AKAP9_MOUSE
ID AKAP9_MOUSE Reviewed; 3797 AA.
AC Q70FJ1; Q3TH74; Q80TR6;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 2.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=A-kinase anchor protein 9;
DE Short=AKAP-9;
DE AltName: Full=Protein kinase A-anchoring protein 9;
DE Short=PRKA9;
GN Name=Akap9; Synonyms=Kiaa0803;
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] (ISOFORM 2).
RC STRAIN=BALB/cJ; TISSUE=Brain;
RA Kemmner W.A.;
RT "Cloning mouse AKAP9.";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-582 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Stomach;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC 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).
CC -!- FUNCTION: Scaffolding protein that assembles several protein kinases
CC and phosphatases on the centrosome and Golgi apparatus. Required to
CC maintain the integrity of the Golgi apparatus. Required for microtubule
CC nucleation at the cis-side of the Golgi apparatus. Required for
CC association of the centrosomes with the poles of the bipolar mitotic
CC spindle during metaphase. In complex with PDE4DIP isoform 2/MMG8/SMYLE,
CC recruits CAMSAP2 to the Golgi apparatus and tethers non-centrosomal
CC minus-end microtubules to the Golgi, an important step for polarized
CC cell movement. In complex with PDE4DIP isoform 2, EB1/MAPRE1 and
CC CDK5RAP2, contributes to microtubules nucleation and extension also
CC from the centrosome to the cell periphery.
CC {ECO:0000250|UniProtKB:Q99996}.
CC -!- SUBUNIT: Interacts with the regulatory region of protein kinase N
CC (PKN), protein phosphatase 2A (PP2A), protein phosphatase 1 (PP1) and
CC the immature non-phosphorylated form of PKC epsilon. Interacts with
CC CIP4 and FNBP1. Interacts with chloride intracellular channel proteins
CC CLIC1, CLIC4 and CLIC5. CSNK1D binding promotes its centrosomal
CC subcellular location. Interacts with GM130/GOLGA2; leading to
CC recruitment to the Golgi apparatus. Interacts with KCNQ1; targets
CC protein kinase A (PKA) catalytic and regulatory subunits and protein
CC phosphatase 1 (PP1), to the heterodimer KCNQ1-KCNE1. Interacts with
CC PDE4DIP isoform 2; this interaction stabilizes both proteins. In
CC complex with PDE4DIP isoform 2, recruits CAMSAP2 to the Golgi
CC apparatus. Forms a pericentrosomal complex with CDK5RAP2, EB1/MAPRE1
CC and PDE4DIP isoform 2; within this complex, MAPRE1 binding to CDK5RAP2
CC may be mediated by PDE4DIP. Interacts with MAPRE1 and MAPRE3. Interacts
CC (via C-terminus) with CAMSAP2; this interaction is much stronger in the
CC presence of PDE4DIP isoform 2. Interacts with CAMSAP3. Interacts (via
CC C-terminus) with the gamma-tubulin ring complex (gamma-TuRC), composed
CC of gamma-tubulin, TUBGCP2, TUBGCP3, TUBGCP4, TUBGCP5 and TUBGCP6.
CC {ECO:0000250|UniProtKB:Q99996}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:Q99996}.
CC Cytoplasm {ECO:0000250|UniProtKB:Q99996}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q99996}. Note=Cytoplasmic in parietal cells.
CC Recruited to the Golgi apparatus by GM130/GOLGA2. Localization at the
CC centrosome versus Golgi apparatus may be cell type-dependent. Recruited
CC to the centrosome in the presence of CDK5RAP2.
CC {ECO:0000250|UniProtKB:Q99996}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q70FJ1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q70FJ1-2; Sequence=VSP_039481;
CC Name=3;
CC IsoId=Q70FJ1-3; Sequence=VSP_039482;
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 -!- MISCELLANEOUS: [Isoform 2]: Incomplete sequence. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Incomplete sequence. {ECO:0000305}.
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DR EMBL; AJ582913; CAE46960.1; -; mRNA.
DR EMBL; AK122374; BAC65656.2; -; Transcribed_RNA.
DR EMBL; AK168404; BAE40324.1; -; mRNA.
DR CCDS; CCDS19070.1; -. [Q70FJ1-2]
DR RefSeq; NP_919444.2; NM_194462.2.
DR BioGRID; 221564; 21.
DR IntAct; Q70FJ1; 7.
DR MINT; Q70FJ1; -.
DR STRING; 10090.ENSMUSP00000046129; -.
DR iPTMnet; Q70FJ1; -.
DR PhosphoSitePlus; Q70FJ1; -.
DR EPD; Q70FJ1; -.
DR jPOST; Q70FJ1; -.
DR MaxQB; Q70FJ1; -.
