AKAP2_RAT
ID AKAP2_RAT Reviewed; 870 AA.
AC Q5U301;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=A-kinase anchor protein 2;
DE Short=AKAP-2;
GN Name=Akap2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122; SER-476; SER-641 AND
RP SER-730, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 (By
CC similarity). {ECO:0000250}.
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. {ECO:0000250}.
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DR EMBL; BC085790; AAH85790.1; -; mRNA.
DR AlphaFoldDB; Q5U301; -.
DR CORUM; Q5U301; -.
DR STRING; 10116.ENSRNOP00000015576; -.
DR iPTMnet; Q5U301; -.
DR PhosphoSitePlus; Q5U301; -.
DR PaxDb; Q5U301; -.
DR PeptideAtlas; Q5U301; -.
DR PRIDE; Q5U301; -.
DR UCSC; RGD:1305135; rat.
DR RGD; 1305135; Akap2.
DR eggNOG; ENOG502QR7I; Eukaryota.
DR InParanoid; Q5U301; -.
DR PRO; PR:Q5U301; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
DR GO; GO:0051018; F:protein kinase A binding; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0007015; P:actin filament organization; ISO:RGD.
DR GO; GO:0008104; P:protein localization; ISO:RGD.
DR GO; GO:0007178; P:transmembrane receptor protein serine/threonine kinase signaling pathway; ISO:RGD.
DR InterPro; IPR029304; AKAP2_C.
DR Pfam; PF15304; AKAP2_C; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Isopeptide bond; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..870
FT /note="A-kinase anchor protein 2"
FT /id="PRO_0000380090"
FT REGION 14..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 103..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..589
FT /note="PKA-RII subunit binding domain"
FT /evidence="ECO:0000250"
FT REGION 595..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 740..814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 213..307
FT /evidence="ECO:0000255"
FT COILED 720..755
FT /evidence="ECO:0000255"
FT COMPBIAS 14..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..165
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..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..549
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..664
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2D5"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES 472
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2D5"
FT MOD_RES 476
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 528
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2D5"
FT MOD_RES 537
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2D5"
FT MOD_RES 641
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 730
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 758
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2D5"
FT MOD_RES 789
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2D5"
FT MOD_RES 796
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"
SQ SEQUENCE 870 AA; 95941 MW; 516C22DA6D7A2DD2 CRC64;
MEIGVSVAEC KSVPGITSTP HSKDHSSPFY SPSHNGLLTD HHESLDNDVA REIQYLDEVL
EANCCDSSVD GTYNGISSPE PGAAILVSSL GSPAHSATKV EPIEKASGRQ LPPHIELSRS
PSDSMAEGER ANGHSTDQPQ DMLGNSLQAP ASPSSSTSSH CSSRDGEFTL TTLKKEAKFE
LRAFHEDKKP SKLFEEDEHE KEQFCIRKVR PSEEMIELEK ERRELIRSQA VKKNPGIAAK
WWNPPQKKTI EEQLDEEHLE SHRKYKERKE KRAQQEQLQL QQQQQQQLQQ LQQLQQQQQQ
QLSTSQLCTA PAAHEHLDSI EHTKEDVVTE QIDFSAARKQ FQQMENSRQT LAKGQSTPRL
FSIKPFYKPL GSINSDKPPT ILRPATIGGT VEDSSTQAAK EQKALCVSES QSAGAGTGNA
ATQGKEGPYS EPSKRGPLSK LWAEDGEFTS ARAVLTVVKD EDHGILDQFS RSVNVSLTQE
ELDSGLDELS VRSQDTTVLE TLSNDFSMDN ISDSGASNET PNALQENSLA DFSLPQTPQT
DNPSEGREGV SKSFSDHGFY SPSSTLGDSP SVDDPLEYQA GLLVQNAIQQ AIAEQVDKAE
VHTSKEGSEQ QEPGAMVEEA GSQAPGSEKP QGMFAPPQVS SPVQEKRDVL PKILPGEDKT
LREKGPSQPP TAVQPSGPVN MKETRPEGGY FSKYSEAAEL RSTASLLATQ ESDVMVGPFK
LRSRKQRTLS MIEEEIRAAQ EREEELKRQR QVRQSTPSPR AQNAPSLPSR TTCYKTAPGK
IEKVKPPPSP TTEGPSLQPD LAPEEAAGAQ RPKNLMQTLM EDYETHKSKR RERMDDSSVL
EATRVNRRKS ALALRWEAGI YANQEEEDNE
