AKA10_MOUSE
ID AKA10_MOUSE Reviewed; 662 AA.
AC O88845; Q5SUB5; Q5SUB7; Q7TPE7; Q8BQL6;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 3.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=A-kinase anchor protein 10, mitochondrial;
DE Short=AKAP-10;
DE AltName: Full=Dual specificity A kinase-anchoring protein 2;
DE Short=D-AKAP-2;
DE AltName: Full=Protein kinase A-anchoring protein 10;
DE Short=PRKA10;
DE Flags: Precursor;
GN Name=Akap10;
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] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 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 [MRNA] OF 160-662 (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=9326583; DOI=10.1073/pnas.94.21.11184;
RA Huang L.J.-S., Durick K., Weiner J.A., Chun J., Taylor S.S.;
RT "D-AKAP2, a novel protein kinase A anchoring protein with a putative RGS
RT domain.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:11184-11189(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 177-662 (ISOFORM 1).
RC STRAIN=B5/EGFP; TISSUE=Trophoblast stem cell;
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 SUBCELLULAR LOCATION.
RX PubMed=11248059; DOI=10.1073/pnas.051633398;
RA Wang L., Sunahara R.K., Krumins A., Perkins G., Crochiere M.L., Mackey M.,
RA Bell S., Ellisman M.H., Taylor S.S.;
RT "Cloning and mitochondrial localization of full-length D-AKAP2, a protein
RT kinase A anchoring protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3220-3225(2001).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, Spleen, 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: Differentially targeted protein that binds to type I and II
CC regulatory subunits of protein kinase A and anchors them to the
CC mitochondria or the plasma membrane. Although the physiological
CC relevance between PKA and AKAPS with mitochondria is not fully
CC understood, one idea is that BAD, a proapoptotic member, is
CC phosphorylated and inactivated by mitochondria-anchored PKA. It cannot
CC be excluded too that it may facilitate PKA as well as G protein signal
CC transduction, by acting as an adapter for assembling multiprotein
CC complexes. With its RGS domain, it could lead to the interaction to G-
CC alpha proteins, providing a link between the signaling machinery and
CC the downstream kinase.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11248059}.
CC Membrane {ECO:0000269|PubMed:11248059}. Cytoplasm
CC {ECO:0000269|PubMed:11248059}. Note=Predominantly mitochondrial but
CC also membrane associated and cytoplasmic.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O88845-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O88845-2; Sequence=VSP_014873, VSP_014876;
CC Name=3;
CC IsoId=O88845-3; Sequence=VSP_014874, VSP_014875;
CC -!- TISSUE SPECIFICITY: Highly expressed in testis, kidney and lung,
CC followed by brain, skeletal muscle, liver, spleen and heart. Also
CC expressed in brown adipose tissue and pancreas.
CC -!- DOMAIN: RII-alpha binding site, predicted to form an amphipathic helix,
CC could participate in protein-protein interactions with a complementary
CC surface on the R-subunit dimer.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC61898.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH54105.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK049399; BAC33735.1; -; mRNA.
DR EMBL; AL646042; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF021833; AAC61898.1; ALT_FRAME; mRNA.
DR EMBL; BC054105; AAH54105.1; ALT_INIT; mRNA.
DR CCDS; CCDS24821.1; -. [O88845-1]
DR RefSeq; NP_064305.2; NM_019921.3. [O88845-1]
DR AlphaFoldDB; O88845; -.
DR SMR; O88845; -.
DR IntAct; O88845; 2.
DR STRING; 10090.ENSMUSP00000099710; -.
DR iPTMnet; O88845; -.
DR PhosphoSitePlus; O88845; -.
DR EPD; O88845; -.
DR jPOST; O88845; -.
DR MaxQB; O88845; -.
DR PaxDb; O88845; -.
DR PeptideAtlas; O88845; -.
DR PRIDE; O88845; -.
DR ProteomicsDB; 285791; -. [O88845-1]
DR ProteomicsDB; 285792; -. [O88845-2]
DR ProteomicsDB; 285793; -. [O88845-3]
DR Antibodypedia; 26069; 266 antibodies from 35 providers.
DR DNASU; 56697; -.
DR Ensembl; ENSMUST00000058173; ENSMUSP00000054418; ENSMUSG00000047804. [O88845-2]
DR Ensembl; ENSMUST00000102650; ENSMUSP00000099710; ENSMUSG00000047804. [O88845-1]
DR Ensembl; ENSMUST00000108710; ENSMUSP00000104350; ENSMUSG00000047804. [O88845-3]
DR GeneID; 56697; -.
