ID   AKAP9_HUMAN             Reviewed;        3907 AA.
AC   Q99996; A4D1F0; A4D1F2; A4D1F4; O14869; O43355; O94895; Q75N20; Q9UQH3;
AC   Q9UQQ4; Q9Y6B8; Q9Y6Y2;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   25-APR-2018, sequence version 4.
DT   27-MAR-2024, entry version 217.
DE   RecName: Full=A-kinase anchor protein 9;
DE            Short=AKAP-9;
DE   AltName: Full=A-kinase anchor protein 350 kDa;
DE            Short=AKAP 350;
DE            Short=hgAKAP 350;
DE   AltName: Full=A-kinase anchor protein 450 kDa;
DE            Short=AKAP 450;
DE   AltName: Full=AKAP 120-like protein;
DE   AltName: Full=Centrosome- and Golgi-localized PKN-associated protein {ECO:0000303|PubMed:10358086};
DE            Short=CG-NAP {ECO:0000303|PubMed:10358086};
DE   AltName: Full=Protein hyperion {ECO:0000303|Ref.4};
DE   AltName: Full=Protein kinase A-anchoring protein 9;
DE            Short=PRKA9;
DE   AltName: Full=Protein yotiao {ECO:0000303|PubMed:9482789};
GN   Name=AKAP9; Synonyms=AKAP350, AKAP450, KIAA0803;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION (ISOFORM 4), AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=9482789; DOI=10.1523/jneurosci.18-06-02017.1998;
RA   Lin J.W., Wyszynski M., Madhavan R., Sealock R., Kim J.U., Sheng M.;
RT   "Yotiao, a novel protein of neuromuscular junction and brain that interacts
RT   with specific splice variants of NMDA receptor subunit NR1.";
RL   J. Neurosci. 18:2017-2027(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY, AND
RP   VARIANT GLN-1335 INS.
RX   PubMed=10202149; DOI=10.1093/emboj/18.7.1858;
RA   Witczak O., Skaalhegg B.S., Keryer G., Bornens M., Tasken K., Jahnsen T.,
RA   Oerstavik S.;
RT   "Cloning and characterization of a cDNA encoding an A-kinase anchoring
RT   protein located in the centrosome, AKAP450.";
RL   EMBO J. 18:1858-1868(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND VARIANTS ILE-463 AND SER-2979.
RC   TISSUE=Brain;
RX   PubMed=10358086; DOI=10.1074/jbc.274.24.17267;
RA   Takahashi M., Shibata H., Shimakawa M., Miyamoto M., Mukai H., Ono Y.;
RT   "Characterization of a novel giant scaffolding protein, CG-NAP, that
RT   anchors multiple signaling enzymes to centrosome and the Golgi apparatus.";
RL   J. Biol. Chem. 274:17267-17274(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Kemmner W.A., Deiss S., Schwarz U.;
RT   "Cloning of Hyperion.";
RL   Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA   Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA   Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA   Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA   Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA   Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA   Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA   Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA   Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA   Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA   Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA   Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA   Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA   Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA   Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA   McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA   Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12690205; DOI=10.1126/science.1083423;
RA   Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA   Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA   Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA   Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA   Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA   Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA   Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA   Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA   Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA   Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA   Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA   Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA   Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA   Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA   Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA   Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA   Adams M.D., Tsui L.-C.;
RT   "Human chromosome 7: DNA sequence and biology.";
RL   Science 300:767-772(2003).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 311-3907 (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP   [MRNA] OF 2145-3907 (ISOFORM 6), SUBCELLULAR LOCATION, AND VARIANT
RP   SER-2979.
RC   TISSUE=Gastric parietal cell, and Lung;
RX   PubMed=9915845; DOI=10.1074/jbc.274.5.3055;
RA   Schmidt P.H., Dransfield D.T., Claudio J.O., Hawley R.G., Trotter K.W.,
RA   Milgram S.L., Goldenring J.R.;
RT   "AKAP350, a multiply spliced protein kinase A-anchoring protein associated
RT   with centrosomes.";
RL   J. Biol. Chem. 274:3055-3066(1999).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2200-3907 (ISOFORMS 2/3), AND
RP   VARIANT SER-2979.
RC   TISSUE=Brain;
RX   PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA   Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA   Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XI. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 5:277-286(1998).
RN   [9]
RP   INTERACTION WITH CLIC1; CLIC4 AND CLIC5.
RX   PubMed=12163479; DOI=10.1074/jbc.m112277200;
RA   Shanks R.A., Larocca M.C., Berryman M., Edwards J.C., Urushidani T.,
RA   Navarre J., Goldenring J.R.;
RT   "AKAP350 at the Golgi apparatus. II. Association of AKAP350 with a novel
RT   chloride intracellular channel (CLIC) family member.";
RL   J. Biol. Chem. 277:40973-40980(2002).
RN   [10]
RP   INTERACTION WITH CSNK1D, AND SUBCELLULAR LOCATION.
RX   PubMed=12270714; DOI=10.1016/s0022-2836(02)00857-4;
RA   Sillibourne J.E., Milne D.M., Takahashi M., Ono Y., Meek D.W.;
RT   "Centrosomal anchoring of the protein kinase CK1delta mediated by
RT   attachment to the large, coiled-coil scaffolding protein CG-NAP/AKAP450.";
RL   J. Mol. Biol. 322:785-797(2002).
RN   [11]
RP   INTERACTION WITH KCNQ1.
RX   PubMed=11799244; DOI=10.1126/science.1066843;
RA   Marx S.O., Kurokawa J., Reiken S., Motoike H., D'Armiento J., Marks A.R.,
RA   Kass R.S.;
RT   "Requirement of a macromolecular signaling complex for beta adrenergic
RT   receptor modulation of the KCNQ1-KCNE1 potassium channel.";
RL   Science 295:496-499(2002).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Lymphoblast;
RX   PubMed=14654843; DOI=10.1038/nature02166;
RA   Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT   "Proteomic characterization of the human centrosome by protein correlation
RT   profiling.";
RL   Nature 426:570-574(2003).
