TRPV5_MOUSE
ID TRPV5_MOUSE Reviewed; 723 AA.
AC P69744; Q2TB50;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Transient receptor potential cation channel subfamily V member 5;
DE Short=TrpV5;
DE AltName: Full=Calcium transport protein 2;
DE Short=CaT2;
DE AltName: Full=Epithelial calcium channel 1;
DE Short=ECaC1;
DE AltName: Full=Osm-9-like TRP channel 3;
DE Short=OTRPC3;
GN Name=Trpv5;
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 [GENOMIC DNA].
RA Weber K., Zeitz U., Rump A., Erben R., Adamski J.;
RT "Characterization of two epithelial calcium channel genes in mice.";
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF 403-VAL--SER-406.
RX PubMed=12077127; DOI=10.1074/jbc.m202418200;
RA Nilius B., Prenen J., Hoenderop J.G., Vennekens R., Hoefs S., Weidema A.F.,
RA Droogmans G., Bindels R.J.M.;
RT "Fast and slow inactivation kinetics of the Ca2+ channels ECaC1 and ECaC2
RT (TRPV5 and TRPV6). Role of the intracellular loop located between
RT transmembrane segments 2 and 3.";
RL J. Biol. Chem. 277:30852-30858(2002).
RN [6]
RP SUBUNIT, AND INTERACTION WITH TRPV6.
RX PubMed=12574114; DOI=10.1093/emboj/cdg080;
RA Hoenderop J.G., Voets T., Hoefs S., Weidema F., Prenen J., Nilius B.,
RA Bindels R.J.M.;
RT "Homo- and heterotetrameric architecture of the epithelial Ca2+ channels
RT TRPV5 and TRPV6.";
RL EMBO J. 22:776-785(2003).
RN [7]
RP SUBCELLULAR LOCATION, INTERACTION WITH S100A10 AND ANAX2, AND MUTAGENESIS
RP OF THR-593.
RX PubMed=12660155; DOI=10.1093/emboj/cdg162;
RA van de Graaf S.F., Hoenderop J.G., Gkika D., Lamers D., Prenen J.,
RA Rescher U., Gerke V., Staub O., Nilius B., Bindels R.J.M.;
RT "Functional expression of the epithelial Ca(2+) channels (TRPV5 and TRPV6)
RT requires association of the S100A10-annexin 2 complex.";
RL EMBO J. 22:1478-1487(2003).
RN [8]
RP DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=14679186; DOI=10.1172/jci200319826;
RA Hoenderop J.G., van Leeuwen J.P., van der Eerden B.C., Kersten F.F.,
RA van der Kemp A.W., Merillat A.M., Waarsing J.H., Rossier B.C., Vallon V.,
RA Hummler E., Bindels R.J.;
RT "Renal Ca2+ wasting, hyperabsorption, and reduced bone thickness in mice
RT lacking TRPV5.";
RL J. Clin. Invest. 112:1906-1914(2003).
RN [9]
RP INTERACTION WITH CALMODULIN.
RX PubMed=15123711; DOI=10.1074/jbc.m313637200;
RA Lambers T.T., Weidema A.F., Nilius B., Hoenderop J.G., Bindels R.J.M.;
RT "Regulation of the mouse epithelial Ca2(+) channel TRPV6 by the Ca(2+)-
RT sensor calmodulin.";
RL J. Biol. Chem. 279:28855-28861(2004).
RN [10]
RP INTERACTION WITH BSPRY.
RX PubMed=16380433; DOI=10.1681/asn.2005101025;
RA van de Graaf S.F.J., van der Kemp A.W.C.M., van den Berg D.,
RA van Oorschot M., Hoenderop J.G.J., Bindels R.J.M.;
RT "Identification of BSPRY as a novel auxiliary protein inhibiting TRPV5
RT activity.";
RL J. Am. Soc. Nephrol. 17:26-30(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-678 AND SER-682, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
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 [12]
RP DISRUPTION PHENOTYPE.
RX PubMed=27102152; DOI=10.18632/oncotarget.8779;
RA van der Eerden B.C., Koek W.N., Roschger P., Zillikens M.C., Waarsing J.H.,
RA van der Kemp A., Schreuders-Koedam M., Fratzl-Zelman N., Leenen P.J.,
RA Hoenderop J.G., Klaushofer K., Bindels R.J., van Leeuwen J.P.;
RT "Lifelong challenge of calcium homeostasis in male mice lacking TRPV5 leads
RT to changes in bone and calcium metabolism.";
RL Oncotarget 7:24928-24941(2016).
CC -!- FUNCTION: Constitutively active calcium selective cation channel
CC thought to be involved in Ca(2+) reabsorption in kidney and intestine
CC (PubMed:12077127, PubMed:14679186). Required for normal Ca(2+)
CC reabsorption in the kidney distal convoluted tubules (PubMed:14679186).
CC The channel is activated by low internal calcium level and the current
CC exhibits an inward rectification. A Ca(2+)-dependent feedback
CC regulation includes fast channel inactivation and slow current decay
CC (PubMed:12077127). Heteromeric assembly with TRPV6 seems to modify
CC channel properties. TRPV5-TRPV6 heteromultimeric concatemers exhibit
CC voltage-dependent gating (By similarity).
