ID GRK6_HUMAN Reviewed; 576 AA. AC P43250; O60541; Q13652; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2002, sequence version 2. DT 27-MAR-2024, entry version 216. DE RecName: Full=G protein-coupled receptor kinase 6; DE EC=2.7.11.16; DE AltName: Full=G protein-coupled receptor kinase GRK6; GN Name=GRK6; Synonyms=GPRK6; 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 GRK6A). RX PubMed=8366096; DOI=10.1016/s0021-9258(19)36546-9; RA Benovic J.L., Gomez J.; RT "Molecular cloning and expression of GRK6. A new member of the G protein- RT coupled receptor kinase family."; RL J. Biol. Chem. 268:19521-19527(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS GRK6B AND GRK6C). RX PubMed=10506199; DOI=10.1074/jbc.274.41.29381; RA Premont R.T., Macrae A.D., Aparicio S.A., Kendall H.E., Welch J.E., RA Lefkowitz R.J.; RT "The GRK4 subfamily of G protein-coupled receptor kinases. Alternative RT splicing, gene organization, and sequence conservation."; RL J. Biol. Chem. 274:29381-29389(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15372022; DOI=10.1038/nature02919; RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.; RT "The DNA sequence and comparative analysis of human chromosome 5."; RL Nature 431:268-274(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GRK6A). RC TISSUE=Uterus; 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 [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 33-576, AND TISSUE SPECIFICITY. RX PubMed=8415712; DOI=10.1073/pnas.90.20.9398; RA Haribabu B., Snyderman R.; RT "Identification of additional members of human G-protein-coupled receptor RT kinase multigene family."; RL Proc. Natl. Acad. Sci. U.S.A. 90:9398-9402(1993). RN [6] RP PALMITOYLATION AT CYS-561; CYS-562 AND CYS-565, AND MUTAGENESIS OF CYS-561; RP CYS-562 AND CYS-565. RX PubMed=7961702; DOI=10.1016/s0021-9258(18)46852-4; RA Stoffel R.H., Randall R.R., Premont R.T., Lefkowitz R.J., Inglese J.; RT "Palmitoylation of G protein-coupled receptor kinase, GRK6. Lipid RT modification diversity in the GRK family."; RL J. Biol. Chem. 269:27791-27794(1994). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-484 AND THR-485, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [8] RP FUNCTION IN PHOSPHORYLATION OF LRP6. RX PubMed=19801552; DOI=10.1074/jbc.m109.047456; RA Chen M., Philipp M., Wang J., Premont R.T., Garrison T.R., Caron M.G., RA Lefkowitz R.J., Chen W.; RT "G Protein-coupled receptor kinases phosphorylate LRP6 in the Wnt RT pathway."; RL J. Biol. Chem. 284:35040-35048(2009). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-484 AND THR-485, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [10] RP FUNCTION IN PHOSPHORYLATION OF CXCR4. RX PubMed=20048153; DOI=10.1074/jbc.m109.091173; RA Busillo J.M., Armando S., Sengupta R., Meucci O., Bouvier M., Benovic J.L.; RT "Site-specific phosphorylation of CXCR4 is dynamically regulated by RT multiple kinases and results in differential modulation of CXCR4 RT signaling."; RL J. Biol. Chem. 285:7805-7817(2010). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS). RX PubMed=16613860; DOI=10.1074/jbc.m601327200; RA Lodowski D.T., Tesmer V.M., Benovic J.L., Tesmer J.J.; RT "The structure of G protein-coupled receptor kinase (GRK)-6 defines a RT second lineage of GRKs."; RL J. Biol. Chem. 281:16785-16793(2006). