AKAP9_RABIT
ID AKAP9_RABIT Reviewed; 1087 AA.
AC Q28628;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=A-kinase anchor protein 9;
DE Short=AKAP-9;
DE AltName: Full=A-kinase anchor protein 120 kDa;
DE Short=AKAP 120;
DE AltName: Full=Protein kinase A-anchoring protein 9;
DE Short=PRKA9;
DE Flags: Fragment;
GN Name=AKAP9; Synonyms=AKAP120;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=New Zealand white; TISSUE=Gastric parietal cell;
RX PubMed=9148752; DOI=10.1042/bj3220801;
RA Dransfield D.T., Yeh J.L., Bradford A.J., Goldenring J.R.;
RT "Identification and characterization of a novel A-kinase-anchoring protein
RT (AKAP120) from rabbit gastric parietal cells.";
RL Biochem. J. 322:801-808(1997).
CC -!- FUNCTION: Scaffolding protein that assembles several protein kinases
CC and phosphatases on the centrosome and Golgi apparatus. Required to
CC maintain the integrity of the Golgi apparatus. Required for microtubule
CC nucleation at the cis-side of the Golgi apparatus. Required for
CC association of the centrosomes with the poles of the bipolar mitotic
CC spindle during metaphase. In complex with PDE4DIP, recruits CAMSAP2 to
CC the Golgi apparatus and tethers non-centrosomal minus-end microtubules
CC to the Golgi, an important step for polarized cell movement. In complex
CC with PDE4DIP, EB1/MAPRE1 and CDK5RAP2, contributes to microtubules
CC nucleation and extension also from the centrosome to the cell
CC periphery. The interaction with PDE4DIP is isoform-specific.
CC {ECO:0000250|UniProtKB:Q99996}.
CC -!- SUBUNIT: Interacts with the regulatory region of protein kinase N
CC (PKN), protein phosphatase 2A (PP2A), protein phosphatase 1 (PP1) and
CC the immature non-phosphorylated form of PKC epsilon. Interacts with
CC CIP4 and FNBP1. Interacts with chloride intracellular channel proteins
CC CLIC1, CLIC4 and CLIC5. CSNK1D binding promotes its centrosomal
CC subcellular location. Interacts with GM130/GOLGA2; leading to
CC recruitment to the Golgi apparatus. Interacts with KCNQ1; targets
CC protein kinase A (PKA) catalytic and regulatory subunits and protein
CC phosphatase 1 (PP1), to the heterodimer KCNQ1-KCNE1. Interacts with
CC PDE4DIP; this interaction stabilizes both proteins. In complex with
CC PDE4DIP, recruits CAMSAP2 to the Golgi apparatus. Forms a
CC pericentrosomal complex with CDK5RAP2, EB1/MAPRE1 and PDE4DIP; within
CC this complex, MAPRE1 binding to CDK5RAP2 may be mediated by PDE4DIP.
CC The interaction with PDE4DIP is isoform-specific. Interacts with MAPRE1
CC and MAPRE3. Interacts (via C-terminus) with CAMSAP2; this interaction
CC is much stronger in the presence of PDE4DIP. Interacts with CAMSAP3.
CC Interacts (via C-terminus) with the gamma-tubulin ring complex (gamma-
CC TuRC), composed of gamma-tubulin, TUBGCP2, TUBGCP3, TUBGCP4, TUBGCP5
CC and TUBGCP6. {ECO:0000250|UniProtKB:Q99996}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:Q99996}.
CC Cytoplasm {ECO:0000250|UniProtKB:Q99996}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q99996}. Note=Cytoplasmic in parietal cells.
CC Recruited to the Golgi apparatus by GM130/GOLGA2. Localization at the
CC centrosome versus Golgi apparatus may be cell type-dependent. Recruited
CC to the centrosome in the presence of CDK5RAP2.
CC {ECO:0000250|UniProtKB:Q99996}.
CC -!- TISSUE SPECIFICITY: Highly expressed in gastric parietal cells.
CC {ECO:0000269|PubMed:9148752}.
CC -!- DOMAIN: RII-binding site, predicted to form an amphipathic helix, could
CC participate in protein-protein interactions with a complementary
CC surface on the R-subunit dimer. {ECO:0000305|PubMed:9148752}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC35413.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U26360; AAC35413.1; ALT_INIT; mRNA.
