PINK1_TRICA
ID PINK1_TRICA Reviewed; 570 AA.
AC D6WMX4;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Serine/threonine-protein kinase Pink1, mitochondrial {ECO:0000303|PubMed:22645651};
DE EC=2.7.11.1 {ECO:0000269|PubMed:25474007, ECO:0000269|PubMed:26116755, ECO:0000269|PubMed:26784449, ECO:0000269|PubMed:28980524, ECO:0000269|PubMed:29475881, ECO:0000269|PubMed:29991771, ECO:0000269|PubMed:32484300};
DE AltName: Full=PTEN-induced putative kinase 1 {ECO:0000303|PubMed:22645651};
DE Flags: Precursor;
GN Name=Pink1 {ECO:0000303|PubMed:22645651};
GN ORFNames=TcasGA2_TC013202 {ECO:0000312|EMBL:EFA03268.1};
OS Tribolium castaneum (Red flour beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Tenebrionidae; Tenebrionidae incertae sedis; Tribolium.
OX NCBI_TaxID=7070 {ECO:0000312|Proteomes:UP000007266};
RN [1] {ECO:0000312|Proteomes:UP000007266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Georgia GA2 {ECO:0000312|Proteomes:UP000007266};
RX PubMed=18362917; DOI=10.1038/nature06784;
RG Tribolium Genome Sequencing Consortium;
RA Richards S., Gibbs R.A., Weinstock G.M., Brown S.J., Denell R.,
RA Beeman R.W., Gibbs R., Beeman R.W., Brown S.J., Bucher G., Friedrich M.,
RA Grimmelikhuijzen C.J., Klingler M., Lorenzen M., Richards S., Roth S.,
RA Schroder R., Tautz D., Zdobnov E.M., Muzny D., Gibbs R.A., Weinstock G.M.,
RA Attaway T., Bell S., Buhay C.J., Chandrabose M.N., Chavez D.,
RA Clerk-Blankenburg K.P., Cree A., Dao M., Davis C., Chacko J., Dinh H.,
RA Dugan-Rocha S., Fowler G., Garner T.T., Garnes J., Gnirke A., Hawes A.,
RA Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N., Joshi V.,
RA Khan Z.M., Jackson L., Kovar C., Kowis A., Lee S., Lewis L.R., Margolis J.,
RA Morgan M., Nazareth L.V., Nguyen N., Okwuonu G., Parker D., Richards S.,
RA Ruiz S.J., Santibanez J., Savard J., Scherer S.E., Schneider B.,
RA Sodergren E., Tautz D., Vattahil S., Villasana D., White C.S., Wright R.,
RA Park Y., Beeman R.W., Lord J., Oppert B., Lorenzen M., Brown S., Wang L.,
RA Savard J., Tautz D., Richards S., Weinstock G., Gibbs R.A., Liu Y.,
RA Worley K., Weinstock G., Elsik C.G., Reese J.T., Elhaik E., Landan G.,
RA Graur D., Arensburger P., Atkinson P., Beeman R.W., Beidler J., Brown S.J.,
RA Demuth J.P., Drury D.W., Du Y.Z., Fujiwara H., Lorenzen M., Maselli V.,
RA Osanai M., Park Y., Robertson H.M., Tu Z., Wang J.J., Wang S., Richards S.,
RA Song H., Zhang L., Sodergren E., Werner D., Stanke M., Morgenstern B.,
RA Solovyev V., Kosarev P., Brown G., Chen H.C., Ermolaeva O., Hlavina W.,
RA Kapustin Y., Kiryutin B., Kitts P., Maglott D., Pruitt K., Sapojnikov V.,
RA Souvorov A., Mackey A.J., Waterhouse R.M., Wyder S., Zdobnov E.M.,
RA Zdobnov E.M., Wyder S., Kriventseva E.V., Kadowaki T., Bork P., Aranda M.,
RA Bao R., Beermann A., Berns N., Bolognesi R., Bonneton F., Bopp D.,
RA Brown S.J., Bucher G., Butts T., Chaumot A., Denell R.E., Ferrier D.E.,
RA Friedrich M., Gordon C.M., Jindra M., Klingler M., Lan Q., Lattorff H.M.,
RA Laudet V., von Levetsow C., Liu Z., Lutz R., Lynch J.A., da Fonseca R.N.,
RA Posnien N., Reuter R., Roth S., Savard J., Schinko J.B., Schmitt C.,
RA Schoppmeier M., Schroder R., Shippy T.D., Simonnet F., Marques-Souza H.,
RA Tautz D., Tomoyasu Y., Trauner J., Van der Zee M., Vervoort M.,
RA Wittkopp N., Wimmer E.A., Yang X., Jones A.K., Sattelle D.B., Ebert P.R.,
RA Nelson D., Scott J.G., Beeman R.W., Muthukrishnan S., Kramer K.J.,
RA Arakane Y., Beeman R.W., Zhu Q., Hogenkamp D., Dixit R., Oppert B.,
RA Jiang H., Zou Z., Marshall J., Elpidina E., Vinokurov K., Oppert C.,
RA Zou Z., Evans J., Lu Z., Zhao P., Sumathipala N., Altincicek B.,
RA Vilcinskas A., Williams M., Hultmark D., Hetru C., Jiang H.,
RA Grimmelikhuijzen C.J., Hauser F., Cazzamali G., Williamson M., Park Y.,
RA Li B., Tanaka Y., Predel R., Neupert S., Schachtner J., Verleyen P.,
RA Raible F., Bork P., Friedrich M., Walden K.K., Robertson H.M., Angeli S.,
RA Foret S., Bucher G., Schuetz S., Maleszka R., Wimmer E.A., Beeman R.W.,
RA Lorenzen M., Tomoyasu Y., Miller S.C., Grossmann D., Bucher G.;
RT "The genome of the model beetle and pest Tribolium castaneum.";
RL Nature 452:949-955(2008).
