TRPV5_HUMAN
ID TRPV5_HUMAN Reviewed; 729 AA.
AC Q9NQA5; A4D2H7; E9PBZ6; Q8N4C1; Q8NDW5; Q8NDX7; Q8NDX8; Q96PM6;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 180.
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 {ECO:0000303|PubMed:10945469};
DE Short=ECaC;
DE Short=ECaC1;
DE AltName: Full=Osm-9-like TRP channel 3;
DE Short=OTRPC3;
GN Name=TRPV5; Synonyms=ECAC1 {ECO:0000303|PubMed:10945469};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=10945469; DOI=10.1006/geno.2000.6203;
RA Mueller D., Hoenderop J.G., Meij I.C., van den Heuvel L.P.J., Knoers N.V.,
RA den Hollander A.I., Eggert P., Garcia-Nieto V., Claverie-Martin F.,
RA Bindels R.J.M.;
RT "Molecular cloning, tissue distribution, and chromosomal mapping of the
RT human epithelial calcium channel (ECAC1).";
RL Genomics 67:48-53(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11549322; DOI=10.1006/geno.2001.6606;
RA Peng J.-B., Brown E.M., Hediger M.A.;
RT "Structural conservation of the genes encoding CaT1, CaT2, and related
RT cation channels.";
RL Genomics 76:99-109(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT HIS-154.
RA Kelsell R.E.;
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-8; HIS-154; THR-563 AND
RP PHE-712.
RG SeattleSNPs variation discovery resource;
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT HIS-154.
RC TISSUE=Colon;
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 [9]
RP FUNCTION, GLYCOSYLATION AT ASN-358, SUBCELLULAR LOCATION, ACTIVITY
RP REGULATION, AND MUTAGENESIS OF ASN-358.
RX PubMed=18768590; DOI=10.1152/ajprenal.90229.2008;
RA Zhang W., Na T., Peng J.B.;
RT "WNK3 positively regulates epithelial calcium channels TRPV5 and TRPV6 via
RT a kinase-dependent pathway.";
RL Am. J. Physiol. 295:F1472-F1484(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
CC -!- FUNCTION: Constitutively active calcium selective cation channel
CC thought to be involved in Ca(2+) reabsorption in kidney and intestine
CC (PubMed:11549322, PubMed:18768590). Required for normal Ca(2+)
CC reabsorption in the kidney distal convoluted tubules (By similarity).
CC The channel is activated by low internal calcium level and the current
CC exhibits an inward rectification (PubMed:11549322, PubMed:18768590). A
CC Ca(2+)-dependent feedback regulation includes fast channel inactivation
CC and slow current decay (By similarity). Heteromeric assembly with TRPV6
CC seems to modify channel properties. TRPV5-TRPV6 heteromultimeric
CC concatemers exhibit voltage-dependent gating (By similarity).
CC {ECO:0000250|UniProtKB:P69744, ECO:0000250|UniProtKB:Q9XSM3,
CC ECO:0000269|PubMed:11549322, ECO:0000269|PubMed:18768590}.
CC -!- ACTIVITY REGULATION: Activated by WNK3. {ECO:0000269|PubMed:18768590}.
CC -!- SUBUNIT: Homotetramer and probably heterotetramer with TRPV6. Interacts
CC with TRPV6 (By similarity). 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. Interacts with
CC calmodulin. Interacts with BSPRY, which results in its inactivation.
CC {ECO:0000250|UniProtKB:P69744, ECO:0000250|UniProtKB:Q9XSM3}.
CC -!- INTERACTION:
CC Q9NQA5; P05937: CALB1; NbExp=4; IntAct=EBI-751281, EBI-4286943;
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:18768590}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:18768590}. Note=Colocalized with S100A10 and ANAX2
CC along the apical domain of kidney distal tubular cells (By similarity).
CC The expression of the glycosylated form in the cell membrane is
CC increased in the presence of WNK3 (PubMed:18768590).
CC {ECO:0000250|UniProtKB:P69744, ECO:0000269|PubMed:18768590}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NQA5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NQA5-2; Sequence=VSP_057199, VSP_057200;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in kidney, small intestine
CC and pancreas, and at lower levels in testis, prostate, placenta, brain,
CC colon and rectum. {ECO:0000269|PubMed:10945469,
CC ECO:0000269|PubMed:11549322}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:18768590}.
CC -!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family. TrpV
CC subfamily. TRPV5 sub-subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/trpv5/";
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DR EMBL; AJ271207; CAB96365.2; -; mRNA.
DR EMBL; AF304464; AAL04015.1; -; mRNA.
DR EMBL; AJ487965; CAD32312.2; -; mRNA.
