Zinc finger FYVE domain-containing protein 9 (Mothers against decapentaplegic homolog-interacting protein) (Madh-interacting protein) (Novel serine protease) (NSP) (Receptor activation anchor) (hSARA) (Smad anchor for receptor activation)

 ZFYV9_HUMAN             Reviewed;        1425 AA.
 O95405; Q5T0F6; Q5T0F7; Q9UNE1; Q9Y5R7;
 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
 14-AUG-2001, sequence version 2.
 02-DEC-2020, entry version 186.
 RecName: Full=Zinc finger FYVE domain-containing protein 9;
 AltName: Full=Mothers against decapentaplegic homolog-interacting protein;
          Short=Madh-interacting protein;
 AltName: Full=Novel serine protease;
          Short=NSP;
 AltName: Full=Receptor activation anchor;
          Short=hSARA;
 AltName: Full=Smad anchor for receptor activation;
 Name=ZFYVE9; Synonyms=MADHIP, SARA, SMADIP;
 Homo sapiens (Human).
 Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
 Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
 Homo.
 NCBI_TaxID=9606;
 [1]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH SMAD2; SMAD3;
 TGFBR1 AND TGFBR2, FUNCTION, AND SUBCELLULAR LOCATION.
 PubMed=9865696; DOI=10.1016/s0092-8674(00)81701-8;
 Tsukazaki T., Chiang T.A., Davison A.F., Attisano L., Wrana J.L.;
 "SARA, a FYVE domain protein that recruits Smad2 to the TGFbeta receptor.";
 Cell 95:779-791(1998).
 [2]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
 TISSUE=Fetal brain;
 PubMed=9582421; DOI=10.1016/s0169-328x(97)00366-5;
 Meckelein B., Marshall D.C.L., Conn K.J., Pietropaolo M., Van Nostrand W.,
 Abraham C.R.;
 "Identification of a novel serine protease-like molecule in human brain.";
 Brain Res. Mol. Brain Res. 55:181-197(1998).
 [3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 PubMed=16710414; DOI=10.1038/nature04727;
 Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
 Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
 Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
 Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
 Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
 Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
 Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
 Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
 Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
 Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
 Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
 Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
 Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
 Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
 Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
 Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
 Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
 Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
 Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
 McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
 Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
 Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
 Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
 Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
 Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
 White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
 Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
 Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
 Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
 "The DNA sequence and biological annotation of human chromosome 1.";
 Nature 441:315-321(2006).
 [4]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
 Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
 Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
 Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
 Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
 Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
 Hunkapiller M.W., Myers E.W., Venter J.C.;
 Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
 [5]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
 TISSUE=Testis;
 PubMed=15489334; DOI=10.1101/gr.2596504;
 The MGC Project Team;
 "The status, quality, and expansion of the NIH full-length cDNA project:
 the Mammalian Gene Collection (MGC).";
 Genome Res. 14:2121-2127(2004).
 [6]
 SUBCELLULAR LOCATION.
 PubMed=11877415; DOI=10.1074/jbc.m107983200;
 Panopoulou E., Gillooly D.J., Wrana J.L., Zerial M., Stenmark H.,
 Murphy C., Fotsis T.;
 "Early endosomal regulation of Smad-dependent signaling in endothelial
 cells.";
 J. Biol. Chem. 277:18046-18052(2002).
 [7]
 SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
 PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
 Hillman R.T., Green R.E., Brenner S.E.;
 "An unappreciated role for RNA surveillance.";
 Genome Biol. 5:R8.1-R8.16(2004).
 [8]
 FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PML; SMAD2 AND SMAD3.
 PubMed=15356634; DOI=10.1038/nature02783;
 Lin H.K., Bergmann S., Pandolfi P.P.;
 "Cytoplasmic PML function in TGF-beta signalling.";
 Nature 431:205-211(2004).
 [9]
 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 TISSUE=Cervix carcinoma;
 PubMed=18669648; DOI=10.1073/pnas.0805139105;
 Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
 Elledge S.J., Gygi S.P.;
 "A quantitative atlas of mitotic phosphorylation.";
 Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
 [10]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306, AND IDENTIFICATION BY
 MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 TISSUE=Erythroleukemia;
 PubMed=23186163; DOI=10.1021/pr300630k;
 Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
 Mohammed S.;
 "Toward a comprehensive characterization of a human cancer cell
 phosphoproteome.";
 J. Proteome Res. 12:260-271(2013).
 [11]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-668, AND IDENTIFICATION BY
 MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 TISSUE=Liver;
 PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
 Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
 Ye M., Zou H.;
 "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
 phosphoproteome.";
 J. Proteomics 96:253-262(2014).
 [12]
 X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 771-811 IN COMPLEX WITH SMAD2, AND
 MUTAGENESIS.
