PINK1_RAT
ID PINK1_RAT Reviewed; 580 AA.
AC B5DFG1;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Serine/threonine-protein kinase PINK1, mitochondrial {ECO:0000250|UniProtKB:Q9BXM7};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:Q9BXM7};
DE AltName: Full=PTEN-induced putative kinase 1;
DE Flags: Precursor;
GN Name=Pink1 {ECO:0000312|RGD:1305769};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000312|EMBL:AAI69047.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart {ECO:0000312|EMBL:AAI69047.1};
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 [3] {ECO:0000305}
RP INTERACTION WITH NENF, AND SUBCELLULAR LOCATION.
RX PubMed=31536960; DOI=10.1016/j.isci.2019.08.057;
RA Moutaoufik M.T., Malty R., Amin S., Zhang Q., Phanse S., Gagarinova A.,
RA Zilocchi M., Hoell L., Minic Z., Gagarinova M., Aoki H., Stockwell J.,
RA Jessulat M., Goebels F., Broderick K., Scott N.E., Vlasblom J., Musso G.,
RA Prasad B., Lamantea E., Garavaglia B., Rajput A., Murayama K., Okazaki Y.,
RA Foster L.J., Bader G.D., Cayabyab F.S., Babu M.;
RT "Rewiring of the Human Mitochondrial Interactome during Neuronal
RT Reprogramming Reveals Regulators of the Respirasome and Neurogenesis.";
RL IScience 19:1114-1132(2019).
CC -!- FUNCTION: Serine/threonine-protein kinase which protects against
CC mitochondrial dysfunction during cellular stress by phosphorylating
CC mitochondrial proteins such as PRKN and DNM1L, to coordinate
CC mitochondrial quality control mechanisms that remove and replace
CC dysfunctional mitochondrial components. 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. Mediates the translocation and activation
CC of PRKN at the outer membrane (OMM) of dysfunctional/depolarized
CC mitochondria. At the OMM of damaged mitochondria, phosphorylates pre-
CC existing polyubiquitin chains at 'Ser-65', the PINK1-phosphorylated
CC polyubiquitin then recruits PRKN from the cytosol to the OMM where PRKN
CC is fully activated by phosphorylation at 'Ser-65' by PINK1. In damaged
CC mitochondria, mediates the decision between mitophagy or preventing
CC apoptosis by promoting PRKN-dependent poly- or monoubiquitination of
CC VDAC1; polyubiquitination of VDAC1 by PRKN promotes mitophagy, while
CC monoubiquitination of VDAC1 by PRKN decreases mitochondrial calcium
CC influx which ultimately inhibits apoptosis. When cellular stress
CC results in irreversible mitochondrial damage, functions with PRKN to
CC promote clearance of damaged mitochondria via selective autophagy
CC (mitophagy). The PINK1-PRKN pathway also promotes fission of damaged
CC mitochondria by phosphorylating and thus promoting the PRKN-dependent
CC degradation of mitochondrial proteins involved in fission such as MFN2.
CC This prevents the refusion of unhealthy mitochondria with the
CC mitochondrial network or initiates mitochondrial fragmentation
CC facilitating their later engulfment by autophagosomes. Also promotes
CC mitochondrial fission independently of PRKN and ATG7-mediated
CC mitophagy, via the phosphorylation and activation of DNM1L. Regulates
CC motility of damaged mitochondria by promoting the ubiquitination and
CC subsequent degradation of MIRO1 and MIRO2; in motor neurons, this
CC likely inhibits mitochondrial intracellular anterograde transport along
CC the axons which probably increases the chance of the mitochondria
CC undergoing mitophagy in the soma (By similarity). Required for
CC ubiquinone reduction by mitochondrial complex I by mediating
CC phosphorylation of complex I subunit NDUFA10 (By similarity).
CC {ECO:0000250|UniProtKB:Q99MQ3, ECO:0000250|UniProtKB:Q9BXM7}.