RN [2] {ECO:0000312|Proteomes:UP000007266}
RP GENOME REANNOTATION.
RC STRAIN=Georgia GA2 {ECO:0000312|Proteomes:UP000007266};
RX PubMed=19820115; DOI=10.1093/nar/gkp807;
RA Kim H.S., Murphy T., Xia J., Caragea D., Park Y., Beeman R.W.,
RA Lorenzen M.D., Butcher S., Manak J.R., Brown S.J.;
RT "BeetleBase in 2010: revisions to provide comprehensive genomic information
RT for Tribolium castaneum.";
RL Nucleic Acids Res. 38:D437-D442(2010).
RN [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PHOSPHORYLATION AT SER-205, AND
RP MUTAGENESIS OF CYS-130; ALA-194; SER-205; SER-207; GLU-217; HIS-247;
RP GLU-285; LEU-322; LEU-344; ASP-359; GLY-361; CYS-363; GLY-384; PRO-391;
RP GLU-392; GLY-415 AND LEU-462.
RX PubMed=22645651; DOI=10.1098/rsob.110012;
RA Woodroof H.I., Pogson J.H., Begley M., Cantley L.C., Deak M.,
RA Campbell D.G., van Aalten D.M., Whitworth A.J., Alessi D.R., Muqit M.M.;
RT "Discovery of catalytically active orthologues of the Parkinson's disease
RT kinase PINK1: analysis of substrate specificity and impact of mutations.";
RL Open Biol. 1:110012-110012(2011).
RN [4] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ASP-359.
RX PubMed=24751536; DOI=10.1083/jcb.201402104;
RA Kane L.A., Lazarou M., Fogel A.I., Li Y., Yamano K., Sarraf S.A.,
RA Banerjee S., Youle R.J.;
RT "PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiquitin ligase
RT activity.";
RL J. Cell Biol. 205:143-153(2014).
RN [5] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ASP-359.
RX PubMed=25474007; DOI=10.1371/journal.pgen.1004861;
RA Shiba-Fukushima K., Arano T., Matsumoto G., Inoshita T., Yoshida S.,
RA Ishihama Y., Ryu K.Y., Nukina N., Hattori N., Imai Y.;
RT "Phosphorylation of mitochondrial polyubiquitin by PINK1 promotes Parkin
RT mitochondrial tethering.";
RL PLoS Genet. 10:e1004861-e1004861(2014).
RN [6] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND MUTAGENESIS OF ASP-359.
RX PubMed=26116755; DOI=10.15252/embr.201540352;
RA Kazlauskaite A., Martinez-Torres R.J., Wilkie S., Kumar A., Peltier J.,
RA Gonzalez A., Johnson C., Zhang J., Hope A.G., Peggie M., Trost M.,
RA van Aalten D.M., Alessi D.R., Prescott A.R., Knebel A., Walden H.,
RA Muqit M.M.;
RT "Binding to serine 65-phosphorylated ubiquitin primes Parkin for optimal
RT PINK1-dependent phosphorylation and activation.";
RL EMBO Rep. 16:939-954(2015).
RN [7] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, PHOSPHORYLATION, AND MUTAGENESIS OF ASP-359.
RX PubMed=26784449; DOI=10.1371/journal.pone.0146083;
RA Aerts L., Craessaerts K., De Strooper B., Morais V.A.;
RT "In Vitro Comparison of the Activity Requirements and Substrate Specificity
RT of Human and Triboleum castaneum PINK1 Orthologues.";
RL PLoS ONE 11:e0146083-e0146083(2016).
RN [8] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP PHOSPHORYLATION AT SER-205, AND MUTAGENESIS OF LEU-196; SER-205; GLU-217;
RP GLY-285; ASP-337; ASP-359 AND CYS-363.
RX PubMed=29475881; DOI=10.15252/embr.201744981;
RA Rasool S., Soya N., Truong L., Croteau N., Lukacs G.L., Trempe J.F.;
RT "PINK1 autophosphorylation is required for ubiquitin recognition.";
RL EMBO Rep. 19:0-0(2018).
RN [9] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=32484300; DOI=10.15252/embr.201948686;
RA Han H., Tan J., Wang R., Wan H., He Y., Yan X., Guo J., Gao Q., Li J.,
RA Shang S., Chen F., Tian R., Liu W., Liao L., Tang B., Zhang Z.;
RT "PINK1 phosphorylates Drp1S616 to regulate mitophagy-independent
RT mitochondrial dynamics.";
RL EMBO Rep. 21:48686-48686(2020).
