GRK1_BOVIN
ID GRK1_BOVIN Reviewed; 561 AA.
AC P28327;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Rhodopsin kinase GRK1;
DE Short=RK;
DE EC=2.7.11.14 {ECO:0000269|PubMed:12686556, ECO:0000269|PubMed:1527025, ECO:0000269|PubMed:16675451, ECO:0000269|PubMed:1730692, ECO:0000269|PubMed:21299498};
DE AltName: Full=G protein-coupled receptor kinase 1;
DE Flags: Precursor;
GN Name=GRK1; Synonyms=RHOK;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 268-297, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Retina;
RX PubMed=1656454; DOI=10.1073/pnas.88.19.8715;
RA Lorenz W., Inglese J., Palczewski K., Onorato J.J., Caron M.G.,
RA Lefkowitz R.J.;
RT "The receptor kinase family: primary structure of rhodopsin kinase reveals
RT similarities to the beta-adrenergic receptor kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:8715-8719(1991).
RN [2]
RP ISOPRENYLATION AT CYS-558, METHYLATION AT CYS-558, MUTAGENESIS OF CYS-558,
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=1730692; DOI=10.1016/s0021-9258(18)45960-1;
RA Inglese J., Glickman J.F., Lorenz W., Caron M.G., Lefkowitz R.J.;
RT "Isoprenylation of a protein kinase. Requirement of farnesylation/alpha-
RT carboxyl methylation for full enzymatic activity of rhodopsin kinase.";
RL J. Biol. Chem. 267:1422-1425(1992).
RN [3]
RP PHOSPHORYLATION AT SER-21; SER-488 AND THR-489, PARTIAL PROTEIN SEQUENCE,
RP IDENTIFICATION BY MASS SPECTROMETRY, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=1527025; DOI=10.1016/s0021-9258(19)37058-9;
RA Palczewski K., Buczylko J., van Hooser P., Carr S.A., Huddleston M.J.,
RA Crabb J.W.;
RT "Identification of the autophosphorylation sites in rhodopsin kinase.";
RL J. Biol. Chem. 267:18991-18998(1992).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=12686556; DOI=10.1074/jbc.m300447200;
RA Weiergraeber O.H., Senin I.I., Philippov P.P., Granzin J., Koch K.W.;
RT "Impact of N-terminal myristoylation on the Ca2+-dependent conformational
RT transition in recoverin.";
RL J. Biol. Chem. 278:22972-22979(2003).
RN [5]
RP INTERACTION WITH PDE6D, AND SUBCELLULAR LOCATION.
RX PubMed=14561760; DOI=10.1074/jbc.m306559200;
RA Zhang H., Liu X.H., Zhang K., Chen C.K., Frederick J.M., Prestwich G.D.,
RA Baehr W.;
RT "Photoreceptor cGMP phosphodiesterase delta subunit (PDEdelta) functions as
RT a prenyl-binding protein.";
RL J. Biol. Chem. 279:407-413(2004).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH RCVRN, AND MUTAGENESIS OF
RP 1-MET--SER-31.
RX PubMed=16675451; DOI=10.1074/jbc.m602203200;
RA Higgins M.K., Oprian D.D., Schertler G.F.;
RT "Recoverin binds exclusively to an amphipathic peptide at the N terminus of
RT rhodopsin kinase, inhibiting rhodopsin phosphorylation without affecting
RT catalytic activity of the kinase.";
RL J. Biol. Chem. 281:19426-19432(2006).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, INTERACTION WITH RCVRN,
RP AND MUTAGENESIS OF PHE-3.
RX PubMed=21299498; DOI=10.1042/bj20110013;
RA Zernii E.Y., Komolov K.E., Permyakov S.E., Kolpakova T., Dell'orco D.,
RA Poetzsch A., Knyazeva E.L., Grigoriev I.I., Permyakov E.A., Senin I.I.,
RA Philippov P.P., Koch K.W.;
RT "Involvement of the recoverin C-terminal segment in recognition of the
RT target enzyme rhodopsin kinase.";
RL Biochem. J. 435:441-450(2011).
RN [8]
RP INTERACTION WITH RCVRN.
RX PubMed=24189072; DOI=10.1074/jbc.m113.524355;
RA Ranaghan M.J., Kumar R.P., Chakrabarti K.S., Buosi V., Kern D.,
RA Oprian D.D.;
RT "A highly conserved cysteine of neuronal calcium-sensing proteins controls
RT cooperative binding of Ca2+ to recoverin.";
RL J. Biol. Chem. 288:36160-36167(2013).
