ID   ADCK1_HUMAN             Reviewed;         530 AA.
AC   Q86TW2; B3KUD5; Q6PD65; Q9UIE6;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 2.
DT   27-MAR-2024, entry version 152.
DE   RecName: Full=AarF domain-containing protein kinase 1 {ECO:0000303|PubMed:31125351};
DE            EC=2.7.-.- {ECO:0000255|PROSITE-ProRule:PRU00159};
DE   Flags: Precursor;
GN   Name=ADCK1 {ECO:0000303|PubMed:31125351};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12508121; DOI=10.1038/nature01348;
RA   Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA   Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA   Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA   Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA   Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA   Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA   Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA   Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA   Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA   Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA   Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA   Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA   Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA   Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA   Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA   Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA   Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA   Waterston R., Hood L., Weissenbach J.;
RT   "The DNA sequence and analysis of human chromosome 14.";
RL   Nature 421:601-607(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Skin;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-93 (ISOFORM 1).
RC   TISSUE=Placenta;
RA   Li W.B., Gruber C., Jessee J., Polayes D.;
RT   "Full-length cDNA libraries and normalization.";
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   FUNCTION, AND MUTAGENESIS OF ALA-164; LYS-183 AND ASP-315.
RX   PubMed=31125351; DOI=10.1371/journal.pgen.1008184;
RA   Yoon W., Hwang S.H., Lee S.H., Chung J.;
RT   "Drosophila ADCK1 is critical for maintaining mitochondrial structures and
RT   functions in the muscle.";
RL   PLoS Genet. 15:E1008184-E1008184(2019).
RN   [7]
RP   SUBCELLULAR LOCATION.
RX   PubMed=33988507; DOI=10.7554/elife.64943;
RA   Zhang H., Cao X., Tang M., Zhong G., Si Y., Li H., Zhu F., Liao Q., Li L.,
RA   Zhao J., Feng J., Li S., Wang C., Kaulich M., Wang F., Chen L., Li L.,
RA   Xia Z., Liang T., Lu H., Feng X.H., Zhao B.;
RT   "A subcellular map of the human kinome.";
RL   Elife 10:0-0(2021).
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 (PubMed:31125351). The action of this enzyme is
CC       not yet clear (Probable). It is not known if it has protein kinase
CC       activity and what type of substrate it would phosphorylate (Ser, Thr or
CC       Tyr) (Probable). {ECO:0000269|PubMed:31125351, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:33988507}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q86TW2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q86TW2-2; Sequence=VSP_020885;
CC       Name=3;
CC         IsoId=Q86TW2-3; Sequence=VSP_046794;
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. ADCK protein
CC       kinase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAD62620.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAD62620.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
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DR   EMBL; AK096919; BAG53397.1; -; mRNA.
DR   EMBL; AC008372; AAF23326.1; -; Genomic_DNA.
DR   EMBL; CH471061; EAW81310.1; -; Genomic_DNA.
DR   EMBL; BC058906; AAH58906.1; -; mRNA.
DR   EMBL; BX248292; CAD62620.1; ALT_SEQ; mRNA.
DR   CCDS; CCDS45144.1; -. [Q86TW2-3]
DR   CCDS; CCDS9869.1; -. [Q86TW2-2]
DR   RefSeq; NP_001136017.1; NM_001142545.1. [Q86TW2-3]
DR   RefSeq; NP_065154.2; NM_020421.3. [Q86TW2-2]
DR   AlphaFoldDB; Q86TW2; -.
DR   SMR; Q86TW2; -.
DR   BioGRID; 121401; 77.
DR   IntAct; Q86TW2; 51.
DR   STRING; 9606.ENSP00000238561; -.
DR   ChEMBL; CHEMBL4105885; -.
DR   iPTMnet; Q86TW2; -.
DR   PhosphoSitePlus; Q86TW2; -.
DR   SwissPalm; Q86TW2; -.
DR   BioMuta; ADCK1; -.
DR   DMDM; 115503784; -.
DR   CPTAC; non-CPTAC-6012; -.
DR   CPTAC; non-CPTAC-6013; -.
DR   EPD; Q86TW2; -.
DR   jPOST; Q86TW2; -.
DR   MassIVE; Q86TW2; -.
DR   MaxQB; Q86TW2; -.
DR   PaxDb; 9606-ENSP00000238561; -.
DR   PeptideAtlas; Q86TW2; -.
DR   ProteomicsDB; 69740; -. [Q86TW2-1]
DR   ProteomicsDB; 69741; -. [Q86TW2-2]
DR   ProteomicsDB; 84498; -.
DR   Pumba; Q86TW2; -.
DR   Antibodypedia; 26131; 200 antibodies from 28 providers.
DR   DNASU; 57143; -.
DR   Ensembl; ENST00000238561.10; ENSP00000238561.5; ENSG00000063761.16. [Q86TW2-2]
DR   Ensembl; ENST00000341211.5; ENSP00000339663.5; ENSG00000063761.16. [Q86TW2-3]
DR   GeneID; 57143; -.
