ID   HIPK3_HUMAN             Reviewed;        1215 AA.
AC   Q9H422; O14632; Q2PBG4; Q2PBG5; Q92632; Q9HAS2;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   27-MAR-2024, entry version 184.
DE   RecName: Full=Homeodomain-interacting protein kinase 3;
DE            EC=2.7.11.1;
DE   AltName: Full=Androgen receptor-interacting nuclear protein kinase;
DE            Short=ANPK;
DE   AltName: Full=Fas-interacting serine/threonine-protein kinase;
DE            Short=FIST;
DE   AltName: Full=Homolog of protein kinase YAK1;
GN   Name=HIPK3; Synonyms=DYRK6, FIST3, PKY;
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=9373137; DOI=10.1016/s0378-1119(97)00350-8;
RA   Begley D.A., Berkenpas M.B., Sampson K.E., Abraham I.;
RT   "Identification and sequence of human PKY, a putative kinase with increased
RT   expression in multidrug-resistant cells, with homology to yeast protein
RT   kinase Yak1.";
RL   Gene 200:35-43(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=11034606; DOI=10.1084/jem.192.8.1165;
RA   Rochat-Steiner V., Becker K., Micheau O., Schneider P., Burns K.,
RA   Tschopp J.;
RT   "FIST/HIPK3: a Fas/FADD-interacting serine/threonine kinase that induces
RT   FADD phosphorylation and inhibits Fas-mediated Jun NH2-terminal kinase
RT   activation.";
RL   J. Exp. Med. 192:1165-1174(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA   Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA   Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA   Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA   Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-295 (ISOFORMS 1/2).
RA   Becker W., Joost H.G.;
RL   Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=9725910; DOI=10.1091/mbc.9.9.2527;
RA   Moilanen A.-M., Karvonen U., Poukka H., Jaenne O.A., Palvimo J.J.;
RT   "Activation of androgen receptor function by a novel nuclear protein
RT   kinase.";
RL   Mol. Biol. Cell 9:2527-2543(1998).
RN   [6]
RP   INTERACTION WITH UBL1.
RX   PubMed=10961991; DOI=10.1074/jbc.m004293200;
RA   Minty A., Dumont X., Kaghad M., Caput D.;
RT   "Covalent modification of p73alpha by SUMO-1. Two-hybrid screening with p73
RT   identifies novel SUMO-1-interacting proteins and a SUMO-1 interaction
RT   motif.";
RL   J. Biol. Chem. 275:36316-36323(2000).
RN   [7]
RP   FUNCTION.
RX   PubMed=14766760; DOI=10.1074/jbc.m307629200;
RA   Curtin J.F., Cotter T.G.;
RT   "JNK regulates HIPK3 expression and promotes resistance to Fas-mediated
RT   apoptosis in DU 145 prostate carcinoma cells.";
RL   J. Biol. Chem. 279:17090-17100(2004).
RN   [8]
RP   FUNCTION AS KINASE AND IN CAMP SIGNALING PATHWAY, INTERACTION WITH
RP   NR5A1/SF1, AND MUTAGENESIS OF LYS-226.
RX   PubMed=17210646; DOI=10.1128/mcb.02253-06;
RA   Lan H.-C., Li H.-J., Lin G., Lai P.-Y., Chung B.-C.;
RT   "Cyclic AMP stimulates SF-1-dependent CYP11A1 expression through
RT   homeodomain-interacting protein kinase 3-mediated Jun N-terminal kinase and
RT   c-Jun phosphorylation.";
RL   Mol. Cell. Biol. 27:2027-2036(2007).
RN   [9]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-27, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-modification
RT   with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
RN   [10]
RP   VARIANTS [LARGE SCALE ANALYSIS] ARG-142; GLU-170; ARG-191; ASN-500 AND
RP   LEU-729.
RX   PubMed=17344846; DOI=10.1038/nature05610;
RA   Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA   Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA   Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA   Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA   Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA   Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA   Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA   Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA   Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA   Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA   Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA   Futreal P.A., Stratton M.R.;
RT   "Patterns of somatic mutation in human cancer genomes.";
RL   Nature 446:153-158(2007).
