ALPK2_MOUSE
ID ALPK2_MOUSE Reviewed; 2144 AA.
AC Q91ZB0; E9QL35;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 3.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Alpha-protein kinase 2 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:Q86TB3};
DE AltName: Full=Heart alpha-protein kinase {ECO:0000303|PubMed:10021370};
GN Name=Alpk2 {ECO:0000312|MGI:MGI:2449492};
GN Synonyms=Hak {ECO:0000312|MGI:MGI:2449492};
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAK95953.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 670-2144.
RX PubMed=10021370; DOI=10.1016/s0960-9822(99)80006-2;
RA Ryazanov A.G., Pavur K.S., Dorovkov M.V.;
RT "Alpha-kinases: a new class of protein kinases with a novel catalytic
RT domain.";
RL Curr. Biol. 9:R43-R45(1999).
CC -!- FUNCTION: Protein kinase that recognizes phosphorylation sites in which
CC the surrounding peptides have an alpha-helical conformation
CC (PubMed:10021370). Regulates cardiac development and cardiomyocyte
CC differentiation by negatively regulating Wnt/beta-catenin signaling (By
CC similarity). {ECO:0000250|UniProtKB:Q86TB3,
CC ECO:0000303|PubMed:10021370}.
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:Q86TB3};
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:0000305};
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC {ECO:0000250|UniProtKB:Q86TB3}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Alpha-type
CC protein kinase family. ALPK subfamily. {ECO:0000305}.
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DR EMBL; AC157910; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY044451; AAK95953.1; -; mRNA.
DR CCDS; CCDS50310.1; -.
DR RefSeq; NP_001032371.1; NM_001037294.1.
DR AlphaFoldDB; Q91ZB0; -.
DR SMR; Q91ZB0; -.
DR BioGRID; 230413; 1.
DR STRING; 10090.ENSMUSP00000048752; -.
DR iPTMnet; Q91ZB0; -.
DR PhosphoSitePlus; Q91ZB0; -.
DR EPD; Q91ZB0; -.
DR PaxDb; Q91ZB0; -.
DR PRIDE; Q91ZB0; -.
DR ProteomicsDB; 296177; -.
DR Antibodypedia; 22947; 96 antibodies from 23 providers.
DR DNASU; 225638; -.
DR Ensembl; ENSMUST00000035548; ENSMUSP00000048752; ENSMUSG00000032845.
DR GeneID; 225638; -.
DR KEGG; mmu:225638; -.
DR UCSC; uc008feu.3; mouse.
DR CTD; 115701; -.
DR MGI; MGI:2449492; Alpk2.
DR VEuPathDB; HostDB:ENSMUSG00000032845; -.
DR eggNOG; ENOG502QPP5; Eukaryota.
DR GeneTree; ENSGT00940000160524; -.
DR HOGENOM; CLU_002011_0_0_1; -.
DR InParanoid; Q91ZB0; -.
DR OMA; NWEAGNK; -.
DR OrthoDB; 32441at2759; -.
DR TreeFam; TF332629; -.
DR BioGRID-ORCS; 225638; 4 hits in 76 CRISPR screens.
DR ChiTaRS; Alpk2; mouse.
DR PRO; PR:Q91ZB0; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q91ZB0; protein.
DR Bgee; ENSMUSG00000032845; Expressed in heart right ventricle and 73 other tissues.
DR ExpressionAtlas; Q91ZB0; baseline and differential.
DR Genevisible; Q91ZB0; MM.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0055013; P:cardiac muscle cell development; ISS:UniProtKB.
DR GO; GO:1905223; P:epicardium morphogenesis; ISS:UniProtKB.
DR GO; GO:0030010; P:establishment of cell polarity; ISS:UniProtKB.
DR GO; GO:0003007; P:heart morphogenesis; ISS:UniProtKB.
DR GO; GO:0003308; P:negative regulation of Wnt signaling pathway involved in heart development; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0042981; P:regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; ISS:UniProtKB.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR004166; MHCK_EF2_kinase.
DR Pfam; PF02816; Alpha_kinase; 1.
DR Pfam; PF07679; I-set; 2.