RN [10] {ECO:0007744|PDB:5OAT}
RP X-RAY CRYSTALLOGRAPHY (2.78 ANGSTROMS) OF 150-570, FUNCTION, CATALYTIC
RP ACTIVITY, PHOSPHORYLATION AT SER-205, AND MUTAGENESIS OF ALA-194; LYS-196;
RP ARG-216; GLU-217; 222-ARG--LYS-242; 231-ASN--LYS-242; ARG-240;
RP 243-HIS--PHE-253; 261-ILE--LYS-270; ASP-359; LEU-371; TYR-375; ASP-381 AND
RP LYS-382.
RX PubMed=28980524; DOI=10.7554/elife.29985;
RA Kumar A., Tamjar J., Waddell A.D., Woodroof H.I., Raimi O.G., Shaw A.M.,
RA Peggie M., Muqit M.M., van Aalten D.M.;
RT "Structure of PINK1 and mechanisms of Parkinson's disease-associated
RT mutations.";
RL Elife 6:0-0(2017).
RN [11] {ECO:0007744|PDB:5YJ9}
RP X-RAY CRYSTALLOGRAPHY (2.53 ANGSTROMS) OF 153-570 IN COMPLEX WITH ATP
RP ANALOG, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PHOSPHORYLATION AT SER-205;
RP SER-377; THR-386 AND THR-530, MAGNESIUM-BINDING, ACTIVE SITE, AND
RP MUTAGENESIS OF ILE-168; VAL-176; ALA-194; LYS-196; SER-205; GLU-209;
RP ILE-210; LYS-212; GLU-217; VAL-251; MET-294; ASP-337; ASP-341; ASN-342;
RP LEU-344; ASP-359; CYS-362; THR-368; SER-372; THR-376; SER-377; ASP-381;
RP ASN-385; THR-386; GLU-420; ASN-426; TYR-429 AND THR-530.
RX PubMed=29991771; DOI=10.1038/s41598-018-28656-8;
RA Okatsu K., Sato Y., Yamano K., Matsuda N., Negishi L., Takahashi A.,
RA Yamagata A., Goto-Ito S., Mishima M., Ito Y., Oka T., Tanaka K., Fukai S.;
RT "Structural insights into ubiquitin phosphorylation by PINK1.";
RL Sci. Rep. 8:10382-10382(2018).
CC -!- FUNCTION: Acts as a serine/threonine-protein kinase (PubMed:25474007,
CC PubMed:26784449, PubMed:29475881, PubMed:32484300, PubMed:28980524,
CC PubMed:24751536, PubMed:26116755, PubMed:29991771). Exhibits a
CC substrate preference for proline at position P+1 and a general
CC preference at several residues for basic residues such as arginine
CC (PubMed:22645651). Also exhibits moderate preferences for a
CC phosphotyrosine at position P-3 and a tryptophan at P-5
CC (PubMed:22645651). Protects against mitochondrial dysfunction during
CC cellular stress by phosphorylating mitochondrial proteins such as park
CC and likely Drp1, to coordinate mitochondrial quality control mechanisms
CC that remove and replace dysfunctional mitochondrial components
CC (PubMed:25474007, PubMed:32484300, PubMed:28980524, PubMed:24751536,
CC PubMed:26116755, PubMed:29991771). Depending on the severity of
CC mitochondrial damage and/or dysfunction, activity ranges from
CC preventing apoptosis and stimulating mitochondrial biogenesis to
CC regulating mitochondrial dynamics and eliminating severely damaged
CC mitochondria via mitophagy (By similarity). Appears to be particularly
CC important in maintaining the physiology and function of cells with high
CC energy demands that are undergoing stress or altered metabolic
CC environment, including spermatids, muscle cells and neurons such as the
CC dopaminergic (DA) neurons (By similarity). Mediates the translocation
CC and activation of park at the outer membrane (OMM) of
CC dysfunctional/depolarized mitochondria (PubMed:25474007,
CC PubMed:26116755). At the OMM of damaged mitochondria, phosphorylates
CC pre-existing polyubiquitin chains, the Pink1-phosphorylated
CC polyubiquitin then recruits park from the cytosol to the OMM where park
CC is fully activated by phosphorylation at 'Ser-80' by Pink1
CC (PubMed:24751536, PubMed:25474007, PubMed:29475881, PubMed:26116755,
CC PubMed:29991771). When cellular stress results in irreversible
CC mitochondrial damage, functions with park to promote the clearance of
CC dysfunctional and/or depolarized mitochondria by selective autophagy
CC (mitophagy) (By similarity). The Pink1-park pathway also promotes
CC fission and/or inhibits fusion of damaged mitochondria, by
CC phosphorylating and thus promoting the park-dependent degradation of
CC proteins involved in mitochondrial fusion/fission such as Marf, Opa1
CC and fzo (By similarity). This prevents the refusion of unhealthy
CC mitochondria with the mitochondrial network or initiates mitochondrial
CC fragmentation facilitating their later engulfment by autophagosomes (By
CC similarity). Also likely to promote mitochondrial fission independently
CC of park and Atg7-mediated mitophagy, via the phosphorylation and
CC activation of Drp1 (PubMed:32484300). Regulates motility of damaged
CC mitochondria by phosphorylating Miro which likely promotes its park-
CC dependent degradation by the proteasome; in motor neurons, this
CC inhibits mitochondrial intracellular anterograde transport along the
CC axons which probably increases the chance of the mitochondria being
CC eliminated in the soma (By similarity). The Pink1-park pathway is also
CC involved in mitochondrial regeneration processes such as promoting
CC mitochondrial biogenesis, activating localized mitochondrial repair,
CC promoting selective turnover of mitochondrial proteins and initiating
CC the mitochondrial import of endogenous proteins (By similarity).