CC   -!- FUNCTION: Serine/threonine-protein kinase involved in transcription
CC       regulation, apoptosis and steroidogenic gene expression. Phosphorylates
CC       JUN and RUNX2. Seems to negatively regulate apoptosis by promoting FADD
CC       phosphorylation. Enhances androgen receptor-mediated transcription. May
CC       act as a transcriptional corepressor for NK homeodomain transcription
CC       factors. The phosphorylation of NR5A1 activates SF1 leading to
CC       increased steroidogenic gene expression upon cAMP signaling pathway
CC       stimulation. In osteoblasts, supports transcription activation:
CC       phosphorylates RUNX2 that synergizes with SPEN/MINT to enhance FGFR2-
CC       mediated activation of the osteocalcin FGF-responsive element (OCFRE).
CC       {ECO:0000269|PubMed:14766760, ECO:0000269|PubMed:17210646}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1;
CC   -!- SUBUNIT: Interacts with Nkx1-2. Interacts with FAS and DAXX. Probably
CC       part of a complex consisting of HIPK3, FAS and FADD. Interacts with and
CC       stabilizes ligand-bound androgen receptor (AR) (By similarity).
CC       Interacts with UBL1/SUMO-1. Binds to NR5A1/SF1, SPEN/MINT and RUNX2.
CC       {ECO:0000250, ECO:0000269|PubMed:10961991,
CC       ECO:0000269|PubMed:17210646}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11034606}. Nucleus
CC       {ECO:0000269|PubMed:11034606}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=HIPK3;
CC         IsoId=Q9H422-1; Sequence=Displayed;
CC       Name=2; Synonyms=FIST;
CC         IsoId=Q9H422-2; Sequence=VSP_013140;
CC   -!- TISSUE SPECIFICITY: Overexpressed in multidrug resistant cells. Highly
CC       expressed in heart and skeletal muscle, and at lower levels in
CC       placenta, pancreas, brain, spleen, prostate, thymus, testis, small
CC       intestine, colon and leukocytes. Not found in liver and lung.
CC       {ECO:0000269|PubMed:11034606, ECO:0000269|PubMed:9373137,
CC       ECO:0000269|PubMed:9725910}.
CC   -!- PTM: Autophosphorylated, but autophosphorylation is not required for
CC       catalytic activity. {ECO:0000250}.
CC   -!- PTM: May be sumoylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC       protein kinase family. HIPK subfamily. {ECO:0000305}.
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DR   EMBL; AF004849; AAC64294.1; -; mRNA.
DR   EMBL; AF305239; AAG25990.1; -; mRNA.
DR   EMBL; AL122015; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; Y09306; CAA70489.1; ALT_TERM; mRNA.
DR   CCDS; CCDS41634.1; -. [Q9H422-2]
DR   CCDS; CCDS7884.1; -. [Q9H422-1]
DR   RefSeq; NP_001041665.1; NM_001048200.2. [Q9H422-2]
DR   RefSeq; NP_001265092.1; NM_001278163.1. [Q9H422-2]
DR   RefSeq; NP_005725.3; NM_005734.4. [Q9H422-1]
DR   RefSeq; XP_005252786.1; XM_005252729.2.
DR   RefSeq; XP_016872565.1; XM_017017076.1.
DR   RefSeq; XP_016872566.1; XM_017017077.1.
DR   PDB; 7O7I; X-ray; 2.50 A; A=159-562.
DR   PDB; 7O7J; X-ray; 2.81 A; A=159-562.
DR   PDBsum; 7O7I; -.
DR   PDBsum; 7O7J; -.
DR   AlphaFoldDB; Q9H422; -.
DR   SMR; Q9H422; -.
DR   BioGRID; 115420; 36.
DR   IntAct; Q9H422; 22.
DR   MINT; Q9H422; -.
DR   STRING; 9606.ENSP00000304226; -.
DR   BindingDB; Q9H422; -.
DR   ChEMBL; CHEMBL4577; -.
DR   DrugBank; DB12010; Fostamatinib.
DR   DrugCentral; Q9H422; -.
DR   GuidetoPHARMACOLOGY; 2035; -.
DR   GlyGen; Q9H422; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9H422; -.
DR   PhosphoSitePlus; Q9H422; -.
