TRPV6_RAT
ID TRPV6_RAT Reviewed; 767 AA.
AC Q9R186;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-2015, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Transient receptor potential cation channel subfamily V member 6;
DE Short=TrpV6;
DE AltName: Full=Calcium transport protein 1 {ECO:0000303|PubMed:10428857};
DE Short=CaT1 {ECO:0000303|PubMed:11287959};
DE AltName: Full=Epithelial calcium channel 2;
DE Short=ECaC2;
GN Name=Trpv6;
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 STRAIN=Wistar; TISSUE=Intestine;
RX PubMed=10428857; DOI=10.1074/jbc.274.32.22739;
RA Peng J.-B., Chen X.Z., Berger U.V., Vassilev P.M., Tsukaguchi H.,
RA Brown E.M., Hediger M.A.;
RT "Molecular cloning and characterization of a channel-like transporter
RT mediating intestinal calcium absorption.";
RL J. Biol. Chem. 274:22739-22746(1999).
RN [2]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11287959; DOI=10.1038/35070596;
RA Yue L., Peng J.B., Hediger M.A., Clapham D.E.;
RT "CaT1 manifests the pore properties of the calcium-release-activated
RT calcium channel.";
RL Nature 410:705-709(2001).
RN [3]
RP PHOSPHORYLATION AT TYR-201 AND TYR-202, AND MUTAGENESIS OF TYR-201 AND
RP TYR-202.
RX PubMed=17197020; DOI=10.1016/j.ceca.2006.11.008;
RA Sternfeld L., Anderie I., Schmid A., Al-Shaldi H., Krause E., Magg T.,
RA Schreiner D., Hofer H.W., Schulz I.;
RT "Identification of tyrosines in the putative regulatory site of the Ca2+
RT channel TRPV6.";
RL Cell Calcium 42:91-102(2007).
RN [4] {ECO:0007744|PDB:5IWK, ECO:0007744|PDB:5IWP, ECO:0007744|PDB:5IWR, ECO:0007744|PDB:5IWT}
RP X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 41-709, FUNCTION, SUBUNIT,
RP SUBCELLULAR LOCATION, TOPOLOGY, AND REPEATS.
RX PubMed=27296226; DOI=10.1038/nature17975;
RA Saotome K., Singh A.K., Yelshanskaya M.V., Sobolevsky A.I.;
RT "Crystal structure of the epithelial calcium channel TRPV6.";
RL Nature 534:506-511(2016).
RN [5] {ECO:0007744|PDB:6BOB}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.90 ANGSTROMS) OF 41-708, SUBUNIT,
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=29258289; DOI=10.1038/nature25182;
RA McGoldrick L.L., Singh A.K., Saotome K., Yelshanskaya M.V., Twomey E.C.,
RA Grassucci R.A., Sobolevsky A.I.;
RT "Opening of the human epithelial calcium channel TRPV6.";
RL Nature 553:233-237(2018).
RN [6] {ECO:0007744|PDB:5WO6, ECO:0007744|PDB:5WO7, ECO:0007744|PDB:5WO8, ECO:0007744|PDB:5WO9, ECO:0007744|PDB:5WOA}
RP X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 41-709 OF WILD-TYPE AND MUTANT
RP GLN-495, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, TOPOLOGY, AND MUTAGENESIS
RP OF LEU-535.
RX PubMed=28878326; DOI=10.1038/s41598-017-10993-9;
RA Singh A.K., Saotome K., Sobolevsky A.I.;
RT "Swapping of transmembrane domains in the epithelial calcium channel
RT TRPV6.";
RL Sci. Rep. 7:10669-10669(2017).
CC -!- FUNCTION: Calcium selective cation channel that mediates Ca(2+) uptake
CC in various tissues, including the intestine (PubMed:10428857,
CC PubMed:11287959, PubMed:27296226, PubMed:28878326). Important for
CC normal Ca(2+) ion homeostasis in the body, including bone and skin (By
CC similarity). The channel is activated by low internal calcium level,
CC probably including intracellular calcium store depletion, and the
CC current exhibits an inward rectification (PubMed:10428857,
CC PubMed:11287959, PubMed:27296226). Inactivation includes both a rapid
CC Ca(2+)-dependent and a slower Ca(2+)-calmodulin-dependent mechanism;
CC the latter may be regulated by phosphorylation. In vitro, is slowly
CC inhibited by Mg(2+) in a voltage-independent manner. Heteromeric
CC assembly with TRPV5 seems to modify channel properties. TRPV5-TRPV6
CC heteromultimeric concatemers exhibit voltage-dependent gating (By
CC similarity). {ECO:0000250|UniProtKB:Q91WD2,
CC ECO:0000250|UniProtKB:Q9H1D0, ECO:0000269|PubMed:10428857,
CC ECO:0000269|PubMed:11287959, ECO:0000269|PubMed:27296226,
CC ECO:0000269|PubMed:28878326}.