CC Involved in mitochondrial biogenesis by promoting the park-dependent
CC ubiquitination of transcriptional repressor Paris which leads to its
CC subsequent proteasomal degradation and allows activation of the
CC transcription factor srl (By similarity). Functions with park to
CC promote localized mitochondrial repair by activating the translation of
CC specific nuclear-encoded mitochondrial RNAs (nc-mtRNAs) on the
CC mitochondrial surface, including several key electron transport chain
CC component nc-mtRNAs (By similarity). During oogenesis, phosphorylates
CC and inactivates larp on the membrane of defective mitochondria, thus
CC impairing local translation and mtDNA replication and consequently,
CC reducing transmission of deleterious mtDNA mutations to the mature
CC oocyte (By similarity). Exhibits a substrate preference for proline at
CC position P+1 and a general preference at several residues for basic
CC residues such as arginine (PubMed:22645651). Also exhibits moderate
CC preferences for a phosphotyrosine at position P-3 and a tryptophan at
CC P-5 (PubMed:22645651). {ECO:0000250|UniProtKB:Q0KHV6,
CC ECO:0000269|PubMed:22645651, ECO:0000269|PubMed:24751536,
CC ECO:0000269|PubMed:25474007, ECO:0000269|PubMed:26116755,
CC ECO:0000269|PubMed:26784449, ECO:0000269|PubMed:28980524,
CC ECO:0000269|PubMed:29475881, ECO:0000269|PubMed:29991771,
CC ECO:0000269|PubMed:32484300}.
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 Evidence={ECO:0000269|PubMed:22645651, ECO:0000269|PubMed:24751536,
CC ECO:0000269|PubMed:25474007, ECO:0000269|PubMed:26116755,
CC ECO:0000269|PubMed:26784449, ECO:0000269|PubMed:28980524,
CC ECO:0000269|PubMed:29475881, ECO:0000269|PubMed:29991771,
CC ECO:0000269|PubMed:32484300};
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; Evidence={ECO:0000269|PubMed:22645651,
CC ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:25474007,
CC ECO:0000269|PubMed:26116755, ECO:0000269|PubMed:26784449,
CC ECO:0000269|PubMed:28980524, ECO:0000269|PubMed:29475881,
CC ECO:0000269|PubMed:29991771, ECO:0000269|PubMed:32484300};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:22645651, ECO:0000269|PubMed:26116755,
CC ECO:0000269|PubMed:29991771};
CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000269|PubMed:29991771};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=287.5 uM for Drp1 (at 30 degrees Celsius)
CC {ECO:0000269|PubMed:32484300};
CC KM=84.4 uM for ubiquitin (at 30 degrees Celsius)
CC {ECO:0000269|PubMed:32484300};
CC KM=391 uM for ubiquitin (at pH 7.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:29475881};
CC KM=36 uM for ubiquitinated rat Prkn (at pH 7.5 and 30 degrees
CC Celsius) {ECO:0000269|PubMed:29475881};
CC Note=kcat is 4.6 sec(-1) for phosphorylation of Drp1 (at pH 7.5 and
CC 30 degrees Celsius) (PubMed:32484300). kcat is 20.9 sec(-1) for
CC phosphorylation of ubiquitin (at pH 7.5 and 30 degrees Celsius)
CC (PubMed:32484300). kcat is 18 min(-1) for phosphorylation of
CC ubiquitin (at pH 7.5 and 30 degrees Celsius) (PubMed:29475881). kcat
CC is 7.8 min(-1) for phosphorylation of ubiquitinated rat Prkn (at pH
CC 7.5 and 30 degrees Celsius) (PubMed:29475881).
CC {ECO:0000269|PubMed:29475881, ECO:0000269|PubMed:32484300};
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q0KHV6}; Single-pass membrane protein
CC {ECO:0000255}. Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q0KHV6}; Single-pass membrane protein
CC {ECO:0000255}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q0KHV6}.
CC Note=Localizes mostly in mitochondrion, and the smaller proteolytic
CC processed fragment localizes in the cytosol as well (By similarity).
CC When mitochondria are damaged, defective and/or enriched with
CC deleterious mtDNA mutations, Pink1 import is arrested which induces its
CC accumulation on the outer mitochondrial membrane where it acquires
CC kinase activity (By similarity). {ECO:0000250|UniProtKB:Q0KHV6}.
CC -!- PTM: Proteolytically cleaved. In healthy cells, the precursor is
CC continuously imported into mitochondria where it is proteolytically
CC cleaved into its short form by the mitochondrial rhomboid protease rho-
CC 7 (TcasGA2_TC013516). The short form is then released into the cytosol
CC where it rapidly undergoes proteasome-dependent degradation. In
CC unhealthy cells, when cellular stress conditions lead to the loss of
CC mitochondrial membrane potential, mitochondrial import is impaired
CC leading to the precursor accumulating on the outer mitochondrial
CC membrane (OMM). {ECO:0000250|UniProtKB:Q0KHV6}.
CC -!- PTM: Autophosphorylated on Ser-205, which activates kinase activity and
CC is required for substrate recognition (PubMed:29475881,
CC PubMed:22645651, PubMed:28980524, PubMed:26784449, PubMed:29991771).