RN [9]
RP INTERACTION WITH RCVRN.
RX PubMed=26584024; DOI=10.1021/acs.biochem.5b01160;
RA Kumar R.P., Ranaghan M.J., Ganjei A.Y., Oprian D.D.;
RT "Crystal Structure of Recoverin with Calcium Ions Bound to Both Functional
RT EF Hands.";
RL Biochemistry 54:7222-7228(2015).
RN [10] {ECO:0007744|PDB:2I94}
RP STRUCTURE BY NMR OF 1-25, AND INTERACTION WITH RCVRN AND RHO.
RX PubMed=17020884; DOI=10.1074/jbc.m606913200;
RA Ames J.B., Levay K., Wingard J.N., Lusin J.D., Slepak V.Z.;
RT "Structural basis for calcium-induced inhibition of rhodopsin kinase by
RT recoverin.";
RL J. Biol. Chem. 281:37237-37245(2006).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF 1-535 IN COMPLEX WITH ATP, AND
RP PHOSPHORYLATION AT SER-5; THR-8; SER-21; SER-488 AND THR-489.
RX PubMed=18339619; DOI=10.1074/jbc.m708974200;
RA Singh P., Wang B., Maeda T., Palczewski K., Tesmer J.J.;
RT "Structures of rhodopsin kinase in different ligand states reveal key
RT elements involved in G protein-coupled receptor kinase activation.";
RL J. Biol. Chem. 283:14053-14062(2008).
CC -!- FUNCTION: Retina-specific kinase involved in the signal turnoff via
CC phosphorylation of rhodopsin (RHO), the G protein- coupled receptor
CC that initiates the phototransduction cascade (PubMed:12686556,
CC PubMed:16675451, PubMed:21299498). This rapid desensitization is
CC essential for scotopic vision and permits rapid adaptation to changes
CC in illumination (By similarity). May play a role in the maintenance of
CC the outer nuclear layer in the retina (By similarity).
CC {ECO:0000250|UniProtKB:Q9WVL4, ECO:0000269|PubMed:12686556,
CC ECO:0000269|PubMed:16675451, ECO:0000269|PubMed:21299498}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[rhodopsin] = ADP + H(+) + O-phospho-L-
CC threonyl-[rhodopsin]; Xref=Rhea:RHEA:56552, Rhea:RHEA-COMP:14596,
CC Rhea:RHEA-COMP:14597, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.14; Evidence={ECO:0000269|PubMed:12686556,
CC ECO:0000269|PubMed:1527025, ECO:0000269|PubMed:16675451,
CC ECO:0000269|PubMed:1730692, ECO:0000269|PubMed:21299498};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[rhodopsin] = ADP + H(+) + O-phospho-L-seryl-
CC [rhodopsin]; Xref=Rhea:RHEA:23356, Rhea:RHEA-COMP:14594, Rhea:RHEA-
CC COMP:14595, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.14;
CC Evidence={ECO:0000269|PubMed:12686556, ECO:0000269|PubMed:1527025,
CC ECO:0000269|PubMed:16675451, ECO:0000269|PubMed:1730692,
CC ECO:0000269|PubMed:21299498};
CC -!- ACTIVITY REGULATION: Inhibited by RCVRN, which prevents the interaction
CC between GRK1 and RHO (PubMed:12686556, PubMed:21299498). Inhibition is
CC calcium-dependent (PubMed:12686556). {ECO:0000269|PubMed:12686556,
CC ECO:0000269|PubMed:21299498}.
CC -!- SUBUNIT: Interacts (via N-terminus) with RCVRN (via C-terminus); the
CC interaction is Ca(2+)-dependent (PubMed:16675451, PubMed:17020884,
CC PubMed:21299498, PubMed:24189072, PubMed:26584024). Interacts (when
CC prenylated) with PDE6D; this promotes release from membranes
CC (PubMed:14561760). May form a complex composed of RHO, GRK1 and RCVRN
CC in a Ca(2+)-dependent manner; RCVRN prevents the interaction between
CC GRK1 and RHO (PubMed:17020884). {ECO:0000269|PubMed:14561760,
CC ECO:0000269|PubMed:16675451, ECO:0000269|PubMed:17020884,
CC ECO:0000269|PubMed:21299498, ECO:0000269|PubMed:24189072,
CC ECO:0000269|PubMed:26584024}.