DR   BioMuta; HIPK3; -.
DR   DMDM; 61213741; -.
DR   CPTAC; non-CPTAC-6026; -.
DR   CPTAC; non-CPTAC-6027; -.
DR   EPD; Q9H422; -.
DR   jPOST; Q9H422; -.
DR   MassIVE; Q9H422; -.
DR   MaxQB; Q9H422; -.
DR   PaxDb; 9606-ENSP00000304226; -.
DR   PeptideAtlas; Q9H422; -.
DR   ProteomicsDB; 80780; -. [Q9H422-1]
DR   ProteomicsDB; 80781; -. [Q9H422-2]
DR   Antibodypedia; 25715; 244 antibodies from 29 providers.
DR   DNASU; 10114; -.
DR   Ensembl; ENST00000303296.9; ENSP00000304226.4; ENSG00000110422.12. [Q9H422-1]
DR   Ensembl; ENST00000379016.7; ENSP00000368301.3; ENSG00000110422.12. [Q9H422-2]
DR   Ensembl; ENST00000456517.2; ENSP00000398241.1; ENSG00000110422.12. [Q9H422-2]
DR   Ensembl; ENST00000525975.5; ENSP00000431710.1; ENSG00000110422.12. [Q9H422-2]
DR   GeneID; 10114; -.
DR   KEGG; hsa:10114; -.
DR   MANE-Select; ENST00000303296.9; ENSP00000304226.4; NM_005734.5; NP_005725.3.
DR   UCSC; uc001mul.3; human. [Q9H422-1]
DR   AGR; HGNC:4915; -.
DR   CTD; 10114; -.
DR   DisGeNET; 10114; -.
DR   GeneCards; HIPK3; -.
DR   HGNC; HGNC:4915; HIPK3.
DR   HPA; ENSG00000110422; Low tissue specificity.
DR   MIM; 604424; gene.
DR   neXtProt; NX_Q9H422; -.
DR   OpenTargets; ENSG00000110422; -.
DR   PharmGKB; PA29292; -.
DR   VEuPathDB; HostDB:ENSG00000110422; -.
DR   eggNOG; KOG0667; Eukaryota.
DR   GeneTree; ENSGT00940000155960; -.
DR   HOGENOM; CLU_003045_2_0_1; -.
DR   InParanoid; Q9H422; -.
DR   OMA; HEGETGM; -.
DR   OrthoDB; 3095114at2759; -.
DR   PhylomeDB; Q9H422; -.
DR   TreeFam; TF105417; -.
DR   PathwayCommons; Q9H422; -.
DR   SignaLink; Q9H422; -.
DR   SIGNOR; Q9H422; -.
DR   BioGRID-ORCS; 10114; 14 hits in 1186 CRISPR screens.
DR   ChiTaRS; HIPK3; human.
DR   GeneWiki; HIPK3; -.
DR   GenomeRNAi; 10114; -.
DR   Pharos; Q9H422; Tchem.
DR   PRO; PR:Q9H422; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q9H422; Protein.
DR   Bgee; ENSG00000110422; Expressed in endothelial cell and 195 other cell types or tissues.
DR   ExpressionAtlas; Q9H422; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0016604; C:nuclear body; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0016605; C:PML body; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:MGI.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; IBA:GO_Central.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0009299; P:mRNA transcription; IDA:UniProtKB.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR   GO; GO:0043508; P:negative regulation of JUN kinase activity; ISS:UniProtKB.
DR   GO; GO:0018105; P:peptidyl-serine phosphorylation; ISS:UniProtKB.
DR   GO; GO:0018107; P:peptidyl-threonine phosphorylation; ISS:UniProtKB.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR   CDD; cd14229; STKc_HIPK3; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24058; DUAL SPECIFICITY PROTEIN KINASE; 1.
DR   PANTHER; PTHR24058:SF45; HOMEODOMAIN-INTERACTING PROTEIN KINASE 3; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   Genevisible; Q9H422; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Apoptosis; ATP-binding; Cytoplasm;
KW   Isopeptide bond; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Serine/threonine-protein kinase; Transcription;
KW   Transcription regulation; Transferase; Ubl conjugation.