DR KEGG; mmu:56697; -.
DR UCSC; uc007jii.2; mouse. [O88845-1]
DR UCSC; uc007jik.2; mouse. [O88845-3]
DR CTD; 11216; -.
DR MGI; MGI:1890218; Akap10.
DR VEuPathDB; HostDB:ENSMUSG00000047804; -.
DR eggNOG; KOG3590; Eukaryota.
DR GeneTree; ENSGT00390000015077; -.
DR HOGENOM; CLU_022662_0_0_1; -.
DR InParanoid; O88845; -.
DR OMA; QWQAFDL; -.
DR OrthoDB; 644347at2759; -.
DR PhylomeDB; O88845; -.
DR TreeFam; TF105409; -.
DR Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production.
DR BioGRID-ORCS; 56697; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Akap10; mouse.
DR PRO; PR:O88845; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; O88845; protein.
DR Bgee; ENSMUSG00000047804; Expressed in spermatid and 237 other tissues.
DR Genevisible; O88845; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0051018; F:protein kinase A binding; ISS:MGI.
DR GO; GO:0008104; P:protein localization; IDA:MGI.
DR CDD; cd12804; AKAP10_AKB; 1.
DR Gene3D; 1.10.167.10; -; 2.
DR InterPro; IPR037719; AKAP10_AKB_dom.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR044926; RGS_subdomain_2.
DR Pfam; PF00615; RGS; 2.
DR SMART; SM00315; RGS; 2.
DR SUPFAM; SSF48097; SSF48097; 2.
DR PROSITE; PS50132; RGS; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Membrane; Mitochondrion; Phosphoprotein;
KW Reference proteome; Repeat; Transit peptide.
FT TRANSIT 1..28
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 29..662
FT /note="A-kinase anchor protein 10, mitochondrial"
FT /id="PRO_0000030405"
FT DOMAIN 125..369
FT /note="RGS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT DOMAIN 379..505
FT /note="RGS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 634..647
FT /note="PKA-RII subunit binding"
FT COMPBIAS 27..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43572"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43572"
FT VAR_SEQ 1..79
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_014873"
FT VAR_SEQ 548..560
FT /note="SSVKKASIKILKN -> VLANVTLSMGWEA (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_014874"
FT VAR_SEQ 561..662
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_014875"
FT VAR_SEQ 585..662
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_014876"
FT CONFLICT 177
FT /note="V -> S (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="S -> G (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 343..344
FT /note="AQ -> DT (in Ref. 3; AAC61898)"
FT /evidence="ECO:0000305"
FT CONFLICT 405
FT /note="I -> V (in Ref. 4; AAH54105)"
FT /evidence="ECO:0000305"
FT CONFLICT 649
FT /note="Q -> P (in Ref. 4; AAH54105)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 662 AA; 73632 MW; CB31AF0DF13B3AE6 CRC64;
MRGAGPSPRH SPRALRPDPG PAMSFFRRKV KGKEQEKTLD VKSTKASVAV HSPQKSTKNH
ALLEAAGPSH VAINAISANM DSFSSSRTAT LKKQPSHMEA AHFGDLGRSC LDYQTQETKS
SLSKTLEQVL RDTVVLPYFL QFMELRRMEH LVKFWLEAES FHSTTWSRIR AHSLNTVKQS
SLAEPVSPSK RHETPASSVT EALDRRLGDS SSAPLLVTQS EGTDLSSRTQ NPQNHLLLSQ
EGHSARSLHR EVARTGSHQI PTDSQDSSSR LAVGSRNSCS SPLRELSEKL MKSIEQDAVN
TFTKYISPDA AKPIPITEAM RNDIIAKICG EDGQVDPNCF VLAQAVVFSA MEQEHFSEFL
RSHHFCKYQI EVLTSGTVYL ADILFCESAL FYFSEYMEKE DAVNILQFWL AADNFQSQLA
AKKGQYDGQE AQNDAMILYD KYFSLQATHP LGFDDVVRLE IESNICREGG PLPNCFTTPL
RQAWTTMEKV FLPGFLSSNL YYKYLNDLIH SVRGDEFLGG NVSLAAHGSV CLPEESHSGG
SDGSTAQSSV KKASIKILKN FDEAIIVDAA SLDPESLYQR TYAGKMSFGR VSDLGQFIRE
SEPEPDVKKS KGFMFSQAMK KWVQGNTDEA QEELAWKIAK MIVSDVMQQA HHDQPLEKST
KL