RN   [13]
RP   FUNCTION, INTERACTION WITH CIP4 AND FNBP1, AND SUBCELLULAR LOCATION.
RX   PubMed=15047863; DOI=10.1091/mbc.e03-10-0757;
RA   Larocca M.C., Shanks R.A., Tian L., Nelson D.L., Stewart D.M.,
RA   Goldenring J.R.;
RT   "AKAP350 interaction with cdc42 interacting protein 4 at the Golgi
RT   apparatus.";
RL   Mol. Biol. Cell 15:2771-2781(2004).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3865, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA   Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA   Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [15]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH GOLGA2.
RX   PubMed=19242490; DOI=10.1038/emboj.2009.47;
RA   Rivero S., Cardenas J., Bornens M., Rios R.M.;
RT   "Microtubule nucleation at the cis-side of the Golgi apparatus requires
RT   AKAP450 and GM130.";
RL   EMBO J. 28:1016-1028(2009).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153 AND SER-3842, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [17]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1327; SER-1765; SER-3690;
RP   SER-3842 AND SER-3897, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [19]
RP   INTERACTION WITH PDE4DIP, AND SUBCELLULAR LOCATION.
RX   PubMed=25217626; DOI=10.1242/jcs.155408;
RA   Wang Z., Zhang C., Qi R.Z.;
RT   "A newly identified myomegalin isoform functions in Golgi microtubule
RT   organization and ER-Golgi transport.";
RL   J. Cell Sci. 127:4904-4917(2014).
RN   [20]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [21]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=25657325; DOI=10.1091/mbc.e14-09-1366;
RA   Ohta S., Wood L., Toramoto I., Yagyu K., Fukagawa T., Earnshaw W.C.;
RT   "CENP-32 is required to maintain centrosomal dominance in bipolar spindle
RT   assembly.";
RL   Mol. Biol. Cell 26:1225-1237(2015).
RN   [22]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PDE4DIP; GAMMA-TUBULIN
RP   RING COMPLEX AND CAMSAP2.
RX   PubMed=27666745; DOI=10.1016/j.devcel.2016.08.009;
RA   Wu J., de Heus C., Liu Q., Bouchet B.P., Noordstra I., Jiang K., Hua S.,
RA   Martin M., Yang C., Grigoriev I., Katrukha E.A., Altelaar A.F.,
RA   Hoogenraad C.C., Qi R.Z., Klumperman J., Akhmanova A.;
RT   "Molecular pathway of microtubule organization at the Golgi apparatus.";
RL   Dev. Cell 39:44-60(2016).
RN   [23]
RP   FUNCTION, AND INTERACTION WITH PDE4DIP; MAPRE1 AND MAPRE3.
RX   PubMed=28814570; DOI=10.1083/jcb.201701024;
RA   Yang C., Wu J., de Heus C., Grigoriev I., Liv N., Yao Y., Smal I.,
RA   Meijering E., Klumperman J., Qi R.Z., Akhmanova A.;
RT   "EB1 and EB3 regulate microtubule minus end organization and Golgi
RT   morphology.";
RL   J. Cell Biol. 216:3179-3198(2017).
RN   [24]
RP   INTERACTION WITH CAMSAP3.
RX   PubMed=28089391; DOI=10.1016/j.jgg.2016.11.005;
RA   Wang J., Xu H., Jiang Y., Takahashi M., Takeichi M., Meng W.;
RT   "CAMSAP3-dependent microtubule dynamics regulates Golgi assembly in
RT   epithelial cells.";
RL   J. Genet. Genomics 44:39-49(2017).
RN   [25]
RP   FUNCTION, INTERACTION WITH CDK5RAP2; MAPRE1 AND PDE4DIP, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=29162697; DOI=10.1073/pnas.1705682114;
RA   Bouguenina H., Salaun D., Mangon A., Muller L., Baudelet E., Camoin L.,
RA   Tachibana T., Cianferani S., Audebert S., Verdier-Pinard P., Badache A.;
RT   "EB1-binding-myomegalin protein complex promotes centrosomal microtubules
RT   functions.";
RL   Proc. Natl. Acad. Sci. U.S.A. 114:E10687-E10696(2017).
RN   [26]
RP   VARIANTS [LARGE SCALE ANALYSIS] ILE-2409 AND GLN-3297.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
RN   [27]
RP   VARIANT LQT11 LEU-1570.
RX   PubMed=18093912; DOI=10.1073/pnas.0710527105;
RA   Chen L., Marquardt M.L., Tester D.J., Sampson K.J., Ackerman M.J.,
RA   Kass R.S.;
RT   "Mutation of an A-kinase-anchoring protein causes long-QT syndrome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:20990-20995(2007).
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 (PubMed:10202149,
CC       PubMed:15047863). Required for microtubule nucleation at the cis-side
CC       of the Golgi apparatus (PubMed:15047863, PubMed:19242490). Required for
CC       association of the centrosomes with the poles of the bipolar mitotic
CC       spindle during metaphase (PubMed:25657325). In complex with PDE4DIP
CC       isoform 13/MMG8/SMYLE, recruits CAMSAP2 to the Golgi apparatus and
CC       tethers non-centrosomal minus-end microtubules to the Golgi, an
CC       important step for polarized cell movement (PubMed:27666745,
CC       PubMed:28814570). In complex with PDE4DIP isoform 13/MMG8/SMYLE,
CC       EB1/MAPRE1 and CDK5RAP2, contributes to microtubules nucleation and
CC       extension also from the centrosome to the cell periphery
CC       (PubMed:29162697). {ECO:0000269|PubMed:10202149,
CC       ECO:0000269|PubMed:15047863, ECO:0000269|PubMed:19242490,
CC       ECO:0000269|PubMed:25657325, ECO:0000269|PubMed:27666745,
CC       ECO:0000269|PubMed:28814570, ECO:0000269|PubMed:29162697}.