 PubMed=10615055; DOI=10.1126/science.287.5450.92;
 Wu G., Chen Y.-G., Ozdamar B., Gyuricza C.A., Chong P.A., Wrana J.L.,
 Massague J., Shi Y.;
 "Structural basis of Smad2 recognition by the Smad anchor for receptor
 activation.";
 Science 287:92-97(2000).
 [13]
 X-RAY CRYSTALLOGRAPHY (2.74 ANGSTROMS) OF 773-810 IN COMPLEX WITH SMAD3.
 PubMed=12154125; DOI=10.1101/gad.1002002;
 Qin B.Y., Lam S.S., Correia J.J., Lin K.;
 "Smad3 allostery links TGF-beta receptor kinase activation to
 transcriptional control.";
 Genes Dev. 16:1950-1963(2002).
 -!- FUNCTION: Early endosomal protein that functions to recruit SMAD2/SMAD3
     to intracellular membranes and to the TGF-beta receptor. Plays a
     significant role in TGF-mediated signaling by regulating the
     subcellular location of SMAD2 and SMAD3 and modulating the
     transcriptional activity of the SMAD3/SMAD4 complex. Possibly
     associated with TGF-beta receptor internalization.
     {ECO:0000269|PubMed:15356634, ECO:0000269|PubMed:9865696}.
 -!- SUBUNIT: Interacts (via the SBD region) with SMAD2; the interaction
     recruits SMAD2 to the TGF-beta receptor and is disrupted by
     phosphorylation of SMAD2 upon TGF-beta receptor activation. Interacts
     with SMAD3. Interacts with TGFBR1 and TGFBR2; the interaction recruits
     SMAD2 to the TGF-beta receptor. Interacts with PML.
     {ECO:0000269|PubMed:10615055, ECO:0000269|PubMed:12154125,
     ECO:0000269|PubMed:15356634, ECO:0000269|PubMed:9865696}.
 -!- INTERACTION:
     O95405; Q9Y561: LRP12; NbExp=2; IntAct=EBI-296817, EBI-296693;
     O95405; P62136: PPP1CA; NbExp=3; IntAct=EBI-296817, EBI-357253;
     O95405; P36873: PPP1CC; NbExp=5; IntAct=EBI-296817, EBI-356283;
     O95405; P08100: RHO; NbExp=2; IntAct=EBI-296817, EBI-1394177;
     O95405; Q15796: SMAD2; NbExp=2; IntAct=EBI-296817, EBI-1040141;
     O95405; P84022: SMAD3; NbExp=5; IntAct=EBI-296817, EBI-347161;
     O95405; Q13277: STX3; NbExp=3; IntAct=EBI-296817, EBI-1394295;
 -!- SUBCELLULAR LOCATION: Cytoplasm. Early endosome membrane.
 -!- ALTERNATIVE PRODUCTS:
     Event=Alternative splicing; Named isoforms=3;
     Name=1;
       IsoId=O95405-1; Sequence=Displayed;
     Name=2;
       IsoId=O95405-2; Sequence=VSP_004315;
     Name=3;
       IsoId=O95405-3; Sequence=VSP_004316, VSP_004317;
 -!- TISSUE SPECIFICITY: Ubiquitous. In the brain found primarily in the
     cerebrovascular smooth muscle cells and reactive astrocytes.
 -!- DOMAIN: The SMAD binding domain (SBD) interacts with the MH2 domains of
     SMAD2 or SMAD3.
 -!- DOMAIN: The FYVE-type zinc finger is necessary and sufficient for its
     localization into early endosomes and mediates the association with
     PI3P.
 -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
     premature stop codon in the mRNA, leading to nonsense-mediated mRNA
     decay. {ECO:0000305}.
 -!- SEQUENCE CAUTION:
     Sequence=AAC99462.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
     Sequence=AAD31694.1; Type=Frameshift; Evidence={ECO:0000305};
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 EMBL; AF104304; AAC99462.1; ALT_INIT; mRNA.
 EMBL; AF130419; AAD31694.1; ALT_FRAME; mRNA.
 EMBL; AF130420; AAD31695.1; -; mRNA.
 EMBL; AC105754; -; NOT_ANNOTATED_CDS; Genomic_DNA.