DR   KEGG; hsa:57143; -.
DR   MANE-Select; ENST00000238561.10; ENSP00000238561.5; NM_020421.4; NP_065154.2. [Q86TW2-2]
DR   UCSC; uc001xui.3; human. [Q86TW2-1]
DR   AGR; HGNC:19038; -.
DR   CTD; 57143; -.
DR   DisGeNET; 57143; -.
DR   GeneCards; ADCK1; -.
DR   HGNC; HGNC:19038; ADCK1.
DR   HPA; ENSG00000063761; Low tissue specificity.
DR   MIM; 620399; gene.
DR   neXtProt; NX_Q86TW2; -.
DR   OpenTargets; ENSG00000063761; -.
DR   PharmGKB; PA134861355; -.
DR   VEuPathDB; HostDB:ENSG00000063761; -.
DR   eggNOG; KOG1235; Eukaryota.
DR   GeneTree; ENSGT00940000158221; -.
DR   HOGENOM; CLU_006533_2_0_1; -.
DR   InParanoid; Q86TW2; -.
DR   OMA; RCNPEDI; -.
DR   OrthoDB; 177137at2759; -.
DR   PhylomeDB; Q86TW2; -.
DR   TreeFam; TF314889; -.
DR   PathwayCommons; Q86TW2; -.
DR   SignaLink; Q86TW2; -.
DR   BioGRID-ORCS; 57143; 12 hits in 1189 CRISPR screens.
DR   ChiTaRS; ADCK1; human.
DR   GenomeRNAi; 57143; -.
DR   Pharos; Q86TW2; Tchem.
DR   PRO; PR:Q86TW2; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   RNAct; Q86TW2; Protein.
DR   Bgee; ENSG00000063761; Expressed in apex of heart and 179 other cell types or tissues.
DR   ExpressionAtlas; Q86TW2; baseline and differential.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
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; IMP:UniProtKB.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:1903852; P:positive regulation of cristae formation; IMP:UniProtKB.
DR   CDD; cd13969; ADCK1-like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR004147; ABC1_dom.
DR   InterPro; IPR045307; ADCK1_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   PANTHER; PTHR43173:SF28; AARF DOMAIN-CONTAINING PROTEIN KINASE 1; 1.
DR   PANTHER; PTHR43173; ABC1 FAMILY PROTEIN; 1.
DR   Pfam; PF03109; ABC1; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   Genevisible; Q86TW2; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Kinase; Mitochondrion;
KW   Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000305"
FT   CHAIN           ?..530
FT                   /note="AarF domain-containing protein kinase 1"
FT                   /id="PRO_0000252249"
FT   DOMAIN          155..467
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        315
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         161..169
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         183
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   VAR_SEQ         74..148
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_046794"
FT   VAR_SEQ         74..80
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_020885"
FT   MUTAGEN         164
FT                   /note="A->G: No effect on role in maintaining mitochondrial
FT                   structure and function."
FT                   /evidence="ECO:0000269|PubMed:31125351"
FT   MUTAGEN         183
FT                   /note="K->I: No effect on role in maintaining mitochondrial
FT                   structure and function."
FT                   /evidence="ECO:0000269|PubMed:31125351"
FT   MUTAGEN         315
FT                   /note="D->A: No effect on role in maintaining mitochondrial
FT                   structure and function."
FT                   /evidence="ECO:0000269|PubMed:31125351"
FT   CONFLICT        7
FT                   /note="K -> N (in Ref. 1; BAG53397)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   530 AA;  60577 MW;  CBB1DFA87D0F41CF CRC64;
     MARKALKLAS WTSMALAASG IYFYSNKYLD PNDFGAVRVG RAVATTAVIS YDYLTSLKSV
     PYGSEEYLQL RSKSWPVFLQ VHLRSARRLC ELCCANRGTF IKVGQHLGAL DYLLPEEYTS
     TLKVLHSQAP QSSMQEIRQV IREDLGKEIH DLFQSFDDTP LGTASLAQVH KAVLHDGRTV
     AVKVQHPKVR AQSSKDILLM EVLVLAVKQL FPEFEFMWLV DEAKKNLPLE LDFLNEGRNA
     EKVSQMLRHF DFLKVPRIHW DLSTERVLLM EFVDGGQVND RDYMERNKID VNEISRHLGK
     MYSEMIFVNG FVHCDPHPGN VLVRKHPGTG KAEIVLLDHG LYQMLTEEFR LNYCHLWQSL
     IWTDMKRVKE YSQRLGAGDL YPLFACMLTA RSWDSVNRGI SQAPVTATED LEIRNNAANY
     LPQISHLLNH VPRQMLLILK TNDLLRGIEA ALGTRASASS FLNMSRCCIR ALAEHKKKNT
     CSFFRRTQIS FSEAFNLWQI NLHELILRVK GLKLADRVLA LICWLFPAPL
//