DR EMBL; AY206695; AAO13488.1; -; Genomic_DNA.
DR EMBL; AC245427; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236959; EAL23777.1; -; Genomic_DNA.
DR EMBL; CH471198; EAW51896.1; -; Genomic_DNA.
DR EMBL; BC034740; AAH34740.1; -; mRNA.
DR CCDS; CCDS5875.1; -. [Q9NQA5-1]
DR RefSeq; NP_062815.3; NM_019841.6.
DR PDB; 5OEO; NMR; -; C=655-725.
DR PDBsum; 5OEO; -.
DR AlphaFoldDB; Q9NQA5; -.
DR BMRB; Q9NQA5; -.
DR SMR; Q9NQA5; -.
DR BioGRID; 121137; 29.
DR IntAct; Q9NQA5; 13.
DR MINT; Q9NQA5; -.
DR STRING; 9606.ENSP00000265310; -.
DR BindingDB; Q9NQA5; -.
DR ChEMBL; CHEMBL1628474; -.
DR DrugBank; DB11093; Calcium citrate.
DR DrugBank; DB11348; Calcium Phosphate.
DR DrugBank; DB14481; Calcium phosphate dihydrate.
DR GuidetoPHARMACOLOGY; 511; -.
DR TCDB; 1.A.4.2.10; the transient receptor potential ca(2+) channel (trp-cc) family.
DR GlyGen; Q9NQA5; 1 site.
DR iPTMnet; Q9NQA5; -.
DR PhosphoSitePlus; Q9NQA5; -.
DR SwissPalm; Q9NQA5; -.
DR BioMuta; TRPV5; -.
DR DMDM; 62901471; -.
DR EPD; Q9NQA5; -.
DR MassIVE; Q9NQA5; -.
DR MaxQB; Q9NQA5; -.
DR PaxDb; Q9NQA5; -.
DR PeptideAtlas; Q9NQA5; -.
DR PRIDE; Q9NQA5; -.
DR ProteomicsDB; 19327; -.
DR ProteomicsDB; 82119; -. [Q9NQA5-1]
DR Antibodypedia; 32594; 296 antibodies from 35 providers.
DR DNASU; 56302; -.
DR Ensembl; ENST00000442623.1; ENSP00000406572.1; ENSG00000127412.7.
DR GeneID; 56302; -.
DR KEGG; hsa:56302; -.
DR UCSC; uc003wbz.3; human. [Q9NQA5-1]
DR CTD; 56302; -.
DR DisGeNET; 56302; -.
DR GeneCards; TRPV5; -.
DR HGNC; HGNC:3145; TRPV5.
DR HPA; ENSG00000127412; Tissue enriched (kidney).
DR MIM; 606679; gene.
DR neXtProt; NX_Q9NQA5; -.
DR PharmGKB; PA35045; -.
DR VEuPathDB; HostDB:ENSG00000127412; -.
DR eggNOG; KOG3676; Eukaryota.
DR HOGENOM; CLU_062553_0_0_1; -.
DR InParanoid; Q9NQA5; -.
DR OrthoDB; 693004at2759; -.
DR PhylomeDB; Q9NQA5; -.
DR TreeFam; TF314711; -.
DR PathwayCommons; Q9NQA5; -.
DR Reactome; R-HSA-3295583; TRP channels.
DR SignaLink; Q9NQA5; -.
DR SIGNOR; Q9NQA5; -.
DR BioGRID-ORCS; 56302; 11 hits in 1060 CRISPR screens.
DR GeneWiki; TRPV5; -.
DR GenomeRNAi; 56302; -.
DR Pharos; Q9NQA5; Tchem.
DR PRO; PR:Q9NQA5; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9NQA5; protein.
DR Bgee; ENSG00000127412; Expressed in C1 segment of cervical spinal cord and 29 other tissues.
DR ExpressionAtlas; Q9NQA5; baseline and differential.
DR Genevisible; Q9NQA5; HS.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
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; ISS:UniProtKB.
DR GO; GO:0098703; P:calcium ion import across plasma membrane; IDA:UniProtKB.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IDA:UniProtKB.
DR GO; GO:0006816; P:calcium ion transport; ISS:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR GO; GO:0035809; P:regulation of urine volume; ISS:UniProtKB.
DR DisProt; DP01765; -.
DR Gene3D; 1.25.40.20; -; 2.