CC   -!- FUNCTION: [Isoform 4]: Associated with the N-methyl-D-aspartate
CC       receptor and is specifically found in the neuromuscular junction (NMJ)
CC       as well as in neuronal synapses, suggesting a role in the organization
CC       of postsynaptic specializations. {ECO:0000269|PubMed:9482789}.
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 (PubMed:15047863). Interacts with chloride intracellular
CC       channel proteins CLIC1, CLIC4 and CLIC5 (PubMed:12163479). CSNK1D
CC       binding promotes its centrosomal subcellular location
CC       (PubMed:12270714). Interacts with GM130/GOLGA2; leading to recruitment
CC       to the Golgi apparatus (PubMed:19242490). Interacts with KCNQ1; targets
CC       protein kinase A (PKA) catalytic and regulatory subunits and protein
CC       phosphatase 1 (PP1), to the heterodimer KCNQ1-KCNE1 (PubMed:11799244).
CC       Interacts with PDE4DIP isoform 13/MMG8/SMYLE; this interaction
CC       stabilizes both proteins (PubMed:25217626, PubMed:27666745,
CC       PubMed:28814570). In complex with PDE4DIP isoform 13, recruits CAMSAP2
CC       to the Golgi apparatus (PubMed:27666745, PubMed:28814570). Forms a
CC       pericentrosomal complex with CDK5RAP2, EB1/MAPRE1 and PDE4DIP isoform
CC       13; within this complex, MAPRE1 binding to CDK5RAP2 may be mediated by
CC       PDE4DIP (PubMed:29162697). Interacts with MAPRE1 and MAPRE3
CC       (PubMed:28814570). Interacts (via C-terminus) with CAMSAP2; this
CC       interaction is much stronger in the presence of PDE4DIP isoform
CC       13/MMG8/SMYLE (PubMed:27666745). Interacts with CAMSAP3
CC       (PubMed:28089391). Interacts (via C-terminus) with the gamma-tubulin
CC       ring complex (gamma-TuRC), composed of gamma-tubulin, TUBGCP2, TUBGCP3,
CC       TUBGCP4, TUBGCP5 and TUBGCP6 (PubMed:27666745).
CC       {ECO:0000269|PubMed:11799244, ECO:0000269|PubMed:12163479,
CC       ECO:0000269|PubMed:12270714, ECO:0000269|PubMed:15047863,
CC       ECO:0000269|PubMed:19242490, ECO:0000269|PubMed:25217626,
CC       ECO:0000269|PubMed:27666745, ECO:0000269|PubMed:28089391,
CC       ECO:0000269|PubMed:28814570, ECO:0000269|PubMed:29162697}.
CC   -!- INTERACTION:
CC       Q99996; Q9NRI5: DISC1; NbExp=2; IntAct=EBI-1048311, EBI-529989;
CC       Q99996; Q08379: GOLGA2; NbExp=3; IntAct=EBI-1048311, EBI-618309;
CC       Q99996; O60341: KDM1A; NbExp=2; IntAct=EBI-1048311, EBI-710124;
CC       Q99996; PRO_0000449630 [P0DTD1]: rep; Xeno; NbExp=3; IntAct=EBI-1048311, EBI-25475888;
CC       Q99996-2; Q9H2G9: BLZF1; NbExp=3; IntAct=EBI-9641546, EBI-2548012;
CC       Q99996-2; Q6P1W5: C1orf94; NbExp=3; IntAct=EBI-9641546, EBI-946029;
CC       Q99996-2; P52272: HNRNPM; NbExp=3; IntAct=EBI-9641546, EBI-486809;
CC       Q99996-2; Q9UKT9: IKZF3; NbExp=3; IntAct=EBI-9641546, EBI-747204;
CC       Q99996-2; P43360: MAGEA6; NbExp=3; IntAct=EBI-9641546, EBI-1045155;
CC       Q99996-2; Q9Y5V3: MAGED1; NbExp=3; IntAct=EBI-9641546, EBI-716006;
CC       Q99996-2; Q9GZV8: PRDM14; NbExp=3; IntAct=EBI-9641546, EBI-3957793;
CC       Q99996-2; Q8N6K7: SAMD3; NbExp=3; IntAct=EBI-9641546, EBI-748741;
CC       Q99996-2; Q16385: SSX2B; NbExp=4; IntAct=EBI-9641546, EBI-2210673;
CC       Q99996-2; Q9NVV9: THAP1; NbExp=3; IntAct=EBI-9641546, EBI-741515;
CC       Q99996-2; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-9641546, EBI-739895;
CC       Q99996-2; O60763: USO1; NbExp=3; IntAct=EBI-9641546, EBI-356164;
CC       Q99996-2; Q9BTA9: WAC; NbExp=3; IntAct=EBI-9641546, EBI-749118;
CC       Q99996-3; P46379-2: BAG6; NbExp=3; IntAct=EBI-11022349, EBI-10988864;
CC       Q99996-3; Q8WUW1: BRK1; NbExp=3; IntAct=EBI-11022349, EBI-2837444;
CC       Q99996-3; O14645: DNALI1; NbExp=3; IntAct=EBI-11022349, EBI-395638;
CC       Q99996-3; P29692-2: EEF1D; NbExp=3; IntAct=EBI-11022349, EBI-5280572;
CC       Q99996-3; P22607: FGFR3; NbExp=3; IntAct=EBI-11022349, EBI-348399;
CC       Q99996-3; P06396: GSN; NbExp=3; IntAct=EBI-11022349, EBI-351506;
CC       Q99996-3; P01112: HRAS; NbExp=3; IntAct=EBI-11022349, EBI-350145;
CC       Q99996-3; Q9UMF0: ICAM5; NbExp=3; IntAct=EBI-11022349, EBI-6398041;
CC       Q99996-3; O14901: KLF11; NbExp=3; IntAct=EBI-11022349, EBI-948266;
CC       Q99996-3; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-11022349, EBI-2811583;
CC       Q99996-4; P26769: Adcy2; Xeno; NbExp=3; IntAct=EBI-15676518, EBI-1027877;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:15047863,
CC       ECO:0000269|PubMed:19242490, ECO:0000269|PubMed:25217626,
CC       ECO:0000269|PubMed:27666745}. Cytoplasm {ECO:0000269|PubMed:9915845}.
