ID AKAP8_MOUSE Reviewed; 687 AA. AC Q9DBR0; Q9R0L8; DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 27-MAR-2024, entry version 158. DE RecName: Full=A-kinase anchor protein 8; DE Short=AKAP-8; DE AltName: Full=A-kinase anchor protein 95 kDa; DE Short=AKAP 95; GN Name=Akap8; Synonyms=Akap95; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Hattori A., Seki N., Hayashi A., Kozuma S., Muramatsu M., Miyajima N., RA Saito T.; RT "Mouse AKAP95."; RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and NOD; TISSUE=Lung, and Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP INTERACTION WITH MYCBP. RX PubMed=12414807; DOI=10.1074/jbc.m206387200; RA Furusawa M., Taira T., Iguchi-Ariga S.M., Ariga H.; RT "AMY-1 interacts with S-AKAP84 and AKAP95 in the cytoplasm and the nucleus, RT respectively, and inhibits cAMP-dependent protein kinase activity by RT preventing binding of its catalytic subunit to A-kinase-anchoring protein RT (AKAP) complex."; RL J. Biol. Chem. 277:50885-50892(2002). RN [4] RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE. RX PubMed=12082153; DOI=10.1242/jcs.115.14.2931; RA Bomar J., Moreira P., Balise J.J., Collas P.; RT "Differential regulation of maternal and paternal chromosome condensation RT in mitotic zygotes."; RL J. Cell Sci. 115:2931-2940(2002). RN [5] RP FUNCTION, AND INTERACTION WITH CCND1. RX PubMed=14641107; DOI=10.1042/bj20031765; RA Arsenijevic T., Degraef C., Dumont J.E., Roger P.P., Pirson I.; RT "A novel partner for D-type cyclins: protein kinase A-anchoring protein RT AKAP95."; RL Biochem. J. 378:673-679(2004). RN [6] RP INTERACTION WITH CASP3. RX PubMed=16227597; DOI=10.1128/mcb.25.21.9469-9477.2005; RA Kamada S., Kikkawa U., Tsujimoto Y., Hunter T.; RT "A-kinase-anchoring protein 95 functions as a potential carrier for the RT nuclear translocation of active caspase 3 through an enzyme-substrate-like RT association."; RL Mol. Cell. Biol. 25:9469-9477(2005). RN [7] RP SUBCELLULAR LOCATION, INTERACTION WITH FIGN, AND DISRUPTION PHENOTYPE. RX PubMed=16751186; DOI=10.1074/jbc.m603626200; RA Yang Y., Mahaffey C.L., Berube N., Frankel W.N.; RT "Interaction between fidgetin and protein kinase A-anchoring protein AKAP95 RT is critical for palatogenesis in the mouse."; RL J. Biol. Chem. 281:22352-22359(2006). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320 AND SER-325, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006; RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M., RA Thibault P.; RT "The phagosomal proteome in interferon-gamma-activated macrophages."; RL Immunity 30:143-154(2009). RN [9] RP FUNCTION, INTERACTION WITH NFKB1, AND SUBCELLULAR LOCATION. RX PubMed=19531803; DOI=10.1126/scisignal.2000202; RA Wall E.A., Zavzavadjian J.R., Chang M.S., Randhawa B., Zhu X., Hsueh R.C., RA Liu J., Driver A., Bao X.R., Sternweis P.C., Simon M.I., Fraser I.D.; RT "Suppression of LPS-induced TNF-alpha production in macrophages by cAMP is RT mediated by PKA-AKAP95-p105."; RL Sci. Signal. 2:RA28-RA28(2009). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72; SER-320; SER-325 AND RP SER-336, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [11] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-109; ARG-232 AND ARG-276, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, and Embryo; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). CC -!