DR PaxDb; Q70FJ1; -.
DR PeptideAtlas; Q70FJ1; -.
DR PRIDE; Q70FJ1; -.
DR ProteomicsDB; 282060; -. [Q70FJ1-1]
DR ProteomicsDB; 282061; -. [Q70FJ1-2]
DR ProteomicsDB; 282062; -. [Q70FJ1-3]
DR DNASU; 100986; -.
DR GeneID; 100986; -.
DR KEGG; mmu:100986; -.
DR CTD; 10142; -.
DR MGI; MGI:2178217; Akap9.
DR eggNOG; ENOG502QV16; Eukaryota.
DR InParanoid; Q70FJ1; -.
DR OrthoDB; 8180at2759; -.
DR PhylomeDB; Q70FJ1; -.
DR Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-MMU-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-MMU-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-MMU-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-MMU-5576890; Phase 3 - rapid repolarisation.
DR Reactome; R-MMU-5576893; Phase 2 - plateau phase.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-MMU-8854518; AURKA Activation by TPX2.
DR BioGRID-ORCS; 100986; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Akap9; mouse.
DR PRO; PR:Q70FJ1; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q70FJ1; protein.
DR GO; GO:0097729; C:9+2 motile cilium; IDA:MGI.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0036064; C:ciliary basal body; IDA:MGI.
DR GO; GO:0005801; C:cis-Golgi network; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0044307; C:dendritic branch; ISO:MGI.
DR GO; GO:0099147; C:extrinsic component of postsynaptic density membrane; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0005795; C:Golgi stack; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0000242; C:pericentriolar material; IDA:MGI.
DR GO; GO:0034705; C:potassium channel complex; ISO:MGI.
DR GO; GO:0120219; C:subapical part of cell; IDA:MGI.
DR GO; GO:0097060; C:synaptic membrane; ISO:MGI.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; ISO:MGI.
DR GO; GO:0060090; F:molecular adaptor activity; ISS:UniProtKB.
DR GO; GO:0015459; F:potassium channel regulator activity; ISO:MGI.
DR GO; GO:0034237; F:protein kinase A regulatory subunit binding; ISO:MGI.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR GO; GO:0071320; P:cellular response to cAMP; ISO:MGI.
DR GO; GO:0051661; P:maintenance of centrosome location; ISS:UniProtKB.
DR GO; GO:0007020; P:microtubule nucleation; ISS:UniProtKB.
DR GO; GO:0007194; P:negative regulation of adenylate cyclase activity; ISO:MGI.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; ISO:MGI.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:MGI.
DR GO; GO:1901018; P:positive regulation of potassium ion transmembrane transporter activity; ISO:MGI.
DR GO; GO:0031503; P:protein-containing complex localization; ISO:MGI.
DR GO; GO:0098909; P:regulation of cardiac muscle cell action potential involved in regulation of contraction; ISO:MGI.
DR GO; GO:1903358; P:regulation of Golgi organization; ISS:UniProtKB.
DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; ISO:MGI.
DR GO; GO:0060306; P:regulation of membrane repolarization; ISO:MGI.
DR GO; GO:0098962; P:regulation of postsynaptic neurotransmitter receptor activity; ISO:MGI.
DR GO; GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; ISO:MGI.
DR GO; GO:0060009; P:Sertoli cell development; IMP:MGI.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR InterPro; IPR028745; AKAP9/Pericentrin.
DR InterPro; IPR019528; PACT_domain.
DR PANTHER; PTHR44981; PTHR44981; 1.
DR Pfam; PF10495; PACT_coil_coil; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Golgi apparatus; Phosphoprotein; Reference proteome.