CC       Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC       {ECO:0000269|PubMed:12270714, ECO:0000269|PubMed:14654843,
CC       ECO:0000269|PubMed:25657325, ECO:0000269|PubMed:29162697,
CC       ECO:0000269|PubMed:9915845}. Note=Cytoplasmic in parietal cells
CC       (PubMed:9915845). Recruited to the Golgi apparatus by GM130/GOLGA2
CC       (PubMed:25657325). Localization at the centrosome versus Golgi
CC       apparatus may be cell line-dependent. In SKBr3 and HEK293F cells,
CC       exclusively located at the centrosome (PubMed:29162697). In HeLa, MDA-
CC       MB231 and RPE-1 cells, detected at the Golgi apparatus
CC       (PubMed:25217626, PubMed:29162697). In SK-BR-3 cells, recruited to the
CC       centrosome in the presence of CDK5RAP2 (PubMed:29162697).
CC       {ECO:0000269|PubMed:25217626, ECO:0000269|PubMed:25657325,
CC       ECO:0000269|PubMed:29162697, ECO:0000269|PubMed:9915845}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=2;
CC         IsoId=Q99996-2; Sequence=Displayed;
CC       Name=1;
CC         IsoId=Q99996-1; Sequence=VSP_059522, VSP_059526;
CC       Name=3; Synonyms=CG-NAP;
CC         IsoId=Q99996-3; Sequence=VSP_059525;
CC       Name=4; Synonyms=Yotiao;
CC         IsoId=Q99996-4; Sequence=VSP_059522, VSP_059523, VSP_059524;
CC       Name=5;
CC         IsoId=Q99996-5; Sequence=VSP_059522, VSP_059527;
CC       Name=6; Synonyms=AKAP350;
CC         IsoId=Q99996-6; Sequence=VSP_059522, VSP_059525, VSP_059528;
CC   -!- TISSUE SPECIFICITY: Widely expressed (PubMed:10202149). Isoform 4:
CC       Highly expressed in skeletal muscle and in pancreas (PubMed:9482789).
CC       {ECO:0000269|PubMed:10202149, ECO:0000269|PubMed:9482789}.
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:0000250|UniProtKB:Q28628}.
CC   -!- DISEASE: Long QT syndrome 11 (LQT11) [MIM:611820]: A heart disorder
CC       characterized by a prolonged QT interval on the ECG and polymorphic
CC       ventricular arrhythmias. They cause syncope and sudden death in
CC       response to exercise or emotional stress, and can present with a
CC       sentinel event of sudden cardiac death in infancy.
CC       {ECO:0000269|PubMed:18093912}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB86384.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAC60380.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="https://atlasgeneticsoncology.org/gene/42999/AKAP9";
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DR   EMBL; AJ131693; CAB40713.1; -; mRNA.
DR   EMBL; AB019691; BAA78718.1; -; mRNA.
DR   EMBL; AJ010770; CAA09361.1; -; Genomic_DNA.
DR   EMBL; AF026245; AAB86384.1; ALT_FRAME; mRNA.
DR   EMBL; AC004013; AAB96867.2; -; Genomic_DNA.
DR   EMBL; AC000066; AAC60380.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC000120; AAS07419.1; -; Genomic_DNA.
DR   EMBL; CH236949; EAL24155.1; -; Genomic_DNA.
DR   EMBL; CH236949; EAL24156.1; -; Genomic_DNA.
DR   EMBL; CH236949; EAL24157.1; -; Genomic_DNA.
DR   EMBL; AF083037; AAD22767.1; -; mRNA.
DR   EMBL; AF091711; AAD39719.1; -; mRNA.
DR   EMBL; AB018346; BAA34523.1; -; mRNA.
DR   CCDS; CCDS5622.1; -. [Q99996-2]
DR   CCDS; CCDS94141.1; -. [Q99996-3]
DR   PIR; T08880; T08880.
DR   RefSeq; NP_005742.4; NM_005751.4. [Q99996-2]
DR   RefSeq; NP_671714.1; NM_147185.2. [Q99996-3]
DR   SMR; Q99996; -.
DR   BioGRID; 115445; 214.
DR   CORUM; Q99996; -.
DR   DIP; DIP-29942N; -.
DR   IntAct; Q99996; 98.
DR   MINT; Q99996; -.
DR   STRING; 9606.ENSP00000348573; -.
DR   CarbonylDB; Q99996; -.
DR   GlyCosmos; Q99996; 2 sites, 1 glycan.
DR   GlyGen; Q99996; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q99996; -.
DR   MetOSite; Q99996; -.
DR   PhosphoSitePlus; Q99996; -.
DR   SwissPalm; Q99996; -.
DR   BioMuta; AKAP9; -.
DR   DMDM; 14194461; -.
