AKA11_RAT
ID AKA11_RAT Reviewed; 1129 AA.
AC Q62924;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=A-kinase anchor protein 11;
DE Short=AKAP-11;
DE AltName: Full=A-kinase anchor protein 220 kDa;
DE Short=AKAP 220;
DE AltName: Full=Protein kinase A-anchoring protein 11;
DE Short=PRKA11;
GN Name=Akap11; Synonyms=Akap220;
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 [MRNA].
RC TISSUE=Pituitary;
RX PubMed=8621616; DOI=10.1074/jbc.271.16.9460;
RA Lester L.B., Coghlan V.M., Nauert B., Scott J.D.;
RT "Cloning and characterization of a novel A-kinase anchoring protein. AKAP
RT 220, association with testicular peroxisomes.";
RL J. Biol. Chem. 271:9460-9465(1996).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439 AND SER-440, AND
RP 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 type II regulatory subunits of protein kinase A and
CC anchors/targets them.
CC -!- SUBCELLULAR LOCATION: Peroxisome.
CC -!- TISSUE SPECIFICITY: Expressed in brain and testis.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U48288; AAB06559.1; -; mRNA.
DR PIR; T42732; T42732.
DR AlphaFoldDB; Q62924; -.
DR IntAct; Q62924; 2.
DR MINT; Q62924; -.
DR STRING; 10116.ENSRNOP00000054952; -.
DR iPTMnet; Q62924; -.
DR PaxDb; Q62924; -.
DR PRIDE; Q62924; -.
DR UCSC; RGD:2079; rat.
DR RGD; 2079; Akap11.
DR eggNOG; ENOG502QRN4; Eukaryota.
DR InParanoid; Q62924; -.
DR PRO; PR:Q62924; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005777; C:peroxisome; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0019207; F:kinase regulator activity; IDA:MGI.
DR GO; GO:0051018; F:protein kinase A binding; IBA:GO_Central.
DR GO; GO:0034236; F:protein kinase A catalytic subunit binding; IDA:RGD.
DR GO; GO:0034237; F:protein kinase A regulatory subunit binding; IDA:RGD.
DR GO; GO:0008157; F:protein phosphatase 1 binding; IDA:RGD.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; ISO:RGD.
DR GO; GO:1903142; P:positive regulation of establishment of endothelial barrier; IMP:RGD.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:RGD.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0036010; P:protein localization to endosome; ISO:RGD.
DR GO; GO:0003091; P:renal water homeostasis; ISO:RGD.
DR InterPro; IPR008382; SPHK1-interactor_AKAP_110.
DR PANTHER; PTHR10226; PTHR10226; 1.
PE 1: Evidence at protein level;
KW Peroxisome; Phosphoprotein; Reference proteome.
FT CHAIN 1..1129
FT /note="A-kinase anchor protein 11"
FT /id="PRO_0000064518"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 905..918
FT /note="PKA-RII binding region"
FT REGION 962..1061
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 962..995
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1008..1041
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 251
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKA4"
FT MOD_RES 363
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKA4"
FT MOD_RES 434
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKA4"
FT MOD_RES 439
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 440
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 595
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKA4"
FT MOD_RES 742
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKA4"
FT MOD_RES 835
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKA4"
SQ SEQUENCE 1129 AA; 124482 MW; 6380DEED77EF96A0 CRC64;
MQKMQCHLRR PLHSSSSFSS QAVMMTKPMQ EHKKEYTAQQ ALFRPSGIVT SIPVPLAGSA
LLPYHVSSTL YQSKSLSSSE HNKANGGSPQ EHIAMESSAE EVDCFKNTCL PSELSPCSQN
DFKPTNGDID MQSPSKLMSG SMIISNFSTA MVHTIVNETL ESMTSFKATK PVDTNADYLT
KTIKGKPVLS LCDQAAPQQN KASSKDMFAE HLSKSIIKHS LDKSKSVLPN IDKKPVSKEH
MLVLGEESQL TLGETPKFLD FSDNSPQYCV PECKDSVGFG FSLEALPPCS MMTSQKSDLK
GVMKDKVVTR HNLTNTAFEP LSFGQESSFR PSQTLSSAVL TCVDSLHVED KQKIRDRNVI
PDTPPSTPLV PSQTSSEWDI KKLTKQLKGE LAKEFAPATP PSTPHNSSVG SLSENEQTTI
EKEEFMLKLM RSLSEEVESS EGEEHPEMDV KSEHSGKKGQ FADALATHII SLATEVAASH
LDHEITQEFK VQNSHLTVPS QRSMLPALSH SDESIQTCSF ASDMAAGVIA EAEKVANTRS
CMLFGHERTI CHVEGDRGKA EEKLDVEDIA HPREVETCVL SLPSCMPGLT YKYPSCESVT
DEYAGHIIQV LKQEGGNSEL IMDQYASRLA YRSVKSGVRE AAKTVKVKCS LKLFPMHTSH
VKTNKELLFS SKEHHQEVDK KRQRKKYGSH PCKYQTCDRT QDPCRNELSE LYRFSASLAS
SITRDVKKQL TAPKVDLPKS STDCCLFEKS ECVDNRENVT GPEFSKSCQP LQNHGLCQNT
SSLSGYSCGE SAHTVEQYAR KVVGDTLELS LGPAVFLNSE TTTSPDRITY AEKLSPLINE
ACRYCDLKES HGCIRNSAQL FSKQGPCASA KPSSHSKLSS IRQKSRIFHL DVPQIHLNLD
KRAVLAEKIV AEAIEKAERE LSNTSLAADS GIGQDGISFA ESLTTEIMTT AMTNAGHAVS
SSKEVEDFQS TESLGSQQMN LSVGEDSTGS WSNLSFEDDH QDESSSFHHL SESSNGNSSS
WSSLGLEGDL YENNLSFPTS DSDGPDDRES EQEDGAEGLQ PSGKTLLIVN IDVEPGAVDP
QLRVILQWLI PRRRKLENFI FSTLQRRSLS YFQSSYRRED GKWAMSCRL
