PXK_MOUSE
ID PXK_MOUSE Reviewed; 582 AA.
AC Q8BX57; Q3TD60; Q3TEL7; Q3TZZ1; Q3U197; Q3U773; Q3UCS5; Q4FBH7; Q91WB6;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=PX domain-containing protein kinase-like protein;
DE AltName: Full=Modulator of Na,K-ATPase;
DE Short=MONaKA;
GN Name=Pxk {ECO:0000312|MGI:MGI:1289230};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAZ04665.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH ATP1B1 AND ATP1B3.
RC STRAIN=BALB/cJ {ECO:0000312|EMBL:AAZ04665.1};
RC TISSUE=Brain {ECO:0000269|PubMed:16135750};
RX PubMed=16135750; DOI=10.1523/jneurosci.0635-05.2005;
RA Mao H., Ferguson T.S., Cibulsky S.M., Holmqvist M., Ding C., Fei H.,
RA Levitan I.B.;
RT "MONaKA, a novel modulator of the plasma membrane Na,K-ATPase.";
RL J. Neurosci. 25:7934-7943(2005).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAE41231.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC33489.1}, and
RC NOD {ECO:0000312|EMBL:BAE41744.1};
RC TISSUE=Bone marrow {ECO:0000312|EMBL:BAE29537.1},
RC Cerebellum {ECO:0000312|EMBL:BAC33489.1},
RC Spleen {ECO:0000312|EMBL:BAE34065.1}, and
RC Thymus {ECO:0000312|EMBL:BAE41231.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAH16131.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH16131.1};
RC TISSUE=Salivary gland {ECO:0000312|EMBL:AAH16131.1};
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Binds to and modulates brain Na,K-ATPase subunits ATP1B1 and
CC ATP1B3 and may thereby participate in the regulation of electrical
CC excitability and synaptic transmission. May not display kinase
CC activity. {ECO:0000250|UniProtKB:Q7Z7A4, ECO:0000269|PubMed:16135750}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16135750}. Cell
CC membrane {ECO:0000269|PubMed:16135750}; Peripheral membrane protein
CC {ECO:0000269|PubMed:16135750}. Note=Also associates with the plasma
CC membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1 {ECO:0000269|PubMed:16135750}; Synonyms=Long
CC {ECO:0000303|PubMed:16135750};
CC IsoId=Q8BX57-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:16135750}; Synonyms=Short
CC {ECO:0000303|PubMed:16135750};
CC IsoId=Q8BX57-2; Sequence=VSP_051916, VSP_051917;
CC Name=3 {ECO:0000305};
CC IsoId=Q8BX57-3; Sequence=VSP_051914, VSP_051915;
CC -!- TISSUE SPECIFICITY: Isoform 1 is present in all tissues examined.
CC Isoform 2 is found in all tissues except skeletal muscle and very low
CC levels in spleen. Both isoforms are widely expressed throughout the
CC nervous system however levels of isoform 2 are higher in purified
CC hippocampal and cortical neurons whereas glial cells express more
CC isoform 1 than isoform 2. {ECO:0000269|PubMed:16135750}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE33603.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAE33603.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=BAE34065.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; DQ095196; AAZ04664.1; -; mRNA.
DR EMBL; DQ095197; AAZ04665.1; -; mRNA.
DR EMBL; AK048910; BAC33489.1; -; mRNA.
DR EMBL; AK152058; BAE30914.1; -; mRNA.
DR EMBL; AK152789; BAE31498.1; -; mRNA.
DR EMBL; AK153067; BAE31693.1; -; mRNA.
DR EMBL; AK156146; BAE33603.1; ALT_FRAME; mRNA.
DR EMBL; AK157364; BAE34065.1; ALT_FRAME; mRNA.
DR EMBL; AK169565; BAE41231.1; -; mRNA.
DR EMBL; AK170361; BAE41744.1; -; mRNA.
DR EMBL; AK150413; BAE29537.1; -; mRNA.
DR EMBL; AK150337; BAE29479.1; -; mRNA.
DR EMBL; BC016131; AAH16131.1; -; mRNA.
DR CCDS; CCDS26810.1; -. [Q8BX57-1]
DR CCDS; CCDS36799.1; -. [Q8BX57-2]
DR RefSeq; NP_663433.2; NM_145458.3. [Q8BX57-1]
DR RefSeq; NP_840063.1; NM_178279.2. [Q8BX57-2]
DR RefSeq; XP_006518039.1; XM_006517976.3.
DR RefSeq; XP_006518042.1; XM_006517979.3.
DR AlphaFoldDB; Q8BX57; -.
DR SMR; Q8BX57; -.
DR BioGRID; 230057; 4.
DR IntAct; Q8BX57; 1.
DR STRING; 10090.ENSMUSP00000035265; -.
DR iPTMnet; Q8BX57; -.
DR PhosphoSitePlus; Q8BX57; -.
DR EPD; Q8BX57; -.
DR MaxQB; Q8BX57; -.
DR PaxDb; Q8BX57; -.
DR PeptideAtlas; Q8BX57; -.
DR PRIDE; Q8BX57; -.
DR ProteomicsDB; 301929; -. [Q8BX57-1]
DR ProteomicsDB; 301930; -. [Q8BX57-2]
DR ProteomicsDB; 301931; -. [Q8BX57-3]
DR Antibodypedia; 15176; 175 antibodies from 26 providers.
