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A-kinase anchor protein 2 (AKAP-2) (AKAP expressed in kidney and lung) (AKAP-KL) (Protein kinase A-anchoring protein 2) (PRKA2)

 AKAP2_MOUSE             Reviewed;         893 AA.
O54931; A2APJ4; O54932; O54933; Q8C5W1;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
28-JUL-2009, sequence version 3.
12-SEP-2018, entry version 148.
RecName: Full=A-kinase anchor protein 2;
Short=AKAP-2;
AltName: Full=AKAP expressed in kidney and lung;
Short=AKAP-KL;
AltName: Full=Protein kinase A-anchoring protein 2;
Short=PRKA2;
Name=Akap2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), ALTERNATIVE SPLICING
(ISOFORMS 4 AND 5), AND MUTAGENESIS OF ALA-590 AND ILE-598.
TISSUE=Brain;
PubMed=9497389; DOI=10.1074/jbc.273.11.6533;
Dong F., Feldmesser M., Casadevall A., Rubin C.S.;
"Molecular characterization of a cDNA that encodes six isoforms of a
novel murine A kinase anchor protein.";
J. Biol. Chem. 273:6533-6541(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Testis;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
-!- FUNCTION: Binds to regulatory subunit (RII) of protein kinase A.
May be involved in establishing polarity in signaling systems or
in integrating PKA-RII isoforms with downstream effectors to
capture, amplify and focus diffuse, trans-cellular signals carried
by cAMP.
-!- INTERACTION:
P12367:Prkar2a; NbExp=3; IntAct=EBI-645828, EBI-645747;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing, Alternative initiation; Named isoforms=5;
Name=1; Synonyms=KL1A;
IsoId=O54931-1; Sequence=Displayed;
Name=2; Synonyms=KL2A;
IsoId=O54931-2; Sequence=VSP_004099;
Note=Produced by alternative splicing.;
Name=3; Synonyms=KL3A;
IsoId=O54931-3; Sequence=VSP_004097, VSP_004098;
Note=Produced by alternative splicing.;
Name=4; Synonyms=KL1B;
IsoId=O54931-4; Sequence=VSP_018776;
Note=Produced by alternative initiation at Met-125 of isoform
KL1A.;
Name=5; Synonyms=KL2B;
IsoId=O54931-5; Sequence=VSP_018776, VSP_004099;
Note=Produced by alternative initiation at Met-125 of isoform
KL2A.;
-!- TISSUE SPECIFICITY: Highly expressed in lung and weakly in thymus
and cerebellum. Little or no expression in liver, heart and
cerebral cortex. All isoforms are expressed in lung, but KL2A and
KL2B isoforms are the principal isoforms in cerebellum.
-!- DOMAIN: The RII-alpha binding site, predicted to form an
amphipathic helix, could participate in protein-protein
interactions with a complementary surface on the R-subunit dimer.
-!- SEQUENCE CAUTION:
Sequence=AAC02206.1; Type=Frameshift; Positions=875; Evidence={ECO:0000305};
Sequence=AAC02207.1; Type=Frameshift; Positions=875; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF033274; AAC02206.1; ALT_FRAME; mRNA.
EMBL; AF033275; AAC02207.1; ALT_FRAME; mRNA.
EMBL; AF033276; AAC02208.1; -; mRNA.
EMBL; AK077020; BAC36571.1; -; mRNA.
EMBL; AK147420; BAE27901.1; -; mRNA.
EMBL; AL840629; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS18203.1; -. [O54931-2]
CCDS; CCDS18204.1; -. [O54931-1]
CCDS; CCDS18205.1; -. [O54931-3]
PIR; T09225; T09225.
RefSeq; NP_001030609.1; NM_001035532.2. [O54931-2]
RefSeq; NP_001030610.1; NM_001035533.2. [O54931-1]
RefSeq; NP_001291473.1; NM_001304544.1.
UniGene; Mm.331630; -.
UniGene; Mm.467752; -.
ProteinModelPortal; O54931; -.
BioGrid; 198049; 2.
IntAct; O54931; 4.
MINT; O54931; -.
STRING; 10090.ENSMUSP00000117466; -.
iPTMnet; O54931; -.
PhosphoSitePlus; O54931; -.
MaxQB; O54931; -.
PaxDb; O54931; -.
PeptideAtlas; O54931; -.
PRIDE; O54931; -.
Ensembl; ENSMUST00000043456; ENSMUSP00000048678; ENSMUSG00000038729. [O54931-1]
Ensembl; ENSMUST00000098064; ENSMUSP00000095672; ENSMUSG00000038729. [O54931-2]
Ensembl; ENSMUST00000102902; ENSMUSP00000099966; ENSMUSG00000038729. [O54931-3]
Ensembl; ENSMUST00000102903; ENSMUSP00000099967; ENSMUSG00000038729. [O54931-3]
Ensembl; ENSMUST00000107598; ENSMUSP00000103224; ENSMUSG00000038729. [O54931-2]
GeneID; 11641; -.