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; PF00023; Ank; 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; 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; Alternative splicing; ANK repeat; Calcium; Calcium channel;
KW Calcium transport; Calmodulin-binding; Cell membrane; Glycoprotein;
KW Ion channel; Ion transport; Membrane; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..729
FT /note="Transient receptor potential cation channel
FT subfamily V member 5"
FT /id="PRO_0000215350"
FT TOPO_DOM 1..327
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9XSM3"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9XSM3"
FT TOPO_DOM 349..385
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9XSM3"
FT TRANSMEM 386..408
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9XSM3"
FT TOPO_DOM 409..419
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9XSM3"
FT TRANSMEM 420..442
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9XSM3"
FT TOPO_DOM 443..448
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9XSM3"
FT TRANSMEM 449..469
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9XSM3"
FT TOPO_DOM 470..492
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9XSM3"
FT TRANSMEM 493..513
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9XSM3"
FT INTRAMEM 524..544
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:Q9XSM3"
FT TRANSMEM 557..577
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9XSM3"
FT TOPO_DOM 578..729
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9XSM3"
FT REPEAT 44..74
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 78..107
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 116..145
FT /note="ANK 3"
FT /evidence="ECO:0000255"
FT REPEAT 162..191
FT /note="ANK 4"
FT /evidence="ECO:0000255"
FT REPEAT 195..228
FT /note="ANK 5"
FT /evidence="ECO:0000255"
FT REPEAT 239..268
FT /note="ANK 6"
FT /evidence="ECO:0000255"
FT REGION 598..602
FT /note="Interaction with S100A10"
FT /evidence="ECO:0000250|UniProtKB:P69744"
FT REGION 650..653
FT /note="Involved in Ca(2+)-dependent inactivation"
FT /evidence="ECO:0000250"
FT REGION 654..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 700..729
FT /note="Involved in Ca(2+)-dependent inactivation"
FT /evidence="ECO:0000250"
FT BINDING 542
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 685
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P69744"
FT MOD_RES 689
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P69744"
FT CARBOHYD 358
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:18768590"
FT VAR_SEQ 375..381
FT /note="EAYETRE -> VILLRRG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_057199"
FT VAR_SEQ 382..729
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_057200"
FT VARIANT 8
FT /note="A -> V (in dbSNP:rs4252372)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_022247"
FT VARIANT 154
FT /note="R -> H (in dbSNP:rs4236480)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3,
FT ECO:0000269|Ref.4"
FT /id="VAR_022248"
FT VARIANT 563
FT /note="A -> T (in dbSNP:rs4252499)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_022249"
FT VARIANT 712
FT /note="L -> F (in dbSNP:rs4252509)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_022250"
FT MUTAGEN 358
FT /note="N->Q: Loss of glycosylation."
FT /evidence="ECO:0000269|PubMed:18768590"
FT HELIX 699..709
FT /evidence="ECO:0007829|PDB:5OEO"
FT STRAND 719..722
FT /evidence="ECO:0007829|PDB:5OEO"
SQ SEQUENCE 729 AA; 82551 MW; A10FB80205FD0DBB CRC64;
MGGFLPKAEG PGSQLQKLLP SFLVREQDWD QHLDKLHMLQ QKRILESPLL RASKENDLSV
LRQLLLDCTC DVRQRGALGE TALHIAALYD NLEAALVLME AAPELVFEPT TCEAFAGQTA
LHIAVVNQNV NLVRALLTRR ASVSARATGT AFRRSPRNLI YFGEHPLSFA ACVNSEEIVR
LLIEHGADIR AQDSLGNTVL HILILQPNKT FACQMYNLLL SYDGHGDHLQ PLDLVPNHQG
LTPFKLAGVE GNTVMFQHLM QKRRHIQWTY GPLTSILYDL TEIDSWGEEL SFLELVVSSD
KREARQILEQ TPVKELVSFK WNKYGRPYFC ILAALYLLYM ICFTTCCVYR PLKFRGGNRT
HSRDITILQQ KLLQEAYETR EDIIRLVGEL VSIVGAVIIL LLEIPDIFRV GASRYFGKTI
LGGPFHVIII TYASLVLVTM VMRLTNTNGE VVPMSFALVL GWCSVMYFTR GFQMLGPFTI
MIQKMIFGDL MRFCWLMAVV ILGFASAFYI IFQTEDPTSL GQFYDYPMAL FTTFELFLTV
IDAPANYDVD LPFMFSIVNF AFAIIATLLM LNLFIAMMGD THWRVAQERD ELWRAQVVAT
TVMLERKLPR CLWPRSGICG CEFGLGDRWF LRVENHNDQN PLRVLRYVEV FKNSDKEDDQ
EHPSEKQPSG AESGTLARAS LALPTSSLSR TASQSSSHRG WEILRQNTLG HLNLGLNLSE
GDGEEVYHF
