ENTP4_HUMAN
ID ENTP4_HUMAN Reviewed; 616 AA.
AC Q9Y227; D3DSS3; O15092;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Ectonucleoside triphosphate diphosphohydrolase 4;
DE Short=NTPDase 4;
DE EC=3.6.1.15 {ECO:0000269|PubMed:10858452, ECO:0000269|PubMed:9556635};
DE EC=3.6.1.6 {ECO:0000269|PubMed:10858452, ECO:0000269|PubMed:9556635};
DE AltName: Full=Golgi UDPase {ECO:0000303|PubMed:9556635};
DE AltName: Full=Lysosomal apyrase-like protein of 70 kDa {ECO:0000303|PubMed:10393803};
DE AltName: Full=Uridine-diphosphatase {ECO:0000303|PubMed:9556635};
DE Short=UDPase {ECO:0000303|PubMed:9556635};
DE EC=3.6.1.42 {ECO:0000269|PubMed:10858452, ECO:0000269|PubMed:9556635};
GN Name=ENTPD4 {ECO:0000312|HGNC:HGNC:14573};
GN Synonyms=KIAA0392, LALP70 {ECO:0000303|PubMed:10858452}, LYSAL1;
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 2), CATALYTIC ACTIVITY, COFACTOR,
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND SUBSTRATE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9556635; DOI=10.1074/jbc.273.18.11392;
RA Wang T.-F., Guidotti G.;
RT "Golgi localization and functional expression of human uridine
RT diphosphatase.";
RL J. Biol. Chem. 273:11392-11399(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Pancreatic adenocarcinoma;
RX PubMed=10393803; DOI=10.1242/jcs.112.15.2473;
RA Biederbick A., Rose S., Elsaesser H.-P.;
RT "A human intracellular apyrase-like protein, LALP70, localizes to
RT lysosomal/autophagic vacuoles.";
RL J. Cell Sci. 112:2473-2484(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), ALTERNATIVE SPLICING,
RP CATALYTIC ACTIVITY, FUNCTION, AND COFACTOR.
RX PubMed=10858452; DOI=10.1074/jbc.m001245200;
RA Biederbick A., Kosan C., Kunz J., Elsaesser H.-P.;
RT "First apyrase splice variants have different enzymatic properties.";
RL J. Biol. Chem. 275:19018-19024(2000).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 59-616 (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [7]
RP VARIANT VAL-341.
RX PubMed=21248752; DOI=10.1038/nature09639;
RA Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H.,
RA Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J.,
RA Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M.,
RA Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L.,
RA Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J.,
RA Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A.,
RA Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K.,
RA Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.;
RT "Exome sequencing identifies frequent mutation of the SWI/SNF complex gene
RT PBRM1 in renal carcinoma.";
RL Nature 469:539-542(2011).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 58-559, DISULFIDE BOND, AND
RP GLYCOSYLATION AT ASN-404 AND ASN-407.
RX PubMed=32767432; DOI=10.1002/pro.3926;
RA Gorelik A., Labriola J.M., Illes K., Nagar B.;
RT "Crystal structure of the nucleotide-metabolizing enzyme NTPDase4.";
RL Protein Sci. 29:2054-2061(2020).
CC -!- FUNCTION: [Isoform 1]: Catalyzes the hydrolysis of nucleoside
CC triphosphates and diphosphates in a calcium- or magnesium-dependent
CC manner, with a preference for pyrimidines. Preferentially hydrolyzes
CC UTP and TTP. AMP, ADP, ATP and UMP are not substrates (PubMed:10858452,
CC PubMed:9556635). Preferentially activated by Ca(2+) over Mg(2+)
CC (PubMed:10858452). {ECO:0000269|PubMed:10858452,
CC ECO:0000269|PubMed:9556635}.
CC -!- FUNCTION: [Isoform 2]: Has a broad substrate specificity with the
CC ability of cleaving all nucleotide di- and triphosphates with the
CC exception of adenosine di- and triphosphate (ADP and ATP).