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:0000250|UniProtKB:Q9BXM7};
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:0000250|UniProtKB:Q9BXM7};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9BXM7};
CC -!- SUBUNIT: Interacts with PRKN (By similarity). Interacts with FBXO7 (By
CC similarity). Forms a complex with PRKN and PARK7 (By similarity).
CC Interacts with NENF (PubMed:31536960). {ECO:0000250|UniProtKB:Q9BXM7,
CC ECO:0000269|PubMed:31536960}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:31536960}; Single-pass membrane protein
CC {ECO:0000255}. Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q99MQ3}; Single-pass membrane protein
CC {ECO:0000255}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9BXM7}.
CC Note=Localizes mostly in mitochondrion and the two smaller proteolytic
CC processed fragments localize mainly in cytosol. When mitochondria lose
CC mitochondrial membrane potential following damage, PINK1 import is
CC arrested, which induces its accumulation in the outer mitochondrial
CC membrane, where it acquires kinase activity.
CC {ECO:0000250|UniProtKB:Q9BXM7}.
CC -!- PTM: Proteolytically cleaved. In healthy cells, the precursor is
CC continuously imported into the inner mitochondrial membrane (IMM),
CC where it is proteolytically cleaved by mitochondrial-processing
CC peptidase (MPP) and then undergoes further proteolytic cleavage by PARL
CC or AFG3L2 to give rise to the 52 kDa short form. The 52 kDa short form
CC is then released into the cytosol where it rapidly undergoes
CC proteasome-dependent degradation. In unhealthy cells, when cellular
CC stress conditions lead to the loss of mitochondrial membrane potential,
CC mitochondrial import is impaired leading to the precursor accumulating
CC on the outer mitochondrial membrane (OMM). If accumulation at the OMM
CC fails and it is imported into the depolarized mitochondria, it
CC undergoes cleavage by the IMM protease OMA1, promoting its subsequent
CC degradation by the proteasome. {ECO:0000250|UniProtKB:Q9BXM7}.
CC -!- PTM: Autophosphorylated. Loss of mitochondrial membrane potential
CC results in the precursor accumulating on the outer mitochondrial
CC membrane (OMM) where it is activated by autophosphorylation.
CC Autophosphorylation at Ser-227 and Ser-401 is sufficient and essential
CC for selective recruitment of PRKN to depolarized mitochondria, via
CC PINK1-dependent phosphorylation of ubiquitin and maybe PRKN.
CC {ECO:0000250|UniProtKB:Q9BXM7}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AABR07050212; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC169047; AAI69047.1; -; mRNA.
DR AlphaFoldDB; B5DFG1; -.
DR SMR; B5DFG1; -.
DR STRING; 10116.ENSRNOP00000058880; -.
DR ABCD; B5DFG1; 4 sequenced antibodies.
DR Ensembl; ENSRNOT00000083474; ENSRNOP00000069316; ENSRNOG00000015385.
DR RGD; 1305769; Pink1.
DR GeneTree; ENSGT00390000001206; -.
DR HOGENOM; CLU_022208_1_0_1; -.
DR OMA; MMILQLL; -.
DR TreeFam; TF313183; -.
DR Reactome; R-RNO-5205685; PINK1-PRKN Mediated Mitophagy.
DR PRO; PR:B5DFG1; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000015385; Expressed in skeletal muscle tissue and 19 other tissues.
DR ExpressionAtlas; B5DFG1; baseline and differential.
DR GO; GO:0097449; C:astrocyte projection; ISO:RGD.
DR GO; GO:0030424; C:axon; ISO:RGD.
DR GO; GO:0044297; C:cell body; ISO:RGD.
DR GO; GO:0000785; C:chromatin; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005856; C:cytoskeleton; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0030426; C:growth cone; IDA:RGD.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:RGD.
DR GO; GO:0005758; C:mitochondrial intermembrane space; ISO:RGD.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; ISO:RGD.
DR GO; GO:0055131; F:C3HC4-type RING finger domain binding; ISO:RGD.