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.72 ANGSTROMS) IN COMPLEX WITH AMP AND RP SANGIVAMYCIN, AND MUTAGENESIS OF ILE-6; VAL-7; ASN-9 AND LEU-12. RX PubMed=20729810; DOI=10.1038/emboj.2010.206; RA Boguth C.A., Singh P., Huang C.C., Tesmer J.J.; RT "Molecular basis for activation of G protein-coupled receptor kinases."; RL EMBO J. 29:3249-3259(2010). RN [13] RP VARIANTS [LARGE SCALE ANALYSIS] GLN-31; MET-73 AND MET-275. 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: Specifically phosphorylates the activated forms of G protein- CC coupled receptors. Such receptor phosphorylation initiates beta- CC arrestin-mediated receptor desensitization, internalization, and CC signaling events leading to their desensitization. Seems to be involved CC in the desensitization of D2-like dopamine receptors in striatum and CC chemokine receptor CXCR4 which is critical for CXCL12-induced cell CC chemotaxis (By similarity). Phosphorylates rhodopsin (RHO) (in vitro) CC and a non G-protein-coupled receptor: LRP6 during Wnt signaling (in CC vitro). {ECO:0000250, ECO:0000269|PubMed:19801552, CC ECO:0000269|PubMed:20048153}. CC -!- CATALYTIC ACTIVITY: CC Reaction=[G-protein-coupled receptor] + ATP = [G-protein-coupled CC receptor]-phosphate + ADP + H(+); Xref=Rhea:RHEA:12008, Rhea:RHEA- CC COMP:11260, Rhea:RHEA-COMP:11261, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546, CC ChEBI:CHEBI:456216; EC=2.7.11.16; CC -!- SUBUNIT: Interacts with GIT1. {ECO:0000250|UniProtKB:P97711}. CC -!- INTERACTION: CC P43250; P05067: APP; NbExp=3; IntAct=EBI-722747, EBI-77613; CC P43250; P08238: HSP90AB1; NbExp=2; IntAct=EBI-722747, EBI-352572; CC P43250; P52205: ROM1; Xeno; NbExp=9; IntAct=EBI-722747, EBI-8176947; CC P43250-2; P05067: APP; NbExp=3; IntAct=EBI-6428342, EBI-77613; CC -!- SUBCELLULAR LOCATION: Membrane; Lipid-anchor. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=GRK6A; CC IsoId=P43250-1; Sequence=Displayed; CC Name=GRK6B; CC IsoId=P43250-2; Sequence=VSP_004938; CC Name=GRK6C; CC IsoId=P43250-3; Sequence=VSP_041813, VSP_041814; CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:8415712}. CC -!- PTM: It is uncertain whether palmitoylation is on Cys-561 and/or Cys- CC 562 and/or Cys-565. {ECO:0000269|PubMed:7961702}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr CC protein kinase family. GPRK 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; L16862; AAA60175.1; -; mRNA. DR EMBL; AF040751; AAC09273.1; -; mRNA. DR EMBL; AF040752; AAC09274.1; -; mRNA. DR EMBL; AC145098; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC009277; AAH09277.1; -; mRNA. DR EMBL; U00686; AAA03565.1; -; mRNA. DR CCDS; CCDS34303.1; -. [P43250-1] DR CCDS; CCDS43406.1; -. [P43250-3] DR PIR; A48765; A48765. DR RefSeq; NP_001004105.1; NM_001004105.2. [P43250-3] DR RefSeq; NP_001004106.1; NM_001004106.2. [P43250-1] DR RefSeq; NP_002073.2; NM_002082.3. [P43250-2] DR PDB; 2ACX; X-ray; 2.60 A; A/B=1-576. DR PDB; 3NYN; X-ray; 2.72 A; A/B=2-576. DR PDB; 3NYO; X-ray; 2.92 A; A/B=2-576. DR PDBsum; 2ACX; -. DR PDBsum; 3NYN; -. DR PDBsum; 3NYO; -. DR AlphaFoldDB; P43250; -. DR SMR; P43250; -. DR BioGRID; 109128; 132. DR IntAct; P43250; 102. DR MINT; P43250; -. DR STRING; 9606.ENSP00000347655; -. DR BindingDB; P43250; -. DR ChEMBL; CHEMBL6144; -. DR GuidetoPHARMACOLOGY; 1470; -. DR CarbonylDB; P43250; -. DR iPTMnet; P43250; -. DR PhosphoSitePlus; P43250; -. DR SwissPalm; P43250; -. DR BioMuta; GRK6; -. DR DMDM; 20141386; -. DR EPD; P43250; -. DR jPOST; P43250; -. DR MassIVE; P43250; -. DR