CC Preferentially hydrolyzes CTP, UDP, CDP, GTP and GDP. Can use either
CC Ca(2+) or Mg(2+) equally. {ECO:0000269|PubMed:10858452,
CC ECO:0000269|PubMed:9556635}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-diphosphate + H2O = a ribonucleoside 5'-
CC phosphate + H(+) + phosphate; Xref=Rhea:RHEA:36799,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:58043; EC=3.6.1.6;
CC Evidence={ECO:0000269|PubMed:10858452, ECO:0000269|PubMed:9556635};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36800;
CC Evidence={ECO:0000305|PubMed:10858452};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC Evidence={ECO:0000269|PubMed:10858452, ECO:0000269|PubMed:9556635};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23681;
CC Evidence={ECO:0000269|PubMed:10858452, ECO:0000269|PubMed:9556635};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + UDP = H(+) + phosphate + UMP; Xref=Rhea:RHEA:64876,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57865, ChEBI:CHEBI:58223; EC=3.6.1.6;
CC Evidence={ECO:0000269|PubMed:10858452, ECO:0000269|PubMed:9556635};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64877;
CC Evidence={ECO:0000305|PubMed:10858452};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + UTP = H(+) + phosphate + UDP; Xref=Rhea:RHEA:64900,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:46398, ChEBI:CHEBI:58223;
CC Evidence={ECO:0000269|PubMed:10858452};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CTP + H2O = CDP + H(+) + phosphate; Xref=Rhea:RHEA:29387,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37563,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58069;
CC Evidence={ECO:0000269|PubMed:10858452, ECO:0000269|PubMed:9556635};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29388;
CC Evidence={ECO:0000305|PubMed:10858452};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP + H2O = GMP + H(+) + phosphate; Xref=Rhea:RHEA:22156,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58115, ChEBI:CHEBI:58189; EC=3.6.1.42;
CC Evidence={ECO:0000269|PubMed:10858452, ECO:0000269|PubMed:9556635};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000269|PubMed:10858452};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000305|PubMed:10858452};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + TTP = H(+) + phosphate + TDP; Xref=Rhea:RHEA:65580,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61417, ChEBI:CHEBI:63527;
CC Evidence={ECO:0000269|PubMed:10858452};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65581;
CC Evidence={ECO:0000305};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:10858452, ECO:0000269|PubMed:9556635};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:10858452, ECO:0000269|PubMed:9556635};
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasmic vesicle, autophagosome
CC membrane {ECO:0000269|PubMed:10393803}; Multi-pass membrane protein
CC {ECO:0000305}. Lysosome membrane {ECO:0000269|PubMed:10393803}; Multi-
CC pass membrane protein.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Golgi apparatus membrane
CC {ECO:0000269|PubMed:9556635}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=LALP70 {ECO:0000303|PubMed:10393803};
CC IsoId=Q9Y227-1; Sequence=Displayed;
CC Name=2; Synonyms=LALP70V {ECO:0000303|PubMed:10858452};
CC IsoId=Q9Y227-2; Sequence=VSP_003614;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highest expression in testis and lowest
CC in bladder. {ECO:0000269|PubMed:10393803, ECO:0000269|PubMed:9556635}.
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family. {ECO:0000305}.
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DR EMBL; AF016032; AAC17217.1; -; mRNA.
DR EMBL; AJ131358; CAB40415.1; -; mRNA.
DR EMBL; AJ246165; CAB45655.1; -; Genomic_DNA.
DR EMBL; AJ246166; CAB45655.1; JOINED; Genomic_DNA.
DR EMBL; AJ246167; CAB45655.1; JOINED; Genomic_DNA.
DR EMBL; AJ246168; CAB45655.1; JOINED; Genomic_DNA.
DR EMBL; AJ246169; CAB45655.1; JOINED; Genomic_DNA.
DR EMBL; AJ246170; CAB45655.1; JOINED; Genomic_DNA.
DR EMBL; AJ246171; CAB45655.1; JOINED; Genomic_DNA.
DR EMBL; AJ246172; CAB45655.1; JOINED; Genomic_DNA.
DR EMBL; AJ246173; CAB45655.1; JOINED; Genomic_DNA.