DR GO; GO:0010857; F:calcium-dependent protein kinase activity; ISO:RGD.
DR GO; GO:0016301; F:kinase activity; ISO:RGD.
DR GO; GO:0000287; F:magnesium ion binding; ISO:RGD.
DR GO; GO:0002020; F:protease binding; ISO:RGD.
DR GO; GO:0004672; F:protein kinase activity; ISO:RGD.
DR GO; GO:0043422; F:protein kinase B binding; ISO:RGD.
DR GO; GO:0106310; F:protein serine kinase activity; ISO:RGD.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
DR GO; GO:1904841; F:TORC2 complex binding; ISO:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:RGD.
DR GO; GO:0000422; P:autophagy of mitochondrion; ISO:RGD.
DR GO; GO:1904881; P:cellular response to hydrogen sulfide; IDA:RGD.
DR GO; GO:0071456; P:cellular response to hypoxia; ISO:RGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; ISO:RGD.
DR GO; GO:0097237; P:cellular response to toxic substance; ISO:RGD.
DR GO; GO:0014046; P:dopamine secretion; IEA:Ensembl.
DR GO; GO:0072655; P:establishment of protein localization to mitochondrion; ISO:RGD.
DR GO; GO:0030097; P:hemopoiesis; ISO:RGD.
DR GO; GO:0035556; P:intracellular signal transduction; ISO:RGD.
DR GO; GO:0072656; P:maintenance of protein location in mitochondrion; ISO:RGD.
DR GO; GO:0000266; P:mitochondrial fission; HMP:RGD.
DR GO; GO:0007005; P:mitochondrion organization; ISO:RGD.
DR GO; GO:0099074; P:mitochondrion to lysosome transport; ISO:RGD.
DR GO; GO:0000423; P:mitophagy; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
DR GO; GO:1902902; P:negative regulation of autophagosome assembly; ISO:RGD.
DR GO; GO:1903147; P:negative regulation of autophagy of mitochondrion; ISO:RGD.
DR GO; GO:0031999; P:negative regulation of fatty acid beta-oxidation; HMP:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:1903384; P:negative regulation of hydrogen peroxide-induced neuron intrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:1903298; P:negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:1903751; P:negative regulation of intrinsic apoptotic signaling pathway in response to hydrogen peroxide; ISO:RGD.
DR GO; GO:0016242; P:negative regulation of macroautophagy; ISO:RGD.
DR GO; GO:0090258; P:negative regulation of mitochondrial fission; ISO:RGD.
DR GO; GO:1901525; P:negative regulation of mitophagy; ISO:RGD.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:RGD.
DR GO; GO:1901215; P:negative regulation of neuron death; IMP:RGD.
DR GO; GO:1903202; P:negative regulation of oxidative stress-induced cell death; ISO:RGD.
DR GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; ISO:RGD.
DR GO; GO:0036289; P:peptidyl-serine autophosphorylation; ISO:RGD.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:RGD.
DR GO; GO:1904925; P:positive regulation of autophagy of mitochondrion in response to mitochondrial depolarization; IMP:RGD.
DR GO; GO:0033605; P:positive regulation of catecholamine secretion; ISO:RGD.
DR GO; GO:1903852; P:positive regulation of cristae formation; ISO:RGD.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:RGD.
DR GO; GO:0033603; P:positive regulation of dopamine secretion; ISO:RGD.
DR GO; GO:1901727; P:positive regulation of histone deacetylase activity; ISO:RGD.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISO:RGD.
DR GO; GO:0016239; P:positive regulation of macroautophagy; ISO:RGD.
DR GO; GO:1902958; P:positive regulation of mitochondrial electron transport, NADH to ubiquinone; ISO:RGD.
DR GO; GO:0090141; P:positive regulation of mitochondrial fission; IMP:RGD.
DR GO; GO:0098779; P:positive regulation of mitophagy in response to mitochondrial depolarization; ISO:RGD.
DR GO; GO:1904783; P:positive regulation of NMDA glutamate receptor activity; IMP:RGD.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:RGD.