DR   EPD; Q99996; -.
DR   jPOST; Q99996; -.
DR   MassIVE; Q99996; -.
DR   MaxQB; Q99996; -.
DR   PaxDb; 9606-ENSP00000348573; -.
DR   PeptideAtlas; Q99996; -.
DR   ProteomicsDB; 78566; -. [Q99996-1]
DR   ProteomicsDB; 78567; -. [Q99996-2]
DR   ProteomicsDB; 78568; -. [Q99996-3]
DR   ProteomicsDB; 78569; -. [Q99996-4]
DR   ProteomicsDB; 78570; -. [Q99996-5]
DR   ProteomicsDB; 78571; -. [Q99996-6]
DR   Pumba; Q99996; -.
DR   Antibodypedia; 1376; 199 antibodies from 30 providers.
DR   DNASU; 10142; -.
DR   Ensembl; ENST00000356239.8; ENSP00000348573.3; ENSG00000127914.19. [Q99996-2]
DR   Ensembl; ENST00000680766.1; ENSP00000505204.1; ENSG00000127914.19. [Q99996-3]
DR   GeneID; 10142; -.
DR   KEGG; hsa:10142; -.
DR   MANE-Select; ENST00000356239.8; ENSP00000348573.3; NM_005751.5; NP_005742.4.
DR   UCSC; uc003ulg.4; human. [Q99996-2]
DR   AGR; HGNC:379; -.
DR   CTD; 10142; -.
DR   DisGeNET; 10142; -.
DR   GeneCards; AKAP9; -.
DR   GeneReviews; AKAP9; -.
DR   HGNC; HGNC:379; AKAP9.
DR   HPA; ENSG00000127914; Low tissue specificity.
DR   MalaCards; AKAP9; -.
DR   MIM; 604001; gene.
DR   MIM; 611820; phenotype.
DR   neXtProt; NX_Q99996; -.
DR   OpenTargets; ENSG00000127914; -.
DR   Orphanet; 130; Brugada syndrome.
DR   Orphanet; 101016; Romano-Ward syndrome.
DR   PharmGKB; PA24673; -.
DR   VEuPathDB; HostDB:ENSG00000127914; -.
DR   eggNOG; ENOG502QV16; Eukaryota.
DR   GeneTree; ENSGT00730000110871; -.
DR   HOGENOM; CLU_000187_0_0_1; -.
DR   InParanoid; Q99996; -.
DR   OMA; HYVAIQL; -.
DR   OrthoDB; 3030508at2759; -.
DR   PhylomeDB; Q99996; -.
DR   TreeFam; TF105408; -.
DR   PathwayCommons; Q99996; -.
DR   Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR   Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
DR   Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
DR   Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR   Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
DR   Reactome; R-HSA-5576890; Phase 3 - rapid repolarisation.
DR   Reactome; R-HSA-5576893; Phase 2 - plateau phase.
DR   Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
DR   Reactome; R-HSA-6802952; Signaling by BRAF and RAF1 fusions.
DR   Reactome; R-HSA-8854518; AURKA Activation by TPX2.
DR   SignaLink; Q99996; -.
DR   SIGNOR; Q99996; -.
DR   BioGRID-ORCS; 10142; 16 hits in 1174 CRISPR screens.
DR   ChiTaRS; AKAP9; human.
DR   GeneWiki; AKAP9; -.
DR   GenomeRNAi; 10142; -.
DR   Pharos; Q99996; Tbio.
DR   PRO; PR:Q99996; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; Q99996; Protein.
DR   Bgee; ENSG00000127914; Expressed in jejunal mucosa and 198 other cell types or tissues.
DR   ExpressionAtlas; Q99996; baseline and differential.
DR   GO; GO:0005813; C:centrosome; IDA:HPA.
DR   GO; GO:0005801; C:cis-Golgi network; IDA:SYSCILIA_CCNET.
DR   GO; GO:0005856; C:cytoskeleton; TAS:ProtInc.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0044307; C:dendritic branch; IEA:Ensembl.
DR   GO; GO:0099147; C:extrinsic component of postsynaptic density membrane; IEA:Ensembl.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR   GO; GO:0005795; C:Golgi stack; IDA:UniProtKB.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR   GO; GO:0034705; C:potassium channel complex; IDA:MGI.
DR   GO; GO:0097060; C:synaptic membrane; IBA:GO_Central.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:BHF-UCL.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0060090; F:molecular adaptor activity; IDA:UniProtKB.
DR   GO; GO:0015459; F:potassium channel regulator activity; IMP:BHF-UCL.
DR   GO; GO:0034237; F:protein kinase A regulatory subunit binding; IDA:MGI.
DR   GO; GO:0005102; F:signaling receptor binding; TAS:ProtInc.
DR   GO; GO:0044325; F:transmembrane transporter binding; IPI:BHF-UCL.
DR   GO; GO:0071320; P:cellular response to cAMP; IMP:BHF-UCL.
DR   GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
DR   GO; GO:0051661; P:maintenance of centrosome location; IMP:UniProtKB.
DR   GO; GO:0007020; P:microtubule nucleation; IMP:UniProtKB.
DR   GO; GO:0031116; P:positive regulation of microtubule polymerization; IMP:UniProtKB.
DR   GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IMP:BHF-UCL.
DR   GO; GO:1901018; P:positive regulation of potassium ion transmembrane transporter activity; IMP:BHF-UCL.
DR   GO; GO:0031503; P:protein-containing complex localization; IDA:MGI.
DR   GO; GO:0098909; P:regulation of cardiac muscle cell action potential involved in regulation of contraction; IMP:BHF-UCL.
DR   GO; GO:1903358; P:regulation of Golgi organization; IDA:UniProtKB.
DR   GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IMP:BHF-UCL.
