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Serine/threonine-protein kinase PINK1, mitochondrial (EC 2.7.11.1) (BRPK) (PTEN-induced putative kinase protein 1)

 PINK1_MOUSE             Reviewed;         580 AA.
Q99MQ3; A2AM77; Q7TMZ3; Q811I8; Q91XU5;
07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
07-JUN-2004, sequence version 2.
20-JUN-2018, entry version 144.
RecName: Full=Serine/threonine-protein kinase PINK1, mitochondrial;
EC=2.7.11.1 {ECO:0000269|PubMed:24652937};
AltName: Full=BRPK;
AltName: Full=PTEN-induced putative kinase protein 1;
Flags: Precursor;
Name=Pink1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090 {ECO:0000312|EMBL:AAK28061.1};
[1] {ECO:0000312|EMBL:BAB55651.1}
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB55651.1};
TISSUE=Lung {ECO:0000312|EMBL:BAB55651.1};
PubMed=11494141; DOI=10.1038/sj.onc.1204608;
Unoki M., Nakamura Y.;
"Growth-suppressive effects of BPOZ and EGR2, two genes involved in
the PTEN signaling pathway.";
Oncogene 20:4457-4465(2001).
[2] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
STRAIN=ICR {ECO:0000312|EMBL:AAK28061.1};
TISSUE=Testis {ECO:0000312|EMBL:AAK28061.1};
PubMed=14607334; DOI=10.1016/S0304-3835(03)00443-9;
Nakajima A., Kataoka K., Hong M., Sakaguchi M., Huh N.-H.;
"BRPK, a novel protein kinase showing increased expression in mouse
cancer cell lines with higher metastatic potential.";
Cancer Lett. 201:195-201(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4] {ECO:0000305}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH67066.1}, and
Czech II {ECO:0000312|EMBL:AAH44743.1};
TISSUE=Eye {ECO:0000312|EMBL:AAH67066.1}, and
Mammary gland {ECO:0000312|EMBL:AAH44743.1};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
DISRUPTION PHENOTYPE.
PubMed=18687901; DOI=10.1073/pnas.0802076105;
Gautier C.A., Kitada T., Shen J.;
"Loss of PINK1 causes mitochondrial functional defects and increased
sensitivity to oxidative stress.";
Proc. Natl. Acad. Sci. U.S.A. 105:11364-11369(2008).
[6]
DISRUPTION PHENOTYPE.
PubMed=20049710; DOI=10.1002/emmm.200900006;
Morais V.A., Verstreken P., Roethig A., Smet J., Snellinx A.,
Vanbrabant M., Haddad D., Frezza C., Mandemakers W.,
Vogt-Weisenhorn D., Van Coster R., Wurst W., Scorrano L.,
De Strooper B.;
"Parkinson's disease mutations in PINK1 result in decreased Complex I
activity and deficient synaptic function.";
EMBO Mol. Med. 1:99-111(2009).
[7]
SUBUNIT.
PubMed=19229105; DOI=10.1172/JCI37617;
Xiong H., Wang D., Chen L., Choo Y.S., Ma H., Tang C., Xia K.,
Jiang W., Ronai Z., Zhuang X., Zhang Z.;
"Parkin, PINK1, and DJ-1 form a ubiquitin E3 ligase complex promoting
unfolded protein degradation.";
J. Clin. Invest. 119:650-660(2009).
[8]
FUNCTION.
PubMed=24784582; DOI=10.1038/nature13392;
Koyano F., Okatsu K., Kosako H., Tamura Y., Go E., Kimura M.,
Kimura Y., Tsuchiya H., Yoshihara H., Hirokawa T., Endo T., Fon E.A.,
Trempe J.F., Saeki Y., Tanaka K., Matsuda N.;
"Ubiquitin is phosphorylated by PINK1 to activate parkin.";
Nature 510:162-166(2014).
[9]
FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
PubMed=24652937; DOI=10.1126/science.1249161;
Morais V.A., Haddad D., Craessaerts K., De Bock P.J., Swerts J.,
Vilain S., Aerts L., Overbergh L., Gruenewald A., Seibler P.,
Klein C., Gevaert K., Verstreken P., De Strooper B.;
"PINK1 loss-of-function mutations affect mitochondrial complex I
activity via NdufA10 ubiquinone uncoupling.";
Science 344:203-207(2014).