DR EMBL; AJ246174; CAB45655.1; JOINED; Genomic_DNA.
DR EMBL; AJ246175; CAB45655.1; JOINED; Genomic_DNA.
DR EMBL; AJ246176; CAB45655.1; JOINED; Genomic_DNA.
DR EMBL; CH471080; EAW63622.1; -; Genomic_DNA.
DR EMBL; CH471080; EAW63623.1; -; Genomic_DNA.
DR EMBL; AB002390; BAA21575.1; -; mRNA.
DR CCDS; CCDS47827.1; -. [Q9Y227-2]
DR CCDS; CCDS6041.1; -. [Q9Y227-1]
DR RefSeq; NP_001122402.1; NM_001128930.2. [Q9Y227-2]
DR RefSeq; NP_004892.1; NM_004901.4. [Q9Y227-1]
DR PDB; 6WG5; X-ray; 2.60 A; A=58-559.
DR PDBsum; 6WG5; -.
DR AlphaFoldDB; Q9Y227; -.
DR SMR; Q9Y227; -.
DR BioGRID; 114951; 22.
DR IntAct; Q9Y227; 11.
DR STRING; 9606.ENSP00000351520; -.
DR ChEMBL; CHEMBL3313834; -.
DR GlyGen; Q9Y227; 4 sites, 2 O-linked glycans (2 sites).
DR iPTMnet; Q9Y227; -.
DR PhosphoSitePlus; Q9Y227; -.
DR SwissPalm; Q9Y227; -.
DR BioMuta; ENTPD4; -.
DR DMDM; 18203627; -.
DR EPD; Q9Y227; -.
DR jPOST; Q9Y227; -.
DR MassIVE; Q9Y227; -.
DR MaxQB; Q9Y227; -.
DR PaxDb; Q9Y227; -.
DR PeptideAtlas; Q9Y227; -.
DR PRIDE; Q9Y227; -.
DR ProteomicsDB; 85614; -. [Q9Y227-1]
DR ProteomicsDB; 85615; -. [Q9Y227-2]
DR Antibodypedia; 2720; 128 antibodies from 19 providers.
DR DNASU; 9583; -.
DR Ensembl; ENST00000358689.9; ENSP00000351520.4; ENSG00000197217.13. [Q9Y227-1]
DR Ensembl; ENST00000417069.6; ENSP00000408573.2; ENSG00000197217.13. [Q9Y227-2]
DR GeneID; 9583; -.
DR KEGG; hsa:9583; -.
DR MANE-Select; ENST00000358689.9; ENSP00000351520.4; NM_004901.5; NP_004892.1.
DR UCSC; uc003xdl.4; human. [Q9Y227-1]
DR CTD; 9583; -.
DR DisGeNET; 9583; -.
DR GeneCards; ENTPD4; -.
DR HGNC; HGNC:14573; ENTPD4.
DR HPA; ENSG00000197217; Low tissue specificity.
DR MIM; 607577; gene.
DR neXtProt; NX_Q9Y227; -.
DR OpenTargets; ENSG00000197217; -.
DR PharmGKB; PA30502; -.
DR VEuPathDB; HostDB:ENSG00000197217; -.
DR eggNOG; KOG1386; Eukaryota.
DR GeneTree; ENSGT01050000244974; -.
DR HOGENOM; CLU_010246_6_0_1; -.
DR InParanoid; Q9Y227; -.
DR OMA; QDEIGPP; -.
DR OrthoDB; 1337265at2759; -.
DR PhylomeDB; Q9Y227; -.
DR TreeFam; TF354343; -.
DR BioCyc; MetaCyc:HS09501-MON; -.
DR PathwayCommons; Q9Y227; -.
DR Reactome; R-HSA-8850843; Phosphate bond hydrolysis by NTPDase proteins.
DR SignaLink; Q9Y227; -.
DR BioGRID-ORCS; 9583; 8 hits in 1078 CRISPR screens.
DR ChiTaRS; ENTPD4; human.
DR GenomeRNAi; 9583; -.
DR Pharos; Q9Y227; Tbio.
DR PRO; PR:Q9Y227; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q9Y227; protein.