MaxQB; P43250; -. DR PaxDb; 9606-ENSP00000433511; -. DR PeptideAtlas; P43250; -. DR ProteomicsDB; 55602; -. [P43250-1] DR ProteomicsDB; 55603; -. [P43250-2] DR ProteomicsDB; 55604; -. [P43250-3] DR Pumba; P43250; -. DR ABCD; P43250; 1 sequenced antibody. DR Antibodypedia; 17408; 442 antibodies from 37 providers. DR DNASU; 2870; -. DR Ensembl; ENST00000355472.10; ENSP00000347655.5; ENSG00000198055.11. [P43250-1] DR Ensembl; ENST00000355958.9; ENSP00000348230.5; ENSG00000198055.11. [P43250-3] DR Ensembl; ENST00000528793.5; ENSP00000433511.1; ENSG00000198055.11. [P43250-2] DR GeneID; 2870; -. DR KEGG; hsa:2870; -. DR MANE-Select; ENST00000355472.10; ENSP00000347655.5; NM_001004106.3; NP_001004106.1. DR UCSC; uc003mgq.3; human. [P43250-1] DR AGR; HGNC:4545; -. DR CTD; 2870; -. DR DisGeNET; 2870; -. DR GeneCards; GRK6; -. DR HGNC; HGNC:4545; GRK6. DR HPA; ENSG00000198055; Tissue enhanced (bone). DR MIM; 600869; gene. DR neXtProt; NX_P43250; -. DR OpenTargets; ENSG00000198055; -. DR PharmGKB; PA28942; -. DR VEuPathDB; HostDB:ENSG00000198055; -. DR eggNOG; KOG0986; Eukaryota. DR GeneTree; ENSGT00940000158544; -. DR InParanoid; P43250; -. DR OMA; NYLNPKC; -. DR OrthoDB; 2906348at2759; -. DR PhylomeDB; P43250; -. DR TreeFam; TF313940; -. DR BRENDA; 2.7.11.16; 2681. DR PathwayCommons; P43250; -. DR Reactome; R-HSA-418555; G alpha (s) signalling events. DR SignaLink; P43250; -. DR SIGNOR; P43250; -. DR BioGRID-ORCS; 2870; 16 hits in 1189 CRISPR screens. DR ChiTaRS; GRK6; human. DR EvolutionaryTrace; P43250; -. DR GeneWiki; GRK6; -. DR GenomeRNAi; 2870; -. DR Pharos; P43250; Tchem. DR PRO; PR:P43250; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; P43250; Protein. DR Bgee; ENSG00000198055; Expressed in granulocyte and 203 other cell types or tissues. DR ExpressionAtlas; P43250; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0047696; F:beta-adrenergic receptor kinase activity; IDA:CACAO. DR GO; GO:0004703; F:G protein-coupled receptor kinase activity; IBA:GO_Central. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:Reactome. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; TAS:ProtInc. DR GO; GO:0009966; P:regulation of signal transduction; IBA:GO_Central. DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW. DR CDD; cd05630; STKc_GRK6; 1. DR Gene3D; 6.10.250.2260; -; 1. DR Gene3D; 1.10.167.10; Regulator of G-protein Signalling 4, domain 2; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR000961; AGC-kinase_C. DR InterPro; IPR000239; GPCR_kinase. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR016137; RGS. DR InterPro; IPR036305; RGS_sf. DR InterPro; IPR044926; RGS_subdomain_2. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR24355:SF15; G PROTEIN-COUPLED RECEPTOR KINASE 6; 1. DR PANTHER; PTHR24355; G PROTEIN-COUPLED RECEPTOR KINASE/RIBOSOMAL PROTEIN S6 KINASE; 1. DR Pfam; PF00069; Pkinase; 1. DR Pfam; PF00615; RGS; 1. DR PRINTS; PR00717; GPCRKINASE. DR SMART; SM00315; RGS; 1. DR SMART; SM00133; S_TK_X; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR SUPFAM; SSF48097; Regulator of G-protein signaling, RGS; 1. DR PROSITE; PS51285; AGC_KINASE_CTER; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50132; RGS; 1. DR Genevisible; P43250; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ATP-binding; Kinase; Lipoprotein; KW Membrane; Nucleotide-binding; Palmitate; Phosphoprotein; KW Reference proteome; Serine/threonine-protein