CC Loss of mitochondrial membrane potential results in the precursor
CC accumulating on the outer mitochondrial membrane (OMM) where it is
CC activated by autophosphorylation at Ser-205 (By similarity).
CC Autophosphorylation is sufficient and essential for selective
CC recruitment of park to depolarized mitochondria, likely via Pink1-
CC dependent phosphorylation of polyubiquitin chains (PubMed:24751536).
CC Also autophosphorylated at Ser-377, Thr-386 and possibly Thr-530
CC (PubMed:29991771). Another report found evidence of autophosphorylation
CC at Ser-154, Thr-186, Thr-218, Ser-267 and Thr-530, as well as a number
CC of other minor sites, but determined that phosphorylation at these
CC sites is not required for enzyme activity and may not occur in vivo
CC (PubMed:29475881). {ECO:0000250|UniProtKB:Q0KHV6,
CC ECO:0000269|PubMed:22645651, ECO:0000269|PubMed:24751536,
CC ECO:0000269|PubMed:26784449, ECO:0000269|PubMed:28980524,
CC ECO:0000269|PubMed:29475881, ECO:0000269|PubMed:29991771}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {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; KQ971343; EFA03268.1; -; Genomic_DNA.
DR RefSeq; XP_968367.1; XM_963274.4.
DR PDB; 5OAT; X-ray; 2.78 A; A/B/C/D/E/F=150-570.
DR PDB; 5YJ9; X-ray; 2.53 A; D=153-570.
DR PDB; 7MP8; X-ray; 3.00 A; A=121-570.
DR PDB; 7MP9; X-ray; 2.80 A; A=121-570.
DR PDBsum; 5OAT; -.
DR PDBsum; 5YJ9; -.
DR PDBsum; 7MP8; -.
DR PDBsum; 7MP9; -.
DR SMR; D6WMX4; -.
DR STRING; 7070.TC013202-PA; -.
DR ChEMBL; CHEMBL4295537; -.
DR EnsemblMetazoa; TC013202_001; TC013202_001; TC013202.
DR GeneID; 656767; -.
DR KEGG; tca:656767; -.
DR eggNOG; KOG4158; Eukaryota.
DR HOGENOM; CLU_022208_0_0_1; -.
DR InParanoid; D6WMX4; -.
DR OMA; FGQHARK; -.
DR OrthoDB; 314975at2759; -.
DR PhylomeDB; D6WMX4; -.
DR Proteomes; UP000007266; Linkage group 5.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:ParkinsonsUK-UCL.
DR GO; GO:1904544; P:positive regulation of free ubiquitin chain polymerization; IMP:ParkinsonsUK-UCL.
DR GO; GO:0090141; P:positive regulation of mitochondrial fission; IBA:GO_Central.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:ParkinsonsUK-UCL.
DR GO; GO:0046777; P:protein autophosphorylation; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
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; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Autophagy; Cytoplasm; Kinase; Magnesium;
KW Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW Mitochondrion outer membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..5
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 6..570
FT /note="Serine/threonine-protein kinase Pink1,
FT mitochondrial"
FT /evidence="ECO:0000255"
FT /id="PRO_0000454926"
FT TOPO_DOM 6..96
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT TRANSMEM 97..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 121..570
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 162..484
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 337
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000269|PubMed:29991771"
FT BINDING 196
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000269|PubMed:29991771, ECO:0007744|PDB:5YJ9"
FT BINDING 217
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:29991771,
FT ECO:0007744|PDB:5YJ9"
FT BINDING 295
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:29991771,
FT ECO:0007744|PDB:5YJ9"
FT BINDING 297
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:29991771,
FT ECO:0007744|PDB:5YJ9"
FT BINDING 300
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:29991771,
FT ECO:0007744|PDB:5YJ9"
FT BINDING 341
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:29991771,
FT ECO:0007744|PDB:5YJ9"
FT BINDING 342
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:29991771,
FT ECO:0007744|PDB:5YJ9"
FT BINDING 359
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:29991771,
FT ECO:0007744|PDB:5YJ9"
FT BINDING 359
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:28980524,
FT ECO:0000269|PubMed:29991771, ECO:0007744|PDB:5OAT,
FT ECO:0007744|PDB:5YJ9"
FT BINDING 359
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:29991771,
FT ECO:0007744|PDB:5YJ9"
FT SITE 44
FT /note="Important for interaction with substrates Prkn and
FT ubiquitin"
FT /evidence="ECO:0000269|PubMed:29475881"
FT SITE 48
FT /note="Important for interaction with substrates Prkn and
FT ubiquitin"
FT /evidence="ECO:0000269|PubMed:29475881"
FT SITE 68
FT /note="Important for interaction with substrates Prkn and
FT ubiquitin"
FT /evidence="ECO:0000269|PubMed:29475881"
FT SITE 72
FT /note="Important for interaction with substrates Prkn and
FT ubiquitin"
FT /evidence="ECO:0000269|PubMed:29475881"
FT MOD_RES 205
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:22645651,
FT ECO:0000269|PubMed:28980524, ECO:0000269|PubMed:29475881,
FT ECO:0000269|PubMed:29991771"
FT MOD_RES 377
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:29991771"
FT MOD_RES 386
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:29991771"
FT MOD_RES 530
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:29991771"
FT MUTAGEN 130
FT /note="C->G: Moderately reduces enzyme activity."