DR   GO; GO:0060306; P:regulation of membrane repolarization; IMP:BHF-UCL.
DR   GO; GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; IMP:BHF-UCL.
DR   GO; GO:0051602; P:response to electrical stimulus; IEA:Ensembl.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR   InterPro; IPR028745; AKAP9/Pericentrin.
DR   InterPro; IPR005539; ELK_dom.
DR   InterPro; IPR019528; PACT_domain.
DR   PANTHER; PTHR44981:SF1; A-KINASE ANCHOR PROTEIN 9; 1.
DR   PANTHER; PTHR44981; PERICENTRIN-LIKE PROTEIN, ISOFORM F; 1.
DR   Pfam; PF10495; PACT_coil_coil; 1.
DR   SMART; SM01188; ELK; 4.
DR   Genevisible; Q99996; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Disease variant; Golgi apparatus; Long QT syndrome; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..3907
FT                   /note="A-kinase anchor protein 9"
FT                   /id="PRO_0000064534"
FT   REGION          1..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1682..1713
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2542..2555
FT                   /note="PKA-RII subunit binding domain"
FT   REGION          3377..3405
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          152..902
FT                   /evidence="ECO:0000255"
FT   COILED          932..1010
FT                   /evidence="ECO:0000255"
FT   COILED          1088..1173
FT                   /evidence="ECO:0000255"
FT   COILED          1241..1268
FT                   /evidence="ECO:0000255"
FT   COILED          1324..1380
FT                   /evidence="ECO:0000255"
FT   COILED          1422..1447
FT                   /evidence="ECO:0000255"
FT   COILED          1573..1647
FT                   /evidence="ECO:0000255"
FT   COILED          1845..2443
FT                   /evidence="ECO:0000255"
FT   COILED          2532..2549
FT                   /evidence="ECO:0000255"
FT   COILED          2591..2764
FT                   /evidence="ECO:0000255"
FT   COILED          3061..3088
FT                   /evidence="ECO:0000255"
FT   COILED          3120..3466
FT                   /evidence="ECO:0000255"
FT   COILED          3583..3685
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..18
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1695..1713
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         153
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         1327
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1765
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         3690
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         3842
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         3865
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17525332"
FT   MOD_RES         3897
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         16
FT                   /note="K -> KIEELSLAFLVRQ (in isoform 1, isoform 4, isoform
FT                   5 and isoform 6)"
FT                   /id="VSP_059522"
FT   VAR_SEQ         1625..3900
FT                   /note="Missing (in isoform 4)"
FT                   /id="VSP_059523"
FT   VAR_SEQ         2163..2171
FT                   /note="SADTFQKVE -> E (in isoform 3 and isoform 6)"
FT                   /id="VSP_059525"
FT   VAR_SEQ         2883..2903
FT                   /note="GSSIPELAHSDAYQTREICSS -> VFGFYNMCFSTLC (in isoform
FT                   1)"
FT                   /id="VSP_059526"
FT   VAR_SEQ         2884..2945
FT                   /note="Missing (in isoform 5)"
FT                   /id="VSP_059527"
FT   VAR_SEQ         3897..3907
FT                   /note="STTQFHAGMRR -> ALSLTTSWQHHSARPTAPLFFEILSHSLG (in
FT                   isoform 6)"
FT                   /id="VSP_059528"
FT   VAR_SEQ         3901..3907
FT                   /note="FHAGMRR -> LAQVRVL (in isoform 4)"
FT                   /id="VSP_059524"
FT   VARIANT         463
FT                   /note="M -> I (in dbSNP:rs6964587)"
FT                   /evidence="ECO:0000269|PubMed:10358086"
FT                   /id="VAR_024249"
FT   VARIANT         1335
FT                   /note="K -> KQ"
FT                   /evidence="ECO:0000269|PubMed:10202149"
FT                   /id="VAR_010926"
FT   VARIANT         1570
FT                   /note="S -> L (in LQT11; dbSNP:rs121908566)"
FT                   /evidence="ECO:0000269|PubMed:18093912"
FT                   /id="VAR_043489"
FT   VARIANT         2409
FT                   /note="M -> I (in a colorectal cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035785"
FT   VARIANT         2484
FT                   /note="K -> R (in dbSNP:rs35759833)"