kinase; Transferase; KW Wnt signaling pathway. FT CHAIN 1..576 FT /note="G protein-coupled receptor kinase 6" FT /id="PRO_0000085974" FT DOMAIN 53..171 FT /note="RGS" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171" FT DOMAIN 186..448 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT DOMAIN 449..514 FT /note="AGC-kinase C-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618" FT REGION 1..185 FT /note="N-terminal" FT ACT_SITE 311 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 192..200 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT BINDING 215 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT BINDING 264..270 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT BINDING 315..318 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT MOD_RES 484 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332" FT MOD_RES 485 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332" FT MOD_RES 566 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O70293" FT MOD_RES 568 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O70293" FT LIPID 561 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000305|PubMed:7961702" FT LIPID 562 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000305|PubMed:7961702" FT LIPID 565 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000305|PubMed:7961702" FT VAR_SEQ 560..576 FT /note="DCCGNCSDSEEELPTRL -> RIAVETAATARKSSPPASSPQPEAPTSSWR FT (in isoform GRK6B)" FT /evidence="ECO:0000303|PubMed:10506199" FT /id="VSP_004938" FT VAR_SEQ 560 FT /note="D -> R (in isoform GRK6C)" FT /evidence="ECO:0000303|PubMed:10506199" FT /id="VSP_041813" FT VAR_SEQ 561..576 FT /note="Missing (in isoform GRK6C)" FT /evidence="ECO:0000303|PubMed:10506199" FT /id="VSP_041814" FT VARIANT 31 FT /note="R -> Q (in a gastric adenocarcinoma sample; somatic FT mutation; dbSNP:rs141014084)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040524" FT VARIANT 73 FT /note="T -> M (in dbSNP:rs56382815)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040525" FT VARIANT 275 FT /note="I -> M (in a breast infiltrating ductal carcinoma FT sample; somatic mutation)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040526" FT MUTAGEN 6 FT /note="I->A: 12-13 fold defects in kinase activity; FT 180-fold defects in kinase activity; when associated with FT A-7." FT /evidence="ECO:0000269|PubMed:20729810" FT MUTAGEN 7 FT /note="V->A: 12-13 fold defects in kinase activity; FT 180-fold defects in kinase activity; when associated with FT A-6." FT /evidence="ECO:0000269|PubMed:20729810" FT MUTAGEN 9 FT /note="N->A: 140-fold defects in kinase activity." FT /evidence="ECO:0000269|PubMed:20729810" FT MUTAGEN 12 FT /note="L->A: 1100-fold defects in kinase activity." FT /evidence="ECO:0000269|PubMed:20729810" FT MUTAGEN 561 FT /note="C->S: Abolishes palmitoylation; when associated with FT S-562 and S-565." FT /evidence="ECO:0000269|PubMed:7961702" FT MUTAGEN 562 FT /note="C->S: Abolishes palmitoylation; when associated with FT S-561 and S-565." FT /evidence="ECO:0000269|PubMed:7961702" FT MUTAGEN 565 FT /note="C->S: Abolishes palmitoylation; when associated with FT S-561 and S-562." FT /evidence="ECO:0000269|PubMed:7961702" FT CONFLICT 60..61 FT /note="QP -> HA (in Ref. 1; AAA60175)" FT /evidence="ECO:0000305" FT CONFLICT 104..105 FT /note="QL -> HV (in Ref. 1; AAA60175)" FT /evidence="ECO:0000305" FT HELIX 3..18 FT /evidence="ECO:0007829|PDB:3NYN" FT STRAND 