FT /evidence="ECO:0000269|PubMed:22645651"
FT MUTAGEN 168
FT /note="I->N: Abolishes phosphorylation of ubiquitin."
FT /evidence="ECO:0000269|PubMed:29991771"
FT MUTAGEN 176
FT /note="V->N: Abolishes phosphorylation of ubiquitin."
FT /evidence="ECO:0000269|PubMed:29991771"
FT MUTAGEN 194
FT /note="A->D: Almost complete loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:22645651,
FT ECO:0000269|PubMed:28980524"
FT MUTAGEN 194
FT /note="A->N: Abolishes phosphorylation of ubiquitin."
FT /evidence="ECO:0000269|PubMed:29991771"
FT MUTAGEN 196
FT /note="K->A: Almost complete loss of enzyme activity, but
FT still undergoes autophosphorylation at Ser-205 and is able
FT to bind rat Prkn. Abolishes phosphorylation of
FT polyubiquitin chains at Ser-65; when associated with A-337
FT and A-359."
FT /evidence="ECO:0000269|PubMed:25474007,
FT ECO:0000269|PubMed:28980524, ECO:0000269|PubMed:29475881,
FT ECO:0000269|PubMed:29991771"
FT MUTAGEN 205
FT /note="S->A: Strongly reduces enzyme activity. Abolishes
FT phosphorylation of rat ubiquitin and strongly reduced
FT phosphorylation of rat Prkn."
FT /evidence="ECO:0000269|PubMed:22645651,
FT ECO:0000269|PubMed:29475881"
FT MUTAGEN 205
FT /note="S->D: Phosphomimetic mutant which retains some
FT residual ubiquitin phosphorylation activity; when
FT associated with D-377, E-386 and E-530."
FT /evidence="ECO:0000269|PubMed:29991771"
FT MUTAGEN 205
FT /note="S->N: Strongly reduces enzyme activity. Abolishes
FT phosphorylation of rat ubiquitin and strongly reduced
FT phosphorylation of rat Prkn."
FT /evidence="ECO:0000269|PubMed:29475881"
FT MUTAGEN 207
FT /note="S->A: No effect on enzyme activity."
FT /evidence="ECO:0000269|PubMed:22645651"
FT MUTAGEN 209
FT /note="E->R: Drastically reduces phosphorylation of
FT ubiquitin."
FT /evidence="ECO:0000269|PubMed:29991771"
FT MUTAGEN 210
FT /note="I->N: Drastically reduces phosphorylation of
FT ubiquitin."
FT /evidence="ECO:0000269|PubMed:29991771"
FT MUTAGEN 212
FT /note="K->A: Slight reduction in phosphorylation of
FT ubiquitin."
FT /evidence="ECO:0000269|PubMed:28980524"
FT MUTAGEN 216
FT /note="R->A: Reduced phosphorylation of ubiquitin."
FT /evidence="ECO:0000269|PubMed:28980524"
FT MUTAGEN 217
FT /note="E->A: Abolishes phosphorylation of ubiquitin."
FT /evidence="ECO:0000269|PubMed:29991771"
FT MUTAGEN 217
FT /note="E->K: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:22645651,
FT ECO:0000269|PubMed:28980524, ECO:0000269|PubMed:29475881,
FT ECO:0000269|PubMed:29991771"
FT MUTAGEN 222..242
FT /note="Missing: No effect on enzyme activity."
FT /evidence="ECO:0000269|PubMed:28980524"
FT MUTAGEN 231..242
FT /note="Missing: No effect on enzyme activity."
FT /evidence="ECO:0000269|PubMed:28980524"
FT MUTAGEN 240
FT /note="R->A: Reduced phosphorylation of ubiquitin."
FT /evidence="ECO:0000269|PubMed:28980524"
FT MUTAGEN 243..253
FT /note="Missing: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:28980524"
FT MUTAGEN 247
FT /note="H->Q: Strongly reduces enzyme activity."
FT /evidence="ECO:0000269|PubMed:22645651"
FT MUTAGEN 251
FT /note="V->N: Reduced phosphorylation of ubiquitin."
FT /evidence="ECO:0000269|PubMed:29991771"
FT MUTAGEN 251
FT /note="V->R: Abolishes phosphorylation of ubiquitin."
FT /evidence="ECO:0000269|PubMed:29991771"
FT MUTAGEN 261..270
FT /note="Missing: Strongly reduces enzyme activity. Unable to
FT phosphorylate ubiquitin and park, but retains its
FT autophosphorylation activity."
FT /evidence="ECO:0000269|PubMed:28980524"
FT MUTAGEN 285
FT /note="G->D: Strongly reduces enzyme activity."
FT /evidence="ECO:0000269|PubMed:22645651,
FT ECO:0000269|PubMed:29475881"
FT MUTAGEN 294
FT /note="M->A,L: Decreases phosphorylation of ubiquitin."
FT /evidence="ECO:0000269|PubMed:29991771"
FT MUTAGEN 294
FT /note="M->N: Abolishes phosphorylation of ubiquitin."
FT /evidence="ECO:0000269|PubMed:29991771"
FT MUTAGEN 322
FT /note="L->P: Almost complete loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:22645651"
FT MUTAGEN 337
FT /note="D->A: Abolishes enzyme activity, loss of
FT autophosphorylation and phosphorylation of ubiquitin.
