PIEZ1_MOUSE
ID PIEZ1_MOUSE Reviewed; 2547 AA.
AC E2JF22;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Piezo-type mechanosensitive ion channel component 1;
DE AltName: Full=Protein FAM38A;
GN Name=Piezo1; Synonyms=Fam38a;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=20813920; DOI=10.1126/science.1193270;
RA Coste B., Mathur J., Schmidt M., Earley T.J., Ranade S., Petrus M.J.,
RA Dubin A.E., Patapoutian A.;
RT "Piezo1 and Piezo2 are essential components of distinct mechanically
RT activated cation channels.";
RL Science 330:55-60(2010).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1385 AND SER-1646, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1627; SER-1631 AND SER-1646,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22343900; DOI=10.1038/nature10812;
RA Coste B., Xiao B., Santos J.S., Syeda R., Grandl J., Spencer K.S.,
RA Kim S.E., Schmidt M., Mathur J., Dubin A.E., Montal M., Patapoutian A.;
RT "Piezo proteins are pore-forming subunits of mechanically activated
RT channels.";
RL Nature 483:176-181(2012).
RN [5]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=23479567; DOI=10.1182/blood-2013-02-482489;
RA Andolfo I., Alper S.L., De Franceschi L., Auriemma C., Russo R.,
RA De Falco L., Vallefuoco F., Esposito M.R., Vandorpe D.H., Shmukler B.E.,
RA Narayan R., Montanaro D., D'Armiento M., Vetro A., Limongelli I.,
RA Zuffardi O., Glader B.E., Schrier S.L., Brugnara C., Stewart G.W.,
RA Delaunay J., Iolascon A.;
RT "Multiple clinical forms of dehydrated hereditary stomatocytosis arise from
RT mutations in PIEZO1.";
RL Blood 121:3925-3935(2013).
RN [6]
RP INTERACTION WITH PKD2, AND FUNCTION.
RX PubMed=24157948; DOI=10.1038/embor.2013.170;
RA Peyronnet R., Martins J.R., Duprat F., Demolombe S., Arhatte M., Jodar M.,
RA Tauc M., Duranton C., Paulais M., Teulon J., Honore E., Patel A.;
RT "Piezo1-dependent stretch-activated channels are inhibited by Polycystin-2
RT in renal tubular epithelial cells.";
RL EMBO Rep. 14:1143-1148(2013).
RN [7]
RP INTERACTION WITH STOML3.
RX PubMed=24662763; DOI=10.1038/ncomms4520;
RA Poole K., Herget R., Lapatsina L., Ngo H.D., Lewin G.R.;
RT "Tuning Piezo ion channels to detect molecular-scale movements relevant for
RT fine touch.";
RL Nat. Commun. 5:3520-3520(2014).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=24958852; DOI=10.1073/pnas.1409233111;
RA Ranade S.S., Qiu Z., Woo S.H., Hur S.S., Murthy S.E., Cahalan S.M., Xu J.,
RA Mathur J., Bandell M., Coste B., Li Y.S., Chien S., Patapoutian A.;
RT "Piezo1, a mechanically activated ion channel, is required for vascular
RT development in mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:10347-10352(2014).
RN [9]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=25119035; DOI=10.1038/nature13701;
RA Li J., Hou B., Tumova S., Muraki K., Bruns A., Ludlow M.J., Sedo A.,
RA Hyman A.J., McKeown L., Young R.S., Yuldasheva N.Y., Majeed Y.,
RA Wilson L.A., Rode B., Bailey M.A., Kim H.R., Fu Z., Carter D.A., Bilton J.,
RA Imrie H., Ajuh P., Dear T.N., Cubbon R.M., Kearney M.T., Prasad R.K.,
RA Evans P.C., Ainscough J.F., Beech D.J.;
RT "Piezo1 integration of vascular architecture with physiological force.";
RL Nature 515:279-282(2014).
RN [10]
RP FUNCTION, ACTIVITY REGULATION, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=29799007; DOI=10.1038/s41467-018-04436-w;
RA Tsuchiya M., Hara Y., Okuda M., Itoh K., Nishioka R., Shiomi A., Nagao K.,
RA Mori M., Mori Y., Ikenouchi J., Suzuki R., Tanaka M., Ohwada T., Aoki J.,
RA Kanagawa M., Toda T., Nagata Y., Matsuda R., Takayama Y., Tominaga M.,
RA Umeda M.;
RT "Cell surface flip-flop of phosphatidylserine is critical for PIEZO1-
RT mediated myotube formation.";
RL Nat. Commun. 9:2049-2049(2018).