CC -!- SUBUNIT: Homotetramer (PubMed:27296226, PubMed:29258289,
CC PubMed:28878326). Probably forms also heterotetramers with TRPV5.
CC Interacts with TRPV5. Interacts with S100A10 and probably with the
CC ANAX2-S100A10 heterotetramer. The interaction with S100A10 is required
CC for the trafficking to the plasma membrane. Interacts with calmodulin.
CC Interacts with BSPRY. Interacts with TCAF1 and TCAF2 (By similarity).
CC {ECO:0000250|UniProtKB:Q9H1D0, ECO:0000269|PubMed:27296226,
CC ECO:0000269|PubMed:28878326, ECO:0000269|PubMed:29258289}.
CC -!- INTERACTION:
CC Q9R186; Q9R186: Trpv6; NbExp=3; IntAct=EBI-7198720, EBI-7198720;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10428857,
CC ECO:0000269|PubMed:17197020, ECO:0000269|PubMed:27296226,
CC ECO:0000269|PubMed:28878326, ECO:0000269|PubMed:29258289}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:27296226,
CC ECO:0000269|PubMed:28878326, ECO:0000269|PubMed:29258289}.
CC -!- TISSUE SPECIFICITY: Expressed in duodenum, proximal jejunum, cecum, and
CC colon. {ECO:0000269|PubMed:10428857}.
CC -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:Q91WD2,
CC ECO:0000250|UniProtKB:Q9H1D0}.
CC -!- PTM: Phosphorylation at Tyr-201 and Tyr-202 by SRC leads to an
CC increased calcium influx through the channel. Probably dephosphorylated
CC at these sites by PTPN1. {ECO:0000269|PubMed:17197020}.
CC -!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family. TrpV
CC subfamily. TRPV6 sub-subfamily. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-41 is the initiator. In
CC human and mouse, initiation starts at a conserved non-canonical ACG
CC threonine codon decoded as Met-1 upstream of the canonical initiation
CC at Met-41. {ECO:0000250|UniProtKB:Q91WD2,
CC ECO:0000250|UniProtKB:Q9H1D0}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD47636.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical ACG threonine codon.; Evidence={ECO:0000250|UniProtKB:Q9H1D0};
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DR EMBL; AF160798; AAD47636.1; ALT_SEQ; mRNA.
DR RefSeq; NP_446138.1; NM_053686.1.
DR PDB; 5IWK; X-ray; 3.25 A; A=41-709.
DR PDB; 5IWP; X-ray; 3.65 A; A=41-709.
DR PDB; 5IWR; X-ray; 3.85 A; A=41-709.
DR PDB; 5IWT; X-ray; 3.80 A; A=41-709.
DR PDB; 5WO6; X-ray; 3.31 A; A=41-708.
DR PDB; 5WO7; X-ray; 3.25 A; A=41-709.
DR PDB; 5WO8; X-ray; 3.40 A; A=41-709.
DR PDB; 5WO9; X-ray; 3.70 A; A=41-709.
DR PDB; 5WOA; X-ray; 3.90 A; A=41-709.
DR PDB; 6BOB; EM; 3.90 A; A/B/C/D=41-708.
DR PDB; 6D7O; X-ray; 3.45 A; A=41-709.
DR PDB; 6D7P; X-ray; 3.37 A; A=41-709.
DR PDB; 6D7Q; X-ray; 3.50 A; A=41-709.
DR PDB; 6D7V; X-ray; 4.30 A; A=41-709.
DR PDB; 6D7X; X-ray; 3.60 A; A=41-709.
DR PDB; 6E2G; EM; 3.60 A; A/B/C/D=41-767.
DR PDB; 7D2K; X-ray; 3.70 A; A=41-709.
DR PDBsum; 5IWK; -.
DR PDBsum; 5IWP; -.
DR PDBsum; 5IWR; -.
DR PDBsum; 5IWT; -.
