IPYR_HUMAN
ID IPYR_HUMAN Reviewed; 289 AA.
AC Q15181; Q2M348; Q5SQT7; Q6P7P4; Q9UQJ5; Q9Y5B1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Inorganic pyrophosphatase;
DE EC=3.6.1.1;
DE AltName: Full=Pyrophosphate phospho-hydrolase;
DE Short=PPase;
GN Name=PPA1; Synonyms=IOPPP, PP;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Heart;
RX PubMed=10542310; DOI=10.1016/s0167-4781(99)00175-x;
RA Fairchild T.A., Patejunas G.;
RT "Cloning and expression profile of human inorganic pyrophosphatase.";
RL Biochim. Biophys. Acta 1447:133-136(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Saito T., Hattori A., Miyajima N.;
RT "Putative inorganic pyrophosphatase.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kanni L., Johansson M., Karlsson A.;
RT "Cloning of a human inorganic pyrophosphatase cDNA.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Dai F.Y., Yu L., Hu P.R., Xin Y.R., Xu Y.F., Zhao S.Y.;
RT "Cloning and characterization of a novel human cDNA homology to bovine
RT inorganic pyrophosphatase mRNA.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Adrenal gland;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Lymph, and Uterus;
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-286.
RA Rumsfeld J., Ziegelbauer K., Spaltmann F.;
RT "Cloning, expression, affinity purification and characterization of
RT polyhistidine-tagged cytosolic Saccharomyces cerevisiae and human inorganic
RT pyrophosphatases for differential screening of compounds for antifungal
RT activity.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP PROTEIN SEQUENCE OF 10-18; 26-41; 58-70; 80-88; 110-128; 140-191; 193-221
RP AND 239-253, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 83-196.
RA Lacroix J., Vigneron M., Kedinger C.;
RT "Partial sequence of the human inorganic pyrophosphatase.";
RL Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-57 AND LYS-228, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP VARIANT [LARGE SCALE ANALYSIS] ASN-57.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphosphate + H2O = H(+) + 2 phosphate; Xref=Rhea:RHEA:24576,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:43474; EC=3.6.1.1;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously.
CC {ECO:0000269|PubMed:10542310}.
CC -!- SIMILARITY: Belongs to the PPase family. {ECO:0000305}.
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DR EMBL; AF154065; AAD34643.1; -; mRNA.
DR EMBL; AB026723; BAA84702.1; -; mRNA.
DR EMBL; AF217186; AAG36780.1; -; mRNA.
DR EMBL; AF092439; AAP97214.1; -; mRNA.
DR EMBL; AF119665; AAF17222.1; -; mRNA.
DR EMBL; AL731540; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001022; AAH01022.3; -; mRNA.
DR EMBL; BC061581; AAH61581.2; -; mRNA.
DR EMBL; BC105034; AAI05035.1; -; mRNA.
DR EMBL; BC105036; AAI05037.1; -; mRNA.
DR EMBL; BC107882; AAI07883.1; -; mRNA.
DR EMBL; AF108211; AAD24964.1; -; mRNA.
DR EMBL; Z48605; CAA88494.1; -; mRNA.
DR CCDS; CCDS7299.1; -.
DR RefSeq; NP_066952.1; NM_021129.3.
DR PDB; 6C45; X-ray; 2.39 A; A/B/C/D=1-289.
DR PDB; 7BTN; X-ray; 2.38 A; A=1-289.
DR PDB; 7CMO; X-ray; 3.40 A; A/B/C/D=1-289.
DR PDBsum; 6C45; -.
DR PDBsum; 7BTN; -.
DR PDBsum; 7CMO; -.
DR AlphaFoldDB; Q15181; -.
DR SMR; Q15181; -.
DR BioGRID; 111460; 124.
DR IntAct; Q15181; 29.
DR MINT; Q15181; -.
DR STRING; 9606.ENSP00000362329; -.
DR GlyGen; Q15181; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q15181; -.
DR MetOSite; Q15181; -.
DR PhosphoSitePlus; Q15181; -.
DR SwissPalm; Q15181; -.
DR BioMuta; PPA1; -.
DR DMDM; 8247940; -.
DR REPRODUCTION-2DPAGE; IPI00015018; -.
DR EPD; Q15181; -.
DR jPOST; Q15181; -.
DR MassIVE; Q15181; -.
DR PaxDb; Q15181; -.
DR PeptideAtlas; Q15181; -.
DR PRIDE; Q15181; -.
DR ProteomicsDB; 60485; -.
DR TopDownProteomics; Q15181; -.
DR Antibodypedia; 14866; 255 antibodies from 32 providers.
DR DNASU; 5464; -.
DR Ensembl; ENST00000373232.8; ENSP00000362329.2; ENSG00000180817.12.
DR GeneID; 5464; -.
DR KEGG; hsa:5464; -.
DR MANE-Select; ENST00000373232.8; ENSP00000362329.2; NM_021129.4; NP_066952.1.
DR CTD; 5464; -.
DR DisGeNET; 5464; -.
DR GeneCards; PPA1; -.
DR HGNC; HGNC:9226; PPA1.
DR HPA; ENSG00000180817; Low tissue specificity.
DR MIM; 179030; gene.
DR neXtProt; NX_Q15181; -.
DR OpenTargets; ENSG00000180817; -.
DR PharmGKB; PA33550; -.
DR VEuPathDB; HostDB:ENSG00000180817; -.
DR eggNOG; KOG1626; Eukaryota.