DR DNASU; 218699; -.
DR Ensembl; ENSMUST00000112689; ENSMUSP00000108309; ENSMUSG00000033885. [Q8BX57-2]
DR Ensembl; ENSMUST00000225653; ENSMUSP00000152987; ENSMUSG00000033885. [Q8BX57-1]
DR GeneID; 218699; -.
DR KEGG; mmu:218699; -.
DR UCSC; uc007ser.2; mouse. [Q8BX57-3]
DR UCSC; uc007ses.2; mouse. [Q8BX57-2]
DR UCSC; uc007set.2; mouse. [Q8BX57-1]
DR CTD; 54899; -.
DR MGI; MGI:1289230; Pxk.
DR VEuPathDB; HostDB:ENSMUSG00000033885; -.
DR eggNOG; KOG2101; Eukaryota.
DR GeneTree; ENSGT00390000017669; -.
DR HOGENOM; CLU_036868_0_0_1; -.
DR InParanoid; Q8BX57; -.
DR OMA; NKDYWTV; -.
DR OrthoDB; 995721at2759; -.
DR PhylomeDB; Q8BX57; -.
DR TreeFam; TF324116; -.
DR BioGRID-ORCS; 218699; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Pxk; mouse.
DR PRO; PR:Q8BX57; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q8BX57; protein.
DR Bgee; ENSMUSG00000033885; Expressed in granulocyte and 259 other tissues.
DR ExpressionAtlas; Q8BX57; baseline and differential.
DR Genevisible; Q8BX57; MM.
DR GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0006954; P:inflammatory response; ISO:MGI.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IEP:UniProtKB.
DR GO; GO:0032780; P:negative regulation of ATP-dependent activity; IDA:UniProtKB.
DR GO; GO:0043271; P:negative regulation of ion transport; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR CDD; cd06871; PX_MONaKA; 1.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR037903; MONaKA_PX.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR003124; WH2_dom.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF02205; WH2; 1.
DR SMART; SM00312; PX; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50195; PX; 1.
DR PROSITE; PS51082; WH2; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cell membrane; Cytoplasm; Membrane;
KW Reference proteome.
FT CHAIN 1..582
FT /note="PX domain-containing protein kinase-like protein"
FT /id="PRO_0000086593"
FT DOMAIN 14..126
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT DOMAIN 88..481
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 548..567
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 433..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..460
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..540
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 368..448
FT /note="VAVLESTLSCEACKNGMPTVSRLLQMPLFSDVLLTTSEKPQFKIPTKLKEAL
FT RIAKECIEKRLTEEQKQIHQHRRLTRAQS -> GQYRAWQWGVLGSGSLQSCLSAYQTP
FT RRMEGQLSCSPARALNMWMVCLSVHLSEASGETSVNCTVILKAGQWKENCGQLGF (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_051914"
FT VAR_SEQ 449..582
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_051915"
FT VAR_SEQ 510..515
FT /note="GLSSAL -> VEHAPL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16135750"
FT /id="VSP_051916"
FT VAR_SEQ 516..582
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16135750"
FT /id="VSP_051917"
FT CONFLICT 244
FT /note="K -> R (in Ref. 2; BAE34065)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="L -> P (in Ref. 2; BAE30914/BAE31498/BAE31693)"
FT /evidence="ECO:0000305"
FT CONFLICT 489
FT /note="Missing (in Ref. 1; AAZ04665 and 2; BAC33489/
FT BAE29479/BAE29537/BAE41744/BAE34065)"
FT /evidence="ECO:0000305"
FT CONFLICT 523
FT /note="P -> R (in Ref. 2; BAE41744)"
FT /evidence="ECO:0000305"
FT CONFLICT 539
FT /note="M -> T (in Ref. 2; BAE34065 and 3; AAH16131)"
FT /evidence="ECO:0000305"
FT CONFLICT 579
FT /note="P -> S (in Ref. 2; BAE29537/BAE29479)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 582 AA; 65231 MW; ED554975AECE04AA CRC64;
MAFMEKPPAG KVLLDDTVPL TAAVEASQSL QSHTEYIIRV QRGISAENSW QIVRRYSDFD
LLNNSLQITG LSLPLPPKKL IGNMDREFIA ERQRGLQNYL NVIMANHVLS NCELLKKFLD
PNNYSANYTE IALQQVSMFF RSEPKWEVVE PLKDIGWRIR KKYFLMKIKN QPKERLVLSW
ADLGPDKYLS DKDFQCLIKL LPSCVHPYIY RVTFATASES SALLIRAFNE KGTLKDLIYK
AKPKDPFLKK YCNPKKTQGL ELQQIKTYGR QILEALKFLH DKGFPYGHLH AANVMLDGNT
CRLLDLENSL LGLPSFYRSY FTQFRKINTL ESVDVHCFGH LLYEMTYGRP PDSVPVDSFP
PASSLAVVAV LESTLSCEAC KNGMPTVSRL LQMPLFSDVL LTTSEKPQFK IPTKLKEALR
IAKECIEKRL TEEQKQIHQH RRLTRAQSHH GSEEERKRRK ILARKKSKRS AVENSEEQPV
KHSNSNNSAG SGASSPLTSP SSPTPPSTAG LSSALPPPPP PPPPPPPPAG PSPTSATEMP
APFLPQPVNG VNRGALLSSI QNFQKGTLRK AQTCDHSAPK IG