GeneID; 677884; -.
KEGG; mmu:11641; -.
KEGG; mmu:677884; -.
UCSC; uc008syj.2; mouse. [O54931-2]
UCSC; uc008syk.2; mouse. [O54931-3]
UCSC; uc008syl.2; mouse. [O54931-1]
CTD; 11217; -.
CTD; 677884; -.
MGI; MGI:1306795; Akap2.
eggNOG; ENOG410IG9A; Eukaryota.
eggNOG; ENOG410ZMFZ; LUCA.
GeneTree; ENSGT00530000063206; -.
HOGENOM; HOG000231745; -.
HOVERGEN; HBG050477; -.
InParanoid; O54931; -.
KO; K16519; -.
PhylomeDB; O54931; -.
TreeFam; TF105402; -.
ChiTaRS; Akap2; mouse.
PRO; PR:O54931; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000038729; Expressed in 33 organ(s), highest expression level in lung.
CleanEx; MM_AKAP2; -.
ExpressionAtlas; O54931; baseline and differential.
Genevisible; O54931; MM.
GO; GO:0032991; C:protein-containing complex; ISO:MGI.
GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
GO; GO:0051018; F:protein kinase A binding; IPI:MGI.
GO; GO:0007015; P:actin filament organization; IDA:MGI.
GO; GO:0051291; P:protein heterooligomerization; ISO:MGI.
GO; GO:0008104; P:protein localization; IPI:MGI.
GO; GO:0007178; P:transmembrane receptor protein serine/threonine kinase signaling pathway; IPI:MGI.
InterPro; IPR029304; AKAP2_C.
Pfam; PF15304; AKAP2_C; 1.
1: Evidence at protein level;
Alternative initiation; Alternative splicing; Coiled coil;
Complete proteome; Isopeptide bond; Phosphoprotein;
Reference proteome; Ubl conjugation.
CHAIN 1 893 A-kinase anchor protein 2.
/FTId=PRO_0000020657.
REGION 586 599 PKA-RII subunit binding domain.
COILED 255 316 {ECO:0000255}.
COILED 729 766 {ECO:0000255}.
COMPBIAS 274 311 Gln-rich.
MOD_RES 122 122 Phosphoserine.
{ECO:0000250|UniProtKB:Q5U301}.
MOD_RES 152 152 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y2D5}.
MOD_RES 357 357 Phosphoserine.
{ECO:0000250|UniProtKB:Q5U301}.
MOD_RES 482 482 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y2D5}.
MOD_RES 486 486 Phosphoserine.
{ECO:0000250|UniProtKB:Q5U301}.
MOD_RES 538 538 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y2D5}.
MOD_RES 547 547 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9Y2D5}.
MOD_RES 651 651 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y2D5}.
MOD_RES 740 740 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y2D5}.
MOD_RES 768 768 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y2D5}.
MOD_RES 799 799 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y2D5}.
MOD_RES 806 806 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y2D5}.
CROSSLNK 174 174 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:Q9Y2D5}.
CROSSLNK 174 174 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q9Y2D5}.
VAR_SEQ 1 124 Missing (in isoform 4 and isoform 5).
{ECO:0000305}.
/FTId=VSP_018776.
VAR_SEQ 790 795 KIEKVK -> PGGHTG (in isoform 3).
{ECO:0000303|PubMed:9497389}.
/FTId=VSP_004097.
VAR_SEQ 796 893 Missing (in isoform 3).
{ECO:0000303|PubMed:9497389}.
/FTId=VSP_004098.
VAR_SEQ 849 861 Missing (in isoform 2 and isoform 5).
{ECO:0000303|PubMed:16141072,
ECO:0000303|PubMed:9497389}.
/FTId=VSP_004099.
MUTAGEN 590 590 A->S: No effect on binding to RII.
{ECO:0000269|PubMed:9497389}.
MUTAGEN 598 598 I->A: Reduces binding to RII.
{ECO:0000269|PubMed:9497389}.
CONFLICT 120 120 S -> I (in Ref. 1; AAC02206/AAC02207/
AAC02208). {ECO:0000305}.
CONFLICT 264 264 K -> R (in Ref. 1; AAC02206/AAC02207/
AAC02208). {ECO:0000305}.
CONFLICT 531 531 P -> T (in Ref. 1; AAC02206/AAC02207/
AAC02208). {ECO:0000305}.
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


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