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MAP/microtubule affinity-regulating kinase 4 (EC 2.7.11.1)

 MARK4_MOUSE             Reviewed;         752 AA.
Q8CIP4; Q80T81;
08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
12-SEP-2018, entry version 131.
RecName: Full=MAP/microtubule affinity-regulating kinase 4;
EC=2.7.11.1 {ECO:0000250|UniProtKB:Q96L34};
Name=Mark4; Synonyms=Kiaa1860;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
PubMed=16973293; DOI=10.1016/j.neuroscience.2006.07.052;
Moroni R.F., De Biasi S., Colapietro P., Larizza L., Beghini A.;
"Distinct expression pattern of microtubule-associated
protein/microtubule affinity-regulating kinase 4 in differentiated
neurons.";
Neuroscience 143:83-94(2006).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 29-752 (ISOFORMS 1 AND 2), AND TISSUE
SPECIFICITY.
PubMed=15009667; DOI=10.1046/j.1471-4159.2003.02228.x;
Schneider A., Laage R., von Ahsen O., Fischer A., Rossner M.,
Scheek S., Grunewald S., Kuner R., Weber D., Kruger C., Klaussner B.,
Gotz B., Hiemisch H., Newrzella D., Martin-Villalba A., Bach A.,
Schwaninger M.;
"Identification of regulated genes during permanent focal cerebral
ischaemia: characterization of the protein kinase 9b5/MARKL1/MARK4.";
J. Neurochem. 88:1114-1126(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 119-752 (ISOFORM 1).
TISSUE=Pancreatic islet;
PubMed=12693553; DOI=10.1093/dnares/10.1.35;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
Nakajima D., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
II. The complete nucleotide sequences of 400 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 10:35-48(2003).
[4]
SEQUENCE REVISION.
Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
PROTEIN SEQUENCE OF 299-308, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=OF1; TISSUE=Hippocampus;
Lubec G., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-423, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=22992738; DOI=10.1074/jbc.M112.388934;
Sun C., Tian L., Nie J., Zhang H., Han X., Shi Y.;
"Inactivation of MARK4, an AMP-activated protein kinase (AMPK)-related
kinase, leads to insulin hypersensitivity and resistance to diet-
induced obesity.";
J. Biol. Chem. 287:38305-38315(2012).
[8]
FUNCTION.
PubMed=24989893; DOI=10.1111/boc.201400004;
Feng M., Tian L., Gan L., Liu Z., Sun C.;
"Mark4 promotes adipogenesis and triggers apoptosis in 3T3-L1
adipocytes by activating JNK1 and inhibiting p38MAPK pathways.";
Biol. Cell 106:294-307(2014).
-!- FUNCTION: Serine/threonine-protein kinase (By similarity).
Phosphorylates the microtubule-associated protein MAPT/TAU (By
similarity). Also phosphorylates the microtubule-associated
proteins MAP2 and MAP4 (By similarity). Involved in regulation of
the microtubule network, causing reorganization of microtubules
into bundles (By similarity). Required for the initiation of
axoneme extension during cilium assembly (By similarity).
Regulates the centrosomal location of ODF2 and phosphorylates ODF2
in vitro (By similarity). Plays a role in cell cycle progression,
specifically in the G1/S checkpoint (By similarity). Reduces
neuronal cell survival (By similarity). Plays a role in energy
homeostasis by regulating satiety and metabolic rate
(PubMed:22992738). Promotes adipogenesis by activating JNK1 and
inhibiting the p38MAPK pathway, and triggers apoptosis by
activating the JNK1 pathway (PubMed:24989893). Phosphorylates
mTORC1 complex member RPTOR and acts as a negative regulator of
the mTORC1 complex, probably due to disruption of the interaction
between phosphorylated RPTOR and the RRAGA/RRAGC heterodimer which
is required for mTORC1 activation (By similarity).
{ECO:0000250|UniProtKB:Q96L34, ECO:0000269|PubMed:22992738,
ECO:0000269|PubMed:24989893}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000250|UniProtKB:Q96L34}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:Q96L34};
-!- ACTIVITY REGULATION: Activated by phosphorylation on Thr-214.
{ECO:0000250|UniProtKB:Q96L34}.
-!- SUBUNIT: Interacts with MAPT/TAU. Interacts with gamma-tubulin.
Interacts with ODF2. Interacts with USP9X.
{ECO:0000250|UniProtKB:Q96L34}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome {ECO:0000250|UniProtKB:Q96L34}.
Cytoplasm, cytoskeleton, microtubule organizing center
{ECO:0000250|UniProtKB:Q96L34}. Cytoplasm, cytoskeleton, cilium
axoneme {ECO:0000250|UniProtKB:Q96L34}. Cytoplasm, cytoskeleton,
cilium basal body {ECO:0000250|UniProtKB:Q96L34}. Cytoplasm
{ECO:0000250|UniProtKB:Q96L34}. Cell projection, dendrite
{ECO:0000250|UniProtKB:Q96L34}. Note=Localized at the tips of
neurite-like processes in differentiated neuroblast cells.