FT Abolishes phosphorylation of polyubiquitin chains at Ser-
FT 65; when associated with A-196 and A-359."
FT /evidence="ECO:0000269|PubMed:29991771"
FT MUTAGEN 337
FT /note="D->H: Abolishes phosphorylation of ubiquitin."
FT /evidence="ECO:0000269|PubMed:29991771"
FT MUTAGEN 337
FT /note="D->N: Abolishes enzyme activity. Able to undergo
FT autophosphorylation and bind to rat Prkn."
FT /evidence="ECO:0000269|PubMed:29475881"
FT MUTAGEN 341
FT /note="D->A: Abolishes phosphorylation of ubiquitin."
FT /evidence="ECO:0000269|PubMed:29991771"
FT MUTAGEN 342
FT /note="N->A: Abolishes phosphorylation of ubiquitin."
FT /evidence="ECO:0000269|PubMed:29991771"
FT MUTAGEN 342
FT /note="N->S: Abolishes phosphorylation of ubiquitin."
FT /evidence="ECO:0000269|PubMed:29991771"
FT MUTAGEN 344
FT /note="L->N: No effect on phosphorylation of ubiquitin."
FT /evidence="ECO:0000269|PubMed:29991771"
FT MUTAGEN 344
FT /note="L->P: Almost complete loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:22645651"
FT MUTAGEN 344
FT /note="L->R: Abolishes phosphorylation of ubiquitin."
FT /evidence="ECO:0000269|PubMed:29991771"
FT MUTAGEN 359
FT /note="D->A: Abolishes enzyme activity. No effect on
FT autophosphorylation activity. However, another report found
FT that it significantly reduced autophosphorylation.
FT Abolishes phosphorylation of polyubiquitin chains at Ser-
FT 65; when associated with A-196 and A-337."
FT /evidence="ECO:0000269|PubMed:22645651,
FT ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:25474007,
FT ECO:0000269|PubMed:26116755, ECO:0000269|PubMed:26784449,
FT ECO:0000269|PubMed:28980524, ECO:0000269|PubMed:29991771"
FT MUTAGEN 359
FT /note="D->N: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:29475881"
FT MUTAGEN 361
FT /note="G->A: Almost complete loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:22645651"
FT MUTAGEN 362
FT /note="C->A: Slight reduction in phosphorylation of
FT ubiquitin."
FT /evidence="ECO:0000269|PubMed:29991771"
FT MUTAGEN 363
FT /note="C->R: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:22645651"
FT MUTAGEN 363
FT /note="C->S: No effect on phosphorylation of rat
FT ubiquitin."
FT /evidence="ECO:0000269|PubMed:29475881"
FT MUTAGEN 368
FT /note="T->A: No effect on autophosphorylation levels; when
FT associated with A-372."
FT /evidence="ECO:0000269|PubMed:29991771"
FT MUTAGEN 371
FT /note="L->A: Almost complete loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:28980524"
FT MUTAGEN 372
FT /note="S->A: No effect on autophosphorylation levels; when
FT associated with A-368."
FT /evidence="ECO:0000269|PubMed:29991771"
FT MUTAGEN 375
FT /note="Y->A: Almost complete loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:28980524"
FT MUTAGEN 376
FT /note="T->A: No effect on autophosphorylation."
FT /evidence="ECO:0000269|PubMed:29991771"
FT MUTAGEN 377
FT /note="S->D: Phosphomimetic mutant which retains some
FT residual ubiquitin phosphorylation activity; when
FT associated with D-205, E-386 and E-530."
FT /evidence="ECO:0000269|PubMed:29991771"
FT MUTAGEN 381
FT /note="D->A: Reduced phosphorylation of ubiquitin."
FT /evidence="ECO:0000269|PubMed:28980524"
FT MUTAGEN 381
FT /note="D->R: Drastically reduces phosphorylation of
FT ubiquitin."
FT /evidence="ECO:0000269|PubMed:29991771"
FT MUTAGEN 382
FT /note="K->A: Almost complete loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:28980524"
FT MUTAGEN 384
FT /note="G->V: Almost complete loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:22645651"
FT MUTAGEN 385
FT /note="N->A: Drastically reduces phosphorylation of
FT ubiquitin."
FT /evidence="ECO:0000269|PubMed:29991771"
FT MUTAGEN 386
FT /note="T->A: Decreased autophosphorylation levels."
FT /evidence="ECO:0000269|PubMed:29991771"
FT MUTAGEN 386
FT /note="T->E: Phosphomimetic mutant which retains some
FT residual ubiquitin phosphorylation activity; when
FT associated with D-205, D-377 and E-530."
FT /evidence="ECO:0000269|PubMed:29991771"
FT MUTAGEN 391
FT /note="P->R: Almost complete loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:22645651"
FT MUTAGEN 392
FT /note="E->G: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:22645651"
FT MUTAGEN 415
FT /note="G->E: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:22645651"
FT MUTAGEN 420
FT /note="E->A: Slight reduction in phosphorylation of
FT ubiquitin."
FT /evidence="ECO:0000269|PubMed:29991771"
FT MUTAGEN 426
FT /note="N->A: Slight reduction in phosphorylation of
FT ubiquitin."
FT /evidence="ECO:0000269|PubMed:29991771"
FT MUTAGEN 429
FT /note="Y->A: Drastically reduces phosphorylation of
FT ubiquitin."