CC {ECO:0000250|UniProtKB:Q9XSM3, ECO:0000269|PubMed:12077127,
CC ECO:0000269|PubMed:14679186}.
CC -!- ACTIVITY REGULATION: Activated by WNK3. {ECO:0000250|UniProtKB:Q9NQA5}.
CC -!- SUBUNIT: Homotetramer and probably heterotetramer with TRPV6. Interacts
CC with TRPV6 (PubMed:12574114). Interacts with S100A10 and probably with
CC the ANAX2-S100A10 heterotetramer. The interaction with S100A10 is
CC required for the trafficking to the plasma membrane (PubMed:12660155).
CC Interacts with calmodulin (PubMed:15123711). Interacts with BSPRY,
CC which results in its inactivation (PubMed:16380433).
CC {ECO:0000269|PubMed:12574114, ECO:0000269|PubMed:12660155,
CC ECO:0000269|PubMed:15123711, ECO:0000269|PubMed:16380433}.
CC -!- INTERACTION:
CC P69744; Q80UE6: Wnk4; NbExp=2; IntAct=EBI-538447, EBI-295378;
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:12660155}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:12660155}. Note=Colocalized with S100A10 and ANAX2
CC along the apical domain of kidney distal tubular cells.
CC {ECO:0000269|PubMed:12660155}.
CC -!- TISSUE SPECIFICITY: Detected in kidney cortex (at protein level).
CC {ECO:0000269|PubMed:14679186}.
CC -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:Q9NQA5}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice appear grossly normal and are
CC fertile. They display polyuria and increased urinary excretion of
CC Ca(2+), due to defective Ca(2+) reabsorption in the kidney distal
CC convoluted tubules. Likewise, they display increased urinary excretion
CC of phosphate. Besides, their urine has a lower pH. The polyuria and the
CC urine acidification may be a response to the high urinary Ca(2+)
CC levels, preventing the formation of kidney stones (PubMed:14679186).
CC Serum Ca(2+) and phosphate levels are normal, probably due to increased
CC expression of TRPV6 and increased Ca(2+) absorption in the intestine.
CC The increased expression of TRPV6 may be due to the increased serum
CC levels of 1,25-dihydroxy-vitamin D3 that are observed in mutant mice
CC (PubMed:14679186, PubMed:27102152). Age-related changes in trabecular
CC and cortical bone mass are accelerated in male mutant mice, including
CC reduced trabecular and cortical bone thickness. Still, this has no
CC effect on bone strength (PubMed:27102152).
CC {ECO:0000269|PubMed:14679186, ECO:0000269|PubMed:27102152}.
CC -!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family. TrpV
CC subfamily. TRPV5 sub-subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK085479; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF336378; AAM53408.1; -; Genomic_DNA.
DR EMBL; AK085479; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC110554; AAI10555.1; -; mRNA.
DR EMBL; BC110555; AAI10556.1; -; mRNA.
DR EMBL; CH466533; EDL13503.1; -; Genomic_DNA.
DR CCDS; CCDS20053.1; -.
DR RefSeq; NP_001007573.1; NM_001007572.2.
DR RefSeq; XP_017176952.1; XM_017321463.1.
DR AlphaFoldDB; P69744; -.
DR SMR; P69744; -.
DR BioGRID; 228781; 4.
DR CORUM; P69744; -.
DR IntAct; P69744; 2.
DR MINT; P69744; -.
DR STRING; 10090.ENSMUSP00000031901; -.
DR iPTMnet; P69744; -.
DR PhosphoSitePlus; P69744; -.
DR PaxDb; P69744; -.
DR PRIDE; P69744; -.
DR ProteomicsDB; 297527; -.
DR Antibodypedia; 32594; 296 antibodies from 35 providers.
DR DNASU; 194352; -.
DR Ensembl; ENSMUST00000031901; ENSMUSP00000031901; ENSMUSG00000036899.
DR GeneID; 194352; -.
DR KEGG; mmu:194352; -.
DR UCSC; uc009bqd.1; mouse.
DR CTD; 56302; -.
DR MGI; MGI:2429764; Trpv5.
DR VEuPathDB; HostDB:ENSMUSG00000036899; -.
DR eggNOG; KOG3676; Eukaryota.
DR GeneTree; ENSGT00940000161809; -.
DR HOGENOM; CLU_012795_2_0_1; -.
DR InParanoid; P69744; -.
DR OMA; SFKWRKY; -.
DR OrthoDB; 693004at2759; -.
DR PhylomeDB; P69744; -.
DR TreeFam; TF314711; -.
DR Reactome; R-MMU-3295583; TRP channels.
DR BioGRID-ORCS; 194352; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Trpv5; mouse.
DR PRO; PR:P69744; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P69744; protein.
DR Bgee; ENSMUSG00000036899; Expressed in right kidney and 33 other tissues.
DR ExpressionAtlas; P69744; baseline and differential.
DR GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR GO; GO:0034704; C:calcium channel complex; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; ISO:MGI.
