HIPK3_HUMAN
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 03-AUG-2022, entry version 175.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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. [Q9H422-1]
DR RefSeq; XP_016872565.1; XM_017017076.1. [Q9H422-1]
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; 34.
DR IntAct; Q9H422; 23.
DR MINT; Q9H422; -.
DR STRING; 9606.ENSP00000304226; -.
DR BindingDB; Q9H422; -.
DR ChEMBL; CHEMBL4577; -.
DR DrugBank; DB12010; Fostamatinib.
DR DrugCentral; Q9H422; -.
DR GuidetoPHARMACOLOGY; 2035; -.
DR iPTMnet; Q9H422; -.
DR PhosphoSitePlus; Q9H422; -.
DR BioMuta; HIPK3; -.
DR DMDM; 61213741; -.
DR EPD; Q9H422; -.
DR jPOST; Q9H422; -.
DR MassIVE; Q9H422; -.
DR MaxQB; Q9H422; -.
DR PaxDb; Q9H422; -.
DR PeptideAtlas; Q9H422; -.
DR PRIDE; Q9H422; -.
DR ProteomicsDB; 80780; -. [Q9H422-1]
DR ProteomicsDB; 80781; -. [Q9H422-2]
DR Antibodypedia; 25715; 213 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 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; CQPLKKG; -.
DR OrthoDB; 59821at2759; -.
DR PhylomeDB; Q9H422; -.
DR TreeFam; TF105417; -.
DR PathwayCommons; Q9H422; -.
DR SignaLink; Q9H422; -.
DR SIGNOR; Q9H422; -.
DR BioGRID-ORCS; 10114; 14 hits in 1109 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 193 other tissues.
DR ExpressionAtlas; Q9H422; baseline and differential.
DR Genevisible; Q9H422; HS.
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 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 Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
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