FT CHAIN 1..3797
FT /note="A-kinase anchor protein 9"
FT /id="PRO_0000395481"
FT REGION 1..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1643..1668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2418..2453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2498..2510
FT /note="PKA-RII subunit binding domain"
FT /evidence="ECO:0000250"
FT REGION 2600..2693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3271..3296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 140..607
FT /evidence="ECO:0000255"
FT COILED 640..976
FT /evidence="ECO:0000255"
FT COILED 1808..2377
FT /evidence="ECO:0000255"
FT COILED 2975..3325
FT /evidence="ECO:0000255"
FT COMPBIAS 21..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2434..2453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2600..2623
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2640..2666
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3282..3296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99996"
FT MOD_RES 1288
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99996"
FT MOD_RES 3732
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99996"
FT MOD_RES 3755
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99996"
FT MOD_RES 3787
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99996"
FT VAR_SEQ 104..121
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_039481"
FT VAR_SEQ 3436..3454
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12693553"
FT /id="VSP_039482"
FT CONFLICT 62
FT /note="S -> N (in Ref. 1; CAE46960)"
FT /evidence="ECO:0000305"
FT CONFLICT 2388
FT /note="S -> L (in Ref. 1; CAE46960)"
FT /evidence="ECO:0000305"
FT CONFLICT 2775
FT /note="L -> Q (in Ref. 1; CAE46960)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3797 AA; 436214 MW; CA30D11FF5696124 CRC64;
MEDEERQRKL AAGKAKLARF RQRKAQYDGD IPKKQKKKRT SSSKHDSSLH TDQQSGELCS
ESSQRVDLAG NPDCSGPERK HGQVFSAEPE SEISTTADEC SSEINGCNSV MKPRKPTDPL
REEEFSLDDS SSEQGAQSSQ TCLQMVEKEL AEKQHDIEEL TQELEEMRAS FGTEGLKQLQ
EFEAAIKQRD GIITQLTANL QQARREKDDT MVEFLELTEQ SQKLQIQFQH LQANETLQNS
TLSRTATDLL QAKRQIFTQQ QQLQDYQKKE EDLQAQISFL QEKLRAFEME KDRKIENLNA
KEIQEKQALI DELNTRVVEE EKKTVELKNK VTTADELLGG LHEQLTQRNQ EIQSLKLELG
NSQQNERKCS EEIKELMRTV EELQKRNLKD SWLETSAVRR VEQETQRKLS HLQAELDEMY
GKQIVQMKQE LINQHMSQIE ELKSQHKREM ENTLKSDTNA AISKEQVNLM NAAINELNVR
LQETHAQKEE LKGELGVVLG EKSALQSQSN DLLEEVRFLR EQVQKARQTI AEQENRLSEA
RKSLSTVEDL KAEIVAASES RKELELKHEA EITNYKIKLE MLEKEKNAVL DRMAESQEAE
LERLRTQPLF SHEEELSKLK EDLEVEHRIN IEKLKDNLGI HYKQQIDGLQ NEMNRKMESM
QCETDNLITQ QNQLILENSK LRDLQECLVN SKSEEMNLQI NELQKEIEIL KQEEKEKGTL
EQEVQELQLK TEQLEKQLKE KEDDLQEKCA QLDAENNILK EEKRVLEDKL KMYSPSEQEE
RSIAVDPSTS KLADSRWQKE VAMLRKETED LQQQCLYLNE EIEKQRNTFA FAEKNFEVNY
QELQREYTCL LKIRDDLEAT QTKQALEYES KLRALEEELL SKRGNPXAPK GKSSGIFPSE
TLEIGEVVEK DTTELMEKLE VTKREKLELS EKVSGLSEQL KQTHCTINSL SAEXRALKQE
KEQLLLRCGE LELLANPSGT ENAAVCPVQM SSYQAGLVMG KVGDSGGSIS KISKDLAEES
KPMIEDKIPF KESGREQLLL PTRAQEPSHA TVEPCESEKL QQELHALKAE QDDLRLQMEA