DR PDBsum; 5WO6; -.
DR PDBsum; 5WO7; -.
DR PDBsum; 5WO8; -.
DR PDBsum; 5WO9; -.
DR PDBsum; 5WOA; -.
DR PDBsum; 6BOB; -.
DR PDBsum; 6D7O; -.
DR PDBsum; 6D7P; -.
DR PDBsum; 6D7Q; -.
DR PDBsum; 6D7V; -.
DR PDBsum; 6D7X; -.
DR PDBsum; 6E2G; -.
DR PDBsum; 7D2K; -.
DR AlphaFoldDB; Q9R186; -.
DR SMR; Q9R186; -.
DR DIP; DIP-47769N; -.
DR IntAct; Q9R186; 1.
DR MINT; Q9R186; -.
DR STRING; 10116.ENSRNOP00000020616; -.
DR TCDB; 1.A.4.2.7; the transient receptor potential ca(2+) channel (trp-cc) family.
DR GlyGen; Q9R186; 1 site.
DR iPTMnet; Q9R186; -.
DR PhosphoSitePlus; Q9R186; -.
DR PaxDb; Q9R186; -.
DR GeneID; 114246; -.
DR KEGG; rno:114246; -.
DR UCSC; RGD:69335; rat.
DR CTD; 55503; -.
DR RGD; 69335; Trpv6.
DR eggNOG; KOG3676; Eukaryota.
DR InParanoid; Q9R186; -.
DR OrthoDB; 693004at2759; -.
DR Reactome; R-RNO-3295583; TRP channels.
DR PRO; PR:Q9R186; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IC:RGD.
DR GO; GO:0034704; C:calcium channel complex; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005227; F:calcium activated cation channel activity; TAS:RGD.
DR GO; GO:0005262; F:calcium channel activity; IDA:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005216; F:ion channel activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0055074; P:calcium ion homeostasis; ISS:UniProtKB.
DR GO; GO:0070509; P:calcium ion import; IDA:RGD.
DR GO; GO:0098703; P:calcium ion import across plasma membrane; IMP:UniProtKB.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IDA:UniProtKB.
DR GO; GO:0006816; P:calcium ion transport; ISO:RGD.
DR GO; GO:0035898; P:parathyroid hormone secretion; ISO:RGD.
DR GO; GO:0051289; P:protein homotetramerization; IPI:UniProtKB.
DR GO; GO:0051592; P:response to calcium ion; ISS:UniProtKB.
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; IPR008344; TRPV5/TRPV6.
DR InterPro; IPR008345; TrpV6.
DR PANTHER; PTHR10582; PTHR10582; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR PRINTS; PR01415; ANKYRIN.
DR PRINTS; PR01765; ECACCHANNEL.
DR PRINTS; PR01766; ECACCHANNEL1.
DR SMART; SM00248; ANK; 5.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
PE 1: Evidence at protein level;
KW 3D-structure; ANK repeat; Calcium; Calcium channel; Calcium transport;
KW Calmodulin-binding; Cell membrane; Glycoprotein; Ion channel;
KW Ion transport; Membrane; Metal-binding; Phosphoprotein; Reference proteome;
KW Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..767
FT /note="Transient receptor potential cation channel
FT subfamily V member 6"
FT /id="PRO_0000215356"
FT TOPO_DOM 1..366
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:27296226,
FT ECO:0000269|PubMed:28878326"
FT TRANSMEM 367..387
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:27296226,
FT ECO:0000269|PubMed:28878326"
FT TOPO_DOM 388..424
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:27296226,
FT ECO:0000269|PubMed:28878326"
FT TRANSMEM 425..447
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:27296226,
FT ECO:0000269|PubMed:28878326"
FT TOPO_DOM 448..462
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:27296226,
FT ECO:0000269|PubMed:28878326"
FT TRANSMEM 463..482
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:27296226,
FT ECO:0000269|PubMed:28878326"