-!- FUNCTION: Protects against mitochondrial dysfunction during
cellular stress by phosphorylating mitochondrial proteins
(PubMed:24652937). Involved in the clearance of damaged
mitochondria via selective autophagy (mitophagy) by mediating
activation and translocation of PRKN (PubMed:24784582). Targets
PRKN to dysfunctional depolarized mitochondria through the
phosphorylation of MFN2 (By similarity). Activates PRKN in 2
steps: (1) by mediating phosphorylation at 'Ser-65' of PRKN and
(2) mediating phosphorylation of ubiquitin, converting PRKN to its
fully-active form (PubMed:24784582). Required for ubiquinone
reduction by mitochondrial complex I by mediating phosphorylation
of complex I subunit NDUFA10 (PubMed:24652937).
{ECO:0000250|UniProtKB:Q9BXM7, ECO:0000269|PubMed:24652937,
ECO:0000269|PubMed:24784582}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:24652937}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- SUBUNIT: Interacts with PRKN and FBXO7 (By similarity). Forms a
complex with PRKN and PARK7 (PubMed:19229105).
{ECO:0000250|UniProtKB:Q9BXM7}.
-!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
{ECO:0000250|UniProtKB:Q9BXM7}; Single-pass membrane protein
{ECO:0000250|UniProtKB:Q9BXM7}. Mitochondrion inner membrane
{ECO:0000269|PubMed:24652937}; Single-pass membrane protein
{ECO:0000255}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9BXM7}.
-!- TISSUE SPECIFICITY: High levels expressed in testis, lower levels
in brain, heart, lung, liver and kidney.
{ECO:0000269|PubMed:14607334}.
-!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:Q9BXM7}.
-!- PTM: Two shorter forms of 55 kDa and 48 kDa seem to be produced by
proteolytic cleavage and localize mainly in cytosol.
{ECO:0000250|UniProtKB:Q9BXM7}.
-!- DISRUPTION PHENOTYPE: Mitochondrial dysfunctions (PubMed:18687901,
PubMed:20049710). Mice do not show gross structural defects in
mitochondria, although the number of larger mitochondria is
selectively increased (PubMed:18687901). Mitochondrial respiration
is impaired in the striatum, which is rich in dopaminergic
terminals, but not in the cerebral cortex in young mice
(PubMed:18687901). Mitochondrial respiration activities in the
cerebral cortex are decreased in 2 years old mice
(PubMed:18687901). Mice show defects in mitochondrial complex I
and a decrease in mitochondrial membrane potential
(PubMed:20049710). {ECO:0000269|PubMed:18687901,
ECO:0000269|PubMed:20049710}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
-----------------------------------------------------------------------
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EMBL; AB053476; BAB55651.1; -; mRNA.
EMBL; AF316872; AAK28061.1; -; mRNA.
EMBL; AL807249; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC044743; AAH44743.1; -; mRNA.
EMBL; BC054349; AAH54349.1; -; mRNA.
EMBL; BC067066; AAH67066.1; -; mRNA.
CCDS; CCDS18825.1; -.
RefSeq; NP_081156.2; NM_026880.2.
UniGene; Mm.18539; -.
ProteinModelPortal; Q99MQ3; -.
SMR; Q99MQ3; -.
BioGrid; 213129; 2.
IntAct; Q99MQ3; 1.
STRING; 10090.ENSMUSP00000030536; -.
iPTMnet; Q99MQ3; -.
PhosphoSitePlus; Q99MQ3; -.
PaxDb; Q99MQ3; -.
PRIDE; Q99MQ3; -.
Ensembl; ENSMUST00000030536; ENSMUSP00000030536; ENSMUSG00000028756.
GeneID; 68943; -.
KEGG; mmu:68943; -.
UCSC; uc008vku.1; mouse.
CTD; 65018; -.
MGI; MGI:1916193; Pink1.
eggNOG; KOG4158; Eukaryota.
eggNOG; ENOG410YE6P; LUCA.
GeneTree; ENSGT00390000001206; -.
HOVERGEN; HBG053601; -.
InParanoid; Q99MQ3; -.
KO; K05688; -.
OMA; FLVMKNY; -.
OrthoDB; EOG091G03V6; -.
PhylomeDB; Q99MQ3; -.
TreeFam; TF313183; -.
Reactome; R-MMU-5205685; Pink/Parkin Mediated Mitophagy.
ChiTaRS; Pink1; mouse.
PRO; PR:Q99MQ3; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000028756; -.
CleanEx; MM_PINK1; -.
ExpressionAtlas; Q99MQ3; baseline and differential.
Genevisible; Q99MQ3; MM.
GO; GO:0097449; C:astrocyte projection; ISO:MGI.
GO; GO:0030424; C:axon; ISO:MGI.
GO; GO:0044297; C:cell body; ISO:MGI.
GO; GO:0000785; C:chromatin; ISO:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005856; C:cytoskeleton; ISO:MGI.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0030426; C:growth cone; ISO:MGI.
