ALPK3_MOUSE
ID ALPK3_MOUSE Reviewed; 1680 AA.
AC Q924C5; D3YUT2; Q5DTY6; Q8C7A3;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Alpha-protein kinase 3 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:Q96QP1};
DE AltName: Full=Myocytic induction/differentiation originator {ECO:0000303|PubMed:11418590};
DE Short=Midori {ECO:0000303|PubMed:11418590};
GN Name=Alpk3 {ECO:0000312|MGI:MGI:2151224};
GN Synonyms=Kiaa1330 {ECO:0000303|Ref.3};
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=BALB/cJ;
RX PubMed=11418590; DOI=10.1074/jbc.m100485200;
RA Hosoda T., Monzen K., Hiroi Y., Oka T., Takimoto E., Yazaki Y., Nagai R.,
RA Komuro I.;
RT "A novel myocyte-specific gene midori promotes the differentiation of
RT P19CL6 cells into cardiomyocytes.";
RL J. Biol. Chem. 276:35978-35989(2001).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 527-1680.
RC TISSUE=Brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1468-1680.
RC STRAIN=C57BL/6J; TISSUE=Heart;
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 [5]
RP PROTEIN SEQUENCE OF 1612-1622, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229 AND SER-1199, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, and Lung;
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).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21441111; DOI=10.1177/0300985811402841;
RA Van Sligtenhorst I., Ding Z.M., Shi Z.Z., Read R.W., Hansen G., Vogel P.;
RT "Cardiomyopathy in alpha-kinase 3 (ALPK3)-deficient mice.";
RL Vet. Pathol. 49:131-141(2012).
CC -!- FUNCTION: Involved in cardiomyocyte differentiation.
CC {ECO:0000269|PubMed:11418590, ECO:0000269|PubMed:21441111}.
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:Q96QP1};
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:0000250|UniProtKB:Q96QP1};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11418590}.
CC -!- TISSUE SPECIFICITY: Expressed in the heart and skeletal muscle of adult
CC mice. {ECO:0000269|PubMed:11418590}.
CC -!- DEVELOPMENTAL STAGE: First detected in the cardiac crescent at 7.5 dpc
CC when the developing heart became visible and remains through to 10.5
CC dpc. {ECO:0000269|PubMed:11418590}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable and were born at the expected
CC Mendelian ratio. They however develop spontaneous cardiomyopathy with
CC features of both hypertrophic and dilated forms of cardiomyopathy.
CC Cardiac hypertrophy is characterized by increased thickness of both
CC left and right ventricular walls and by significantly increased heart
CC weight. Some features are also associated with dilated cardiomyopathy.
CC Cardiomyocytes show an altered architecture, characterized by reduced
CC numbers of abnormal intercalated disks. {ECO:0000269|PubMed:21441111}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Alpha-type
CC protein kinase family. ALPK subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK60496.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF338872; AAK60496.1; ALT_FRAME; mRNA.
DR EMBL; JH584275; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK220384; BAD90441.1; -; Transcribed_RNA.
DR EMBL; AK052268; BAC34907.1; -; mRNA.
DR CCDS; CCDS40004.1; -.
DR RefSeq; NP_473426.2; NM_054085.2.
DR AlphaFoldDB; Q924C5; -.
DR SMR; Q924C5; -.
DR STRING; 10090.ENSMUSP00000102971; -.
DR iPTMnet; Q924C5; -.
DR PhosphoSitePlus; Q924C5; -.
DR PaxDb; Q924C5; -.
DR PRIDE; Q924C5; -.
DR ProteomicsDB; 296101; -.
DR ProteomicsDB; 367490; -.
DR Antibodypedia; 15507; 57 antibodies from 20 providers.
DR DNASU; 116904; -.
DR Ensembl; ENSMUST00000107348; ENSMUSP00000102971; ENSMUSG00000038763.
DR GeneID; 116904; -.
DR KEGG; mmu:116904; -.
DR CTD; 57538; -.
DR MGI; MGI:2151224; Alpk3.
DR VEuPathDB; HostDB:ENSMUSG00000038763; -.
DR eggNOG; ENOG502QPP5; Eukaryota.
DR GeneTree; ENSGT00940000158534; -.
DR HOGENOM; CLU_003270_1_0_1; -.
DR InParanoid; Q924C5; -.
DR OMA; QQVTTAW; -.
DR OrthoDB; 32441at2759; -.
DR TreeFam; TF332629; -.
DR BioGRID-ORCS; 116904; 2 hits in 74 CRISPR screens.
DR PRO; PR:Q924C5; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q924C5; protein.
DR Bgee; ENSMUSG00000038763; Expressed in temporalis muscle and 70 other tissues.
DR GO; GO:0005634; C:nucleus; IDA: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; IMP:MGI.
DR GO; GO:0055007; P:cardiac muscle cell differentiation; IMP:BHF-UCL.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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; 1.