FT TOPO_DOM 483..488
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:27296226,
FT ECO:0000269|PubMed:28878326"
FT TRANSMEM 489..508
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:27296226,
FT ECO:0000269|PubMed:28878326"
FT TOPO_DOM 509..528
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:27296226,
FT ECO:0000269|PubMed:28878326"
FT TRANSMEM 529..551
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:27296226,
FT ECO:0000269|PubMed:28878326"
FT TOPO_DOM 552..564
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:27296226,
FT ECO:0000269|PubMed:28878326"
FT INTRAMEM 565..584
FT /note="Pore-forming"
FT /evidence="ECO:0000269|PubMed:27296226,
FT ECO:0000269|PubMed:28878326"
FT TOPO_DOM 585..595
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:27296226,
FT ECO:0000269|PubMed:28878326"
FT TRANSMEM 596..616
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:27296226,
FT ECO:0000269|PubMed:28878326"
FT TOPO_DOM 617..767
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:27296226,
FT ECO:0000269|PubMed:28878326"
FT REPEAT 84..114
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 118..147
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 156..185
FT /note="ANK 3"
FT /evidence="ECO:0000255"
FT REPEAT 202..231
FT /note="ANK 4"
FT /evidence="ECO:0000255"
FT REPEAT 235..276
FT /note="ANK 5"
FT /evidence="ECO:0000255"
FT REPEAT 278..307
FT /note="ANK 6"
FT /evidence="ECO:0000255"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..143
FT /note="Interaction with calmodulin"
FT /evidence="ECO:0000250"
FT REGION 637..641
FT /note="Interaction with S100A10"
FT /evidence="ECO:0000250"
FT REGION 689..707
FT /note="Interaction with calmodulin"
FT /evidence="ECO:0000250"
FT MOTIF 580..584
FT /note="Selectivity filter"
FT /evidence="ECO:0000269|PubMed:27296226"
FT BINDING 581
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000269|PubMed:27296226,
FT ECO:0007744|PDB:5IWK, ECO:0007744|PDB:5IWP"
FT MOD_RES 201
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000269|PubMed:17197020"
FT MOD_RES 202
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000269|PubMed:17197020"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 201
FT /note="Y->F: Prevents up-regulation of the channel by
FT phosphorylation; when associated with F-202."
FT /evidence="ECO:0000269|PubMed:17197020"
FT MUTAGEN 202
FT /note="Y->F: Prevents up-regulation of the channel by
FT phosphorylation; when associated with F-201."
FT /evidence="ECO:0000269|PubMed:17197020"
FT MUTAGEN 535
FT /note="L->Q: Alters subunit assembly via domain swapping
FT and reduces channel activity."
FT /evidence="ECO:0000269|PubMed:28878326"
FT HELIX 70..86
FT /evidence="ECO:0007829|PDB:5WO7"
FT HELIX 88..94
FT /evidence="ECO:0007829|PDB:5WO7"
FT HELIX 98..105
FT /evidence="ECO:0007829|PDB:5WO7"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:5WO8"
FT HELIX 122..128
FT /evidence="ECO:0007829|PDB:5WO7"
FT HELIX 132..141
FT /evidence="ECO:0007829|PDB:5WO7"
FT HELIX 143..146
FT /evidence="ECO:0007829|PDB:5WO7"
FT TURN 154..157
FT /evidence="ECO:0007829|PDB:5WO7"
FT HELIX 160..166
FT /evidence="ECO:0007829|PDB:5WO7"
FT HELIX 170..178
FT /evidence="ECO:0007829|PDB:5WO7"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:5WO7"