FT   CHAIN           1..1215
FT                   /note="Homeodomain-interacting protein kinase 3"
FT                   /id="PRO_0000085998"
FT   DOMAIN          197..525
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          767..944
FT                   /note="Interaction with AR"
FT                   /evidence="ECO:0000250"
FT   REGION          796..891
FT                   /note="Interaction with FAS"
FT                   /evidence="ECO:0000250"
FT   REGION          855..1011
FT                   /note="Required for localization to nuclear speckles"
FT                   /evidence="ECO:0000250"
FT   REGION          866..918
FT                   /note="SUMO interaction motifs (SIM); required for nuclear
FT                   localization and kinase activity"
FT                   /evidence="ECO:0000250"
FT   REGION          870..880
FT                   /note="Interaction with UBL1"
FT                   /evidence="ECO:0000305"
FT   REGION          912..987
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        912..935
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        947..964
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        967..981
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        322
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         203..211
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         226
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         359
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ERH7"
FT   CROSSLNK        27
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        1208
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         770..790
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:11034606"
FT                   /id="VSP_013140"
FT   VARIANT         142
FT                   /note="Q -> R (in dbSNP:rs34193811)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_040549"
FT   VARIANT         170
FT                   /note="G -> E (in dbSNP:rs34698015)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_040550"
FT   VARIANT         191
FT                   /note="C -> R (in dbSNP:rs35689361)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_040551"
FT   VARIANT         474
FT                   /note="V -> I (in dbSNP:rs266472)"
FT                   /id="VAR_051627"
FT   VARIANT         500
FT                   /note="S -> N (in dbSNP:rs11032229)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_040552"
FT   VARIANT         729
FT                   /note="P -> L (in dbSNP:rs55807239)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_040553"
FT   MUTAGEN         226
FT                   /note="K->R: Loss of kinase activity and impaired
FT                   activation of SF1."
FT                   /evidence="ECO:0000269|PubMed:17210646"
FT   CONFLICT        69
FT                   /note="N -> K (in Ref. 2; AAG25990)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        111
FT                   /note="A -> V (in Ref. 1; AAC64294)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1148
FT                   /note="Q -> K (in Ref. 2; AAG25990)"
FT                   /evidence="ECO:0000305"
FT   STRAND          193..195
FT                   /evidence="ECO:0007829|PDB:7O7I"
FT   STRAND          197..205
FT                   /evidence="ECO:0007829|PDB:7O7I"
FT   STRAND          210..216
FT                   /evidence="ECO:0007829|PDB:7O7I"
FT   STRAND          222..228
FT                   /evidence="ECO:0007829|PDB:7O7I"
FT   HELIX           232..234
FT                   /evidence="ECO:0007829|PDB:7O7I"
FT   HELIX           235..249
