GRK6_HUMAN
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 03-AUG-2022, entry version 207.
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}.
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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; 56.
DR IntAct; P43250; 102.
DR MINT; P43250; -.
DR STRING; 9606.ENSP00000433511; -.
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; P43250; -.
DR PeptideAtlas; P43250; -.
DR PRIDE; P43250; -.
DR ProteomicsDB; 55602; -. [P43250-1]
DR ProteomicsDB; 55603; -. [P43250-2]
DR ProteomicsDB; 55604; -. [P43250-3]
DR ABCD; P43250; 1 sequenced antibody.
DR Antibodypedia; 17408; 396 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 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; TQCTERL; -.
DR OrthoDB; 1104340at2759; -.
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; 14 hits in 1110 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 201 other tissues.
DR ExpressionAtlas; P43250; baseline and differential.
DR Genevisible; P43250; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:Reactome.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
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 Gene3D; 1.10.167.10; -; 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 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; SSF48097; SSF48097; 1.
DR SUPFAM; SSF56112; SSF56112; 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.
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; 180-
FT fold defects in kinase activity; when associated with A-7."
FT /evidence="ECO:0000269|PubMed:20729810"
FT MUTAGEN 7
FT /note="V->A: 12-13 fold defects in kinase activity; 180-
FT fold defects in kinase activity; when associated with 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