CC -!- INTERACTION:
CC P28327; P21457: RCVRN; NbExp=2; IntAct=EBI-7865560, EBI-8592784;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:14561760,
CC ECO:0000269|PubMed:1527025, ECO:0000305|PubMed:1730692}; Lipid-anchor
CC {ECO:0000269|PubMed:14561760, ECO:0000305|PubMed:1730692}. Cell
CC projection, cilium, photoreceptor outer segment
CC {ECO:0000250|UniProtKB:Q9WVL4}. Note=Subcellular location is not
CC affected by light or dark conditions. {ECO:0000250|UniProtKB:Q9WVL4}.
CC -!- TISSUE SPECIFICITY: Rod outer segments of retina photoreceptor cells
CC (at protein level) (PubMed:1656454, PubMed:1730692, PubMed:1527025).
CC Retina (PubMed:1656454). {ECO:0000269|PubMed:1527025,
CC ECO:0000269|PubMed:1656454, ECO:0000269|PubMed:1730692}.
CC -!- PTM: Autophosphorylated, Ser-21 is a minor site of autophosphorylation
CC compared to Ser-488 and Thr-489. Phosphorylation at Ser-21 is regulated
CC by light and activated by cAMP (Probable). {ECO:0000305|PubMed:1527025,
CC ECO:0000305|PubMed:18339619}.
CC -!- PTM: Farnesylation is required for full activity.
CC {ECO:0000269|PubMed:1730692}.
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; M73836; AAA30752.1; -; mRNA.
DR PIR; A41365; A41365.
DR RefSeq; NP_776598.1; NM_174173.2.
DR PDB; 2I94; NMR; -; B=1-25.
DR PDB; 3C4W; X-ray; 2.70 A; A/B=1-535.
DR PDB; 3C4X; X-ray; 2.90 A; A/B=1-535.
DR PDB; 3C4Y; X-ray; 7.51 A; A/B=1-535.
DR PDB; 3C4Z; X-ray; 1.84 A; A=1-535.
DR PDB; 3C50; X-ray; 2.60 A; A/B=1-535.
DR PDB; 3C51; X-ray; 3.55 A; A/B=1-535.
DR PDB; 3QC9; X-ray; 2.70 A; A/B/C/D=1-535.
DR PDB; 3T8O; X-ray; 2.50 A; A=1-535.
DR PDB; 4L9I; X-ray; 2.32 A; A/B=30-533.
DR PDB; 4PNI; X-ray; 1.85 A; A=1-561.
DR PDB; 4WBO; X-ray; 2.81 A; A/B/C/D=1-535.
DR PDB; 7MT8; EM; 5.80 A; G=1-535.
DR PDB; 7MT9; EM; 7.00 A; G=1-535.
DR PDB; 7MTA; EM; 4.10 A; G=1-535.
DR PDB; 7MTB; EM; 4.00 A; G=1-535.
DR PDBsum; 2I94; -.
DR PDBsum; 3C4W; -.
DR PDBsum; 3C4X; -.
DR PDBsum; 3C4Y; -.
DR PDBsum; 3C4Z; -.
DR PDBsum; 3C50; -.
DR PDBsum; 3C51; -.
DR PDBsum; 3QC9; -.
DR PDBsum; 3T8O; -.
DR PDBsum; 4L9I; -.
DR PDBsum; 4PNI; -.
DR PDBsum; 4WBO; -.
DR PDBsum; 7MT8; -.
DR PDBsum; 7MT9; -.
DR PDBsum; 7MTA; -.
DR PDBsum; 7MTB; -.
DR AlphaFoldDB; P28327; -.
DR BMRB; P28327; -.
DR SMR; P28327; -.
DR BioGRID; 158786; 1.
DR IntAct; P28327; 3.
DR MINT; P28327; -.
DR STRING; 9913.ENSBTAP00000042484; -.
DR BindingDB; P28327; -.
DR ChEMBL; CHEMBL3879860; -.
DR iPTMnet; P28327; -.
DR PaxDb; P28327; -.
DR PRIDE; P28327; -.
DR Ensembl; ENSBTAT00000045068; ENSBTAP00000042484; ENSBTAG00000019963.
DR GeneID; 281457; -.
DR KEGG; bta:281457; -.
DR CTD; 6011; -.
DR VEuPathDB; HostDB:ENSBTAG00000019963; -.
DR VGNC; VGNC:29654; GRK1.
DR eggNOG; KOG0986; Eukaryota.
DR GeneTree; ENSGT00940000159927; -.