DR SMART; SM00811; Alpha_kinase; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; SSF48726; 2.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51158; ALPHA_KINASE; 1.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Immunoglobulin domain; Kinase; Membrane;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..2144
FT /note="Alpha-protein kinase 2"
FT /id="PRO_0000291383"
FT DOMAIN 7..105
FT /note="Ig-like 1"
FT DOMAIN 1759..1847
FT /note="Ig-like 2"
FT DOMAIN 1874..2106
FT /note="Alpha-type protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00501"
FT REGION 425..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 845..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 881..907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1011..1065
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1316..1340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1471..1509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1565..1587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1629..1696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1720..1754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2109..2144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..463
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..515
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1024..1045
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1480..1494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1570..1587
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1630..1659
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1720..1753
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 33..98
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1781..1831
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 670..671
FT /note="TH -> VD (in Ref. 2; AAK95953)"
FT /evidence="ECO:0000305"
FT CONFLICT 849
FT /note="S -> Y (in Ref. 2; AAK95953)"
FT /evidence="ECO:0000305"
FT CONFLICT 1354
FT /note="I -> M (in Ref. 2; AAK95953)"
FT /evidence="ECO:0000305"
FT CONFLICT 1710
FT /note="A -> V (in Ref. 2; AAK95953)"
FT /evidence="ECO:0000305"
FT CONFLICT 2114
FT /note="K -> R (in Ref. 2; AAK95953)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2144 AA; 233298 MW; ACBCEA70E0BE1C26 CRC64;
MTDPGCPERR TLCFLSTLLS QKVPEKSDVV LRCMIAGQPK PEVTWYKNGQ AIDLGGTVSS
YEFFENQYIH LLHLSCCTQS DAAVYQVSAR NCVGMICCSA SLEVQCLQDP QVSPDPGGGR
DAAGECKTEI REEDSINHTD EKWNPCKKGE STADSFLDKF NHLSSPQIVA RGDSGASNSE
NPQYIKETRQ RMGQYNSNNM QENSFNSNNT AEKQDVSQLW TVNATVPGLV SDGLGYEESN
ESVSPSHQTP KVQKYISFSL PLPETTLGPY PEDSNSINMQ PGPQVSSEDS DSDYELCPEI
TLTYTEEFSD DDLEYLECSD VMTDYSNAVW QRSLQGTDRV FLLESDDEEM EFNECGLGGC
EHFFTEMGCG PQVSGGMWSM NVATGFCSYH SQPQEVRVRS SGTSGHSPLP LHSEMTLTLG
PHQDETAKMT EPGRAPLPTA PEAVENDCSG IRGETRDNPE AGEEFSGDNL QTMDKVETEA
SVKPLSGGSD KTEVKQGLES LARERTDEKY PGSKKAALRP TRARRPGMKA NTKKQLLRDS
APKGTLDLLP KEPTRQPLPG SYGQEPTHTE AGAPGWDSHF HAEVCIPLPA EQDSKILRPP
ADPLSKEEDS SFEGGGALLN KLFEASQIPD RTDHLQMQIQ ETIGESSSLD QMLAFSVPAE
ESSTFAGATT HSVSNLSEIN RENLSLAQYP GLESCPQSLQ QEGRPNRDRD LPGALWAESA
CELSLLEDNE EEESQPPASV ALPQGDGVPC REPEGLSDSF PQPTAPSLPL ENVGSGSRVR
EAAGGVGCFE AGDQETCYAT MDLLVGAPVD KYLPQEICPE DLELTEGQSE VCDLCSPDKI
LAVLQTQGSE PPRSTDKRSQ DGKSAEGLLF NSTFTWDTAK EASEDAVGET AADVENPPST
FSSTLPYSER GFGETQPLCS ETISFVKDSE GSYRSSSLSI PAAIDTLASY SSDRECSKEQ
SAESTANVDC HQVTREMEGI STNAAEVHEI KCHSVSVPQD NDFDVGADQV SCEARDEDNS
QSLPDDDSQS GRSLSSSTGE ATGETLVPAP SSAGDHGHFS MPEGQGLCSR ALQMDNQPVC
QSQAMEGAHS RGLEEHFQEK GSGMKHGIRP QSTSHQVSLS ANDFQEILPS IPTMQQETNV
EPLEHSLADS REEIECSSDP RTSDLVVAEK TVGEDSHLVV SVPALPDILL GEKDDVGLGS
WAVGGKVKII TLEAPVFEIW PPELVRHPGY KEAEAGLTMP GRSWALSDIL RAGATRSEPG
ALGGAAWVPS PQADALMALG ANRDTWLGAA PDRQANCNCL SSQCLSQPRF LESSVDPVED
KELEVTDSPS EVSKTGEMEM PETLNEEQEE TQQILRHPAV VNQSVNFPRI LESSVDPIDD
RGELEGVWPE KPEPSDSSVE GNEFIVGNTC QRVDIQPASL QLPHPQDSGE IIPYEHTTNQ
NRVDGERAEA KTSLPDKAKA EAEAVVWQAQ GPGEEGQGIP SVCSMSQTQD GGDRSLGEAG
QRGTDETEVI SPLSPLSSCL TGVTHTCVKA ETNNSTGHIY GGSEPRTRQS VIPMKTEKGT
IESKCGNHVR SSDDLTNTPC TSSPKGNVTR LSISHGLEEL KSEKLQIAET KPLNSSDSPT
MTLALISGEC ESEKDPKSLL RRDPCPKGST LDSGKKSRDQ QQKPVAAQVS KAPGDQSAMA
GSEEGKKKQE ASGSGHLTAG IKKKILSRVA ALRLRLEEKE NSRKNSIVKK TPKFERSLSR
TDEKRDPKRA PCKAEGKAPV LLKRIQAEMA PEHSGNIKLS CQFSEIHEDS TVCWTKDSKS
IAQAKKSAGD NSSVSLAIVQ AGQKDQGLYY CCLKNSYGKV TAEFNLTAEV LKQLSSHTEY
RGCEEIEFSQ LIFKEDVFND SYFGDHLRGQ ISTEELHFGE GVHRKAFRSK VMQGLMPVFQ
PGHACVLKVH NAVAHGTRNN DELVQRNYKL AAQECYVQNT ARYYAKIYAA EAQPLEGFGE
VPEIIPIFLI HRPENNIPYA TVEEELIGEF VKYSIRDGKE INFLRRDSEA GQKCCTFQHW
VYQKTSGCLL VTDMQGVGMK LTDVGIATLA RGYKGFKGNC SMTFIDQFRA LHQCNKYCKM
LGLKSLQNNS QKPKKPIVGK GRVPTNATQV KTPESETPPA ERKT