FT /evidence="ECO:0000269|PubMed:29991771"
FT MUTAGEN 462
FT /note="L->P: Almost complete loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:22645651"
FT MUTAGEN 530
FT /note="T->E: Phosphomimetic mutant which retains some
FT residual ubiquitin phosphorylation activity; when
FT associated with D-205, D-377 and E-386."
FT /evidence="ECO:0000269|PubMed:29991771"
FT HELIX 122..154
FT /evidence="ECO:0007829|PDB:7MP9"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:5OAT"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:5YJ9"
FT STRAND 172..179
FT /evidence="ECO:0007829|PDB:5YJ9"
FT STRAND 193..199
FT /evidence="ECO:0007829|PDB:5YJ9"
FT STRAND 203..206
FT /evidence="ECO:0007829|PDB:5YJ9"
FT HELIX 208..216
FT /evidence="ECO:0007829|PDB:5YJ9"
FT TURN 217..220
FT /evidence="ECO:0007829|PDB:5YJ9"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:5OAT"
FT HELIX 232..240
FT /evidence="ECO:0007829|PDB:5OAT"
FT STRAND 253..257
FT /evidence="ECO:0007829|PDB:5YJ9"
FT STRAND 289..295
FT /evidence="ECO:0007829|PDB:5YJ9"
FT STRAND 298..300
FT /evidence="ECO:0007829|PDB:5YJ9"
FT HELIX 301..304
FT /evidence="ECO:0007829|PDB:5YJ9"
FT HELIX 311..330
FT /evidence="ECO:0007829|PDB:5YJ9"
FT STRAND 342..346
FT /evidence="ECO:0007829|PDB:5YJ9"
FT STRAND 354..357
FT /evidence="ECO:0007829|PDB:5YJ9"
FT HELIX 360..362
FT /evidence="ECO:0007829|PDB:5OAT"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:7MP8"
FT TURN 367..369
FT /evidence="ECO:0007829|PDB:5YJ9"
FT STRAND 372..374
FT /evidence="ECO:0007829|PDB:5YJ9"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:5OAT"
FT STRAND 386..388
FT /evidence="ECO:0007829|PDB:7MP9"
FT HELIX 391..394
FT /evidence="ECO:0007829|PDB:5YJ9"
FT STRAND 399..401
FT /evidence="ECO:0007829|PDB:5OAT"
FT STRAND 403..405
FT /evidence="ECO:0007829|PDB:5YJ9"
FT HELIX 409..421
FT /evidence="ECO:0007829|PDB:5YJ9"
FT STRAND 429..432
FT /evidence="ECO:0007829|PDB:5OAT"
FT TURN 436..438
FT /evidence="ECO:0007829|PDB:5YJ9"
FT HELIX 441..443
FT /evidence="ECO:0007829|PDB:5YJ9"
FT HELIX 453..462
FT /evidence="ECO:0007829|PDB:5YJ9"
FT HELIX 467..469
FT /evidence="ECO:0007829|PDB:5YJ9"
FT HELIX 473..485
FT /evidence="ECO:0007829|PDB:5YJ9"
FT HELIX 488..491
FT /evidence="ECO:0007829|PDB:5YJ9"
FT STRAND 492..495
FT /evidence="ECO:0007829|PDB:7MP8"
FT HELIX 500..515
FT /evidence="ECO:0007829|PDB:5YJ9"
FT STRAND 519..522
FT /evidence="ECO:0007829|PDB:7MP9"
FT HELIX 523..525
FT /evidence="ECO:0007829|PDB:7MP9"
FT HELIX 533..535
FT /evidence="ECO:0007829|PDB:7MP9"
FT HELIX 537..548
FT /evidence="ECO:0007829|PDB:5YJ9"
FT HELIX 552..564
FT /evidence="ECO:0007829|PDB:5YJ9"
SQ SEQUENCE 570 AA; 64072 MW; E58A6C0EA9809A1E CRC64;
MSVRAVGSRL FKHGRSLIQQ FCKRDLNTTI GDKINAVSQA TAAPSSLPKT QIPKNFALRN
VGVQLGLQAR RILIDNVLNR VTNSLSAELR KKATRRILFG DSAPFFALVG VSIASGTGIL
TKEEELEGVC WEIREAISKI KWQYYDIDES RFESNPITLN DLSLGKPIAK GTNGVVYSAK
VKDDETDDNK YPFALKMMFN YDIQSNSMEI LKAMYRETVP ARMYYSNHDL NNWEIELANR
RKHLPPHPNI VAIFSVFTDL IQELEGSKDL YPAALPPRLH PEGEGRNMSL FLLMKRYDCN
LQSFLSTAPS TRTSLLLLAQ LLEGVAHMTA HGIAHRDLKS DNLLLDTSEP ESPILVISDF
GCCLADKTNG LSLPYTSYEM DKGGNTALMA PEIICQKPGT FSVLNYSKAD LWAVGAIAYE
IFNCHNPFYG PSRLKNFNYK EGDLPKLPDE VPTVIQALVA NLLKRNPNKR LDPEVAANVC
QLFLWAPSTW LKPGLKVPTS GEILQWLLSL TTKVLCEGKI NNKSFGEKFT RNWRRTYPEY
LLISSFLCRA KLANVRNALH WIQENLPELD