DR HOGENOM; CLU_000288_63_41_1; -.
DR InParanoid; P28327; -.
DR OMA; PASKSGM; -.
DR OrthoDB; 1104340at2759; -.
DR TreeFam; TF313940; -.
DR BioCyc; MetaCyc:MON-4461; -.
DR BRENDA; 2.7.11.14; 908.
DR SABIO-RK; P28327; -.
DR EvolutionaryTrace; P28327; -.
DR Proteomes; UP000009136; Chromosome 12.
DR Bgee; ENSBTAG00000019963; Expressed in retina and 3 other tissues.
DR ExpressionAtlas; P28327; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0097381; C:photoreceptor disc membrane; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004703; F:G protein-coupled receptor kinase activity; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0050254; F:rhodopsin kinase activity; ISS:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0022400; P:regulation of rhodopsin mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0009966; P:regulation of signal transduction; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR CDD; cd05608; STKc_GRK1; 1.
DR Gene3D; 1.10.167.10; -; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR000239; GPCR_kinase.
DR InterPro; IPR032965; GRK1.
DR InterPro; IPR037716; GRK1_dom.
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:SF11; PTHR24355:SF11; 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; 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; ATP-binding; Cell projection; Direct protein sequencing;
KW Kinase; Lipoprotein; Membrane; Methylation; Nucleotide-binding;
KW Phosphoprotein; Prenylation; Reference proteome; Sensory transduction;
KW Serine/threonine-protein kinase; Transferase; Vision.
FT CHAIN 1..558
FT /note="Rhodopsin kinase GRK1"
FT /id="PRO_0000024373"
FT PROPEP 559..561
FT /note="Removed in mature form"
FT /id="PRO_0000024374"
FT DOMAIN 58..172
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT DOMAIN 187..452
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000269|PubMed:18339619"
FT DOMAIN 453..518
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 1..186
FT /note="N-terminal"
FT REGION 1..15
FT /note="Interaction with RCVRN"
FT /evidence="ECO:0000269|PubMed:16675451,
FT ECO:0000269|PubMed:17020884"
FT REGION 453..561
FT /note="C-terminal"
FT REGION 536..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 314
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 193..201
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000269|PubMed:18339619"
FT BINDING 216
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 265..267
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:18339619"
FT BINDING 332
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:18339619"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18339619"
FT MOD_RES 8
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18339619"
FT MOD_RES 21
FT /note="Phosphoserine; by PKA and autocatalysis"
FT /evidence="ECO:0000305|PubMed:1527025,
FT ECO:0000305|PubMed:18339619"
FT MOD_RES 488
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:1527025,
FT ECO:0000269|PubMed:18339619"
FT MOD_RES 489
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:1527025,
FT ECO:0000269|PubMed:18339619"
FT MOD_RES 558
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000269|PubMed:1730692"
FT LIPID 558
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000269|PubMed:1730692"
FT MUTAGEN 1..31
FT /note="Missing: Abolishes phosphorylation of RHO."
FT /evidence="ECO:0000269|PubMed:16675451"
FT MUTAGEN 3
FT /note="F->A: Reduces interaction with RCVRN."
FT /evidence="ECO:0000269|PubMed:21299498"
FT MUTAGEN 558
FT /note="C->S: 75% decrease in enzymatic activity."
