PXK_RAT
ID PXK_RAT Reviewed; 580 AA.
AC Q4FZZ1; Q7TNZ7;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
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|EMBL:AAP92800.1, ECO:0000312|RGD:727819};
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;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAP92800.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley {ECO:0000312|EMBL:AAP92800.1};
RA Shan Y.X., Yu L.;
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
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).
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 activity
CC (By similarity). {ECO:0000250|UniProtKB:Q7Z7A4,
CC ECO:0000250|UniProtKB:Q8BX57}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Also
CC associates with the plasma membrane. {ECO:0000250}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. {ECO:0000305}.
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DR EMBL; AY327408; AAP92800.1; -; mRNA.
DR EMBL; BC098901; AAH98901.1; -; mRNA.
DR RefSeq; NP_877973.1; NM_182821.1.
DR RefSeq; XP_006251837.1; XM_006251775.1.
DR AlphaFoldDB; Q4FZZ1; -.
DR SMR; Q4FZZ1; -.
DR STRING; 10116.ENSRNOP00000010763; -.
DR ChEMBL; CHEMBL2176805; -.
DR iPTMnet; Q4FZZ1; -.
DR PhosphoSitePlus; Q4FZZ1; -.
DR PaxDb; Q4FZZ1; -.
DR Ensembl; ENSRNOT00000010763; ENSRNOP00000010763; ENSRNOG00000008024.
DR GeneID; 306203; -.
DR KEGG; rno:306203; -.
DR CTD; 54899; -.
DR RGD; 727819; Pxk.
DR eggNOG; KOG2101; Eukaryota.
DR GeneTree; ENSGT00390000017669; -.
DR HOGENOM; CLU_036868_0_0_1; -.
DR InParanoid; Q4FZZ1; -.
DR OrthoDB; 995721at2759; -.
DR PhylomeDB; Q4FZZ1; -.
DR PRO; PR:Q4FZZ1; -.
DR Proteomes; UP000002494; Chromosome 15.
DR Genevisible; Q4FZZ1; RN.
DR GO; GO:0034451; C:centriolar satellite; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0006954; P:inflammatory response; ISO:RGD.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISS:UniProtKB.
DR GO; GO:0032780; P:negative regulation of ATP-dependent activity; ISO:RGD.
DR GO; GO:0043271; P:negative regulation of ion transport; ISO:RGD.
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; 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 2: Evidence at transcript level;
KW Actin-binding; Cell membrane; Cytoplasm; Membrane; Reference proteome.
FT CHAIN 1..580
FT /note="PX domain-containing protein kinase-like protein"
FT /id="PRO_0000086594"
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 549..568
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 433..551
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 CONFLICT 489
FT /note="Missing (in Ref. 1; AAP92800)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 580 AA; 65098 MW; C40F1923DC99C1BB CRC64;
MAFMEKPPAR KVLLDDTVPL TAAVEASQSL QSHTEYIIRV QRGISAENSW QIVRRYSDFD
LLNNSLQITG LSLPLPPKKL IGNMDREFIA ERQKGLQNYL NVIMANHVLS NCELLKKFLD
PNNYSANYTE IALQQVSMFF RSEPKWEVVE PLKDIGWRIR KKYFLMKIKN QPKERLVLSW
ADLGPDKYLS DKDFQCLIKL LPSCVHPYIY RVTFATASES SALLIRTFND KGTLKDLIYK
AKPKDPFLKK YCNPKKTQGL ELQQIKTYGR QILEVLKFLH DKGFPYGHLH AANVMLDGNT
CRLLDLENSL LGLPSFYRSY FTQFRKINTL ESVDVHCFGH LLYEMTYGRP PDSVPVDSFP
PASSMAVVAV LESTLSCEAC KNGMPTVSRL LQMPLFSDVL LTTSEKPQFK IPTKLREALR
IAKECIEKRL TEEQKQIHQH RRLTRAQSHH GSEEERKRRK ILARKKSKRS AVENSEEQPV
KHSNANNSAG SGASSPLTSP SSPTPPSTAG LSSALPPPPP PPPPPPPPAG PSPGTEMPAP
PLPQAVNGVN RGALLSSIQN FQKGTLRKAK TCDHSAPKIG
