AKA10_PIG
ID AKA10_PIG Reviewed; 650 AA.
AC P57770;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=A-kinase anchor protein 10, mitochondrial;
DE Short=AKAP-10;
DE AltName: Full=Dual specificity A kinase-anchoring protein 2;
DE Short=D-AKAP-2;
DE AltName: Full=Protein kinase A-anchoring protein 10;
DE Short=PRKA10;
DE Flags: Precursor; Fragment;
GN Name=AKAP10;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RA Rao T.V.S., Knox C., Wileman T., Miskin J., Ryan M.;
RT "Sus scrofa protein kinase A anchoring protein with an RGS domain.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Differentially targeted protein that binds to type I and II
CC regulatory subunits of protein kinase A and anchors them to the
CC mitochondria or the plasma membrane. Although the physiological
CC relevance between PKA and AKAPS with mitochondria is not fully
CC understood, one idea is that BAD, a proapoptotic member, is
CC phosphorylated and inactivated by mitochondria-anchored PKA. It cannot
CC be excluded too that it may facilitate PKA as well as G protein signal
CC transduction, by acting as an adapter for assembling multiprotein
CC complexes. With its RGS domain, it could lead to the interaction to G-
CC alpha proteins, providing a link between the signaling machinery and
CC the downstream kinase (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Membrane
CC {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Predominantly
CC mitochondrial but also membrane associated and cytoplasmic.
CC {ECO:0000250}.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAG35731.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF208387; AAG35731.1; ALT_INIT; mRNA.
DR RefSeq; NP_999303.1; NM_214138.1.
DR AlphaFoldDB; P57770; -.
DR SMR; P57770; -.
DR STRING; 9823.ENSSSCP00000020144; -.
DR PaxDb; P57770; -.
DR PeptideAtlas; P57770; -.
DR PRIDE; P57770; -.
DR GeneID; 397262; -.
DR KEGG; ssc:397262; -.
DR CTD; 11216; -.
DR eggNOG; KOG3590; Eukaryota.
DR HOGENOM; CLU_992263_0_0_1; -.
DR InParanoid; P57770; -.
DR OrthoDB; 644347at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0051018; F:protein kinase A binding; IEA:InterPro.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR CDD; cd12804; AKAP10_AKB; 1.
DR Gene3D; 1.10.167.10; -; 3.
DR InterPro; IPR037719; AKAP10_AKB_dom.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR044926; RGS_subdomain_2.
DR Pfam; PF00615; RGS; 2.
DR SMART; SM00315; RGS; 2.
DR SUPFAM; SSF48097; SSF48097; 2.
DR PROSITE; PS50132; RGS; 2.
PE 2: Evidence at transcript level;
KW Cytoplasm; Membrane; Mitochondrion; Phosphoprotein; Reference proteome;
KW Repeat; Transit peptide.
FT TRANSIT <1..16
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 17..650
FT /note="A-kinase anchor protein 10, mitochondrial"
FT /id="PRO_0000030406"
FT DOMAIN 113..356
FT /note="RGS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT DOMAIN 366..493
FT /note="RGS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 622..635
FT /note="PKA-RII subunit binding"
FT COMPBIAS 29..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43572"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43572"
FT NON_TER 1
SQ SEQUENCE 650 AA; 71704 MW; 323F802E71E35149 CRC64;
RALRPDPGPA MSFFRRKARG REQEKTSDVP SGKASISVHS PQKSTKNHAL LEAAGPSPVA
ISAISANMDS FSRSRTATLK KQPSHMEAAH FGDLGRSCLD YQAQETKSSL SKTLEQVLRD
AVVLPYFIQF MELRRMEHLV KFWLEAESFH STTWSRIRAH SLNTVKQSSL AEPVSPTQKH
ETAAAPVTES LDQRLEEPSS AQLLLTQSEG IDLTDRTSNT QNHLLLSPEC DGARALHPAA
ARTGARRASL EPQESCRLTV ASRNSPSSPL KEVSGKLMKS IEQDAVNTFT KYISPDAAKP
IPITEAMRND IIAKICGEDG QVDPNCFVLA QSIVFSAMEQ EHFSEFLRSH HFCKYQIEVL
TSGTVYLADI LFCESALFYS SEYMEKEDAV NILQFWLAAD NFQSQPAAKK GQYDGQEAQN
DAMILYDKYF SLQATHPLGF DDVVRLEIES NNICREGGPL PNCFTTPLRQ AWTTMEKVFL
PGFLSSSLYY KYLNDLIHSV RGDEFLGASA SLAAQGSGGP PDDPLPGASD PSASQSSVKK
ASVKILKNFD EAIIVDAASL DPESLYQRTY AGKMTFGRVS DLGQFIRESE PEPDVKKSKG
SMFSQAMKKW VQGNSDEAQE ELAWKIAKMI VSDVMQQAQC AQPGETSAKL