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 1: Evidence at protein level;
KW Developmental protein; Direct protein sequencing; Disulfide bond;
KW Immunoglobulin domain; Kinase; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1680
FT /note="Alpha-protein kinase 3"
FT /id="PRO_0000291531"
FT DOMAIN 77..173
FT /note="Ig-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 1251..1339
FT /note="Ig-like 2"
FT /evidence="ECO:0000255"
FT DOMAIN 1367..1600
FT /note="Alpha-type protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00501"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 785..950
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1078..1128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1147..1244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1603..1680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..426
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..608
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..637
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..693
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..748
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 820..838
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 870..927
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1081..1112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1147..1169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1220..1244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1619..1680
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1199
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT DISULFID 1273..1323
FT /evidence="ECO:0000250|UniProtKB:Q86TB3,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 38
FT /note="S -> N (in Ref. 1; AAK60496)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="L -> LL (in Ref. 1; AAK60496)"
FT /evidence="ECO:0000305"
FT CONFLICT 408
FT /note="V -> A (in Ref. 1; AAK60496)"
FT /evidence="ECO:0000305"
FT CONFLICT 413
FT /note="L -> P (in Ref. 1; AAK60496)"
FT /evidence="ECO:0000305"
FT CONFLICT 662..664
FT /note="Missing (in Ref. 1; AAK60496 and 3; BAD90441)"
FT /evidence="ECO:0000305"
FT CONFLICT 928
FT /note="A -> T (in Ref. 1; AAK60496 and 3; BAD90441)"
FT /evidence="ECO:0000305"
FT CONFLICT 1299
FT /note="S -> R (in Ref. 3; BAD90441)"
FT /evidence="ECO:0000305"
FT CONFLICT 1648
FT /note="S -> G (in Ref. 4; BAC34907)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1680 AA; 180115 MW; 3339AA79D9763C88 CRC64;
MGSRRAAGRG WGLGGRAGAG GDSEDDGPVW TPGPASRSYL LSVRPEASLS SNRLSHPSSG
RSTFCSIIAQ LTEETQPLFE TTLKSRAVSE DSDVRFTCIV TGYPEPEVTW YKDDIELDRY
CGLPKYEITH QGNRHTLQLY RCQEEDAAIY QASARNTKGI VSCSGVLEVG TMTEYKIHQR
WFAKLKRKAA AKMREIEQSW KHGKEASGEA DTLLRKISPD RFQRKRRLSG VEEAVLSTPV
REMEEGSSAA WQEGETESAQ HPGLGLINSF APGEAPTNGE PAPENGEDEE RGLLTYICEV
MELGPQNSPP KESGAKKKRK DEESKPGEQK LELEKAEGSQ CSSENVVPST DKPNSSRREK
STDTQPAQTQ PRGRVARGPG IESTRKTASV LGIQDKVQDV PAPAPAPVPA PALAPAPVPV
PAPTPVPSRS SEQVYFSLKD MFMETTRAGR SQEEEKPPPP STRVAGESPP GKTPVKSRLE
KVPMVSSQPT SSMVPPPIKP LNRKRFAPPK SKVESTTTSL SSQTSESMAQ SLGKALPSAS
TQVPTPPARR RHGTRDSPLQ GQTSHKTPGE ALESPATVAP TKSANSSSDT VSVDHDSSGN
QGATEPMDTE TQEDGRTLVD GRTGSRKKTH TDGKLQVDGR TQGDGAQDRA HASPRTQAGE
KAPTDVVTQG SERPQSDRSS WKNLVTQRRV DMQVGQMQAG ERWQQDPGDA RIQEEEKETQ
SAAGSIPVAF ETQSEQLSMA SLSSLPGALK GSPSGCPRES QAIECFEKST EAPCVQERSD
LMLRSEEAAF RSHEDGLLGP PSGNRTYPTQ LPPEGHSEHL GGQTHQRSEQ EDSLSQCPKK
EQPQEPLHVG LSGGHSTGLS QEVPAMPSLP GTGLTSSLQE ELPGTAASLH TNTDVPLPSR
DQDFPSSAPT LQLGPGSPTQ SHPPEAMATS SEGACAKEPN VDGRSSGTRS CDPGLIDSLK
NYLLLLLKLS SPETSEARAE SQEVADTGGL TSSSTLVPTM EVAGLSPRTS RRILERVENN
HLVQSAQTLL LSPCTSRRLT GLLDREVQAG QQALAAAQCS RGPCPTPLTI PAIVVGEEGS
AGEDSEERTS QESDKKGLLG EVEGHTVESR TQEPCQEEAM PGEALTGLPA ATPEELALGA
RRKRFLPKVR AGSDGEANKA EERESPTVSP RGPRKGLTPG SPGTPGRERR SPTQARKASM
LEVPGAEEEP ATGDLVSRSK DSGLDSEPAV DEGKQEALAK QRKAKDLLKA PQVIRKIRVE
QFPDSSGSLK LWCQFFNIVS DSVLTWAKDQ HPVGEVNRSA GDEGPAALAI VQASPTDCGV
YRCTIQNEHG SASTDFCLSP EVLSGFISRE EGEVGEEIEM TPMVFAKGLA DSGCWGDKLF
GRLVSEELRG GGHGLQKASR AKVIYGLEPI FESGRTCIIK VSSLLVFGPS SETSLLGRNY
DVTIQGCKIQ NMSREYCKIF AAEARAASGF GEVPEIIPLY LIYRPANNIP YATLEEDLGK
PLQTYCSRQW GCAGAPAAAS SSEALQKCQT FQHWLYQWTN GSFLVTDLTG ADWKMTDVQI
ATKLRGYQGL KESCFPALLD QFASSHQCNT YCDMLGLKPL KGPEAAHPQA KAKGSKSPSA
GRKGSQLSPQ PQKKGLPSPQ GSRKSAPSSR ATLQASQAAT VQLLGQPPVQ DGSSKAQSMR