QRICLFVVYS THADQVRAHM EKEREEALCS LKDELISAQQ KKIDELHKMH QCQLQNVKIQ
ETGDEPLQVL IERLQKAVSE KCFHISKTLN NVFDECYTPL KCEMNIEEKE NSGVYTSQNQ
SPELQEYRYE VQDFQESMQV LLGKVTEECR KLSGLQTRLG KIHEQQTDGV ALEFAEQNAA
EEEAGLLSGC SQSALQSTDV SLESKVSSLP ASEKNRECER QVQELQSPVA AGQLQLTETE
ASHRAEIECL QQRLEAASEA PVQPSLSIDS VVFKGSGAQK PVYCGSCLRE YVDGTAKFSD
RFEVRQETNM VNLMEKQYQE RLEEEIAKVI VSMSIAFAQQ TELSRLSEGK ENTIQSEQAH
TLCSQNKHQL NDITSQSQVG LQTFEATDKB FKEEFKPLSK ELGEYRKAVP LSSHDDLDDI
LKSEEHGLAI SEEIFSKDET FIVRKSMHDE VLVSSMDTSR QLILNEQLED MRQELVRQYE
EHQQATEMLR QAHMQQMERQ REDQEQLQEE IKRLNEQLTQ KSSIDTEHVV SERERVLLEE
LEALKQLPLA GRKELCCELR HSSTQTQDGH DDQEVEEQTL KDKTLERSPE DALLDRNLSN
ERYALKKANN RLLKILLEVV KTTSAAEETI GRHVLGILDR SSKGQTASSL LWRSEADASA
TTCAPEDCAR AMDESIPSYP GTAIATHDSI WSKVTEEGAE LSQRLVRSGF AGPVIDPENE
ELMLNISSRL QAAVEKLLEA ISETNTQLEH AKVTQTELMR ESFRQKQEAT ESLHCLEELR
ERLQEESRAR EQLAEELNKA ESVIDGYSDE KTLFERQIQE KTDIIEHLEQ EVLCMNNRLQ
ELESDQRRVE EERQLLCRQR EAMRAEAGPV EQQFLQETEK LMKEKLEVQC QAEKVRGDLQ
KQVKALEIDV EEQVSRFIEL EQEKNAELTD LRQQSQALEK QLEKMRKFLD EQAIDREHER
DVFQQEIQKL EHQLKAAPRI QPVSEHQARE VEQLTNHLKE KTDRCSELLL SKEQLQRDIQ
ERNEEIEKLE CRVRELEQAL LASAEPFPKV EDQKRSGAVA ADPELSLEVQ LQAERDATDR
KQKEITNLEE QLEQFREELE NKNDEVQELL MQLEIQRKES TTRLQELQQE NRLFKDEIEK
LGFAMKESDS VSTRDQPMLF GKFAQLIQEK EIEIDRLNEQ FIKLQQQLKL TTDNKVIEEQ
KEQIQDLETQ IERLMSEREH EKKQREEEVE QLTGVVEKLQ QEVVSTEQQR EGARTLPEDE
ESFKHQLDKV TAEKLVLEQQ VETTNQVMTH MNNVLKEINF KMDQITQSLC NLNKECASNE
ELPSLPKESV HMTVHELGSD NLQPEDAPAQ DVTKPLEKQT SLTRLQESPE ASRTQEIESL
ASSVGAKDVE LTQCREQTET IQEQAQSETD RLQKKLTDLQ RSLEKFAAAL VSQVQMEAAQ
EYVPFHQEKQ PVSSAPGSTD IQNANGLTGA STESLIPTVT LRLAEVESRV AEVHSGTMSE
KLVGIVGGNA SETEKRVIEL QKLLEEAEER PEEGGEQSSR DGEVRESYMT SLQKDLGQVK
DPLTEAKEKL SYSLEKEKRT GEQESREAPI PEPPSVEVGG CSGLTERTDK VSSSGNQTLQ
ILLRDAAIQT DLQSESSQEE VRDTINQLTK KMEHIQELHA AEILDMESRH ILETESLKKE
HYVAIQLLTK ECETLKEMTQ CLRCKEGSSI PELADSVAYQ SREVYSSDSE SDWGQSQGFD
TAIEGREEGE TSADLFPKKI KGLVKAVHSE GMQVLSLSSP LCDDGEDRSI QQLSESWLKE
RQAYLNTISS LKDLISKMQV RRETEVYDRC HLSDWRGELL LACQRVFIKE RSVLLATFQT
ELTSLSTRDV DGLLNSLEQR IQEQGIEYHT AMDCLQKADR RSLLAEIEDL RAQINGGKMT
LEREQGTEKS SQELLDCSMQ QKQSLEMQLE LSSLRDRAAE LQEQLSSEKM VVAELKSELA
QAKLELGTTL KAQHKRLKEL EAFRSEVKEK TDEIHFLSDT LAREQKNSLE LQWALEKEKA
RSGHHEEREK EELEDLKFSL EDQKRRNTQL NLLLEQQKQL LNESQQKIES QKMLHDAQLS
EEQGRNLGLQ ALLESEQVRI QEMKSTLDKE RELYAQLQSR EDGGQPPPAL PSEDLLKELQ
KQLEEKHSRI VELLSETEKY KLDSLQTRQQ MEKDRQVHQK TLQTEQEANT QGQKKMQELQ
SKVEELQRQL QEKRQQVYKL DLEGKRLQGL MQEFQKQELE PEEKPGSRGL VDQNLNEPAT
WNFTDDRTRN WVLQQKMGEA KDRNFTKLIE INGGELDHNH DLEMIRQTLQ HVASKLQHVA
QKACSRLQFE TAGDDAFIWI QENIDGIILQ LQKLTGQPGD EHSLGPPSSS CGSLTESLMR
QNTELTRLIN QLTEEKNTLR SIVIKLEELN RCYWHTGASR DCCSRFSFID PADIEAIIAS
EKEVWNREKL SLQKALKRAE AKVYKLKAEL RNDALLRNLG PDTDHAALQK IYNKYLRASS
FRKALIYQKK YLLLLLGGFQ ECEDVTLGVL ARMGGHLALK DSKTITNHPK AFSRFRSAVR
VSIAISRMKF LVRRWQQVTS TSSININRDG FGLSPGIEKT DPFYHSPGGL ELYGEPRHTM
YRSRFDLDYP RSLLPLQNRY PGTPGDLNSI SMASSQLHQY NPDKSLTDYV TRLEALRRRL
GAIQSGSTTQ FHFGMRR