- FUNCTION: Anchoring protein that mediates the subcellular CC compartmentation of cAMP-dependent protein kinase (PKA type II). Acts CC as an anchor for a PKA-signaling complex onto mitotic chromosomes, CC which is required for maintenance of chromosomes in a condensed form CC throughout mitosis. Recruits condensin complex subunit NCAPD2 to CC chromosomes required for chromatin condensation; the function appears CC to be independent from PKA-anchoring (By similarity). Specifically CC involved in recruitment of CAPD2 to, and condensation of maternal but CC not paternal chromosomes (PubMed:12082153). May help to deliver cyclin CC D/E to CDK4 to facilitate cell cycle progression (PubMed:14641107). CC Required for cell cycle G2/M transition and histone deacetylation CC during mitosis. In mitotic cells recruits HDAC3 to the vicinity of CC chromatin leading to deacetylation and subsequent phosphorylation at CC 'Ser-10' of histone H3; in this function may act redundantly with CC AKAP8L. Involved in nuclear retention of RPS6KA1 upon ERK activation CC thus inducing cell proliferation. May be involved in regulation of DNA CC replication by acting as scaffold for MCM2. Enhances HMT activity of CC the KMT2 family MLL4/WBP7 complex and is involved in transcriptional CC regulation. In a teratocarcinoma cell line is involved in retinoic CC acid-mediated induction of developmental genes implicating H3 'Lys-4' CC methylation. May be involved in recruitment of active CASP3 to the CC nucleus in apoptotic cells. May act as a carrier protein of GJA1 for CC its transport to the nucleus. May play a repressive role in the CC regulation of rDNA transcription. Preferentially binds GC-rich DNA in CC vitro. In cells, associates with ribosomal RNA (rRNA) chromatin, CC preferentially with rRNA promoter and transcribed regions (By CC similarity). Involved in modulation of Toll-like receptor signaling. CC Required for the cAMP-dependent suppression of TNF-alpha in early CC stages of LPS-induced macrophage activation; the function probably CC implicates targeting of PKA to NFKB1 (PubMed:19531803). CC {ECO:0000250|UniProtKB:O43823, ECO:0000250|UniProtKB:Q63014}. CC -!- SUBUNIT: Binds to the PKA RII-alpha regulatory subunit PRKAR2A (By CC similarity). Interacts (via C-terminus) with FIGN (PubMed:16751186). CC Interacts with NCAPD2, CCND3, CCNE1, MCM2, RPS6KA1, DDX5, PDE4A (By CC similarity). Interacts with MYCBP; MYCBP is translocated to the nucleus CC and the interaction prevents the association of the PKA catalytic CC subunit leading to suppression of PKA activity (PubMed:12414807). CC Interacts with CCND1, CASP3 (PubMed:14641107, PubMed:16227597). CC Interacts with NFKB1; detetcted in the cytoplasm (PubMed:19531803). CC Interacts with DPY30; mediating AKAP8 association with at least the CC MLL4/WBP7 HMT complex. Interacts with HDAC3; increased during mitosis. CC Interacts with GJA1; in the nucleus and in the nuclear membrane; the CC nuclear association increases with progress of cell cycle G1, S and G2 CC phase and decreases in M phase (By similarity). CC {ECO:0000250|UniProtKB:O43823, ECO:0000250|UniProtKB:Q5VK71, CC ECO:0000250|UniProtKB:Q63014, ECO:0000269|PubMed:12414807, CC ECO:0000269|PubMed:14641107, ECO:0000269|PubMed:16227597, CC ECO:0000269|PubMed:16751186, ECO:0000269|PubMed:19531803}. CC -!- INTERACTION: CC Q9DBR0; Q9ERZ6: Fign; NbExp=4; IntAct=EBI-4285802, EBI-11111349; CC Q9DBR0; P25799: Nfkb1; NbExp=4; IntAct=EBI-4285802, EBI-643958; CC -!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000269|PubMed:16751186}. CC Nucleus, nucleolus {ECO:0000250|UniProtKB:O43823}. Cytoplasm CC {ECO:0000269|PubMed:19531803}. Note=Associated with the nuclear matrix CC (By similarity). Exhibits partial localization to the nucleolus in CC interphase, possibly to the fibrillary center and/or to the dense CC fibrillary component (By similarity). Redistributed and detached from CC condensed chromatin during mitosis (By similarity). Localizes CC specifically to the vicinity of the meiotic spindle in metaphase II CC oocytes (PubMed:12082153). {ECO:0000250|UniProtKB:O43823, CC ECO:0000269|PubMed:12082153}. CC -!- DEVELOPMENTAL STAGE: Weakly expressed in metaphase II oocytes. Strongly CC up-regulated after fertilization at the pronuclear stage and restricted CC to the female pronucleus. Subsequently localized to the nucleus of each CC blastomere and on condensed chromosomes in mitotic cells. CC {ECO:0000269|PubMed:12082153}. CC -!