DR GO; GO:0005262; F:calcium channel activity; IDA:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
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; IMP:UniProtKB.
DR GO; GO:0098703; P:calcium ion import across plasma membrane; ISS:UniProtKB.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IMP:UniProtKB.
DR GO; GO:0006816; P:calcium ion transport; IDA:UniProtKB.
DR GO; GO:0060402; P:calcium ion transport into cytosol; ISO:MGI.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; NAS:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR GO; GO:0035809; P:regulation of urine volume; IMP: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; IPR008346; TRPV5.
DR InterPro; IPR008344; TRPV5/TRPV6.
DR PANTHER; PTHR10582; PTHR10582; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR PRINTS; PR01415; ANKYRIN.
DR PRINTS; PR01765; ECACCHANNEL.
DR PRINTS; PR01767; ECACCHANNEL2.
DR SMART; SM00248; ANK; 4.
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 ANK repeat; Calcium; Calcium channel; Calcium transport;
KW Calmodulin-binding; Cell membrane; Ion channel; Ion transport; Membrane;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..723
FT /note="Transient receptor potential cation channel
FT subfamily V member 5"
FT /id="PRO_0000215351"
FT TOPO_DOM 1..320
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9XSM3"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9XSM3"
FT TOPO_DOM 342..378
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9XSM3"
FT TRANSMEM 379..401
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9XSM3"
FT TOPO_DOM 402..412
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9XSM3"
FT TRANSMEM 413..435
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9XSM3"
FT TOPO_DOM 436..441
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9XSM3"
FT TRANSMEM 442..462
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9XSM3"
FT TOPO_DOM 463..485
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9XSM3"
FT TRANSMEM 486..506
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9XSM3"
FT INTRAMEM 517..537
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:Q9XSM3"
FT TRANSMEM 550..570
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9XSM3"
FT TOPO_DOM 571..723
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9XSM3"
FT REPEAT 38..68
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 72..101
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 110..139
FT /note="ANK 3"
FT /evidence="ECO:0000255"
FT REPEAT 156..185
FT /note="ANK 4"
FT /evidence="ECO:0000255"
FT REPEAT 189..222
FT /note="ANK 5"
FT /evidence="ECO:0000255"
FT REPEAT 232..261
FT /note="ANK 6"
FT /evidence="ECO:0000255"
FT REGION 591..595
FT /note="Interaction with S100A10"
FT /evidence="ECO:0000269|PubMed:12660155"
FT REGION 643..646
FT /note="Involved in Ca(2+)-dependent inactivation"
FT /evidence="ECO:0000250"
FT REGION 651..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..723
FT /note="Involved in Ca(2+)-dependent inactivation"
FT /evidence="ECO:0000250"
FT COMPBIAS 657..673
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 535
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 678
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 682
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MUTAGEN 403..406
FT /note="VGAS->LGVT: Induces faster Ca(2+)-dependent channel
FT inactivation."
FT /evidence="ECO:0000269|PubMed:12077127"
FT MUTAGEN 593
FT /note="T->A: Abolishes interaction with S100A10, plasma
FT membrane localization and channel activity."
FT /evidence="ECO:0000269|PubMed:12660155"
FT CONFLICT 302
FT /note="E -> K (in Ref. 2; AK085479)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 723 AA; 82218 MW; 6668C67C47CBB443 CRC64;
MGAKTPWIQL QKLLNWWVRD QDWNQHVDQL HMLQQKSIWE SPLLRAAKEN DMCTLKKLQH
DQNCDFRQRG ALGETALHVA ALYDNLDAAI MLMEAAPYLV TESTLCEPFV GQTALHIAVM
NQNVNLVRAL LARGASASAR ATGSAFHRSS HNLIYYGEHP LSFAACVGSE EIVRLLIEHG
ADIRAQDSLG NTVLHILVLQ PNKTFACQMY NLLLSYDGGD HLKSLELVPN NQGLTPFKLA
GVEGNTVMFQ HLMQKRKRIQ WSFGPLTSSL YDLTEIDSWG EELSFLELVV SSKKKEARQI
LEQTPVKELV SLKWKKYGQP YFCLLGALYI FYMVCFTTCC VYRPLKFRDA NRTHVRDNTI
MEQKSLQEAY VTYQDKIRLV GELVTVIGAV IILLLEIPDI FRVGASRYFG QTVLGGPFHV
IIITYASLVL LTMAMRLTNV NGEVVPMSMA LVLGWCSVMY FARGFQMLGP FTIMIQKMIF
GDLLRFCWLM AMVILGFASA FYIIFQTEDP DNLGEFSDYP TAMFSTFELF LTIIDGPANY
RVDLPFMYSV TYATFAIIAT LLMLNLFIAM MGDTHWRVAQ ERDELWRAQV VATTVMLERK
MPRFLWPRSG ICGCEYGLGD RWFLRVEHHQ EQNPYRVLRY VEAFKSSDKE EVQEQLSEKQ
PSGTETGTLA RGSVVLQTPP LSRTTSLSSN SHRGWEILRR NTLGHLNLGL DPGEGDGEEI
YQF