DR GeneTree; ENSGT00390000017004; -.
DR HOGENOM; CLU_040684_0_2_1; -.
DR InParanoid; Q15181; -.
DR OMA; TLEHRIF; -.
DR OrthoDB; 1398991at2759; -.
DR PhylomeDB; Q15181; -.
DR TreeFam; TF300887; -.
DR BRENDA; 3.6.1.1; 2681.
DR PathwayCommons; Q15181; -.
DR Reactome; R-HSA-379716; Cytosolic tRNA aminoacylation.
DR Reactome; R-HSA-71737; Pyrophosphate hydrolysis.
DR SignaLink; Q15181; -.
DR BioGRID-ORCS; 5464; 582 hits in 1044 CRISPR screens.
DR ChiTaRS; PPA1; human.
DR GenomeRNAi; 5464; -.
DR Pharos; Q15181; Tbio.
DR PRO; PR:Q15181; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q15181; protein.
DR Bgee; ENSG00000180817; Expressed in cerebellar vermis and 205 other tissues.
DR ExpressionAtlas; Q15181; baseline and differential.
DR Genevisible; Q15181; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0004427; F:inorganic diphosphatase activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR GO; GO:0006796; P:phosphate-containing compound metabolic process; IBA:GO_Central.
DR CDD; cd00412; pyrophosphatase; 1.
DR Gene3D; 3.90.80.10; -; 1.
DR InterPro; IPR008162; Pyrophosphatase.
DR InterPro; IPR036649; Pyrophosphatase_sf.
DR PANTHER; PTHR10286; PTHR10286; 1.
DR Pfam; PF00719; Pyrophosphatase; 1.
DR SUPFAM; SSF50324; SSF50324; 1.
DR PROSITE; PS00387; PPASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Hydrolase;
KW Magnesium; Metal-binding; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..289
FT /note="Inorganic pyrophosphatase"
FT /id="PRO_0000137567"
FT BINDING 116
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 57
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 228
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT VARIANT 57
FT /note="K -> N (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036358"
FT CONFLICT 12
FT /note="P -> A (in Ref. 8; AAD24964)"
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="L -> I (in Ref. 10; CAA88494)"
FT /evidence="ECO:0000305"
FT CONFLICT 96..97
FT /note="AI -> TL (in Ref. 10; CAA88494)"
FT /evidence="ECO:0000305"
FT CONFLICT 105..114
FT /note="GHNDKHTGCC -> HEKDKSTNCF (in Ref. 10; CAA88494)"
FT /evidence="ECO:0000305"
FT CONFLICT 129..140
FT /note="VCARGEIIGVKV -> ILSCGEVIHVKI (in Ref. 10; CAA88494)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="M -> L (in Ref. 10; CAA88494)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="V -> L (in Ref. 10; CAA88494)"
FT /evidence="ECO:0000305"
FT CONFLICT 161..162
FT /note="VD -> AN (in Ref. 10; CAA88494)"
FT /evidence="ECO:0000305"
FT CONFLICT 165..173
FT /note="DAANYNDIN -> EASKFHDID (in Ref. 10; CAA88494)"
FT /evidence="ECO:0000305"
FT CONFLICT 177..178
FT /note="RL -> KF (in Ref. 10; CAA88494)"
FT /evidence="ECO:0000305"
FT CONFLICT 187..188
FT /note="VD -> LN (in Ref. 10; CAA88494)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="R -> L (in Ref. 10; CAA88494)"
FT /evidence="ECO:0000305"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:7BTN"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:7BTN"
FT STRAND 18..22
FT /evidence="ECO:0007829|PDB:7BTN"
FT TURN 31..34
FT /evidence="ECO:0007829|PDB:7BTN"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:7BTN"
FT STRAND 43..50
FT /evidence="ECO:0007829|PDB:7BTN"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:7BTN"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:7BTN"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:7BTN"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:6C45"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:7BTN"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:7BTN"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:6C45"
FT STRAND 135..148
FT /evidence="ECO:0007829|PDB:7BTN"
FT STRAND 151..160
FT /evidence="ECO:0007829|PDB:7BTN"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:7BTN"
FT HELIX 172..178
FT /evidence="ECO:0007829|PDB:7BTN"
FT HELIX 182..194
FT /evidence="ECO:0007829|PDB:7BTN"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:6C45"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:7BTN"
FT STRAND 206..211
FT /evidence="ECO:0007829|PDB:7BTN"
FT HELIX 213..231
FT /evidence="ECO:0007829|PDB:7BTN"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:7BTN"
FT HELIX 256..264
FT /evidence="ECO:0007829|PDB:7BTN"
FT HELIX 278..281
FT /evidence="ECO:0007829|PDB:7BTN"
SQ SEQUENCE 289 AA; 32660 MW; E3973C9E6F8CA5CD CRC64;
MSGFSTEERA APFSLEYRVF LKNEKGQYIS PFHDIPIYAD KDVFHMVVEV PRWSNAKMEI
ATKDPLNPIK QDVKKGKLRY VANLFPYKGY IWNYGAIPQT WEDPGHNDKH TGCCGDNDPI
DVCEIGSKVC ARGEIIGVKV LGILAMIDEG ETDWKVIAIN VDDPDAANYN DINDVKRLKP
GYLEATVDWF RRYKVPDGKP ENEFAFNAEF KDKDFAIDII KSTHDHWKAL VTKKTNGKGI
SCMNTTLSES PFKCDPDAAR AIVDALPPPC ESACTVPTDV DKWFHHQKN
