO:0000269|PubMed:19864432}.
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         ECO:0000269|PubMed:19864432};
CC   -!- ACTIVITY REGULATION: ATP binding enhances channel sensitivity to
CC       agonists. Ca(2+)-calmodulin prevents the ATP-mediated increased
CC       sensitivity to agonists. {ECO:0000269|PubMed:19864432}.
CC   -!- SUBUNIT: Homotetramer (By similarity). Interacts with Ca(2+)-calmodulin
CC       (PubMed:19864432). {ECO:0000250|UniProtKB:Q9HBA0,
CC       ECO:0000269|PubMed:19864432}.
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000305|PubMed:11081638, ECO:0000305|PubMed:19864432}; Multi-pass
CC       membrane protein {ECO:0000250|UniProtKB:Q9EPK8}. Cell junction,
CC       adherens junction {ECO:0000250|UniProtKB:Q9EPK8}.
CC   -!- DOMAIN: The ANK repeat region mediates interaction with Ca(2+)-
CC       calmodulin and ATP binding (PubMed:19864432). The ANK repeat region
CC       mediates interaction with phosphatidylinositol-4,5-bisphosphate and
CC       related phosphatidylinositides (PubMed:25256292).
CC       {ECO:0000269|PubMed:19864432, ECO:0000269|PubMed:25256292}.
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; AF261883; AAG28026.1; -; mRNA.
DR   EMBL; AADN04000193; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_990023.1; NM_204692.1.
DR   PDB; 3JXI; X-ray; 2.30 A; A/B/C/D=133-382.
DR   PDB; 3JXJ; X-ray; 2.80 A; A/B=133-382.
DR   PDB; 3W9F; X-ray; 1.90 A; A/B/C/D=133-382.
DR   PDB; 3W9G; X-ray; 2.00 A; A/B/C/D=133-382.
DR   PDB; 6F55; NMR; -; B=121-135.
DR   PDBsum; 3JXI; -.
DR   PDBsum; 3JXJ; -.
DR   PDBsum; 3W9F; -.
DR   PDBsum; 3W9G; -.
DR   PDBsum; 6F55; -.
DR   AlphaFoldDB; A0A1D5PXA5; -.
DR   SASBDB; A0A1D5PXA5; -.
DR   SMR; A0A1D5PXA5; -.
DR   PaxDb; 9031-ENSGALP00000008256; -.
DR   GeneID; 395427; -.
DR   KEGG; gga:395427; -.
DR   CTD; 59341; -.
DR   VEuPathDB; HostDB:geneid_395427; -.
DR   eggNOG; KOG3676; Eukaryota.
DR   InParanoid; A0A1D5PXA5; -.
DR   PRO; PR:A0A1D5PXA5; -.
DR   Proteomes; UP000000539; Unassembled WGS sequence.
DR   GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005262; F:calcium channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005261; F:monoatomic cation channel activity; ISS:UniProtKB.
DR   GO; GO:0006874; P:intracellular calcium ion homeostasis; ISS:UniProtKB.
DR   GO; GO:0007231; P:osmosensory signaling pathway; IBA:GO_Central.
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.
PE   1: Evidence at protein level;
KW   3D-structure; ANK repeat; ATP-binding; Calcium; Calcium channel;
KW   Calcium transport; Calmodulin-binding; Cell junction; Cell membrane;
KW   Ion channel; Ion transport; Lipid-binding; Membrane; Metal-binding;
KW   Nucleotide-binding; Reference proteome; Repeat; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..852
FT                   /note="Transient receptor potential cation channel
FT                   subfamily V member 4"
FT                   /id="PRO_0000443481"
FT   TOPO_DOM        1..455
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:O35433"
FT   TRANSMEM        456..476
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:O35433"
FT   TOPO_DOM        477..493
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:O35433"
FT   TRANSMEM        494..520
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:O35433"
FT   TOPO_DOM        521..533
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:O35433"
FT   TRANSMEM        534..554
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:O35433"
FT   TOPO_DOM        555..558
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:O35433"
FT   TRANSMEM        559..579
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:O35433"
FT   TOPO_DOM        580..594
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:O35433"
FT   TRANSMEM        595..622
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:O35433"
FT   TOPO_DOM        623..651
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:O35433"
FT   INTRAMEM        652..671
FT                   /note="Pore-forming"
FT                   /evidence="ECO:0000250|UniProtKB:O35433"
FT   TOPO_DOM        672..679
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:O35433"
FT   TRANSMEM        680..708
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:O35433"
FT   TOPO_DOM        709..852
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:O35433"
FT   REPEAT          223..252
FT                   /note="ANK 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          270..299
FT                   /note="ANK 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          355..387
FT                   /note="ANK 3"
FT                   /evidence="ECO:0000255"
FT   REGION          30..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           665..668
FT                   /note="Selectivity filter"
FT                   /evidence="ECO:0000250|UniProtKB:O35433"
FT   BINDING         178
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HBA0"
FT   BINDING         183
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HBA0"
FT   BINDING         187
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HBA0"
FT   BINDING         222..225
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HBA0"
FT   BINDING         234
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HBA0"
FT   BINDING         235..237
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:0000305|PubMed:25256292,
FT                   ECO:0007744|PDB:3W9F"
FT   BINDING         282..285
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:0000305|PubMed:25256292,
FT                   ECO:0007744|PDB:3W9F"
FT   BINDING         330
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:0000305|PubMed:25256292,
FT                   ECO:0007744|PDB:3W9F"
FT   BINDING         668
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   MUTAGEN         178
FT                   /note="K->A: Strongly decreased affinity for ATP and
FT                   Ca(2+)-calmodulin. Abolishes ATP-mediated increase in
FT                   channel sensitivity to agonists."
