AKAP1_RAT
ID AKAP1_RAT Reviewed; 854 AA.
AC O88884; O88980;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 154.
DE RecName: Full=A-kinase anchor protein 1, mitochondrial;
DE AltName: Full=A-kinase anchor protein 121 kDa;
DE Short=AKAP 121;
DE AltName: Full=Dual specificity A-kinase-anchoring protein 1;
DE Short=D-AKAP-1;
DE AltName: Full=Protein kinase A-anchoring protein 1;
DE Short=PRKA1;
DE AltName: Full=Spermatid A-kinase anchor protein 84;
DE Short=S-AKAP84;
DE Flags: Precursor;
GN Name=Akap1 {ECO:0000312|RGD:620826}; Synonyms=Akap;
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] (ISOFORMS 1 AND 2).
RC TISSUE=Thyroid;
RX PubMed=9722570; DOI=10.1074/jbc.273.36.23361;
RA Feliciello A., Rubin C.S., Avvedimento E.V., Gottesman M.E.;
RT "Expression of a kinase anchor protein 121 is regulated by hormones in
RT thyroid and testicular germ cells.";
RL J. Biol. Chem. 273:23361-23366(1998).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101 AND SER-103, 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 I and II regulatory subunits of protein kinase
CC A and anchors them to the cytoplasmic face of the mitochondrial outer
CC membrane (By similarity). Involved in mitochondrial-mediated antiviral
CC innate immunity (By similarity). Promotes translocation of NDUFS1 into
CC mitochondria to regulate mitochondrial membrane respiratory chain NADH
CC dehydrogenase (Complex I) activity (By similarity).
CC {ECO:0000250|UniProtKB:O08715, ECO:0000250|UniProtKB:Q92667}.
CC -!- SUBUNIT: Interacts with SLC8A3. Interacts with CFAP91. Interacts with
CC CLPB (By similarity). Interacts with NDUFS1 (By similarity).
CC {ECO:0000250|UniProtKB:O08715, ECO:0000250|UniProtKB:Q92667}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:O08715}. Mitochondrion
CC {ECO:0000250|UniProtKB:O08715}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=AKAP121;
CC IsoId=O88884-1; Sequence=Displayed;
CC Name=2; Synonyms=S-AKAP84;
CC IsoId=O88884-2; Sequence=VSP_002854, VSP_002855;
CC -!- TISSUE SPECIFICITY: Testis specific.
CC -!- INDUCTION: By thyroid stimulating hormone (TSH) and cAMP or cAMP-
CC analog.
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.
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DR EMBL; AF068202; AAC33895.1; -; mRNA.
DR EMBL; AF092523; AAC61775.1; -; mRNA.
DR RefSeq; NP_446117.1; NM_053665.1. [O88884-1]
DR AlphaFoldDB; O88884; -.
DR SMR; O88884; -.
DR BioGRID; 250302; 2.
DR IntAct; O88884; 2.
DR MINT; O88884; -.
DR STRING; 10116.ENSRNOP00000052543; -.
DR iPTMnet; O88884; -.
DR PhosphoSitePlus; O88884; -.
DR PaxDb; O88884; -.
DR PRIDE; O88884; -.
DR GeneID; 114124; -.
DR KEGG; rno:114124; -.
DR CTD; 8165; -.
DR RGD; 620826; Akap1.
DR eggNOG; KOG2279; Eukaryota.
DR InParanoid; O88884; -.
DR OrthoDB; 196526at2759; -.
DR PhylomeDB; O88884; -.
DR Reactome; R-RNO-983231; Factors involved in megakaryocyte development and platelet production.
DR PRO; PR:O88884; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005811; C:lipid droplet; IDA:RGD.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0030061; C:mitochondrial crista; IDA:RGD.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0031594; C:neuromuscular junction; IDA:RGD.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:RGD.
DR GO; GO:0048487; F:beta-tubulin binding; IDA:RGD.
DR GO; GO:0008017; F:microtubule binding; IDA:RGD.
DR GO; GO:0060090; F:molecular adaptor activity; IDA:RGD.
DR GO; GO:0034237; F:protein kinase A regulatory subunit binding; IDA:RGD.
DR GO; GO:0019901; F:protein kinase binding; IDA:RGD.
DR GO; GO:0030346; F:protein phosphatase 2B binding; IDA:RGD.
DR GO; GO:0019903; F:protein phosphatase binding; IDA:RGD.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0140374; P:antiviral innate immune response; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
DR GO; GO:0071320; P:cellular response to cAMP; IEP:RGD.