GO; GO:0031307; C:integral component of mitochondrial outer membrane; ISO:MGI.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
GO; GO:0005758; C:mitochondrial intermembrane space; ISO:MGI.
GO; GO:0005741; C:mitochondrial outer membrane; ISO:MGI.
GO; GO:0005742; C:mitochondrial outer membrane translocase complex; IEA:Ensembl.
GO; GO:0005739; C:mitochondrion; HDA:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
GO; GO:0031932; C:TORC2 complex; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0055131; F:C3HC4-type RING finger domain binding; ISO:MGI.
GO; GO:0010857; F:calcium-dependent protein kinase activity; ISO:MGI.
GO; GO:0016301; F:kinase activity; IDA:MGI.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0002020; F:protease binding; ISO:MGI.
GO; GO:0004672; F:protein kinase activity; ISO:MGI.
GO; GO:0043422; F:protein kinase B binding; ISO:MGI.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0000422; P:autophagy of mitochondrion; ISS:UniProtKB.
GO; GO:1904881; P:cellular response to hydrogen sulfide; ISO:MGI.
GO; GO:0071456; P:cellular response to hypoxia; IMP:ParkinsonsUK-UCL.
GO; GO:0034599; P:cellular response to oxidative stress; IMP:ParkinsonsUK-UCL.
GO; GO:0097237; P:cellular response to toxic substance; IMP:BHF-UCL.
GO; GO:0072655; P:establishment of protein localization to mitochondrion; ISO:MGI.
GO; GO:0035556; P:intracellular signal transduction; IDA:UniProtKB.
GO; GO:0072656; P:maintenance of protein location in mitochondrion; ISO:MGI.
GO; GO:0007005; P:mitochondrion organization; ISO:MGI.
GO; GO:0099074; P:mitochondrion to lysosome transport; ISO:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
GO; GO:1902902; P:negative regulation of autophagosome assembly; ISO:MGI.
GO; GO:1903147; P:negative regulation of autophagy of mitochondrion; ISO:MGI.
GO; GO:0010629; P:negative regulation of gene expression; IMP:ParkinsonsUK-UCL.
GO; GO:1903384; P:negative regulation of hydrogen peroxide-induced neuron intrinsic apoptotic signaling pathway; ISO:MGI.
GO; GO:1903298; P:negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway; IMP:ParkinsonsUK-UCL.
GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; ISS:UniProtKB.
GO; GO:1903751; P:negative regulation of intrinsic apoptotic signaling pathway in response to hydrogen peroxide; ISO:MGI.
GO; GO:0016242; P:negative regulation of macroautophagy; ISO:MGI.
GO; GO:0090258; P:negative regulation of mitochondrial fission; ISO:MGI.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:ParkinsonsUK-UCL.
GO; GO:1901215; P:negative regulation of neuron death; ISO:MGI.
GO; GO:1903202; P:negative regulation of oxidative stress-induced cell death; ISO:MGI.
GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; ISO:MGI.
GO; GO:0036289; P:peptidyl-serine autophosphorylation; ISO:MGI.
GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:MGI.
GO; GO:1904925; P:positive regulation of autophagy of mitochondrion in response to mitochondrial depolarization; ISO:MGI.
GO; GO:0033605; P:positive regulation of catecholamine secretion; IMP:MGI.
GO; GO:1903852; P:positive regulation of cristae formation; ISO:MGI.
GO; GO:0051091; P:positive regulation of DNA binding transcription factor activity; IMP:ParkinsonsUK-UCL.
GO; GO:0033603; P:positive regulation of dopamine secretion; IMP:MGI.
GO; GO:1901727; P:positive regulation of histone deacetylase activity; IMP:MGI.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISO:MGI.
GO; GO:0016239; P:positive regulation of macroautophagy; ISO:MGI.
GO; GO:1902958; P:positive regulation of mitochondrial electron transport, NADH to ubiquinone; IMP:MGI.
GO; GO:0090141; P:positive regulation of mitochondrial fission; ISO:MGI.
GO; GO:0098779; P:positive regulation of mitophagy in response to mitochondrial depolarization; ISO:MGI.
GO; GO:1904783; P:positive regulation of NMDA glutamate receptor activity; ISO:MGI.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:MGI.
GO; GO:0035307; P:positive regulation of protein dephosphorylation; IMP:ParkinsonsUK-UCL.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; ISO:MGI.
GO; GO:0032226; P:positive regulation of synaptic transmission, dopaminergic; IMP:MGI.
GO; GO:0045727; P:positive regulation of translation; IMP:ParkinsonsUK-UCL.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0050821; P:protein stabilization; IMP:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
GO; GO:1900407; P:regulation of cellular response to oxidative stress; ISO:MGI.