 EMBL; AL513218; -; NOT_ANNOTATED_CDS; Genomic_DNA.
 EMBL; CH471059; EAX06790.1; -; Genomic_DNA.
 EMBL; CH471059; EAX06791.1; -; Genomic_DNA.
 EMBL; BC032680; AAH32680.1; -; mRNA.
 CCDS; CCDS563.1; -. [O95405-1]
 CCDS; CCDS564.1; -. [O95405-2]
 RefSeq; NP_004790.2; NM_004799.3. [O95405-1]
 RefSeq; NP_015563.2; NM_007324.3. [O95405-2]
 RefSeq; XP_011540739.1; XM_011542437.2. [O95405-1]
 PDB; 1DEV; X-ray; 2.20 A; B/D=771-811.
 PDB; 1MK2; X-ray; 2.74 A; B=773-810.
 PDB; 4BKW; X-ray; 2.53 A; A=895-1425.
 PDB; 5MJY; X-ray; 2.25 A; E/F=1-22.
 PDBsum; 1DEV; -.
 PDBsum; 1MK2; -.
 PDBsum; 4BKW; -.
 PDBsum; 5MJY; -.
 SMR; O95405; -.
 BioGRID; 114773; 48.
 CORUM; O95405; -.
 IntAct; O95405; 42.
 MINT; O95405; -.
 STRING; 9606.ENSP00000287727; -.
 iPTMnet; O95405; -.
 PhosphoSitePlus; O95405; -.
 BioMuta; ZFYVE9; -.
 EPD; O95405; -.
 jPOST; O95405; -.
 MassIVE; O95405; -.
 MaxQB; O95405; -.
 PaxDb; O95405; -.
 PeptideAtlas; O95405; -.
 PRIDE; O95405; -.
 ProteomicsDB; 50856; -. [O95405-1]
 ProteomicsDB; 50857; -. [O95405-2]
 ProteomicsDB; 50858; -. [O95405-3]
 Antibodypedia; 32995; 104 antibodies.
 DNASU; 9372; -.
 Ensembl; ENST00000287727; ENSP00000287727; ENSG00000157077. [O95405-1]
 Ensembl; ENST00000357206; ENSP00000349737; ENSG00000157077. [O95405-2]
 Ensembl; ENST00000371591; ENSP00000360647; ENSG00000157077. [O95405-1]
 GeneID; 9372; -.
 KEGG; hsa:9372; -.
 UCSC; uc001cto.5; human. [O95405-1]
 CTD; 9372; -.
 DisGeNET; 9372; -.
 EuPathDB; HostDB:ENSG00000157077.14; -.
 GeneCards; ZFYVE9; -.
 HGNC; HGNC:6775; ZFYVE9.
 HPA; ENSG00000157077; Low tissue specificity.
 MIM; 603755; gene.
 neXtProt; NX_O95405; -.
 OpenTargets; ENSG00000157077; -.
 PharmGKB; PA30532; -.
 eggNOG; KOG1841; Eukaryota.
 GeneTree; ENSGT00940000154290; -.
 HOGENOM; CLU_004326_1_0_1; -.
 InParanoid; O95405; -.
 OMA; HIQWVED; -.
 OrthoDB; 278124at2759; -.
 PhylomeDB; O95405; -.
 TreeFam; TF324904; -.
 PathwayCommons; O95405; -.
 Reactome; R-HSA-2173788; Downregulation of TGF-beta receptor signaling. [O95405-1]
 Reactome; R-HSA-2173789; TGF-beta receptor signaling activates SMADs. [O95405-1]
 Reactome; R-HSA-3304356; SMAD2/3 Phosphorylation Motif Mutants in Cancer. [O95405-1]
 Reactome; R-HSA-3656532; TGFBR1 KD Mutants in Cancer. [O95405-1]
 SignaLink; O95405; -.
 SIGNOR; O95405; -.
 BioGRID-ORCS; 9372; 6 hits in 850 CRISPR screens.
 ChiTaRS; ZFYVE9; human.
 EvolutionaryTrace; O95405; -.
 GeneWiki; Zinc_finger_FYVE_domain-containing_protein_9; -.
 GenomeRNAi; 9372; -.
 Pharos; O95405; Tbio.
 PRO; PR:O95405; -.
 Proteomes; UP000005640; Chromosome 1.
 RNAct; O95405; protein.
 Bgee; ENSG00000157077; Expressed in frontal cortex and 204 other tissues.