FT                   /evidence="ECO:0000269|PubMed:19864432"
FT   MUTAGEN         183
FT                   /note="K->A: Strongly decreased affinity for ATP and
FT                   slightly decreased affinity for Ca(2+)-calmodulin."
FT                   /evidence="ECO:0000269|PubMed:19864432"
FT   MUTAGEN         205
FT                   /note="K->A: No significant effect on affinity for ATP and
FT                   Ca(2+)-calmodulin."
FT                   /evidence="ECO:0000269|PubMed:19864432"
FT   CONFLICT        47
FT                   /note="V -> G (in Ref. 1; AAG28026)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        131
FT                   /note="I -> V (in Ref. 1; AAG28026)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        741
FT                   /note="V -> A (in Ref. 1; AAG28026)"
FT                   /evidence="ECO:0000305"
FT   STRAND          131..133
FT                   /evidence="ECO:0007829|PDB:6F55"
FT   HELIX           137..146
FT                   /evidence="ECO:0007829|PDB:3W9F"
FT   HELIX           149..152
FT                   /evidence="ECO:0007829|PDB:3W9F"
FT   HELIX           155..161
FT                   /evidence="ECO:0007829|PDB:3W9F"
FT   HELIX           169..171
FT                   /evidence="ECO:0007829|PDB:3W9F"
FT   TURN            174..176
FT                   /evidence="ECO:0007829|PDB:3W9F"
FT   HELIX           180..185
FT                   /evidence="ECO:0007829|PDB:3W9F"
FT   STRAND          189..191
FT                   /evidence="ECO:0007829|PDB:3JXJ"
FT   HELIX           195..205
FT                   /evidence="ECO:0007829|PDB:3W9F"
FT   HELIX           209..214
FT                   /evidence="ECO:0007829|PDB:3W9F"
FT   STRAND          220..225
FT                   /evidence="ECO:0007829|PDB:3W9F"
FT   HELIX           227..233
FT                   /evidence="ECO:0007829|PDB:3W9F"
FT   HELIX           237..245
FT                   /evidence="ECO:0007829|PDB:3W9F"
FT   STRAND          260..262
FT                   /evidence="ECO:0007829|PDB:3W9F"
FT   HELIX           274..280
FT                   /evidence="ECO:0007829|PDB:3W9F"
FT   HELIX           284..292
FT                   /evidence="ECO:0007829|PDB:3W9F"
FT   HELIX           310..317
FT                   /evidence="ECO:0007829|PDB:3W9F"
FT   HELIX           322..342
FT                   /evidence="ECO:0007829|PDB:3W9F"
FT   HELIX           348..350
FT                   /evidence="ECO:0007829|PDB:3W9F"
FT   HELIX           359..365
FT                   /evidence="ECO:0007829|PDB:3W9F"
FT   HELIX           369..382
FT                   /evidence="ECO:0007829|PDB:3W9F"
SQ   SEQUENCE   852 AA;  96282 MW;  0A799C76C6598845 CRC64;
     MADPEDPRDA GDVLGDDSFP LSSLANLFEV EDTPSPAEPS RGPPGAVDGK QNLRMKFHGA
     FRKGPPKPME LLESTIYESS VVPAPKKAPM DSLFDYGTYR QHPSENKRWR RRVVEKPVAG
     TKGPAPNPPP ILKVFNRPIL FDIVSRGSPD GLEGLLSFLL THKKRLTDEE FREPSTGKTC
     LPKALLNLSA GRNDTIPILL DIAEKTGNMR EFINSPFRDV YYRGQTALHI AIERRCKHYV
     ELLVEKGADV HAQARGRFFQ PKDEGGYFYF GELPLSLAAC TNQPHIVHYL TENGHKQADL
     RRQDSRGNTV LHALVAIADN TRENTKFVTK MYDLLLIKCA KLFPDTNLEA LLNNDGLSPL
     MMAAKTGKIG IFQHIIRREI ADEDVRHLSR KFKDWAYGPV YSSLYDLSSL DTCGEEVSVL
     EILVYNSKIE NRHEMLAVEP INELLRDKWR KFGAVSFYIS VVSYLCAMII FTLIAYYRPM
     EGPPPYPYTT TIDYLRLAGE IITLLTGILF FFSNIKDLFM KKCPGVNSFF IDGSFQLLYF
     IYSVLVIVTA GLYLGGVEAY LAVMVFALVL GWMNALYFTR GLKLTGTYSI MIQKILFKDL
     FRFLLVYLLF MIGYASALVS LLNPCPSSES CSEDHSNCTL PTYPSCRDSQ TFSTFLLDLF
     KLTIGMGDLE MLESAKYPGV FIILLVTYII LTFVLLLNML IALMGETVGQ VSKESKHIWK
     LQWATTILDI ERSFPLFLRR VFRSGEMVTV GKGTDGTPDR RWCFRVDEVN WSHWNQNLGI
     ISEDPGKSDT YQYYGFSHTV GRLRRDRWST VVPRVVELNK SCPTEDVVVP LGTMGTAEAR
     ERRHGQTPSS PL
//