Detected in the cytoplasm and neuropil of the hippocampus.
{ECO:0000250|UniProtKB:Q96L34}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=MARK4L;
IsoId=Q8CIP4-1; Sequence=Displayed;
Name=2; Synonyms=MARK4S;
IsoId=Q8CIP4-2; Sequence=VSP_058199;
-!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 show similar
expression patterns in the central nervous system and are present
in the same subsets of neurons including pyramidal and non-
pyramidal neurons in the cerebral cortex and hippocampus,
cerebellar Purkinje cells, and interneurons and motor neurons in
the spinal cord but not in glial cells (at protein level)
(PubMed:16973293). Isoform 2 is the major isoform in brain and
cerebellum (PubMed:16973293, PubMed:15009667). Also expressed in
spleen, liver, small intestine, colon, kidney, tongue, testis and
lung (PubMed:16973293, PubMed:15009667). Isoform 1 and isoform 2
are expressed at similar levels in heart (PubMed:16973293).
{ECO:0000269|PubMed:15009667, ECO:0000269|PubMed:16973293}.
-!- PTM: Ubiquitinated with 'Lys-29'- and 'Lys-33'-linked
polyubiquitins which appear to impede LKB1-mediated
phosphorylation. Deubiquitinated by USP9X (By similarity).
{ECO:0000250|UniProtKB:Q96L34}.
-!- PTM: Phosphorylated at Thr-214 by STK11/LKB1 in complex with
STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39.
Phosphorylated throughout the cell cycle.
{ECO:0000250|UniProtKB:Q96L34}.
-!- DISRUPTION PHENOTYPE: Hyperphagia, hyperactivity and
hypermetabolism leading to protection from diet-induced obesity,
and improved glucose homeostasis due to up-regulation of AMPK
kinase activity. {ECO:0000269|PubMed:22992738}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
Ser/Thr protein kinase family. SNF1 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AY151083; AAN60072.1; -; mRNA.
EMBL; AX305103; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AX305104; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AK122565; BAC65847.2; -; mRNA.
CCDS; CCDS20903.1; -. [Q8CIP4-1]
RefSeq; NP_758483.1; NM_172279.1. [Q8CIP4-1]
RefSeq; XP_006539892.1; XM_006539829.3. [Q8CIP4-2]
UniGene; Mm.260504; -.
ProteinModelPortal; Q8CIP4; -.
SMR; Q8CIP4; -.
BioGrid; 231328; 4.
DIP; DIP-60721N; -.
IntAct; Q8CIP4; 4.
STRING; 10090.ENSMUSP00000082862; -.
iPTMnet; Q8CIP4; -.
PhosphoSitePlus; Q8CIP4; -.
MaxQB; Q8CIP4; -.
PaxDb; Q8CIP4; -.
PeptideAtlas; Q8CIP4; -.
PRIDE; Q8CIP4; -.
DNASU; 232944; -.
Ensembl; ENSMUST00000085715; ENSMUSP00000082862; ENSMUSG00000030397. [Q8CIP4-1]
GeneID; 232944; -.
KEGG; mmu:232944; -.
UCSC; uc009flx.1; mouse. [Q8CIP4-1]
CTD; 57787; -.
MGI; MGI:1920955; Mark4.
eggNOG; KOG0586; Eukaryota.
eggNOG; ENOG410XNQ0; LUCA.
GeneTree; ENSGT00900000140806; -.
HOGENOM; HOG000233025; -.
HOVERGEN; HBG052453; -.
InParanoid; Q8CIP4; -.
KO; K08798; -.
OMA; LAHEATP; -.
OrthoDB; EOG091G0D1E; -.
PhylomeDB; Q8CIP4; -.
TreeFam; TF315213; -.
Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
ChiTaRS; Mark4; mouse.
PRO; PR:Q8CIP4; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000030397; Expressed in 264 organ(s), highest expression level in olfactory bulb.
CleanEx; MM_MARK4; -.
ExpressionAtlas; Q8CIP4; baseline and differential.
Genevisible; Q8CIP4; MM.
GO; GO:0005813; C:centrosome; ISS:UniProtKB.
GO; GO:0036064; C:ciliary basal body; ISO:MGI.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0030425; C:dendrite; ISS:UniProtKB.
GO; GO:0000930; C:gamma-tubulin complex; ISO:MGI.
GO; GO:0005874; C:microtubule; ISO:MGI.
GO; GO:0015630; C:microtubule cytoskeleton; ISS:UniProtKB.
GO; GO:0005815; C:microtubule organizing center; ISS:UniProtKB.
GO; GO:0030496; C:midbody; ISO:MGI.
GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0043015; F:gamma-tubulin binding; ISS:UniProtKB.
GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
GO; GO:0050321; F:tau-protein kinase activity; ISS:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0044782; P:cilium organization; ISO:MGI.
GO; GO:0030010; P:establishment of cell polarity; IEA:InterPro.
GO; GO:0001578; P:microtubule bundle formation; ISS:UniProtKB.