 Genevisible; O95405; HS.
 GO; GO:0005829; C:cytosol; IDA:HPA.
 GO; GO:0005769; C:early endosome; IBA:GO_Central.
 GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
 GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
 GO; GO:0032991; C:protein-containing complex; IMP:CAFA.
 GO; GO:0005545; F:1-phosphatidylinositol binding; IDA:UniProtKB.
 GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
 GO; GO:0006897; P:endocytosis; NAS:UniProtKB.
 GO; GO:0016197; P:endosomal transport; IBA:GO_Central.
 GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:UniProtKB.
 DisProt; DP00141; -.
 Gene3D; 3.30.40.10; -; 1.
 Gene3D; 4.10.720.10; -; 1.
 IDEAL; IID00112; -.
 InterPro; IPR022557; DUF3480.
 InterPro; IPR035438; SARA/endofin.
 InterPro; IPR024608; SARA_Smad-bd.
 InterPro; IPR037145; SARA_Smad-bd_sf.
 InterPro; IPR000306; Znf_FYVE.
 InterPro; IPR017455; Znf_FYVE-rel.
 InterPro; IPR011011; Znf_FYVE_PHD.
 InterPro; IPR013083; Znf_RING/FYVE/PHD.
 Pfam; PF11979; DUF3480; 1.
 Pfam; PF01363; FYVE; 1.
 Pfam; PF11409; SARA; 1.
 PIRSF; PIRSF037289; SARA/endofin; 1.
 SMART; SM00064; FYVE; 1.
 SUPFAM; SSF57903; SSF57903; 1.
 PROSITE; PS50178; ZF_FYVE; 1.
 1: Evidence at protein level;
 3D-structure; Alternative splicing; Cytoplasm; Endosome; Membrane;
 Metal-binding; Phosphoprotein; Polymorphism; Receptor; Reference proteome;
 Zinc; Zinc-finger.
 CHAIN           1..1425
                 /note="Zinc finger FYVE domain-containing protein 9"
                 /id="PRO_0000098715"
 ZN_FING         699..758
                 /note="FYVE-type"
                 /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
 REGION          767..823
                 /note="SBD"
 MOD_RES         306
                 /note="Phosphoserine"
                 /evidence="ECO:0000244|PubMed:23186163"
 MOD_RES         668
                 /note="Phosphoserine"
                 /evidence="ECO:0000244|PubMed:24275569"
 VAR_SEQ         760..818
                 /note="Missing (in isoform 2)"
                 /evidence="ECO:0000303|PubMed:9582421"
                 /id="VSP_004315"
 VAR_SEQ         760..762
                 /note="AQA -> GKY (in isoform 3)"
                 /evidence="ECO:0000303|PubMed:9582421"
                 /id="VSP_004316"
 VAR_SEQ         763..1425
                 /note="Missing (in isoform 3)"
                 /evidence="ECO:0000303|PubMed:9582421"
                 /id="VSP_004317"
 VARIANT         287
                 /note="Y -> C (in dbSNP:rs9803965)"
                 /id="VAR_052985"
 VARIANT         414
                 /note="Q -> P (in dbSNP:rs3790525)"
                 /id="VAR_052986"
 VARIANT         639
                 /note="I -> V (in dbSNP:rs11809887)"
                 /id="VAR_052987"
 MUTAGEN         782
                 /note="Y->A: Diminishes complex formation with SMAD2."
                 /evidence="ECO:0000269|PubMed:10615055"
 MUTAGEN         782
                 /note="Y->E: Diminishes complex formation with SMAD2."
                 /evidence="ECO:0000269|PubMed:10615055"
 MUTAGEN         783
                 /note="C->A: Diminishes complex formation with SMAD2."
                 /evidence="ECO:0000269|PubMed:10615055"
 MUTAGEN         783
                 /note="C->E: Diminishes complex formation with SMAD2."
                 /evidence="ECO:0000269|PubMed:10615055"
 MUTAGEN         788
                 /note="P->A: Diminishes complex formation with SMAD2."
                 /evidence="ECO:0000269|PubMed:10615055"
 MUTAGEN         788
                 /note="P->E: Diminishes complex formation with SMAD2."
                 /evidence="ECO:0000269|PubMed:10615055"
 MUTAGEN         790
                 /note="Q->A: No effect on complex formation with SMAD2."
                 /evidence="ECO:0000269|PubMed:10615055"
 MUTAGEN         793
                 /note="Q->A: No effect on complex formation with SMAD2."
