ENPP4_HUMAN
ID ENPP4_HUMAN Reviewed; 453 AA.
AC Q9Y6X5; A8K5G1; Q7L2N1;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 3.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Bis(5'-adenosyl)-triphosphatase ENPP4;
DE EC=3.6.1.29;
DE AltName: Full=AP3A hydrolase;
DE Short=AP3Aase;
DE AltName: Full=Ectonucleotide pyrophosphatase/phosphodiesterase family member 4;
DE Short=E-NPP 4;
DE Short=NPP-4;
DE Flags: Precursor;
GN Name=ENPP4; Synonyms=KIAA0879, NPP4;
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 [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:355-364(1998).
RN [2]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Kikuno R.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-144.
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [6]
RP IDENTIFICATION.
RX PubMed=11027689; DOI=10.1074/jbc.m007552200;
RA Gijsbers R., Ceulemans H., Stalmans W., Bollen M.;
RT "Structural and catalytic similarities between nucleotide
RT pyrophosphatases/phosphodiesterases and alkaline phosphatases.";
RL J. Biol. Chem. 276:1361-1368(2001).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=22995898; DOI=10.1182/blood-2012-04-425215;
RA Albright R.A., Chang W.C., Robert D., Ornstein D.L., Cao W., Liu L.,
RA Redick M.E., Young J.I., De La Cruz E.M., Braddock D.T.;
RT "NPP4 is a procoagulant enzyme on the surface of vascular endothelium.";
RL Blood 120:4432-4440(2012).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 16-407 IN COMPLEXES WITH ZINC AND
RP AMP, FUNCTION, CATALYTIC ACTIVITY, DISULFIDE BOND, GLYCOSYLATION AT
RP ASN-155; ASN-166 AND ASN-386, ACTIVE SITE, AND COFACTOR.
RX PubMed=24338010; DOI=10.1074/jbc.m113.505867;
RA Albright R.A., Ornstein D.L., Cao W., Chang W.C., Robert D., Tehan M.,
RA Hoyer D., Liu L., Stabach P., Yang G., De La Cruz E.M., Braddock D.T.;
RT "The molecular basis of purinergic signal metabolism by ecto-nucleotide
RT pyrophosphatase/phosphodiesterases 4 and 1 and implications in stroke.";
RL J. Biol. Chem. 289:3294-3306(2014).
CC -!- FUNCTION: Hydrolyzes extracellular Ap3A into AMP and ADP, and Ap4A into
CC AMP and ATP. Ap3A and Ap4A are diadenosine polyphosphates thought to
CC induce proliferation of vascular smooth muscle cells. Acts as a
CC procoagulant, mediating platelet aggregation at the site of nascent
CC thrombus via release of ADP from Ap3A and activation of ADP receptors.
CC {ECO:0000269|PubMed:22995898, ECO:0000269|PubMed:24338010}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + P(1),P(3)-bis(5'-adenosyl) triphosphate = ADP + AMP + 2
CC H(+); Xref=Rhea:RHEA:13893, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58529, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216;
CC EC=3.6.1.29; Evidence={ECO:0000269|PubMed:22995898,
CC ECO:0000269|PubMed:24338010};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:24338010};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:24338010};
CC -!- INTERACTION:
CC Q9Y6X5; P55061: TMBIM6; NbExp=3; IntAct=EBI-17442870, EBI-1045825;
CC Q9Y6X5; Q9BVK8: TMEM147; NbExp=3; IntAct=EBI-17442870, EBI-348587;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22995898};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:22995898}.
CC -!- TISSUE SPECIFICITY: Expressed on the surface of vascular endothelia.
CC {ECO:0000269|PubMed:22995898}.
CC -!- SIMILARITY: Belongs to the nucleotide pyrophosphatase/phosphodiesterase
CC family. {ECO:0000305}.
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DR EMBL; AB020686; BAA74902.2; -; mRNA.
DR EMBL; AK291276; BAF83965.1; -; mRNA.
DR EMBL; AL035701; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC018054; AAH18054.1; -; mRNA.
DR CCDS; CCDS34468.1; -.
DR PIR; A59389; A59389.
DR RefSeq; NP_055751.1; NM_014936.4.