RN [11]
RP STRUCTURE BY ELECTRON MICROSCOPY (4.80 ANGSTROMS), X-RAY CRYSTALLOGRAPHY
RP (1.45 ANGSTROMS) OF 2214-2457, SUBUNIT, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=26390154; DOI=10.1038/nature15247;
RA Ge J., Li W., Zhao Q., Li N., Chen M., Zhi P., Li R., Gao N., Xiao B.,
RA Yang M.;
RT "Architecture of the mammalian mechanosensitive Piezo1 channel.";
RL Nature 527:64-69(2015).
CC -!- FUNCTION: Pore-forming subunit of a mechanosensitive non-specific
CC cation channel. Generates currents characterized by a linear current-
CC voltage relationship that are sensitive to ruthenium red and
CC gadolinium. Plays a key role in epithelial cell adhesion by maintaining
CC integrin activation through R-Ras recruitment to the ER, most probably
CC in its activated state, and subsequent stimulation of calpain
CC signaling. In the kidney, may contribute to the detection of
CC intraluminal pressure changes and to urine flow sensing. Acts as shear-
CC stress sensor that promotes endothelial cell organization and alignment
CC in the direction of blood flow through calpain activation. Plays a key
CC role in blood vessel formation and vascular structure in both
CC development and adult physiology. Acts as sensor of phosphatidylserine
CC (PS) flipping at the plasma membrane and governs morphogenesis of
CC muscle cells. In myoblasts, flippase-mediated PS enrichment at the
CC inner leaflet of plasma membrane triggers channel activation and Ca2+
CC influx followed by Rho GTPases signal transduction, leading to assembly
CC of cortical actomyosin fibers and myotube formation.
CC {ECO:0000269|PubMed:20813920, ECO:0000269|PubMed:22343900,
CC ECO:0000269|PubMed:24157948, ECO:0000269|PubMed:24958852,
CC ECO:0000269|PubMed:25119035, ECO:0000269|PubMed:29799007}.
CC -!- ACTIVITY REGULATION: Down-regulated by phosphatidylserines exposed on
CC the cell surface. {ECO:0000269|PubMed:29799007}.
CC -!- SUBUNIT: Homotrimer (PubMed:26390154). Interacts with PKD2
CC (PubMed:24157948). Interacts with STOML3 (PubMed:24662763).
CC {ECO:0000269|PubMed:22343900, ECO:0000269|PubMed:24157948,
CC ECO:0000269|PubMed:24662763, ECO:0000269|PubMed:26390154}.
CC -!- INTERACTION:
CC E2JF22; O55143: Atp2a2; NbExp=3; IntAct=EBI-9837938, EBI-770763;
CC E2JF22; E2JF22: Piezo1; NbExp=12; IntAct=EBI-9837938, EBI-9837938;
CC E2JF22; O35245: Pkd2; NbExp=3; IntAct=EBI-9837938, EBI-9823400;
CC E2JF22; P16615-1: ATP2A2; Xeno; NbExp=2; IntAct=EBI-9837938, EBI-11613988;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q92508}; Multi-pass membrane protein.
CC Endoplasmic reticulum-Golgi intermediate compartment membrane
CC {ECO:0000250|UniProtKB:Q0KL00}. Cell membrane
CC {ECO:0000269|PubMed:20813920, ECO:0000269|PubMed:26390154}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:26390154}. Cell projection,
CC lamellipodium membrane {ECO:0000250|UniProtKB:Q92508}. Cell membrane
CC {ECO:0000305|PubMed:29799007}; Multi-pass membrane protein. Note=In
CC erythrocytes, located in the plasma membrane (PubMed:23479567).
CC Accumulates at the leading apical lamellipodia of endothelial cells in
CC response to shear stress (By similarity). Colocalizes with F-actin and
CC MYH9 at the actomyosin cortex in myoblasts.
CC {ECO:0000250|UniProtKB:Q92508, ECO:0000269|PubMed:23479567,
CC ECO:0000269|PubMed:29799007}.
CC -!- TISSUE SPECIFICITY: Expressed in bladder, colon, kidney and skin. Also
CC expressed in bone marrow, liver, lung, spleen and erythrocytes (at
CC protein level). Expressed in myoblasts (at protein level).
CC {ECO:0000269|PubMed:20813920, ECO:0000269|PubMed:23479567,
CC ECO:0000269|PubMed:24958852, ECO:0000269|PubMed:29799007}.
CC -!- DEVELOPMENTAL STAGE: Expressed at least from 9.5 dpc. Expression levels
CC increase up to 15.5 dpc and remain high at least until birth.