DR GO; GO:0035307; P:positive regulation of protein dephosphorylation; ISO:RGD.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:RGD.
DR GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; ISO:RGD.
DR GO; GO:0032226; P:positive regulation of synaptic transmission, dopaminergic; ISO:RGD.
DR GO; GO:0045727; P:positive regulation of translation; ISO:RGD.
DR GO; GO:0006468; P:protein phosphorylation; ISO:RGD.
DR GO; GO:0050821; P:protein stabilization; ISO:RGD.
DR GO; GO:0016567; P:protein ubiquitination; ISO:RGD.
DR GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:1900407; P:regulation of cellular response to oxidative stress; ISO:RGD.
DR GO; GO:0010310; P:regulation of hydrogen peroxide metabolic process; ISO:RGD.
DR GO; GO:0051881; P:regulation of mitochondrial membrane potential; ISO:RGD.
DR GO; GO:0010821; P:regulation of mitochondrion organization; ISO:RGD.
DR GO; GO:0043523; P:regulation of neuron apoptotic process; ISO:RGD.
DR GO; GO:0002082; P:regulation of oxidative phosphorylation; ISO:RGD.
DR GO; GO:1903214; P:regulation of protein targeting to mitochondrion; ISO:RGD.
DR GO; GO:0031396; P:regulation of protein ubiquitination; ISO:RGD.
DR GO; GO:0043254; P:regulation of protein-containing complex assembly; ISO:RGD.
DR GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; ISO:RGD.
DR GO; GO:0022904; P:respiratory electron transport chain; ISO:RGD.
DR GO; GO:0002931; P:response to ischemia; IEP:RGD.
DR GO; GO:0006979; P:response to oxidative stress; ISO:RGD.
DR CDD; cd14018; STKc_PINK1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR040110; PINK1_STKc.
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 ATP-binding; Autophagy; Cytoplasm; Kinase; Magnesium; Membrane;
KW 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..77
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 78..580
FT /note="Serine/threonine-protein kinase PINK1,
FT mitochondrial"
FT /evidence="ECO:0000255"
FT /id="PRO_0000449049"
FT TRANSMEM 94..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 156..510
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 28..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..117
FT /note="Required for outer membrane localization"
FT /evidence="ECO:0000250|UniProtKB:Q9BXM7"
FT ACT_SITE 361
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 162..170
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 218
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 227
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q9BXM7"
FT MOD_RES 401
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q9BXM7"
SQ SEQUENCE 580 AA; 63219 MW; D8CA866625AA24CA CRC64;
MAVRQALGRG LQLGRALLLR FAPKPGPVSG WGKPGPGAAW GRGERPGRVS SPGAQPRPLG
LPLPDRYRFF RQSVAGLAAR IQRQFVVRAR GGAGPCGRAV FLAFGLGLGL IEEKQAESRR
AASACQEIQA IFTQKNKQVS DPLDTRRWQG FRLEDYLIGQ AIGKGCNAAV YEATMPTLPQ
HLEKAKHLGL LGKGPDVVSK GADGEQAPGA PAFPFAIKMM WNISAGSSSE AILSKMSQEL
VPASRMALDG EYGAVTYRRS RDGPKQLAPH PNIIRVFRAF TSSVPLLPGA LADYPDMLPP
HYYPEGLGHG RTLFLVMKNY PCTLRQYLEE QTPSSRLATM MTLQLLEGVD HLVQQGIAHR
DLKSDNILVE WDSDGCPWLV ISDFGCCLAD ERVGLQLPFN SSSVERGGNG SLMAPEVSTA
HSGPHAVIDY SKADTWAVGA IAYEIFGLAN PFYGQGSAHL ESRSYQEAQL PEMPKSVPPE
TRQLVRSLLQ REANKRPSAR IAANVLHLSL WGEHLLALKN LKLDKMIAWL LQQSAATLLA
DRLREKSCVE TKLQMLFLAN LECEALCQAA LLLSSWRAAP