                 /evidence="ECO:0000269|PubMed:10615055"
 MUTAGEN         805
                 /note="V->A: Diminishes complex formation with SMAD2."
                 /evidence="ECO:0000269|PubMed:10615055"
 MUTAGEN         805
                 /note="V->E: Diminishes complex formation with SMAD2."
                 /evidence="ECO:0000269|PubMed:10615055"
 HELIX           4..20
                 /evidence="ECO:0000244|PDB:5MJY"
 HELIX           779..781
                 /evidence="ECO:0000244|PDB:1DEV"
 HELIX           788..792
                 /evidence="ECO:0000244|PDB:1DEV"
 TURN            793..795
                 /evidence="ECO:0000244|PDB:1DEV"
 STRAND          797..800
                 /evidence="ECO:0000244|PDB:1MK2"
 STRAND          804..807
                 /evidence="ECO:0000244|PDB:1DEV"
 STRAND          901..903
                 /evidence="ECO:0000244|PDB:4BKW"
 STRAND          907..909
                 /evidence="ECO:0000244|PDB:4BKW"
 STRAND          918..922
                 /evidence="ECO:0000244|PDB:4BKW"
 HELIX           925..932
                 /evidence="ECO:0000244|PDB:4BKW"
 STRAND          940..945
                 /evidence="ECO:0000244|PDB:4BKW"
 STRAND          948..957
                 /evidence="ECO:0000244|PDB:4BKW"
 STRAND          960..970
                 /evidence="ECO:0000244|PDB:4BKW"
 HELIX           971..973
                 /evidence="ECO:0000244|PDB:4BKW"
 STRAND          977..983
                 /evidence="ECO:0000244|PDB:4BKW"
 HELIX           994..1007
                 /evidence="ECO:0000244|PDB:4BKW"
 STRAND          1017..1019
                 /evidence="ECO:0000244|PDB:4BKW"
 STRAND          1030..1036
                 /evidence="ECO:0000244|PDB:4BKW"
 STRAND          1039..1041
                 /evidence="ECO:0000244|PDB:4BKW"
 STRAND          1050..1060
                 /evidence="ECO:0000244|PDB:4BKW"
 TURN            1061..1063
                 /evidence="ECO:0000244|PDB:4BKW"
 HELIX           1064..1069
                 /evidence="ECO:0000244|PDB:4BKW"
 HELIX           1071..1082
                 /evidence="ECO:0000244|PDB:4BKW"
 STRAND          1089..1091
                 /evidence="ECO:0000244|PDB:4BKW"
 HELIX           1106..1109
                 /evidence="ECO:0000244|PDB:4BKW"
 STRAND          1113..1115
                 /evidence="ECO:0000244|PDB:4BKW"
 STRAND          1127..1131
                 /evidence="ECO:0000244|PDB:4BKW"
 STRAND          1134..1140
                 /evidence="ECO:0000244|PDB:4BKW"
 HELIX           1141..1143
                 /evidence="ECO:0000244|PDB:4BKW"
 HELIX           1144..1152
                 /evidence="ECO:0000244|PDB:4BKW"
 STRAND          1156..1162
                 /evidence="ECO:0000244|PDB:4BKW"
 STRAND          1170..1177
                 /evidence="ECO:0000244|PDB:4BKW"
 STRAND          1183..1192
                 /evidence="ECO:0000244|PDB:4BKW"
 STRAND          1196..1199
                 /evidence="ECO:0000244|PDB:4BKW"
 STRAND          1201..1207
                 /evidence="ECO:0000244|PDB:4BKW"