DR GO; GO:0071375; P:cellular response to peptide hormone stimulus; IEP:RGD.
DR GO; GO:0010614; P:negative regulation of cardiac muscle hypertrophy; IMP:RGD.
DR GO; GO:0035308; P:negative regulation of protein dephosphorylation; IMP:RGD.
DR GO; GO:0042308; P:negative regulation of protein import into nucleus; IMP:RGD.
DR GO; GO:0010738; P:regulation of protein kinase A signaling; IC:RGD.
DR CDD; cd04508; TUDOR; 1.
DR Gene3D; 2.40.50.90; -; 1.
DR Gene3D; 3.30.1370.10; -; 1.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR018459; RII-bd_1.
DR InterPro; IPR035437; SNase_OB-fold_sf.
DR InterPro; IPR002999; Tudor.
DR Pfam; PF00013; KH_1; 1.
DR Pfam; PF10522; RII_binding_1; 1.
DR Pfam; PF00567; TUDOR; 1.
DR SMART; SM00322; KH; 1.
DR SMART; SM00333; TUDOR; 1.
DR SUPFAM; SSF54791; SSF54791; 1.
DR PROSITE; PS50084; KH_TYPE_1; 1.
DR PROSITE; PS50304; TUDOR; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Phosphoprotein; Reference proteome;
KW RNA-binding; Transit peptide; Transmembrane.
FT TRANSIT 1..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 30..854
FT /note="A-kinase anchor protein 1, mitochondrial"
FT /id="PRO_0000016661"
FT DOMAIN 558..622
FT /note="KH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 709..768
FT /note="Tudor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT REGION 62..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..316
FT /note="PKA-RII subunit binding domain"
FT REGION 333..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..437
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92667"
FT MOD_RES 398
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q92667"
FT MOD_RES 484
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q92667"
FT MOD_RES 524
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92667"
FT MOD_RES 543
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92667"
FT VAR_SEQ 523..544
FT /note="GSDGNSMDSVDSCCGLTKPDSP -> VAAPPQERGHFGNGGCAGFFEC (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:9722570"
FT /id="VSP_002854"
FT VAR_SEQ 545..854
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9722570"
FT /id="VSP_002855"
FT CONFLICT 311
FT /note="I -> T (in Ref. 1; AAC61775)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="V -> A (in Ref. 1; AAC61775)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 854 AA; 91747 MW; 6EFBA30F8801A06E CRC64;
MAIQFRSLFP LALPGMLALL GWWWFFSRKK DRLSSNGKQV GTLKVGPAIE DRLPTEEACP
GVLSVTPSVT QPPGKEEQRS MDRPLSDPPA LPRTRQVRRR SESSGNLPSI VDTRLQAGQC
SDENSKVVLS LMGDEAKSIP LGRPLFPKDL SFPYEAVEGC KQESALGRTP GRGWLSQCAA
SGENARETGG AEGTGDAVLG ESVLEEGLLP QECVSEVEKS EFPILAPGGG GGEKVRSGPP
QVDELLKKEE YIVGKLPSSF VGPVHSELVK DEGALVPQVK GSQDRSLARE LDKDKTLPEK
DQIEQTAFQI ISQVILEATE EIRATTVGKT VAQVHPTPGT QPQGQEESCV PASQETSLGQ
EIPDPASTRT GATASPSAGA PPPKTYVSCL SSPLSGPTKD QKPKNSAHHI SLAPCPPPVT
PQRQSLDGAS NPRGDDTFVT CTSNNSQSVL SVTSLGLCSD PVSTSRLEDS CTETISSSGD
KAVTPPLPDS TEPFSNGVLK EELSDLGTED GWTMDTEADH SGGSDGNSMD SVDSCCGLTK
PDSPQTVQAG SNPKKVDLII WEIEVPKHLV GRLIGKQGRY VSFLKQTSGA KIYISTLPYT
QNIQICHIEG SQHHVDKALN LIGKKFKELN LTNIYAPPLP SLALPSLPMT SWLMLPDGIT
VEVIVVNQVN AGHLFVQQHT HPTFHALRSL DQQMYLCYSQ PGIPTLPTPV EITVICAAPG
ADGAWWRAQV VASYEETNEV EIRYVDYGGY KRVKVDVLRQ IRSDFVTLPF QGAEVLLDSV
VPLSDDDHFS PEADAAMSEM TGNTALLAQV TSYSATGLPL IQLWSVVGDE VVLINRSLVE
RGLAQWVDSC YASL
