ADCK1_MOUSE
ID ADCK1_MOUSE Reviewed; 525 AA.
AC Q9D0L4; Q3UKJ2;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=AarF domain-containing protein kinase 1 {ECO:0000305};
DE EC=2.7.-.- {ECO:0000255|PROSITE-ProRule:PRU00159};
DE Flags: Precursor;
GN Name=Adck1;
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 MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Placenta;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Liver;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, and Testis;
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: Appears to be essential for maintaining mitochondrial cristae
CC formation and mitochondrial function by acting via YME1L1 in a kinase-
CC independent manner to regulate essential mitochondrial structural
CC proteins OPA1 and IMMT (By similarity). The action of this enzyme is
CC not yet clear. It is not known if it has protein kinase activity and
CC what type of substrate it would phosphorylate (Ser, Thr or Tyr)
CC (Probable). {ECO:0000250|UniProtKB:Q86TW2, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9D0L4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D0L4-2; Sequence=VSP_020886;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. ADCK protein
CC kinase family. {ECO:0000305}.
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DR EMBL; AK011310; BAB27536.1; -; mRNA.
DR EMBL; AK050868; BAC34439.1; -; mRNA.
DR EMBL; AK145987; BAE26809.1; -; mRNA.
DR EMBL; AK154839; BAE32867.1; -; mRNA.
DR EMBL; BC010539; AAH10539.1; -; mRNA.
DR CCDS; CCDS26087.1; -. [Q9D0L4-1]
DR RefSeq; NP_001264225.1; NM_001277296.1. [Q9D0L4-1]
DR RefSeq; NP_001264226.1; NM_001277297.1. [Q9D0L4-1]
DR RefSeq; NP_082381.1; NM_028105.4. [Q9D0L4-1]
DR AlphaFoldDB; Q9D0L4; -.
DR SMR; Q9D0L4; -.
DR BioGRID; 215160; 2.
DR STRING; 10090.ENSMUSP00000127254; -.
DR PhosphoSitePlus; Q9D0L4; -.
DR SwissPalm; Q9D0L4; -.
DR EPD; Q9D0L4; -.
DR MaxQB; Q9D0L4; -.
DR PaxDb; Q9D0L4; -.
DR PeptideAtlas; Q9D0L4; -.
DR PRIDE; Q9D0L4; -.
DR ProteomicsDB; 285677; -. [Q9D0L4-1]
DR ProteomicsDB; 285678; -. [Q9D0L4-2]
DR Antibodypedia; 26131; 188 antibodies from 28 providers.
DR DNASU; 72113; -.
DR Ensembl; ENSMUST00000101165; ENSMUSP00000098724; ENSMUSG00000021044. [Q9D0L4-1]
DR Ensembl; ENSMUST00000166940; ENSMUSP00000127254; ENSMUSG00000021044. [Q9D0L4-1]
DR Ensembl; ENSMUST00000222695; ENSMUSP00000152821; ENSMUSG00000021044. [Q9D0L4-1]
DR GeneID; 72113; -.
DR KEGG; mmu:72113; -.
DR UCSC; uc007oju.2; mouse. [Q9D0L4-1]
DR CTD; 57143; -.
DR MGI; MGI:1919363; Adck1.
DR VEuPathDB; HostDB:ENSMUSG00000021044; -.
DR eggNOG; KOG1235; Eukaryota.
DR GeneTree; ENSGT00940000158221; -.
DR HOGENOM; CLU_006533_2_0_1; -.
DR InParanoid; Q9D0L4; -.
DR OMA; PYVKGNS; -.
DR OrthoDB; 790106at2759; -.
DR PhylomeDB; Q9D0L4; -.
DR TreeFam; TF314889; -.
DR BioGRID-ORCS; 72113; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Adck1; mouse.
DR PRO; PR:Q9D0L4; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q9D0L4; protein.
DR Bgee; ENSMUSG00000021044; Expressed in saccule of membranous labyrinth and 221 other tissues.
DR Genevisible; Q9D0L4; MM.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0032592; C:integral component of mitochondrial membrane; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0055088; P:lipid homeostasis; IBA:GO_Central.
DR GO; GO:0007005; P:mitochondrion organization; IBA:GO_Central.
DR GO; GO:0010637; P:negative regulation of mitochondrial fusion; ISS:UniProtKB.
DR GO; GO:1903852; P:positive regulation of cristae formation; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR CDD; cd13969; ADCK1-like; 1.
DR InterPro; IPR004147; ABC1_dom.
DR InterPro; IPR045307; ADCK1_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR Pfam; PF03109; ABC1; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Kinase; Nucleotide-binding;
KW Reference proteome; Secreted; Serine/threonine-protein kinase; Signal;
KW Transferase.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..525
FT /note="AarF domain-containing protein kinase 1"
FT /id="PRO_0000252250"
FT DOMAIN 148..477
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 308
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 154..162
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 1..192
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020886"
SQ SEQUENCE 525 AA; 59736 MW; 26947FCC43CDB967 CRC64;
MARKALKLAS WTSVALAASG VYLYSNNYLD PNDFGAVRVG RAVATTAVIS YDYLTSLRSV
PYGSEEYLQR RSQVHLRSAR RLFELCCANR GTFIKVGQHL GALDYLLPEE YTSTLKVLHS
QAPQSSMQEV RQVIREDLGK EIHDLFLSFD DTPLGAASLA QVHKAVLHDG RTVAVKVQHP
KVQAQSSKDI LLMEVLVLAV KQLFPDFEFM WLVDEAKKNL PLELDFLNEG RNAEKVAHML
RHFDFLKVPQ IHWELSTKRV LLMEFVEGGQ VNDRAYMEKN QIDVNEISCH LGKMYSEMIF
VNGFVHCDPH PGNVLVRKRP DTGKAEIVLL DHGLYQVLTE EFRLDYCHLW QSLIWTDMDG
LKQYSQRLGA ADLYPLFACM LTARSWDSVK QGIGQAPVSA TEDSEIRNNA ACYLPEISQL
LNHVPRQMLL ILKTNDLLRS IETTLGTRSS ASSFLNMSRC CIRALAEHKK RDAGSFFRRT
QISFSEAFSL WQINLHELLL RVRALRLACW VSALLGWLTR APHRM
