AKAP9_HUMAN
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 03-AUG-2022, entry version 208.
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 Q99996-2; 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="http://atlasgeneticsoncology.org/Genes/AKAP9ID42999ch7q21.html";
CC ---------------------------------------------------------------------------
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CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
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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 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; 190.
DR CORUM; Q99996; -.
DR DIP; DIP-29942N; -.
DR IntAct; Q99996; 92.
DR MINT; Q99996; -.
DR STRING; 9606.ENSP00000348573; -.
DR CarbonylDB; Q99996; -.
DR GlyGen; Q99996; 2 sites, 1 O-linked glycan (2 sites).
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; Q99996; -.
DR PeptideAtlas; Q99996; -.
DR PRIDE; 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 Antibodypedia; 1376; 190 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 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; EAIVLNC; -.
DR OrthoDB; 8180at2759; -.
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; 14 hits in 1085 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 196 other tissues.
DR ExpressionAtlas; Q99996; baseline and differential.
DR Genevisible; Q99996; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
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:UniProtKB.
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:0007194; P:negative regulation of adenylate cyclase activity; IEA:Ensembl.
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:0098962; P:regulation of postsynaptic neurotransmitter receptor activity; IDA:SynGO.
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; PTHR44981; 1.
DR Pfam; PF10495; PACT_coil_coil; 1.
DR SMART; SM01188; ELK; 4.
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