GO; GO:0010310; P:regulation of hydrogen peroxide metabolic process; IMP:ParkinsonsUK-UCL.
GO; GO:0051881; P:regulation of mitochondrial membrane potential; ISO:MGI.
GO; GO:0010821; P:regulation of mitochondrion organization; ISO:MGI.
GO; GO:0043523; P:regulation of neuron apoptotic process; IMP:BHF-UCL.
GO; GO:0002082; P:regulation of oxidative phosphorylation; ISO:MGI.
GO; GO:0043254; P:regulation of protein complex assembly; ISO:MGI.
GO; GO:1903214; P:regulation of protein targeting to mitochondrion; ISO:MGI.
GO; GO:0031396; P:regulation of protein ubiquitination; ISO:MGI.
GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; ISO:MGI.
GO; GO:0022904; P:respiratory electron transport chain; IMP:ParkinsonsUK-UCL.
GO; GO:0002931; P:response to ischemia; IEA:Ensembl.
GO; GO:0006979; P:response to oxidative stress; ISO:MGI.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 3.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
ATP-binding; Autophagy; Complete proteome; Cytoplasm; Kinase;
Magnesium; Membrane; Metal-binding; Mitochondrion;
Mitochondrion inner membrane; Mitochondrion outer membrane;
Nucleotide-binding; Phosphoprotein; Reference proteome;
Serine/threonine-protein kinase; Transferase; Transit peptide;
Transmembrane; Transmembrane helix.
TRANSIT 1 77 Mitochondrion. {ECO:0000255}.
CHAIN 78 580 Serine/threonine-protein kinase PINK1,
mitochondrial.
/FTId=PRO_0000024370.
TOPO_DOM 78 93 Mitochondrial intermembrane.
{ECO:0000255}.
TRANSMEM 94 110 Helical. {ECO:0000255}.
TOPO_DOM 111 580 Cytoplasmic. {ECO:0000255}.
DOMAIN 156 510 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000305}.
NP_BIND 162 170 ATP. {ECO:0000250|UniProtKB:Q02750,
ECO:0000255|PROSITE-ProRule:PRU00159}.
ACT_SITE 361 361 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 186 186 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 227 227 Phosphoserine.
{ECO:0000250|UniProtKB:Q9BXM7}.
MOD_RES 401 401 Phosphoserine.
{ECO:0000250|UniProtKB:Q9BXM7}.
CONFLICT 9 9 R -> P (in Ref. 1; BAB55651).
{ECO:0000305}.
CONFLICT 48 48 Q -> R (in Ref. 2; AAK28061).
{ECO:0000305}.
CONFLICT 249 249 A -> D (in Ref. 2; AAK28061).
{ECO:0000305}.
CONFLICT 425 425 S -> G (in Ref. 4; AAH54349).
{ECO:0000305}.
CONFLICT 475 475 E -> K (in Ref. 2; AAK28061).
{ECO:0000305}.
CONFLICT 476 476 S -> L (in Ref. 4; AAH54349).
{ECO:0000305}.
SEQUENCE 580 AA; 63181 MW; 8AB6994B8B4E443E CRC64;
MAVRQALGRG LQLGRALLLR FAPKPGPLFG WGKPGPAAAW GRGERPGQVV SPGAQPRPVG
LPLPDRYRFF RQSVAGLAAR IQRQFMVRAR GGAGPCGRAV FLAFGLGLGL IEEKQAEGRR
AASACQEIQA IFTQKTKRVS DPLDTRCWQG FRLEDYLIGQ AIGKGCNAAV YEATMPTLPQ
HLEKAKHLGL IGKGPDVVLK GADGEQAPGT PTFPFAIKMM WNISAGSSSE AILSKMSQEL
VPASRVALAG EYGAVTYRRS RDGPKQLAPH PNIIRVFRAF TSSVPLLPGA LADYPDMLPP
HYYPEGLGHG RTLFLVMKNY PCTLRQYLEE QTPSSRLATM MTLQLLEGVD HLVQQGIAHR
DLKSDNILVE WDSDGCPWLV ISDFGCCLAD QHVGLRLPFN SSSVERGGNG SLMAPEVSTA
HSGPSAVIDY SKADTWAVGA IAYEIFGLAN PFYGQGSAHL ESRSYQEAQL PEMPESVPPE
ARRLVRSLLQ REASKRPSAR LAANVLHLSL WGEHLLALKN LKLDKMIAWL LQQSAATLLA
DRLREKSCVE TKLQMLFLAN LECEALCQAA LLLSSWRAAP


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