DR Bgee; ENSG00000197217; Expressed in Brodmann (1909) area 23 and 197 other tissues.
DR ExpressionAtlas; Q9Y227; baseline and differential.
DR Genevisible; Q9Y227; HS.
DR GO; GO:0000421; C:autophagosome membrane; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0097637; C:integral component of autophagosome membrane; IDA:ParkinsonsUK-UCL.
DR GO; GO:0030173; C:integral component of Golgi membrane; IDA:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0043273; F:CTPase activity; IDA:UniProtKB.
DR GO; GO:0036384; F:cytidine-diphosphatase activity; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IEA:RHEA.
DR GO; GO:0004382; F:guanosine-diphosphatase activity; IDA:UniProtKB.
DR GO; GO:0017110; F:nucleoside-diphosphatase activity; IDA:UniProtKB.
DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IDA:UniProtKB.
DR GO; GO:0045134; F:uridine-diphosphatase activity; IDA:UniProtKB.
DR GO; GO:0046036; P:CTP metabolic process; IDA:UniProtKB.
DR GO; GO:0046712; P:GDP catabolic process; IDA:UniProtKB.
DR GO; GO:0034656; P:nucleobase-containing small molecule catabolic process; IDA:UniProtKB.
DR GO; GO:0009134; P:nucleoside diphosphate catabolic process; IBA:GO_Central.
DR GO; GO:0006256; P:UDP catabolic process; IDA:UniProtKB.
DR InterPro; IPR000407; GDA1_CD39_NTPase.
DR PANTHER; PTHR11782; PTHR11782; 1.
DR Pfam; PF01150; GDA1_CD39; 1.
DR PROSITE; PS01238; GDA1_CD39_NTPASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Cytoplasmic vesicle;
KW Disulfide bond; Glycoprotein; Golgi apparatus; Hydrolase; Lysosome;
KW Magnesium; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..616
FT /note="Ectonucleoside triphosphate diphosphohydrolase 4"
FT /id="PRO_0000209911"
FT TOPO_DOM 1..33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..559
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:10393803,
FT ECO:0000305|PubMed:9556635"
FT TRANSMEM 560..580
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 581..616
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 222
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:O35795"
FT CARBOHYD 404
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:32767432"
FT CARBOHYD 407
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:32767432"
FT DISULFID 368..395
FT /evidence="ECO:0000269|PubMed:32767432"
FT DISULFID 461..490
FT /evidence="ECO:0000269|PubMed:32767432"
FT VAR_SEQ 287..294
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9205841,
FT ECO:0000303|PubMed:9556635"
FT /id="VSP_003614"
FT VARIANT 341
FT /note="I -> V (found in a renal cell carcinoma case;
FT somatic mutation; dbSNP:rs549468877)"
FT /evidence="ECO:0000269|PubMed:21248752"
FT /id="VAR_064711"
FT VARIANT 354
FT /note="K -> E (in dbSNP:rs2272641)"
FT /id="VAR_020444"
FT CONFLICT 43
FT /note="A -> AA (in Ref. 1; AAC17217)"
FT /evidence="ECO:0000305"
FT HELIX 65..75
FT /evidence="ECO:0007829|PDB:6WG5"
FT STRAND 87..95
FT /evidence="ECO:0007829|PDB:6WG5"
FT STRAND 100..108
FT /evidence="ECO:0007829|PDB:6WG5"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:6WG5"