FT HELIX 206..212
FT /evidence="ECO:0007829|PDB:5WO7"
FT HELIX 216..224
FT /evidence="ECO:0007829|PDB:5WO7"
FT HELIX 239..244
FT /evidence="ECO:0007829|PDB:5WO7"
FT HELIX 249..261
FT /evidence="ECO:0007829|PDB:5WO7"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:5WO7"
FT TURN 271..273
FT /evidence="ECO:0007829|PDB:5WO7"
FT HELIX 282..289
FT /evidence="ECO:0007829|PDB:5WO7"
FT HELIX 292..300
FT /evidence="ECO:0007829|PDB:5WO7"
FT STRAND 303..309
FT /evidence="ECO:0007829|PDB:5WO7"
FT STRAND 312..317
FT /evidence="ECO:0007829|PDB:5WO7"
FT TURN 320..322
FT /evidence="ECO:0007829|PDB:5WO7"
FT STRAND 323..326
FT /evidence="ECO:0007829|PDB:5WO8"
FT TURN 327..329
FT /evidence="ECO:0007829|PDB:5WO7"
FT HELIX 331..337
FT /evidence="ECO:0007829|PDB:5WO7"
FT HELIX 341..346
FT /evidence="ECO:0007829|PDB:5WO7"
FT HELIX 352..361
FT /evidence="ECO:0007829|PDB:5WO7"
FT TURN 362..364
FT /evidence="ECO:0007829|PDB:5WO7"
FT HELIX 365..387
FT /evidence="ECO:0007829|PDB:5WO7"
FT HELIX 397..399
FT /evidence="ECO:0007829|PDB:5IWK"
FT TURN 401..404
FT /evidence="ECO:0007829|PDB:5WO7"
FT TURN 418..420
FT /evidence="ECO:0007829|PDB:5WO6"
FT HELIX 421..442
FT /evidence="ECO:0007829|PDB:5WO7"
FT HELIX 443..445
FT /evidence="ECO:0007829|PDB:6D7P"
FT TURN 453..457
FT /evidence="ECO:0007829|PDB:6D7P"
FT HELIX 463..481
FT /evidence="ECO:0007829|PDB:5WO7"
FT TURN 482..484
FT /evidence="ECO:0007829|PDB:5WO7"
FT HELIX 487..489
FT /evidence="ECO:0007829|PDB:5IWK"
FT HELIX 490..501
FT /evidence="ECO:0007829|PDB:5WO7"
FT HELIX 504..510
FT /evidence="ECO:0007829|PDB:5WO7"
FT TURN 511..514
FT /evidence="ECO:0007829|PDB:6D7P"
FT HELIX 515..530
FT /evidence="ECO:0007829|PDB:5WO7"
FT HELIX 533..552
FT /evidence="ECO:0007829|PDB:5WO7"
FT TURN 556..558
FT /evidence="ECO:0007829|PDB:5WO7"
FT HELIX 565..576
FT /evidence="ECO:0007829|PDB:5WO7"
FT STRAND 586..588
FT /evidence="ECO:0007829|PDB:5WO7"
FT HELIX 592..613
FT /evidence="ECO:0007829|PDB:5WO7"
FT TURN 614..617
FT /evidence="ECO:0007829|PDB:5WO7"
FT TURN 618..620
FT /evidence="ECO:0007829|PDB:5IWK"
FT HELIX 622..646
FT /evidence="ECO:0007829|PDB:5WO7"
FT STRAND 649..652
FT /evidence="ECO:0007829|PDB:5WO6"
FT STRAND 655..659
FT /evidence="ECO:0007829|PDB:5WO7"
FT STRAND 662..664
FT /evidence="ECO:0007829|PDB:5WO7"
FT STRAND 668..675
FT /evidence="ECO:0007829|PDB:5WO7"
SQ SEQUENCE 767 AA; 87362 MW; 2197726C2F583720 CRC64;
MGPLQREGRP ALGDANVAPG SSPGGVWHQP QPPKDSAFHP MGWSLPKEKG LILCLWNKFC
RWFHRRESWA QSRDEQNLLQ QKRIWESPLL LAAKENNVQA LIKLLKFEGC EVHQKGAMGE
TALHIAALYD NLEAAMVLME AAPELVFEPM TSELYEGQTA LHIAVINQNV NLVRALLARG
ASVSARATGS VFHYRPHNLI YYGEHPLSFA ACVGSEEIVR LLIEHGADIR AQDSLGNTVL
HILILQPNKT FACQMYNLLL SYDGGDHLKS LELVPNNQGL TPFKLAGVEG NIVMFQHLMQ
KRKHIQWTYG PLTSTLYDLT EIDSSGDDQS LLELIVTTKK REARQILDQT PVKELVSLKW
KRYGRPYFCV LGAIYVLYII CFTMCCVYRP LKPRITNRTN PRDNTLLQQK LLQEAYVTPK
DDLRLVGELV SIVGAVIILL VEIPDIFRLG VTRFFGQTIL GGPFHVIIVT YAFMVLVTMV
MRLTNSDGEV VPMSFALVLG WCNVMYFARG FQMLGPFTIM IQKMIFGDLM RFCWLMAVVI
LGFASAFYII FQTEDPDELG HFYDYPMALF STFELFLTII DGPANYDVDL PFMYSITYAA
FAIIATLLML NLLIAMMGDT HWRVAHERDE LWRAQVVATT VMLERKLPRC LWPRSGICGR
EYGLGDRWFL RVEDRQDLNR QRIRRYAQAF QQQDDLYSED LEKDSGEKLE MARPFGAYLS
FPTPSVSRST SRSSTNWDRL RQGALRKDLQ GIINRGLEDG EGWEYQI
