AKAP2_MOUSE
ID AKAP2_MOUSE Reviewed; 893 AA.
AC O54931; A2APJ4; O54932; O54933; Q8C5W1;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 3.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=A-kinase anchor protein 2;
DE Short=AKAP-2;
DE AltName: Full=AKAP expressed in kidney and lung;
DE Short=AKAP-KL;
DE AltName: Full=Protein kinase A-anchoring protein 2;
DE Short=PRKA2;
GN Name=Akap2;
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] (ISOFORMS 1; 2 AND 3), ALTERNATIVE SPLICING
RP (ISOFORMS 4 AND 5), AND MUTAGENESIS OF ALA-590 AND ILE-598.
RC TISSUE=Brain;
RX PubMed=9497389; DOI=10.1074/jbc.273.11.6533;
RA Dong F., Feldmesser M., Casadevall A., Rubin C.S.;
RT "Molecular characterization of a cDNA that encodes six isoforms of a novel
RT murine A kinase anchor protein.";
RL J. Biol. Chem. 273:6533-6541(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 [3]
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).
CC -!- FUNCTION: Binds to regulatory subunit (RII) of protein kinase A. May be
CC involved in establishing polarity in signaling systems or in
CC integrating PKA-RII isoforms with downstream effectors to capture,
CC amplify and focus diffuse, trans-cellular signals carried by cAMP.
CC -!- INTERACTION:
CC O54931-3; P12367: Prkar2a; NbExp=3; IntAct=EBI-645828, EBI-645747;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=5;
CC Name=1; Synonyms=KL1A;
CC IsoId=O54931-1; Sequence=Displayed;
CC Name=2; Synonyms=KL2A;
CC IsoId=O54931-2; Sequence=VSP_004099;
CC Name=3; Synonyms=KL3A;
CC IsoId=O54931-3; Sequence=VSP_004097, VSP_004098;
CC Name=4; Synonyms=KL1B;
CC IsoId=O54931-4; Sequence=VSP_018776;
CC Name=5; Synonyms=KL2B;
CC IsoId=O54931-5; Sequence=VSP_018776, VSP_004099;
CC -!- TISSUE SPECIFICITY: Highly expressed in lung and weakly in thymus and
CC cerebellum. Little or no expression in liver, heart and cerebral
CC cortex. All isoforms are expressed in lung, but KL2A and KL2B isoforms
CC are the principal isoforms in cerebellum.
CC -!- DOMAIN: The RII-alpha binding site, predicted to form an amphipathic
CC helix, could participate in protein-protein interactions with a
CC complementary surface on the R-subunit dimer.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative splicing.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative splicing.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: Produced by alternative initiation at Met-
CC 125 of isoform KL1A. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 5]: Produced by alternative initiation at Met-
CC 125 of isoform KL2A. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC02206.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAC02207.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF033274; AAC02206.1; ALT_FRAME; mRNA.
DR EMBL; AF033275; AAC02207.1; ALT_FRAME; mRNA.
DR EMBL; AF033276; AAC02208.1; -; mRNA.
DR EMBL; AK077020; BAC36571.1; -; mRNA.
DR EMBL; AK147420; BAE27901.1; -; mRNA.
DR EMBL; AL840629; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; T09225; T09225.
DR RefSeq; NP_001030609.1; NM_001035532.2. [O54931-2]
DR RefSeq; NP_001030610.1; NM_001035533.2. [O54931-1]
DR RefSeq; NP_001291473.1; NM_001304544.1.
DR AlphaFoldDB; O54931; -.
DR SMR; O54931; -.
DR BioGRID; 198049; 3.
DR IntAct; O54931; 4.
DR MINT; O54931; -.
DR STRING; 10090.ENSMUSP00000048678; -.
DR iPTMnet; O54931; -.
DR PhosphoSitePlus; O54931; -.
DR jPOST; O54931; -.
DR MaxQB; O54931; -.
DR PaxDb; O54931; -.
DR PeptideAtlas; O54931; -.
DR PRIDE; O54931; -.
DR ProteomicsDB; 296011; -. [O54931-1]
DR ProteomicsDB; 296012; -. [O54931-2]
DR ProteomicsDB; 296013; -. [O54931-3]
DR ProteomicsDB; 296015; -. [O54931-5]
DR Ensembl; ENSMUST00000043456; ENSMUSP00000048678; ENSMUSG00000038729. [O54931-1]
DR Ensembl; ENSMUST00000098064; ENSMUSP00000095672; ENSMUSG00000038729. [O54931-2]
DR Ensembl; ENSMUST00000102902; ENSMUSP00000099966; ENSMUSG00000038729. [O54931-3]
DR Ensembl; ENSMUST00000102903; ENSMUSP00000099967; ENSMUSG00000038729. [O54931-3]
DR Ensembl; ENSMUST00000107598; ENSMUSP00000103224; ENSMUSG00000038729. [O54931-2]
DR GeneID; 677884; -.
DR KEGG; mmu:677884; -.
DR UCSC; uc008syj.2; mouse. [O54931-2]
DR UCSC; uc008syk.2; mouse. [O54931-3]
DR UCSC; uc008syl.2; mouse. [O54931-1]
DR CTD; 677884; -.
DR MGI; MGI:1306795; Akap2.
DR VEuPathDB; HostDB:ENSMUSG00000038729; -.