GO; GO:0000226; P:microtubule cytoskeleton organization; ISS:UniProtKB.
GO; GO:0007399; P:nervous system development; ISS:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; ISO:MGI.
GO; GO:0045724; P:positive regulation of cilium assembly; ISO:MGI.
GO; GO:1904781; P:positive regulation of protein localization to centrosome; ISO:MGI.
GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
GO; GO:0046605; P:regulation of centrosome cycle; ISO:MGI.
InterPro; IPR028375; KA1/Ssp2_C.
InterPro; IPR001772; KA1_dom.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR033624; MARK/par1.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
InterPro; IPR015940; UBA.
PANTHER; PTHR24346; PTHR24346; 1.
Pfam; PF02149; KA1; 1.
Pfam; PF00069; Pkinase; 1.
Pfam; PF00627; UBA; 1.
SMART; SM00220; S_TKc; 1.
SMART; SM00165; UBA; 1.
SUPFAM; SSF103243; SSF103243; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50032; KA1; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PROSITE; PS50030; UBA; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Cell cycle; Cell division;
Cell projection; Cilium biogenesis/degradation; Complete proteome;
Cytoplasm; Cytoskeleton; Direct protein sequencing; Kinase; Mitosis;
Nucleotide-binding; Phosphoprotein; Reference proteome;
Serine/threonine-protein kinase; Transferase; Ubl conjugation.
CHAIN 1 752 MAP/microtubule affinity-regulating
kinase 4.
/FTId=PRO_0000086308.
DOMAIN 59 310 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 324 368 UBA. {ECO:0000255|PROSITE-
ProRule:PRU00212}.
DOMAIN 703 752 KA1. {ECO:0000255|PROSITE-
ProRule:PRU00565}.
NP_BIND 65 73 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 181 181 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 88 88 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 214 214 Phosphothreonine; by LKB1.
{ECO:0000250|UniProtKB:Q96L34}.
MOD_RES 423 423 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 543 543 Phosphoserine.
{ECO:0000250|UniProtKB:Q96L34}.
VAR_SEQ 628 752 TDEPERIGGPEVTSCHLPWDKTETAPRLLRFPWSVKLTSSR
PPEALMAALRQATAAARCRCRQPQPFLLACLHGGAGGPEPL
SHFEVEVCQLPRPGLRGVLFRRVAGTALAFRTLVTRISNDL
EL -> TLDPSKRQNSNRCVSGASLPQGSKIRSQTNLRESG
DLRSQVAIYLGIKRKPPPGCSDSPGV (in isoform
2). {ECO:0000303|PubMed:15009667}.
/FTId=VSP_058199.
CONFLICT 162 162 F -> L (in Ref. 2; AX305103/AX305104).
{ECO:0000305}.
CONFLICT 268 268 V -> I (in Ref. 2; AX305103/AX305104).
{ECO:0000305}.
CONFLICT 372 372 E -> D (in Ref. 2; AX305103/AX305104).
{ECO:0000305}.
CONFLICT 438 438 S -> T (in Ref. 2; AX305103).
{ECO:0000305}.
CONFLICT 677 677 L -> M (in Ref. 2; AX305103).
{ECO:0000305}.
SEQUENCE 752 AA; 82644 MW; 185FDAE3F0D627DD CRC64;
MSSRTALAPG NDRNSDTHGT LGSGRSSDKG PSWSSRSLGA RCRNSIASCP EEQPHVGNYR
LLRTIGKGNF AKVKLARHIL TGREVAIKII DKTQLNPSSL QKLFREVRIM KGLNHPNIVK
LFEVIETEKT LYLVMEYASA GEVFDYLVSH GRMKEKEARA KFRQIVSAVH YCHQKNIVHR
DLKAENLLLD AEANIKIADF GFSNEFTLGS KLDTFCGSPP YAAPELFQGK KYDGPEVDIW
SLGVILYTLV SGSLPFDGHN LKELRERVLR GKYRVPFYMS TDCESILRRF LVLNPAKRCT
LEQIMKDKWI NIGYEGEELK PYTEPEEDFG DTKRIEVMVG MGYTREEIKE ALTNQKYNEV
TATYLLLGRK TEEGGDRGAP GLALARVRAP SDTTNGTSSS KGSSHNKGQR ASSSTYHRQR
RHSDFCGPSP APLHPKRSPT STGDTELKEE RMPGRKASCS AVGSGSRGLP PSSPMVSSAH
NPNKAEIPER RKDSTSTPNN LPPSMMTRRN TYVCTERPGS ERPSLLPNGK ENSSGTSRVP
PASPSSHSLA PPSGERSRLA RGSTIRSTFH GGQVRDRRAG SGSGGGVQNG PPASPTLAHE
AAPLPSGRPR PTTNLFTKLT SKLTRRVTDE PERIGGPEVT SCHLPWDKTE TAPRLLRFPW
SVKLTSSRPP EALMAALRQA TAAARCRCRQ PQPFLLACLH GGAGGPEPLS HFEVEVCQLP
RPGLRGVLFR RVAGTALAFR TLVTRISNDL EL


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