FT                   /id="VAR_043490"
FT   VARIANT         2792
FT                   /note="N -> S (in dbSNP:rs6960867)"
FT                   /id="VAR_030162"
FT   VARIANT         2979
FT                   /note="P -> S (in dbSNP:rs1063242)"
FT                   /evidence="ECO:0000269|PubMed:10358086,
FT                   ECO:0000269|PubMed:9872452, ECO:0000269|PubMed:9915845"
FT                   /id="VAR_030163"
FT   VARIANT         3297
FT                   /note="E -> Q (in a breast cancer sample; somatic mutation;
FT                   dbSNP:rs756245027)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035786"
FT   VARIANT         3444
FT                   /note="Q -> R (in dbSNP:rs34956633)"
FT                   /id="VAR_043491"
FT   VARIANT         3614
FT                   /note="M -> V (in dbSNP:rs34327395)"
FT                   /id="VAR_043492"
FT   CONFLICT        64
FT                   /note="E -> Q (in Ref. 3; BAA78718)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        542
FT                   /note="E -> G (in Ref. 3; BAA78718)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        626
FT                   /note="R -> S (in Ref. 3; BAA78718)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        651
FT                   /note="N -> S (in Ref. 3; BAA78718)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        901
FT                   /note="H -> N (in Ref. 3; BAA78718)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        944
FT                   /note="K -> N (in Ref. 3; BAA78718)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        968..970
FT                   /note="QKH -> PKP (in Ref. 1; AAB86384 and 2; CAB40713)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        985
FT                   /note="Q -> P (in Ref. 1; AAB86384 and 2; CAB40713)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        989
FT                   /note="Q -> P (in Ref. 1; AAB86384 and 2; CAB40713)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1008
FT                   /note="N -> D (in Ref. 3; BAA78718)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1016
FT                   /note="V -> E (in Ref. 3; BAA78718)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1614
FT                   /note="R -> P (in Ref. 1; AAB86384 and 2; CAB40713)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1691
FT                   /note="N -> T (in Ref. 3; BAA78718)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1695
FT                   /note="V -> G (in Ref. 3; BAA78718)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1790..1791
FT                   /note="Missing (in Ref. 7; AAD22767)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1831
FT                   /note="A -> P (in Ref. 3; BAA78718)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1944
FT                   /note="I -> V (in Ref. 3; BAA78718)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2015
FT                   /note="V -> D (in Ref. 7; AAD22767)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2145..2146
FT                   /note="EI -> HE (in Ref. 7; AAD39719)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2157
FT                   /note="E -> V (in Ref. 3; BAA78718)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2171
FT                   /note="E -> Q (in Ref. 7; AAD39719)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2502
FT                   /note="L -> R (in Ref. 3; BAA78718)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2839
FT                   /note="I -> N (in Ref. 8; BAA34523)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2953
FT                   /note="E -> D (in Ref. 3; BAA78718)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3083
FT                   /note="Q -> H (in Ref. 3; BAA78718)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3214
FT                   /note="Q -> H (in Ref. 3; BAA78718)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3303..3305
FT                   /note="ESE -> QSQ (in Ref. 3; BAA78718)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3747
FT                   /note="P -> A (in Ref. 3; BAA78718)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3829
FT                   /note="T -> S (in Ref. 3; BAA78718)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        Q99996-6:2175
FT                   /note="E -> Q (in Ref. 7; AAD39719)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   3907 AA;  452987 MW;  81761B4341430CDF CRC64;
     MEDEERQKKL EAGKAKLAQF RQRKAQSDGQ SPSKKQKKKR KTSSSKHDVS AHHDLNIDQS