DR RefSeq; NP_001075820.1; NM_001082351.1.
DR AlphaFoldDB; Q28628; -.
DR SMR; Q28628; -.
DR STRING; 9986.ENSOCUP00000003916; -.
DR PRIDE; Q28628; -.
DR GeneID; 100009203; -.
DR KEGG; ocu:100009203; -.
DR CTD; 10142; -.
DR eggNOG; ENOG502QV16; Eukaryota.
DR InParanoid; Q28628; -.
DR OrthoDB; 8180at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0005795; C:Golgi stack; ISS:UniProtKB.
DR GO; GO:0060090; F:molecular adaptor activity; ISS:UniProtKB.
DR GO; GO:0051661; P:maintenance of centrosome location; ISS:UniProtKB.
DR GO; GO:0007020; P:microtubule nucleation; ISS:UniProtKB.
DR GO; GO:1903358; P:regulation of Golgi organization; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR InterPro; IPR028745; AKAP9/Pericentrin.
DR PANTHER; PTHR44981; PTHR44981; 2.
PE 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; Cytoskeleton; Golgi apparatus; Reference proteome.
FT CHAIN <1..>1087
FT /note="A-kinase anchor protein 9"
FT /id="PRO_0000064535"
FT REGION 559..572
FT /note="PKA-RII subunit binding domain"
FT REGION 667..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 5..461
FT /evidence="ECO:0000255"
FT COILED 614..773
FT /evidence="ECO:0000255"
FT COMPBIAS 667..685
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT NON_TER 1087
SQ SEQUENCE 1087 AA; 124756 MW; 9D916BE0CA89FF02 CRC64;
REKLEVQCQA EKVRDDLQKQ VKALEIDVEE QVCRFIELEQ EKNAELMDLR QQNQALEKQL
EKMRKMDLRQ QNQALEKQLE KMRKFLDEQA IDREHERDVF QQEIQKLEQQ LKLVPRFQPI
SEHQTREVEQ LTNHLKEKTD KCSELLLSKE QLQRDVQERN EEIEKLECRV RELEQALLSV
QTLSKRWRTR NSFGAVEPKA ELCLEVQLQA ERDAIDRKEK EITNLEEQLE QFREELENKN
EEVQQLHMQL EIQKKESTTR LQELEQENKL FKDEMEKLGF AIKESDAVSP QDQQVLFGKF
AQIIHEKEVE IDRLNEQIIK LQQQLKITTD NKVIEEKNEL IRDLEAQIEC LMSDQERVRK
NREEEIEQLN EVIEKLQQEL ANIDQKTSVD PSSLSEEADS LKHQLDKVIA EKLALEHQVE
TTNEEMAVTK NVLKETNFKM NQLTQELCSL KREREKMERI QSVPEKSVNM SVGDLSKDKP
EMDLIPTEDA LAQLETQTQL RSSEESSKVS LSSLETKLLQ LESTVSTKDL ELTQCYKQIQ
DMREQGRSET EMLQTKIVSL QKVLEEKVAA ALVSQVQLEA VQEYVKLCAD KPAVSSDPAR
TEVPGLSQLA GNTMESDVSA LTWRISELES QLVEMHSSLI SEKEQVEIAE KNALEKEKKL
QELQKLVQDS ETKQRERERQ SRLHGDLGVL ESTTSEESGV FGELEALRAE SAAPKGELAN
YKELAEKLQE ELLVKETNMA SLPKELSHVR DQLTEAEDKL SHFSEKEDKT EVQEHGTICI
LEPCPGQIGE SFASQTEGAV QVNSHTQTPQ IPVRSVGIQT HSQSDSSPEE VAEIISRFTE
KIEQMRELHA AEILDMESRH ISETETLKRE HCIAVQLLTE ECASLKSLIQ GLRMPEGSSV
PELTHSNAYQ TREVGSSDSG SDWGQGIYLT QSQGFDTASE ARGEEGETST DSFPKKIKGL
LRAVHNEGMQ VLSLTEGPCG DGEDYPGHQL SESWLEERRA YLSTISSLKD FITKMQVQRE
VEVYDSSQSH ENISDWRGEL LLALQQVFLR ERSVLLAAFK TELTALGTRD AAGLLNCLEQ
RIPRTEY