CC {ECO:0000269|PubMed:23479567}.
CC -!- DISRUPTION PHENOTYPE: Embryo lethality at midgestation with defects in
CC vascular remodeling. {ECO:0000269|PubMed:24958852,
CC ECO:0000269|PubMed:25119035}.
CC -!- MISCELLANEOUS: Piezo comes from the Greek 'piesi' meaning pressure.
CC {ECO:0000305|PubMed:20813920}.
CC -!- SIMILARITY: Belongs to the PIEZO (TC 1.A.75) family. {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; HQ215520; ADN28064.1; -; mRNA.
DR CCDS; CCDS90474.1; -.
DR PDB; 3JAC; EM; 4.80 A; A/B/C=1-2547.
DR PDB; 4RAX; X-ray; 1.45 A; A=2214-2457.
DR PDB; 5Z10; EM; 3.97 A; A/B/C=1-2547.
DR PDB; 6B3R; EM; 3.80 A; A/C/E=1-2547.
DR PDB; 6BPZ; EM; 3.80 A; A/B/C=1137-2547.
DR PDB; 6LQI; EM; 4.50 A; A/B/C=1-2547.
DR PDB; 7WLT; EM; 3.46 A; A/C/E=1-2547.
DR PDB; 7WLU; EM; 6.81 A; A/C/E=1-2547.
DR PDBsum; 3JAC; -.
DR PDBsum; 4RAX; -.
DR PDBsum; 5Z10; -.
DR PDBsum; 6B3R; -.
DR PDBsum; 6BPZ; -.
DR PDBsum; 6LQI; -.
DR PDBsum; 7WLT; -.
DR PDBsum; 7WLU; -.
DR AlphaFoldDB; E2JF22; -.
DR SMR; E2JF22; -.
DR DIP; DIP-59655N; -.
DR IntAct; E2JF22; 5.
DR MINT; E2JF22; -.
DR STRING; 10090.ENSMUSP00000089777; -.
DR GuidetoPHARMACOLOGY; 2945; -.
DR TCDB; 1.A.75.1.14; the mechanical nociceptor, piezo (piezo) family.
DR GlyConnect; 2587; 2 N-Linked glycans (1 site).
DR GlyGen; E2JF22; 3 sites, 2 N-linked glycans (1 site).
DR iPTMnet; E2JF22; -.
DR PhosphoSitePlus; E2JF22; -.
DR SwissPalm; E2JF22; -.
DR EPD; E2JF22; -.
DR jPOST; E2JF22; -.
DR MaxQB; E2JF22; -.
DR PaxDb; E2JF22; -.
DR PeptideAtlas; E2JF22; -.
DR PRIDE; E2JF22; -.
DR ProteomicsDB; 289571; -.
DR MGI; MGI:3603204; Piezo1.
DR eggNOG; KOG1893; Eukaryota.
DR InParanoid; E2JF22; -.
DR ChiTaRS; Piezo1; mouse.
DR PRO; PR:E2JF22; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; E2JF22; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005261; F:cation channel activity; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0140135; F:mechanosensitive cation channel activity; IMP:MGI.
DR GO; GO:0008381; F:mechanosensitive ion channel activity; IDA:MGI.
DR GO; GO:0006812; P:cation transport; IMP:UniProtKB.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IBA:GO_Central.
DR GO; GO:0050982; P:detection of mechanical stimulus; IMP:MGI.
DR GO; GO:0033634; P:positive regulation of cell-cell adhesion mediated by integrin; ISS:UniProtKB.
DR GO; GO:0033625; P:positive regulation of integrin activation; ISS:UniProtKB.
DR GO; GO:0010831; P:positive regulation of myotube differentiation; IMP:UniProtKB.
DR GO; GO:0042391; P:regulation of membrane potential; IMP:MGI.
DR InterPro; IPR027272; Piezo.
DR InterPro; IPR031805; Piezo_dom.
DR InterPro; IPR031334; Piezo_RRas-bd_dom.
DR PANTHER; PTHR13167; PTHR13167; 4.
DR Pfam; PF15917; PIEZO; 1.