DR PDB; 4LQY; X-ray; 1.54 A; A=16-407.
DR PDB; 4LR2; X-ray; 1.50 A; A=16-407.
DR PDBsum; 4LQY; -.
DR PDBsum; 4LR2; -.
DR AlphaFoldDB; Q9Y6X5; -.
DR SMR; Q9Y6X5; -.
DR BioGRID; 116542; 20.
DR IntAct; Q9Y6X5; 10.
DR STRING; 9606.ENSP00000318066; -.
DR GlyGen; Q9Y6X5; 8 sites.
DR iPTMnet; Q9Y6X5; -.
DR PhosphoSitePlus; Q9Y6X5; -.
DR BioMuta; ENPP4; -.
DR DMDM; 172045555; -.
DR EPD; Q9Y6X5; -.
DR jPOST; Q9Y6X5; -.
DR MassIVE; Q9Y6X5; -.
DR MaxQB; Q9Y6X5; -.
DR PaxDb; Q9Y6X5; -.
DR PeptideAtlas; Q9Y6X5; -.
DR PRIDE; Q9Y6X5; -.
DR ProteomicsDB; 86816; -.
DR Antibodypedia; 2757; 123 antibodies from 21 providers.
DR DNASU; 22875; -.
DR Ensembl; ENST00000321037.5; ENSP00000318066.3; ENSG00000001561.7.
DR GeneID; 22875; -.
DR KEGG; hsa:22875; -.
DR MANE-Select; ENST00000321037.5; ENSP00000318066.3; NM_014936.5; NP_055751.1.
DR UCSC; uc003oxy.4; human.
DR CTD; 22875; -.
DR DisGeNET; 22875; -.
DR GeneCards; ENPP4; -.
DR HGNC; HGNC:3359; ENPP4.
DR HPA; ENSG00000001561; Low tissue specificity.
DR MIM; 617000; gene.
DR neXtProt; NX_Q9Y6X5; -.
DR OpenTargets; ENSG00000001561; -.
DR PharmGKB; PA27794; -.
DR VEuPathDB; HostDB:ENSG00000001561; -.
DR eggNOG; KOG2645; Eukaryota.
DR GeneTree; ENSGT00940000158831; -.
DR HOGENOM; CLU_017594_1_2_1; -.
DR OMA; FTCIIII; -.
DR OrthoDB; 999163at2759; -.
DR PhylomeDB; Q9Y6X5; -.
DR TreeFam; TF330032; -.
DR BRENDA; 3.6.1.17; 2681.
DR PathwayCommons; Q9Y6X5; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; Q9Y6X5; -.
DR BioGRID-ORCS; 22875; 7 hits in 1072 CRISPR screens.
DR GenomeRNAi; 22875; -.
DR Pharos; Q9Y6X5; Tbio.
DR PRO; PR:Q9Y6X5; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9Y6X5; protein.
DR Bgee; ENSG00000001561; Expressed in bronchial epithelial cell and 197 other tissues.
DR Genevisible; Q9Y6X5; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0047710; F:bis(5'-adenosyl)-triphosphatase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR GO; GO:0030194; P:positive regulation of blood coagulation; IDA:UniProtKB.
DR GO; GO:0046130; P:purine ribonucleoside catabolic process; IDA:UniProtKB.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR029879; ENPP4.
DR InterPro; IPR002591; Phosphodiest/P_Trfase.
DR PANTHER; PTHR10151:SF79; PTHR10151:SF79; 1.