FT /evidence="ECO:0000269|PubMed:1730692"
FT HELIX 13..17
FT /evidence="ECO:0007829|PDB:3C4W"
FT HELIX 20..23
FT /evidence="ECO:0007829|PDB:3C4W"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:3C4W"
FT HELIX 33..36
FT /evidence="ECO:0007829|PDB:3C4Z"
FT HELIX 44..47
FT /evidence="ECO:0007829|PDB:3C4Z"
FT HELIX 48..53
FT /evidence="ECO:0007829|PDB:3C4Z"
FT HELIX 58..62
FT /evidence="ECO:0007829|PDB:3C4Z"
FT HELIX 66..78
FT /evidence="ECO:0007829|PDB:3C4Z"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:3C4Z"
FT HELIX 83..96
FT /evidence="ECO:0007829|PDB:3C4Z"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:3C4Z"
FT HELIX 103..114
FT /evidence="ECO:0007829|PDB:3C4Z"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:3QC9"
FT HELIX 128..135
FT /evidence="ECO:0007829|PDB:3C4Z"
FT TURN 140..143
FT /evidence="ECO:0007829|PDB:4PNI"
FT HELIX 144..154
FT /evidence="ECO:0007829|PDB:3C4Z"
FT HELIX 157..163
FT /evidence="ECO:0007829|PDB:3C4Z"
FT HELIX 166..178
FT /evidence="ECO:0007829|PDB:3C4Z"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:3C4Z"
FT STRAND 187..195
FT /evidence="ECO:0007829|PDB:3C4Z"
FT STRAND 197..206
FT /evidence="ECO:0007829|PDB:3C4Z"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:3C4Z"
FT STRAND 212..219
FT /evidence="ECO:0007829|PDB:3C4Z"
FT HELIX 220..225
FT /evidence="ECO:0007829|PDB:3C4Z"
FT HELIX 229..241
FT /evidence="ECO:0007829|PDB:3C4Z"
FT STRAND 250..255
FT /evidence="ECO:0007829|PDB:3C4Z"
FT STRAND 257..264
FT /evidence="ECO:0007829|PDB:3C4Z"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:3C4W"
FT HELIX 272..277
FT /evidence="ECO:0007829|PDB:3C4Z"
FT STRAND 278..283
FT /evidence="ECO:0007829|PDB:4PNI"
FT HELIX 288..307
FT /evidence="ECO:0007829|PDB:3C4Z"
FT HELIX 317..319
FT /evidence="ECO:0007829|PDB:3C4Z"
FT STRAND 320..322
FT /evidence="ECO:0007829|PDB:3C4Z"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:3C4Z"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:4PNI"
FT TURN 353..355
FT /evidence="ECO:0007829|PDB:3C4Z"
FT HELIX 358..361
FT /evidence="ECO:0007829|PDB:3C4Z"
FT HELIX 369..384
FT /evidence="ECO:0007829|PDB:3C4Z"
FT STRAND 385..387
FT /evidence="ECO:0007829|PDB:3T8O"
FT STRAND 388..390
FT /evidence="ECO:0007829|PDB:4L9I"
FT HELIX 398..407
FT /evidence="ECO:0007829|PDB:3C4Z"
FT HELIX 418..427
FT /evidence="ECO:0007829|PDB:3C4Z"
FT HELIX 432..434
FT /evidence="ECO:0007829|PDB:3C4Z"
FT HELIX 444..447
FT /evidence="ECO:0007829|PDB:3C4Z"
FT HELIX 450..452
FT /evidence="ECO:0007829|PDB:3C4Z"
FT HELIX 457..461
FT /evidence="ECO:0007829|PDB:3C4Z"
FT STRAND 473..475
FT /evidence="ECO:0007829|PDB:3C4Z"
FT HELIX 481..483
FT /evidence="ECO:0007829|PDB:4L9I"
FT HELIX 497..506
FT /evidence="ECO:0007829|PDB:3C4Z"
FT HELIX 512..521
FT /evidence="ECO:0007829|PDB:3C4Z"
FT HELIX 524..528
FT /evidence="ECO:0007829|PDB:3C4Z"
SQ SEQUENCE 561 AA; 62934 MW; 1AC6FEC1B277DDD8 CRC64;
MDFGSLETVV ANSAFIAARG SFDASSGPAS RDRKYLARLK LPPLSKCEAL RESLDLGFEG
MCLEQPIGKR LFQQFLRTHE QHGPALQLWK DIEDYDTADD ALRPQKAQAL RAAYLEPQAQ
LFCSFLDAET VARARAGAGD GLFQPLLRAV LAHLGQAPFQ EFLDSLYFLR FLQWKWLEAQ
PMGEDWFLDF RVLGRGGFGE VFACQMKATG KLYACKKLNK KRLKKRKGYQ GAMVEKKILA
KVHSRFIVSL AYAFETKTDL CLVMTIMNGG DIRYHIYNVD EDNPGFQEPR AIFYTAQIVS
GLEHLHQRNI IYRDLKPENV LLDDDGNVRI SDLGLAVELK AGQTKTKGYA GTPGFMAPEL
LLGEEYDFSV DYFALGVTLY EMIAARGPFR ARGEKVENKE LKQRVLEQAV TYPDKFSPAS
KDFCEALLQK DPEKRLGFRD GSCDGLRTHP LFRDISWRQL EAGMLTPPFV PDSRTVYAKN
IQDVGAFSTV KGVAFEKADT EFFQEFASGT CPIPWQEEMI ETGVFGDLNV WRPDGQMPDD
MKGVSGQEAA PSSKSGMCVL S