FT HELIX 140..144
FT /evidence="ECO:0007829|PDB:6WG5"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:6WG5"
FT HELIX 149..152
FT /evidence="ECO:0007829|PDB:6WG5"
FT HELIX 154..163
FT /evidence="ECO:0007829|PDB:6WG5"
FT HELIX 166..171
FT /evidence="ECO:0007829|PDB:6WG5"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:6WG5"
FT HELIX 180..183
FT /evidence="ECO:0007829|PDB:6WG5"
FT HELIX 187..204
FT /evidence="ECO:0007829|PDB:6WG5"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:6WG5"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:6WG5"
FT HELIX 219..233
FT /evidence="ECO:0007829|PDB:6WG5"
FT TURN 234..237
FT /evidence="ECO:0007829|PDB:6WG5"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:6WG5"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:6WG5"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:6WG5"
FT STRAND 268..272
FT /evidence="ECO:0007829|PDB:6WG5"
FT STRAND 274..282
FT /evidence="ECO:0007829|PDB:6WG5"
FT HELIX 292..301
FT /evidence="ECO:0007829|PDB:6WG5"
FT STRAND 302..306
FT /evidence="ECO:0007829|PDB:6WG5"
FT STRAND 317..326
FT /evidence="ECO:0007829|PDB:6WG5"
FT HELIX 330..343
FT /evidence="ECO:0007829|PDB:6WG5"
FT HELIX 344..346
FT /evidence="ECO:0007829|PDB:6WG5"
FT HELIX 348..352
FT /evidence="ECO:0007829|PDB:6WG5"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:6WG5"
FT STRAND 374..379
FT /evidence="ECO:0007829|PDB:6WG5"
FT STRAND 382..388
FT /evidence="ECO:0007829|PDB:6WG5"
FT HELIX 392..399
FT /evidence="ECO:0007829|PDB:6WG5"
FT HELIX 400..403
FT /evidence="ECO:0007829|PDB:6WG5"
FT HELIX 413..415
FT /evidence="ECO:0007829|PDB:6WG5"
FT HELIX 423..425
FT /evidence="ECO:0007829|PDB:6WG5"
FT STRAND 428..432
FT /evidence="ECO:0007829|PDB:6WG5"
FT HELIX 433..439
FT /evidence="ECO:0007829|PDB:6WG5"
FT TURN 440..442
FT /evidence="ECO:0007829|PDB:6WG5"
FT HELIX 450..461
FT /evidence="ECO:0007829|PDB:6WG5"
FT HELIX 465..474
FT /evidence="ECO:0007829|PDB:6WG5"
FT HELIX 483..501
FT /evidence="ECO:0007829|PDB:6WG5"
FT STRAND 513..515
FT /evidence="ECO:0007829|PDB:6WG5"
FT HELIX 526..534
FT /evidence="ECO:0007829|PDB:6WG5"
FT TURN 535..538
FT /evidence="ECO:0007829|PDB:6WG5"
FT HELIX 539..543
FT /evidence="ECO:0007829|PDB:6WG5"
FT TURN 545..548
FT /evidence="ECO:0007829|PDB:6WG5"
SQ SEQUENCE 616 AA; 70255 MW; 68A7EF7E9CB60544 CRC64;
MGRIGISCLF PASWHFSISP VGCPRILNTN LRQIMVISVL AAAVSLLYFS VVIIRNKYGR
LTRDKKFQRY LARVTDIEAT DTNNPNVNYG IVVDCGSSGS RVFVYCWPRH NGNPHDLLDI
RQMRDKNRKP VVMKIKPGIS EFATSPEKVS DYISPLLNFA AEHVPRAKHK ETPLYILCTA
GMRILPESQQ KAILEDLLTD IPVHFDFLFS DSHAEVISGK QEGVYAWIGI NFVLGRFEHI
EDDDEAVVEV NIPGSESSEA IVRKRTAGIL DMGGVSTQIA YEVPKTVSFA SSQQEEVAKN
LLAEFNLGCD VHQTEHVYRV YVATFLGFGG NAARQRYEDR IFANTIQKNR LLGKQTGLTP
DMPYLDPCLP LDIKDEIQQN GQTIYLRGTG DFDLCRETIQ PFMNKTNETQ TSLNGVYQPP
IHFQNSEFYG FSEFYYCTED VLRMGGDYNA AKFTKAAKDY CATKWSILRE RFDRGLYASH
ADLHRLKYQC FKSAWMFEVF HRGFSFPVNY KSLKTALQVY DKEVQWTLGA ILYRTRFLPL
RDIQQEAFRA SHTHWRGVSF VYNHYLFSGC FLVVLLAILL YLLRLRRIHR RTPRSSSAAA
LWMEEGLPAQ NAPGTL