- PTM: Phosphorylated on tyrosine residues probably by SRC subfamily CC protein kinases; multiple phosphorylation is leading to dissociation CC from nuclear structures implicated in chromatin structural changes. CC {ECO:0000250|UniProtKB:O43823}. CC -!- DISRUPTION PHENOTYPE: AKAP8 and FIGN double mutant mice die soon after CC birth due to cleft palate. {ECO:0000269|PubMed:16751186}. CC -!- SIMILARITY: Belongs to the AKAP95 family. {ECO:0000255|PROSITE- CC ProRule:PRU01140}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB028920; BAA84710.1; -; mRNA. DR EMBL; AK004801; BAB23574.1; -; mRNA. DR EMBL; AK089092; BAC40746.1; -; mRNA. DR CCDS; CCDS37555.1; -. DR RefSeq; NP_062748.2; NM_019774.5. DR AlphaFoldDB; Q9DBR0; -. DR BioGRID; 207953; 31. DR IntAct; Q9DBR0; 27. DR MINT; Q9DBR0; -. DR STRING; 10090.ENSMUSP00000002699; -. DR GlyGen; Q9DBR0; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9DBR0; -. DR PhosphoSitePlus; Q9DBR0; -. DR EPD; Q9DBR0; -. DR jPOST; Q9DBR0; -. DR MaxQB; Q9DBR0; -. DR PaxDb; 10090-ENSMUSP00000002699; -. DR ProteomicsDB; 285797; -. DR Pumba; Q9DBR0; -. DR Antibodypedia; 1427; 407 antibodies from 36 providers. DR DNASU; 56399; -. DR Ensembl; ENSMUST00000002699.7; ENSMUSP00000002699.6; ENSMUSG00000024045.7. DR GeneID; 56399; -. DR KEGG; mmu:56399; -. DR UCSC; uc008bwg.2; mouse. DR AGR; MGI:1928488; -. DR CTD; 10270; -. DR MGI; MGI:1928488; Akap8. DR VEuPathDB; HostDB:ENSMUSG00000024045; -. DR eggNOG; ENOG502QZY2; Eukaryota. DR GeneTree; ENSGT00530000063777; -. DR HOGENOM; CLU_024193_1_0_1; -. DR InParanoid; Q9DBR0; -. DR OMA; CPNRLPS; -. DR OrthoDB; 5311990at2759; -. DR PhylomeDB; Q9DBR0; -. DR TreeFam; TF105407; -. DR BioGRID-ORCS; 56399; 2 hits in 67 CRISPR screens. DR ChiTaRS; Akap8; mouse. DR PRO; PR:Q9DBR0; -. DR Proteomes; UP000000589; Chromosome 17. DR RNAct; Q9DBR0; Protein. DR Bgee; ENSMUSG00000024045; Expressed in retinal neural layer and 286 other cell types or tissues. DR ExpressionAtlas; Q9DBR0; baseline and differential. DR GO; GO:0000785; C:chromatin; ISO:MGI. DR GO; GO:0000793; C:condensed chromosome; IDA:MGI. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0001939; C:female pronucleus; IDA:MGI. DR GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB. DR GO; GO:0005730; C:nucleolus; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0003682; F:chromatin binding; ISO:MGI. DR GO; GO:0003677; F:DNA binding; ISO:MGI. DR GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI. DR GO; GO:0042826; F:histone deacetylase binding; ISO:MGI. DR GO; GO:0051059; F:NF-kappaB binding; IDA:UniProtKB. DR GO; GO:0034237; F:protein kinase A regulatory subunit binding; ISO:MGI. DR GO; GO:0008270; F:zinc ion binding; ISO:MGI. DR GO; GO:0044839; P:cell cycle G2/M phase transition; ISO:MGI. DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:UniProtKB. DR GO; GO:0071380; P:cellular response to prostaglandin E stimulus; IMP:UniProtKB. DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW. DR GO; GO:0007076; P:mitotic chromosome condensation; IDA:MGI. DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IMP:UniProtKB. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR InterPro; IPR007071; AKAP95. DR InterPro; IPR034736; ZF_C2H2_AKAP95. DR PANTHER; PTHR12190:SF6; A-KINASE ANCHOR PROTEIN 8; 1. DR PANTHER; PTHR12190; A-KINASE ANCHOR PROTEIN AKAP 8; 1. DR Pfam; PF04988; AKAP95; 1. DR SUPFAM; SSF56935; Porins; 1. DR PROSITE; PS51799; ZF_C2H2_AKAP95; 2. DR Genevisible; Q9DBR0; MM. PE 1: Evidence at protein level; KW Cytoplasm; DNA-binding; Immunity; Innate immunity; Isopeptide bond; KW Metal-binding; Methylation; Nucleus; Phosphoprotein; Protein transport; KW Reference proteome; Repeat; Transcription; Transcription regulation; KW Transport; Ubl