 STRAND          1218..1222
                 /evidence="ECO:0000244|PDB:4BKW"
 STRAND          1225..1229
                 /evidence="ECO:0000244|PDB:4BKW"
 HELIX           1232..1243
                 /evidence="ECO:0000244|PDB:4BKW"
 STRAND          1248..1250
                 /evidence="ECO:0000244|PDB:4BKW"
 STRAND          1263..1270
                 /evidence="ECO:0000244|PDB:4BKW"
 TURN            1282..1284
                 /evidence="ECO:0000244|PDB:4BKW"
 STRAND          1291..1295
                 /evidence="ECO:0000244|PDB:4BKW"
 STRAND          1302..1304
                 /evidence="ECO:0000244|PDB:4BKW"
 STRAND          1307..1316
                 /evidence="ECO:0000244|PDB:4BKW"
 HELIX           1334..1347
                 /evidence="ECO:0000244|PDB:4BKW"
 HELIX           1348..1350
                 /evidence="ECO:0000244|PDB:4BKW"
 HELIX           1351..1356
                 /evidence="ECO:0000244|PDB:4BKW"
 STRAND          1361..1368
                 /evidence="ECO:0000244|PDB:4BKW"
 STRAND          1373..1379
                 /evidence="ECO:0000244|PDB:4BKW"
 HELIX           1386..1388
                 /evidence="ECO:0000244|PDB:4BKW"
 HELIX           1389..1400
                 /evidence="ECO:0000244|PDB:4BKW"
 STRAND          1413..1422
                 /evidence="ECO:0000244|PDB:4BKW"
 SEQUENCE   1425 AA;  156403 MW;  ADE5CB530C1272C6 CRC64;
 MENYFQAEAY NLDKVLDEFE QNEDETVSST LLDTKWNKIL DPPSHRLSFN PTLASVNESA
 VSNESQPQLK VFSLAHSAPL TTEEEDHCAN GQDCNLNPEI ATMWIDENAV AEDQLIKRNY
 SWDDQCSAVE VGEKKCGNLA CLPDEKNVLV VAVMHNCDKR TLQNDLQDCN NYNSQSLMDA
 FSCSLDNENR QTDQFSFSIN ESTEKDMNSE KQMDPLNRPK TEGRSVNHLC PTSSDSLASV
 CSPSQLKDDG SIGRDPSMSA ITSLTVDSVI SSQGTDGCPA VKKQENYIPD EDLTGKISSP
 RTDLGSPNSF SHMSEGILMK KEPAEESTTE ESLRSGLPLL LKPDMPNGSG RNNDCERCSD
 CLVPNEVRAD ENEGYEHEET LGTTEFLNMT EHFSESQDMT NWKLTKLNEM NDSQVNEEKE
 KFLQISQPED TNGDSGGQCV GLADAGLDLK GTCISESEEC DFSTVIDTPA ANYLSNGCDS
 YGMQDPGVSF VPKTLPSKED SVTEEKEIEE SKSECYSNIY EQRGNEATEG SGLLLNSTGD
 LMKKNYLHNF CSQVPSVLGQ SSPKVVASLP SISVPFGGAR PKQPSNLKLQ IPKPLSDHLQ
 NDFPANSGNN TKNKNDILGK AKLGENSATN VCSPSLGNIS NVDTNGEHLE SYEAEISTRP
 CLALAPDSPD NDLRAGQFGI SARKPFTTLG EVAPVWVPDS QAPNCMKCEA RFTFTKRRHH
 CRACGKVFCA SCCSLKCKLL YMDRKEARVC VICHSVLMNA QAWENMMSAS SQSPNPNNPA
 EYCSTIPPLQ QAQASGALSS PPPTVMVPVG VLKHPGAEVA QPREQRRVWF ADGILPNGEV
 ADAAKLTMNG TSSAGTLAVS HDPVKPVTTS PLPAETDICL FSGSITQVGS PVGSAMNLIP
 EDGLPPILIS TGVKGDYAVE EKPSQISVMQ QLEDGGPDPL VFVLNANLLS MVKIVNYVNR
 KCWCFTTKGM HAVGQSEIVI LLQCLPDEKC LPKDIFNHFV QLYRDALAGN VVSNLGHSFF
 SQSFLGSKEH GGFLYVTSTY QSLQDLVLPT PPYLFGILIQ KWETPWAKVF PIRLMLRLGA
 EYRLYPCPLF SVRFRKPLFG ETGHTIMNLL ADFRNYQYTL PVVQGLVVDM EVRKTSIKIP
 SNRYNEMMKA MNKSNEHVLA GGACFNEKAD SHLVCVQNDD GNYQTQAISI HNQPRKVTGA
 SFFVFSGALK SSSGYLAKSS IVEDGVMVQI TAENMDSLRQ ALREMKDFTI TCGKADAEEP
 QEHIHIQWVD DDKNVSKGVV SPIDGKSMET ITNVKIFHGS EYKANGKVIR WTEVFFLEND
 DQHNCLSDPA DHSRLTEHVA KAFCLALCPH LKLLKEDGMT KLGLRVTLDS DQVGYQAGSN
 GQPLPSQYMN DLDSALVPVI HGGACQLSEG PVVMELIFYI LENIV

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