23..25 FT /evidence="ECO:0007829|PDB:3NYN" FT HELIX 30..33 FT /evidence="ECO:0007829|PDB:2ACX" FT HELIX 40..42 FT /evidence="ECO:0007829|PDB:2ACX" FT HELIX 43..48 FT /evidence="ECO:0007829|PDB:2ACX" FT HELIX 53..57 FT /evidence="ECO:0007829|PDB:2ACX" FT HELIX 61..71 FT /evidence="ECO:0007829|PDB:2ACX" FT HELIX 75..91 FT /evidence="ECO:0007829|PDB:2ACX" FT TURN 95..97 FT /evidence="ECO:0007829|PDB:2ACX" FT HELIX 98..109 FT /evidence="ECO:0007829|PDB:2ACX" FT STRAND 112..114 FT /evidence="ECO:0007829|PDB:2ACX" FT STRAND 117..120 FT /evidence="ECO:0007829|PDB:3NYN" FT HELIX 123..135 FT /evidence="ECO:0007829|PDB:2ACX" FT TURN 139..142 FT /evidence="ECO:0007829|PDB:2ACX" FT HELIX 143..153 FT /evidence="ECO:0007829|PDB:2ACX" FT HELIX 156..162 FT /evidence="ECO:0007829|PDB:2ACX" FT HELIX 165..177 FT /evidence="ECO:0007829|PDB:2ACX" FT HELIX 183..185 FT /evidence="ECO:0007829|PDB:2ACX" FT STRAND 186..195 FT /evidence="ECO:0007829|PDB:2ACX" FT STRAND 198..205 FT /evidence="ECO:0007829|PDB:2ACX" FT TURN 206..208 FT /evidence="ECO:0007829|PDB:2ACX" FT STRAND 211..218 FT /evidence="ECO:0007829|PDB:2ACX" FT HELIX 219..224 FT /evidence="ECO:0007829|PDB:2ACX" FT HELIX 228..240 FT /evidence="ECO:0007829|PDB:2ACX" FT STRAND 249..254 FT /evidence="ECO:0007829|PDB:2ACX" FT STRAND 256..263 FT /evidence="ECO:0007829|PDB:2ACX" FT HELIX 271..276 FT /evidence="ECO:0007829|PDB:2ACX" FT STRAND 277..280 FT /evidence="ECO:0007829|PDB:2ACX" FT HELIX 285..304 FT /evidence="ECO:0007829|PDB:2ACX" FT HELIX 314..316 FT /evidence="ECO:0007829|PDB:2ACX" FT STRAND 317..319 FT /evidence="ECO:0007829|PDB:2ACX" FT STRAND 325..327 FT /evidence="ECO:0007829|PDB:2ACX" FT HELIX 349..351 FT /evidence="ECO:0007829|PDB:2ACX" FT HELIX 354..357 FT /evidence="ECO:0007829|PDB:2ACX" FT STRAND 361..364 FT /evidence="ECO:0007829|PDB:2ACX" FT HELIX 365..380 FT /evidence="ECO:0007829|PDB:2ACX" FT STRAND 384..386 FT /evidence="ECO:0007829|PDB:2ACX" FT STRAND 388..390 FT /evidence="ECO:0007829|PDB:2ACX" FT HELIX 394..403 FT /evidence="ECO:0007829|PDB:2ACX" FT STRAND 410..412 FT /evidence="ECO:0007829|PDB:3NYN" FT HELIX 414..423 FT /evidence="ECO:0007829|PDB:2ACX" FT HELIX 428..430 FT /evidence="ECO:0007829|PDB:2ACX" FT STRAND 435..437 FT /evidence="ECO:0007829|PDB:2ACX" FT HELIX 438..443 FT /evidence="ECO:0007829|PDB:2ACX" FT HELIX 446..448 FT /evidence="ECO:0007829|PDB:2ACX" FT HELIX 453..457 FT /evidence="ECO:0007829|PDB:2ACX" FT HELIX 477..479 FT /evidence="ECO:0007829|PDB:3NYO" FT HELIX 493..502 FT /evidence="ECO:0007829|PDB:2ACX" FT HELIX 508..517 FT /evidence="ECO:0007829|PDB:2ACX" FT HELIX 520..525 FT /evidence="ECO:0007829|PDB:2ACX" FT STRAND 527..530 FT /evidence="ECO:0007829|PDB:2ACX" FT HELIX 549..555 FT /evidence="ECO:0007829|PDB:3NYN" SQ SEQUENCE 576 AA; 65991 MW; 3BF8C3B1CDE2BD74 CRC64; MELENIVANT VLLKAREGGG GNRKGKSKKW RQMLQFPHIS QCEELRLSLE RDYHSLCERQ PIGRLLFREF CATRPELSRC VAFLDGVAEY EVTPDDKRKA CGRQLTQNFL SHTGPDLIPE VPRQLVTNCT QRLEQGPCKD LFQELTRLTH EYLSVAPFAD YLDSIYFNRF LQWKWLERQP VTKNTFRQYR VLGKGGFGEV CACQVRATGK MYACKKLEKK RIKKRKGEAM ALNEKQILEK VNSRFVVSLA YAYETKDALC LVLTLMNGGD LKFHIYHMGQ AGFPEARAVF YAAEICCGLE DLHRERIVYR DLKPENILLD DHGHIRISDL GLAVHVPEGQ TIKGRVGTVG YMAPEVVKNE RYTFSPDWWA LGCLLYEMIA GQSPFQQRKK KIKREEVERL VKEVPEEYSE RFSPQARSLC SQLLCKDPAE RLGCRGGSAR EVKEHPLFKK LNFKRLGAGM LEPPFKPDPQ AIYCKDVLDI EQFSTVKGVE LEPTDQDFYQ KFATGSVPIP WQNEMVETEC FQELNVFGLD GSVPPDLDWK GQPPAPPKKG LLQRLFSRQD CCGNCSDSEE ELPTRL //