conjugation; Zinc; Zinc-finger. FT CHAIN 1..687 FT /note="A-kinase anchor protein 8" FT /id="PRO_0000075382" FT ZN_FING 389..411 FT /note="C2H2 AKAP95-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01140" FT ZN_FING 478..501 FT /note="C2H2 AKAP95-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01140" FT REGION 1..210 FT /note="Interaction with DPY30" FT /evidence="ECO:0000250|UniProtKB:O43823" FT REGION 1..195 FT /note="Interaction with MCM2" FT /evidence="ECO:0000250|UniProtKB:O43823" FT REGION 105..124 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 109..201 FT /note="Interaction with DDX5" FT /evidence="ECO:0000250|UniProtKB:Q63014" FT REGION 185..218 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 277..379 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 384..447 FT /note="Involved in chromatin-binding" FT /evidence="ECO:0000250|UniProtKB:O43823" FT REGION 522..565 FT /note="Involved in condensin complex recruitment" FT /evidence="ECO:0000250|UniProtKB:O43823" FT REGION 568..585 FT /note="RII-binding" FT /evidence="ECO:0000250|UniProtKB:Q63014" FT REGION 572..589 FT /note="Required for interaction with MYCBP" FT /evidence="ECO:0000269|PubMed:12414807" FT REGION 624..659 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 286..303 FT /note="Bipartite nuclear localization signal" FT /evidence="ECO:0000250|UniProtKB:O43823, FT ECO:0000250|UniProtKB:Q63014" FT COMPBIAS 194..218 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 280..379 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 624..645 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 72 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 109 FT /note="Asymmetric dimethylarginine; alternate" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 109 FT /note="Omega-N-methylarginine; alternate" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 199 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O43823" FT MOD_RES 232 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 276 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 320 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19144319, FT ECO:0007744|PubMed:21183079" FT MOD_RES 325 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19144319, FT ECO:0007744|PubMed:21183079" FT MOD_RES 336 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 552 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q63014" FT MOD_RES 659 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q63014" FT CROSSLNK 314 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:O43823" FT CONFLICT 323 FT /note="D -> G (in Ref. 1; BAA84710)" FT /evidence="ECO:0000305" FT CONFLICT 370 FT /note="K -> E (in Ref. 1; BAA84710)" FT /evidence="ECO:0000305" FT CONFLICT 541 FT /note="D -> G (in Ref. 1; BAA84710)" FT /evidence="ECO:0000305" FT CONFLICT 544 FT /note="V -> A (in Ref. 1; BAA84710)" FT /evidence="ECO:0000305" FT CONFLICT 584 FT /note="A -> T (in Ref. 1; BAA84710)" FT /evidence="ECO:0000305" FT CONFLICT 590 FT /note="E -> G (in Ref. 1; BAA84710)" FT /evidence="ECO:0000305" SQ SEQUENCE 687 AA; 76294 MW; BC1E320216A47E10 CRC64; MEQGYGGYGA WSAGPANTQG TYGSGMTSWQ GYENYNYYNA QNTSVPAGTP YSYGPASWEA TKTNDGGLAA GSPAMHVASF APEPCTDNSD SLIAKINQRL DMLSKEGGRG GISSGGEGVQ DRDSSFRFQP YESYDARPCI PEHNPYRPGY GYDYDFDLGT DRNGSFGGTF NDCRDPAPER GSLDGFLRGR GQGRFQDRSN SSTFIRSDPF MPPSASEPLS TTWNELNYMG GRGLGGPSTS RPPPSLFSQS MAPDYSMMGM QGVGGFGGTM PYGCGRSQTR IRDWPRRRGF ERFGPDNMGR KRKQFPLYEE PDAKLARADS DGDLSENDDG AGDLRSGDEE FRGEDDLCDS RKQRGEKEDE DEDVKKRREK QRRRDRMRDR AADRIQFACS VCKFRSFEDE EIQKHLQSKF HKETLRFIST KLPDKTVEFL QEYIINRNKK IEKRRQELLE KESPKPKPDP FKGIGQEHFF KKIEAAHCLA CDMLIPAQHQ LLQRHLHSVD HNHNRRLAAE QFKKTSLHVA KSVLNNKHIV KMLEKYLKGE DPFVNETADL ETEGDENVGE EKEETPEEVA AEVLAEVITA AVKAVEGEGE PAAAHSDVLT EVEGPVDTAE ASSDPHTEKL LEEQTCEAAS ETRSIEDKTR GEAAEARNEA AMPTADAGST LPVIAIPGIM EDELEQTGAE AKDIPTE //