DR Pfam; PF12166; Piezo_RRas_bdg; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cell projection; Coiled coil; Disulfide bond;
KW Endoplasmic reticulum; Glycoprotein; Ion channel; Ion transport; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..2547
FT /note="Piezo-type mechanosensitive ion channel component 1"
FT /id="PRO_0000403959"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 435..455
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 467..487
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 520..540
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 577..597
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 608..628
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 635..655
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 687..707
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 818..838
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 847..867
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 921..941
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 982..1002
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1006..1023
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1038..1058
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1155..1175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1179..1199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1207..1227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1232..1252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1272..1292
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1678..1698
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1700..1720
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1734..1754
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1978..1998
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2019..2039
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2048..2068
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2077..2097
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2145..2165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2193..2213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2214..2457
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:26390154"
FT TRANSMEM 2458..2478
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 347..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1354..1396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1456..1480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1567..1610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1816..1931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1334..1365
FT /evidence="ECO:0000255"
FT COMPBIAS 347..371
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1361..1378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1573..1610
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1816..1836
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1861..1883
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1892..1931
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 758
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q0KL00"
FT MOD_RES 1385
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 1390
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92508"
FT MOD_RES 1627
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1631
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1646
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 2437..2441
FT /evidence="ECO:0000269|PubMed:26390154"
FT STRAND 2224..2232
FT /evidence="ECO:0007829|PDB:4RAX"
FT STRAND 2238..2243
FT /evidence="ECO:0007829|PDB:4RAX"
FT STRAND 2247..2250
FT /evidence="ECO:0007829|PDB:4RAX"
FT HELIX 2253..2263
FT /evidence="ECO:0007829|PDB:4RAX"
FT HELIX 2267..2273
FT /evidence="ECO:0007829|PDB:4RAX"