     QCNEMYINSS QRVESTVIPE STIMRTLHSG EITSHEQGFS VELESEISTT ADDCSSEVNG
     CSFVMRTGKP TNLLREEEFG VDDSYSEQGA QDSPTHLEMM ESELAGKQHE IEELNRELEE
     MRVTYGTEGL QQLQEFEAAI KQRDGIITQL TANLQQARRE KDETMREFLE LTEQSQKLQI
     QFQQLQASET LRNSTHSSTA ADLLQAKQQI LTHQQQLEEQ DHLLEDYQKK KEDFTMQISF
     LQEKIKVYEM EQDKKVENSN KEEIQEKETI IEELNTKIIE EEKKTLELKD KLTTADKLLG
     ELQEQIVQKN QEIKNMKLEL TNSKQKERQS SEEIKQLMGT VEELQKRNHK DSQFETDIVQ
     RMEQETQRKL EQLRAELDEM YGQQIVQMKQ ELIRQHMAQM EEMKTRHKGE MENALRSYSN
     ITVNEDQIKL MNVAINELNI KLQDTNSQKE KLKEELGLIL EEKCALQRQL EDLVEELSFS
     REQIQRARQT IAEQESKLNE AHKSLSTVED LKAEIVSASE SRKELELKHE AEVTNYKIKL
     EMLEKEKNAV LDRMAESQEA ELERLRTQLL FSHEEELSKL KEDLEIEHRI NIEKLKDNLG
     IHYKQQIDGL QNEMSQKIET MQFEKDNLIT KQNQLILEIS KLKDLQQSLV NSKSEEMTLQ
     INELQKEIEI LRQEEKEKGT LEQEVQELQL KTELLEKQMK EKENDLQEKF AQLEAENSIL
     KDEKKTLEDM LKIHTPVSQE ERLIFLDSIK SKSKDSVWEK EIEILIEENE DLKQQCIQLN
     EEIEKQRNTF SFAEKNFEVN YQELQEEYAC LLKVKDDLED SKNKQELEYK SKLKALNEEL
     HLQRINPTTV KMKSSVFDED KTFVAETLEM GEVVEKDTTE LMEKLEVTKR EKLELSQRLS
     DLSEQLKQKH GEISFLNEEV KSLKQEKEQV SLRCRELEII INHNRAENVQ SCDTQVSSLL
     DGVVTMTSRG AEGSVSKVNK SFGEESKIMV EDKVSFENMT VGEESKQEQL ILDHLPSVTK
     ESSLRATQPS ENDKLQKELN VLKSEQNDLR LQMEAQRICL SLVYSTHVDQ VREYMENEKD
     KALCSLKEEL IFAQEEKIKE LQKIHQLELQ TMKTQETGDE GKPLHLLIGK LQKAVSEECS
     YFLQTLCSVL GEYYTPALKC EVNAEDKENS GDYISENEDP ELQDYRYEVQ DFQENMHTLL
     NKVTEEYNKL LVLQTRLSKI WGQQTDGMKL EFGEENLPKE ETEFLSIHSQ MTNLEDIDVN
     HKSKLSSLQD LEKTKLEEQV QELESLISSL QQQLKETEQN YEAEIHCLQK RLQAVSESTV
     PPSLPVDSVV ITESDAQRTM YPGSCVKKNI DGTIEFSGEF GVKEETNIVK LLEKQYQEQL
     EEEVAKVIVS MSIAFAQQTE LSRISGGKEN TASSKQAHAV CQQEQHYFNE MKLSQDQIGF
     QTFETVDVKF KEEFKPLSKE LGEHGKEILL SNSDPHDIPE SKDCVLTISE EMFSKDKTFI
     VRQSIHDEIS VSSMDASRQL MLNEEQLEDM RQELVRQYQE HQQATELLRQ AHMRQMERQR
     EDQEQLQEEI KRLNRQLAQR SSIDNENLVS ERERVLLEEL EALKQLSLAG REKLCCELRN
     SSTQTQNGNE NQGEVEEQTF KEKELDRKPE DVPPEILSNE RYALQKANNR LLKILLEVVK
     TTAAVEETIG RHVLGILDRS SKSQSSASLI WRSEAEASVK SCVHEEHTRV TDESIPSYSG
     SDMPRNDINM WSKVTEEGTE LSQRLVRSGF AGTEIDPENE ELMLNISSRL QAAVEKLLEA
     ISETSSQLEH AKVTQTELMR ESFRQKQEAT ESLKCQEELR ERLHEESRAR EQLAVELSKA
     EGVIDGYADE KTLFERQIQE KTDIIDRLEQ ELLCASNRLQ ELEAEQQQIQ EERELLSRQK
     EAMKAEAGPV EQQLLQETEK LMKEKLEVQC QAEKVRDDLQ KQVKALEIDV EEQVSRFIEL
     EQEKNTELMD LRQQNQALEK QLEKMRKFLD EQAIDREHER DVFQQEIQKL EQQLKVVPRF
     QPISEHQTRE VEQLANHLKE KTDKCSELLL SKEQLQRDIQ ERNEEIEKLE FRVRELEQAL
     LVSADTFQKV EDRKHFGAVE AKPELSLEVQ LQAERDAIDR KEKEITNLEE QLEQFREELE
     NKNEEVQQLH MQLEIQKKES TTRLQELEQE NKLFKDDMEK LGLAIKESDA MSTQDQHVLF
     GKFAQIIQEK EVEIDQLNEQ VTKLQQQLKI TTDNKVIEEK NELIRDLETQ IECLMSDQEC
     VKRNREEEIE QLNEVIEKLQ QELANIGQKT SMNAHSLSEE ADSLKHQLDV VIAEKLALEQ
     QVETANEEMT FMKNVLKETN FKMNQLTQEL FSLKRERESV EKIQSIPENS VNVAIDHLSK
     DKPELEVVLT EDALKSLENQ TYFKSFEENG KGSIINLETR LLQLESTVSA KDLELTQCYK
     QIKDMQEQGQ FETEMLQKKI VNLQKIVEEK VAAALVSQIQ LEAVQEYAKF CQDNQTISSE
     PERTNIQNLN QLREDELGSD ISALTLRISE LESQVVEMHT SLILEKEQVE IAEKNVLEKE
     KKLLELQKLL EGNEKKQREK EKKRSPQDVE VLKTTTELFH SNEESGFFNE LEALRAESVA
     TKAELASYKE KAEKLQEELL VKETNMTSLQ KDLSQVRDHL AEAKEKLSIL EKEDETEVQE
     SKKACMFEPL PIKLSKSIAS QTDGTLKISS SNQTPQILVK NAGIQINLQS ECSSEEVTEI
     ISQFTEKIEK MQELHAAEIL DMESRHISET ETLKREHYVA VQLLKEECGT LKAVIQCLRS
     KEGSSIPELA HSDAYQTREI CSSDSGSDWG QGIYLTHSQG FDIASEGRGE ESESATDSFP
     KKIKGLLRAV HNEGMQVLSL TESPYSDGED HSIQQVSEPW LEERKAYINT ISSLKDLITK
     MQLQREAEVY DSSQSHESFS DWRGELLLAL QQVFLEERSV LLAAFRTELT ALGTTDAVGL
     LNCLEQRIQE QGVEYQAAME CLQKADRRSL LSEIQALHAQ MNGRKITLKR EQESEKPSQE
     LLEYNIQQKQ SQMLEMQVEL SSMKDRATEL QEQLSSEKMV VAELKSELAQ TKLELETTLK
     AQHKHLKELE AFRLEVKDKT DEVHLLNDTL ASEQKKSREL QWALEKEKAK LGRSEERDKE
     ELEDLKFSLE SQKQRNLQLN LLLEQQKQLL NESQQKIESQ RMLYDAQLSE EQGRNLELQV
     LLESEKVRIR EMSSTLDRER ELHAQLQSSD GTGQSRPPLP SEDLLKELQK QLEEKHSRIV
     ELLNETEKYK LDSLQTRQQM EKDRQVHRKT LQTEQEANTE GQKKMHELQS KVEDLQRQLE
     EKRQQVYKLD LEGQRLQGIM QEFQKQELER EEKRESRRIL YQNLNEPTTW SLTSDRTRNW
     VLQQKIEGET KESNYAKLIE MNGGGTGCNH ELEMIRQKLQ CVASKLQVLP QKASERLQFE
     TADDEDFIWV QENIDEIILQ LQKLTGQQGE EPSLVSPSTS CGSLTERLLR QNAELTGHIS
     QLTEEKNDLR NMVMKLEEQI RWYRQTGAGR DNSSRFSLNG GANIEAIIAS EKEVWNREKL
     TLQKSLKRAE AEVYKLKAEL RNDSLLQTLS PDSEHVTLKR IYGKYLRAES FRKALIYQKK
     YLLLLLGGFQ ECEDATLALL ARMGGQPAFT DLEVITNRPK GFTRFRSAVR VSIAISRMKF
     LVRRWHRVTG SVSININRDG FGLNQGAEKT DSFYHSSGGL ELYGEPRHTT YRSRSDLDYI
     RSPLPFQNRY PGTPADFNPG SLACSQLQNY DPDRALTDYI TRLEALQRRL GTIQSGSTTQ
     FHAGMRR
//