FT                   /evidence="ECO:0007829|PDB:7O7I"
FT   TURN            250..252
FT                   /evidence="ECO:0007829|PDB:7O7J"
FT   TURN            255..257
FT                   /evidence="ECO:0007829|PDB:7O7I"
FT   STRAND          261..267
FT                   /evidence="ECO:0007829|PDB:7O7I"
FT   STRAND          270..276
FT                   /evidence="ECO:0007829|PDB:7O7I"
FT   HELIX           282..288
FT                   /evidence="ECO:0007829|PDB:7O7I"
FT   TURN            289..291
FT                   /evidence="ECO:0007829|PDB:7O7I"
FT   HELIX           296..315
FT                   /evidence="ECO:0007829|PDB:7O7I"
FT   HELIX           325..327
FT                   /evidence="ECO:0007829|PDB:7O7I"
FT   STRAND          328..332
FT                   /evidence="ECO:0007829|PDB:7O7I"
FT   TURN            333..335
FT                   /evidence="ECO:0007829|PDB:7O7I"
FT   STRAND          336..342
FT                   /evidence="ECO:0007829|PDB:7O7I"
FT   HELIX           363..365
FT                   /evidence="ECO:0007829|PDB:7O7I"
FT   HELIX           368..372
FT                   /evidence="ECO:0007829|PDB:7O7I"
FT   HELIX           379..394
FT                   /evidence="ECO:0007829|PDB:7O7I"
FT   HELIX           404..415
FT                   /evidence="ECO:0007829|PDB:7O7I"
FT   HELIX           420..424
FT                   /evidence="ECO:0007829|PDB:7O7I"
FT   HELIX           428..431
FT                   /evidence="ECO:0007829|PDB:7O7I"
FT   HELIX           449..456
FT                   /evidence="ECO:0007829|PDB:7O7I"
FT   HELIX           471..474
FT                   /evidence="ECO:0007829|PDB:7O7I"
FT   HELIX           485..505
FT                   /evidence="ECO:0007829|PDB:7O7I"
FT   TURN            510..512
FT                   /evidence="ECO:0007829|PDB:7O7I"
FT   HELIX           516..519
FT                   /evidence="ECO:0007829|PDB:7O7I"
FT   HELIX           523..526
FT                   /evidence="ECO:0007829|PDB:7O7I"
FT   TURN            528..532
FT                   /evidence="ECO:0007829|PDB:7O7I"
FT   HELIX           537..546
FT                   /evidence="ECO:0007829|PDB:7O7I"
SQ   SEQUENCE   1215 AA;  133743 MW;  E952D04786955721 CRC64;
     MASQVLVYPP YVYQTQSSAF CSVKKLKVEP SSCVFQERNY PRTYVNGRNF GNSHPPTKGS
     AFQTKIPFNR PRGHNFSLQT SAVVLKNTAG ATKVIAAQAQ QAHVQAPQIG AWRNRLHFLE
     GPQRCGLKRK SEELDNHSSA MQIVDELSIL PAMLQTNMGN PVTVVTATTG SKQNCTTGEG
     DYQLVQHEVL CSMKNTYEVL DFLGRGTFGQ VVKCWKRGTN EIVAIKILKN HPSYARQGQI
     EVSILARLST ENADEYNFVR AYECFQHRNH TCLVFEMLEQ NLYDFLKQNK FSPLPLKVIR
     PILQQVATAL KKLKSLGLIH ADLKPENIML VDPVRQPYRV KVIDFGSASH VSKTVCSTYL
     QSRYYRAPEI ILGLPFCEAI DMWSLGCVIA ELFLGWPLYP GALEYDQIRY ISQTQGLPGE
     QLLNVGTKST RFFCKETDMS HSGWRLKTLE EHEAETGMKS KEARKYIFNS LDDVAHVNTV
     MDLEGSDLLA EKADRREFVS LLKKMLLIDA DLRITPAETL NHPFVNMKHL LDFPHSNHVK
     SCFHIMDICK SHLNSCDTNN HNKTSLLRPV ASSSTATLTA NFTKIGTLRS QALTTSAHSV
     VHHGIPLQAG TAQFGCGDAF QQTLIICPPA IQGIPATHGK PTSYSIRVDN TVPLVTQAPA
     VQPLQIRPGV LSQTWSGRTQ QMLVPAWQQV TPLAPATTTL TSESVAGSHR LGDWGKMISC
     SNHYNSVMPQ PLLTNQITLS APQPVSVGIA HVVWPQPATT KKNKQCQNRG ILVKLMEWEP
     GREEINAFSW SNSLQNTNIP HSAFISPKII NGKDVEEVSC IETQDNQNSE GEARNCCETS
     IRQDSDSSVS DKQRQTIIIA DSPSPAVSVI TISSDTDEEE TSQRHSLREC KGSLDCEACQ
     STLNIDRMCS LSSPDSTLST SSSGQSSPSP CKRPNSMSDE EQESSCDTVD GSPTSDSSGH
     DSPFAESTFV EDTHENTELV SSADTETKPA VCSVVVPPVE LENGLNADEH MANTDSICQP
     LIKGRSAPGR LNQPSAVGTR QQKLTSAFQQ QHLNFSQVQH FGSGHQEWNG NFGHRRQQAY
     IPTSVTSNPF TLSHGSPNHT AVHAHLAGNT HLGGQPTLLP YPSSATLSSA APVAHLLASP
     CTSRPMLQHP TYNISHPSGI VHQVPVGLNP RLLPSPTIHQ TQYKPIFPPH SYIAASPAYT
     GFPLSPTKLS QYPYM
//