FT HELIX 2278..2280
FT /evidence="ECO:0007829|PDB:4RAX"
FT STRAND 2281..2289
FT /evidence="ECO:0007829|PDB:4RAX"
FT HELIX 2298..2310
FT /evidence="ECO:0007829|PDB:4RAX"
FT STRAND 2315..2324
FT /evidence="ECO:0007829|PDB:4RAX"
FT HELIX 2327..2329
FT /evidence="ECO:0007829|PDB:4RAX"
FT STRAND 2334..2344
FT /evidence="ECO:0007829|PDB:4RAX"
FT HELIX 2349..2357
FT /evidence="ECO:0007829|PDB:4RAX"
FT STRAND 2366..2372
FT /evidence="ECO:0007829|PDB:4RAX"
FT STRAND 2375..2378
FT /evidence="ECO:0007829|PDB:4RAX"
FT STRAND 2380..2383
FT /evidence="ECO:0007829|PDB:4RAX"
FT TURN 2388..2390
FT /evidence="ECO:0007829|PDB:4RAX"
FT HELIX 2394..2397
FT /evidence="ECO:0007829|PDB:4RAX"
FT STRAND 2398..2409
FT /evidence="ECO:0007829|PDB:4RAX"
FT STRAND 2426..2434
FT /evidence="ECO:0007829|PDB:4RAX"
FT STRAND 2443..2450
FT /evidence="ECO:0007829|PDB:4RAX"
SQ SEQUENCE 2547 AA; 292002 MW; 0C24CF18BDF502E3 CRC64;
MEPHVLGAGL YWLLLPCTLL AASLLRFNAL SLVYLLFLLL LPWLPGPSRH SIPGHTGRLL
RALLCLSLLF LVAHLAFQIC LHTVPHLDQF LGQNGSLWVK VSQHIGVTRL DLKDIFNTTR
LVAPDLGVLL ASSLCLGLCG RLTRKAGQSR RTQELQDDDD DDDDDDEDID AAPAVGLKGA
PALATKRRLW LASRFRVTAH WLLMTSGRTL VIVLLALAGI AHPSAFSSIY LVVFLAICTW
WSCHFPLSPL GFNTLCVMVS CFGAGHLICL YCYQTPFIQD MLPPGNIWAR LFGLKNFVDL
PNYSSPNALV LNTKHAWPIY VSPGILLLLY YTATSLLKLH KSCPSELRKE TPREDEEHEL
ELDHLEPEPQ ARDATQGEMP MTTEPDLDNC TVHVLTSQSP VRQRPVRPRL AELKEMSPLH
GLGHLIMDQS YVCALIAMMV WSIMYHSWLT FVLLLWACLI WTVRSRHQLA MLCSPCILLY
GLTLCCLRYV WAMELPELPT TLGPVSLHQL GLEHTRYPCL DLGAMLLYLL TFWLLLRQFV
KEKLLKKQKV PAALLEVTVA DTEPTQTQTL LRSLGELVTG IYVKYWIYVC AGMFIVVSFA
GRLVVYKIVY MFLFLLCLTL FQVYYTLWRK LLRVFWWLVV AYTMLVLIAV YTFQFQDFPT
YWRNLTGFTD EQLGDLGLEQ FSVSELFSSI LIPGFFLLAC ILQLHYFHRP FMQLTDLEHV
PPPGTRHPRW AHRQDAVSEA PLLEHQEEEE VFREDGQSMD GPHQATQVPE GTASKWGLVA
DRLLDLAASF SAVLTRIQVF VRRLLELHVF KLVALYTVWV ALKEVSVMNL LLVVLWAFAL
PYPRFRPMAS CLSTVWTCII IVCKMLYQLK IVNPHEYSSN CTEPFPNNTN LQPLEINQSL
LYRGPVDPAN WFGVRKGYPN LGYIQNHLQI LLLLVFEAVV YRRQEHYRRQ HQQAPLPAQA
VCADGTRQRL DQDLLSCLKY FINFFFYKFG LEICFLMAVN VIGQRMNFMV ILHGCWLVAI
LTRRRREAIA RLWPNYCLFL TLFLLYQYLL CLGMPPALCI DYPWRWSKAI PMNSALIKWL
YLPDFFRAPN STNLISDFLL LLCASQQWQV FSAERTEEWQ RMAGINTDHL EPLRGEPNPI
PNFIHCRSYL DMLKVAVFRY LFWLVLVVVF VAGATRISIF GLGYLLACFY LLLFGTTLLQ
KDTRAQLVLW DCLILYNVTV IISKNMLSLL SCVFVEQMQS NFCWVIQLFS LVCTVKGYYD
PKEMMTRDRD CLLPVEEAGI IWDSICFFFL LLQRRIFLSH YFLHVSADLK ATALQASRGF
ALYNAANLKS INFHRQIEEK SLAQLKRQMK RIRAKQEKYR QSQASRGQLQ SKDPQDPSQE
PGPDSPGGSS PPRRQWWRPW LDHATVIHSG DYFLFESDSE EEEEALPEDP RPAAQSAFQM
AYQAWVTNAQ TVLRQRRERA RQERAEQLAS GGDLNPDVEP VDVPEDEMAG RSHMMQRVLS
TMQFLWVLGQ ATVDGLTRWL RAFTKHHRTM SDVLCAERYL LTQELLRVGE VRRGVLDQLY
VGEDEATLSG PVETRDGPST ASSGLGAEEP LSSMTDDTSS PLSTGYNTRS GSEEIVTDAG
DLQAGTSLHG SQELLANART RMRTASELLL DRRLHIPELE EAERFEAQQG RTLRLLRAGY
QCVAAHSELL CYFIIILNHM VTASAASLVL PVLVFLWAML TIPRPSKRFW MTAIVFTEVM
VVTKYLFQFG FFPWNSYVVL RRYENKPYFP PRILGLEKTD SYIKYDLVQL MALFFHRSQL
LCYGLWDHEE DRYPKDHCRS SVKDREAKEE PEAKLESQSE TGTGHPKEPV LAGTPRDHIQ
GKGSIRSKDV IQDPPEDLKP RHTRHISIRF RRRKETPGPK GTAVMETEHE EGEGKETTER
KRPRHTQEKS KFRERMKAAG RRLQSFCVSL AQSFYQPLQR FFHDILHTKY RAATDVYALM
FLADIVDIII IIFGFWAFGK HSAATDIASS LSDDQVPQAF LFMLLVQFGT MVIDRALYLR
KTVLGKLAFQ VVLVVAIHIW MFFILPAVTE RMFSQNAVAQ LWYFVKCIYF ALSAYQIRCG
YPTRILGNFL TKKYNHLNLF LFQGFRLVPF LVELRAVMDW VWTDTTLSLS NWMCVEDIYA
NIFIIKCSRE TEKKYPQPKG QKKKKIVKYG MGGLIILFLI AIIWFPLLFM SLIRSVVGVV
NQPIDVTVTL KLGGYEPLFT MSAQQPSIVP FTPQAYEELS QQFDPYPLAM QFISQYSPED
IVTAQIEGSS GALWRISPPS RAQMKQELYN GTADITLRFT WNFQRDLAKG GTVEYTNEKH
TLELAPNSTA RRQLAQLLEG RPDQSVVIPH LFPKYIRAPN GPEANPVKQL QPDEEEDYLG
VRIQLRREQV GTGASGEQAG TKASDFLEWW VIELQDCKAD CNLLPMVIFS DKVSPPSLGF
LAGYGIVGLY VSIVLVVGKF VRGFFSEISH SIMFEELPCV DRILKLCQDI FLVRETRELE
LEEELYAKLI FLYRSPETMI KWTRERE