DR Pfam; PF01663; Phosphodiest; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Blood coagulation; Cell membrane; Disulfide bond;
KW Glycoprotein; Hemostasis; Hydrolase; Membrane; Metal-binding;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix; Zinc.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..453
FT /note="Bis(5'-adenosyl)-triphosphatase ENPP4"
FT /id="PRO_0000324795"
FT TOPO_DOM 16..407
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 408..428
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 429..453
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 70
FT /note="AMP-threonine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 34
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 91
FT /ligand="substrate"
FT BINDING 154
FT /ligand="substrate"
FT BINDING 189
FT /ligand="substrate"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT BINDING 193
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT BINDING 237
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 238
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 336
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24338010"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24338010"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 386
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24338010"
FT DISULFID 254..287
FT /evidence="ECO:0000269|PubMed:24338010"
FT DISULFID 394..401
FT /evidence="ECO:0000269|PubMed:24338010"
FT VARIANT 144
FT /note="H -> Q (in dbSNP:rs7451713)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_039884"
FT VARIANT 255
FT /note="I -> V (in dbSNP:rs9381429)"
FT /id="VAR_039885"
FT VARIANT 439
FT /note="S -> A (in dbSNP:rs16874289)"
FT /id="VAR_039886"
FT CONFLICT 39
FT /note="D -> G (in Ref. 3; BAF83965)"
FT /evidence="ECO:0000305"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:4LR2"
FT HELIX 40..43
FT /evidence="ECO:0007829|PDB:4LR2"
FT HELIX 47..54
FT /evidence="ECO:0007829|PDB:4LR2"
FT STRAND 56..63
FT /evidence="ECO:0007829|PDB:4LR2"
FT HELIX 70..79
FT /evidence="ECO:0007829|PDB:4LR2"
FT HELIX 83..86
FT /evidence="ECO:0007829|PDB:4LR2"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:4LR2"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:4LR2"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:4LR2"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:4LR2"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:4LR2"
FT HELIX 119..124
FT /evidence="ECO:0007829|PDB:4LR2"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:4LR2"
FT TURN 137..140
FT /evidence="ECO:0007829|PDB:4LR2"
FT HELIX 160..172
FT /evidence="ECO:0007829|PDB:4LR2"
FT STRAND 178..185
FT /evidence="ECO:0007829|PDB:4LR2"
FT HELIX 189..195
FT /evidence="ECO:0007829|PDB:4LR2"
FT HELIX 200..223
FT /evidence="ECO:0007829|PDB:4LR2"
FT TURN 227..229
FT /evidence="ECO:0007829|PDB:4LR2"
FT STRAND 231..235
FT /evidence="ECO:0007829|PDB:4LR2"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:4LR2"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:4LR2"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:4LR2"
FT STRAND 260..264
FT /evidence="ECO:0007829|PDB:4LR2"
FT STRAND 266..275
FT /evidence="ECO:0007829|PDB:4LR2"
FT HELIX 277..284
FT /evidence="ECO:0007829|PDB:4LR2"
FT STRAND 291..295
FT /evidence="ECO:0007829|PDB:4LR2"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:4LR2"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:4LR2"
FT STRAND 313..318
FT /evidence="ECO:0007829|PDB:4LR2"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:4LR2"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:4LR2"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:4LR2"
FT STRAND 349..353
FT /evidence="ECO:0007829|PDB:4LR2"
FT STRAND 358..366
FT /evidence="ECO:0007829|PDB:4LR2"
FT HELIX 367..369
FT /evidence="ECO:0007829|PDB:4LR2"
FT HELIX 370..378
FT /evidence="ECO:0007829|PDB:4LR2"
FT HELIX 389..395
FT /evidence="ECO:0007829|PDB:4LR2"
SQ SEQUENCE 453 AA; 51641 MW; BC82FA36D9B587C4 CRC64;
MKLLVILLFS GLITGFRSDS SSSLPPKLLL VSFDGFRADY LKNYEFPHLQ NFIKEGVLVE
HVKNVFITKT FPNHYSIVTG LYEESHGIVA NSMYDAVTKK HFSDSNDKDP FWWNEAVPIW
VTNQLQENRS SAAAMWPGTD VPIHDTISSY FMNYNSSVSF EERLNNITMW LNNSNPPVTF
ATLYWEEPDA SGHKYGPEDK ENMSRVLKKI DDLIGDLVQR LKMLGLWENL NVIITSDHGM
TQCSQDRLIN LDSCIDHSYY TLIDLSPVAA ILPKINRTEV YNKLKNCSPH MNVYLKEDIP
NRFYYQHNDR IQPIILVADE GWTIVLNESS QKLGDHGYDN SLPSMHPFLA AHGPAFHKGY
KHSTINIVDI YPMMCHILGL KPHPNNGTFG HTKCLLVDQW CINLPEAIAI VIGSLLVLTM
LTCLIIIMQN RLSVPRPFSR LQLQEDDDDP LIG