DR eggNOG; ENOG502QR7I; Eukaryota.
DR GeneTree; ENSGT00930000151059; -.
DR HOGENOM; CLU_007780_0_0_1; -.
DR InParanoid; O54931; -.
DR OrthoDB; 604893at2759; -.
DR PhylomeDB; O54931; -.
DR TreeFam; TF105402; -.
DR BioGRID-ORCS; 11641; 6 hits in 41 CRISPR screens.
DR BioGRID-ORCS; 677884; 0 hits in 37 CRISPR screens.
DR PRO; PR:O54931; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; O54931; protein.
DR Bgee; ENSMUSG00000038729; Expressed in lung and 72 other tissues.
DR ExpressionAtlas; O54931; baseline and differential.
DR Genevisible; O54931; MM.
DR InterPro; IPR029304; AKAP2_C.
DR Pfam; PF15304; AKAP2_C; 1.
PE 1: Evidence at protein level;
KW Alternative initiation; Alternative splicing; Coiled coil; Isopeptide bond;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..893
FT /note="A-kinase anchor protein 2"
FT /id="PRO_0000020657"
FT REGION 12..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..599
FT /note="PKA-RII subunit binding domain"
FT REGION 604..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 717..825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 255..316
FT /evidence="ECO:0000255"
FT COILED 729..766
FT /evidence="ECO:0000255"
FT COMPBIAS 12..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..275
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..622
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..674
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..761
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..783
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5U301"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2D5"
FT MOD_RES 357
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5U301"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2D5"
FT MOD_RES 486
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5U301"
FT MOD_RES 538
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2D5"
FT MOD_RES 547
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2D5"
FT MOD_RES 651
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2D5"
FT MOD_RES 740
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2D5"
FT MOD_RES 768
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2D5"
FT MOD_RES 799
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2D5"
FT MOD_RES 806
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2D5"
FT CROSSLNK 174
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2D5"
FT CROSSLNK 174
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2D5"
FT VAR_SEQ 1..124
FT /note="Missing (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_018776"
FT VAR_SEQ 790..795
FT /note="KIEKVK -> PGGHTG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9497389"
FT /id="VSP_004097"
FT VAR_SEQ 796..893
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9497389"
FT /id="VSP_004098"
FT VAR_SEQ 849..861
FT /note="Missing (in isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:9497389"
FT /id="VSP_004099"
FT MUTAGEN 590
FT /note="A->S: No effect on binding to RII."
FT /evidence="ECO:0000269|PubMed:9497389"
FT MUTAGEN 598
FT /note="I->A: Reduces binding to RII."
FT /evidence="ECO:0000269|PubMed:9497389"
FT CONFLICT 120
FT /note="S -> I (in Ref. 1; AAC02206/AAC02207/AAC02208)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="K -> R (in Ref. 1; AAC02206/AAC02207/AAC02208)"
FT /evidence="ECO:0000305"
FT CONFLICT 531
FT /note="P -> T (in Ref. 1; AAC02206/AAC02207/AAC02208)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 893 AA; 98579 MW; 4C9ADD7C4362EF49 CRC64;
MEIGVSVAEC KSVPGVTSTP HSKDHSSPFY SPSHNGLLAD HHESLDNDVA REIQYLDEVL
EANCCDSSVD GTYNGISSPE PGAAILVSSL GSPAHSVTEA EPTEKASGRQ VPPHIELSRS
PSDRMAEGER ANGHSTDQPQ DLLGNSLQAP ASPSSSTSSH CSSRDGEFTL TTLKKEAKFE
LRAFHEDKKP SKLFEEDERE KEQFCVRKVR PSEEMIELEK ERRELIRSQA VKKNPGIAAK
WWNPPQEKTI EEQLDEEHLE SHRKYKERKE KRAQQEQLQL QQQQQQQLQQ QQLQQQQLQQ
QQLQQQLQQQ QLSTSQPCTA PAAHKHLDGI EHTKEDVVTE QIDFSAARKQ FQLMENSRQT
LAKGQSTPRL FSIKPYYKPL GSIHSDKPPT ILRPATVGGT LEDGGTQAAK EQKAPCVSES
QSAGAGPANA ATQGKEGPYS EPSKRGPLSK LWAEDGEFTS ARAVLTVVKD EDHGILDQFS
RSVNVSLTQE ELDSGLDELS VRSQDTTVLE TLSNDFSMDN ISDSGASNET PSALQENSLA
DFSLPQTPQT DNPSEGREGV SKSFSDHGFY SPSSTLGDSP SVDDPLEYQA GLLVQNAIQQ
AIAEQVDKAE AHTSKEGSEQ QEPEATVEEA GSQTPGSEKP QGMFAPPQVS SPVQEKRDIL
PKNLPAEDRA LREKGPSQPP TAAQPSGPVN MEETRPEGGY FSKYSEAAEL RSTASLLATQ
ESDVMVGPFK LRSRKQRTLS MIEEEIRAAQ EREEELKRQR QVRQSTPSPR AKNAPSLPSR
TTCYKTAPGK IEKVKPPPSP TTEGPSLQPD LAPEEAAGTQ RPKNLMQTLM EDYETHKSKR
RERMDDSSYT SKLLSCKVTS EVLEATRVNR RKSALALRWE AGIYANQEEE DNE
