AKAP6_HUMAN
ID AKAP6_HUMAN Reviewed; 2319 AA.
AC Q13023; A7E242; A7E2D4; O15028;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 3.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=A-kinase anchor protein 6;
DE Short=AKAP-6;
DE AltName: Full=A-kinase anchor protein 100 kDa;
DE Short=AKAP 100;
DE AltName: Full=Protein kinase A-anchoring protein 6;
DE Short=PRKA6;
DE AltName: Full=mAKAP;
GN Name=AKAP6; Synonyms=AKAP100, KIAA0311;
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 1), AND VARIANT VAL-1492.
RX PubMed=10413680; DOI=10.1242/jcs.112.16.2725;
RA Kapiloff M.S., Shillace R.V., Westphal A.M., Scott J.D.;
RT "mAKAP: an A-kinase anchoring protein targeted to the nuclear membrane of
RT differentiated myocytes.";
RL J. Cell Sci. 112:2725-2736(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1666-2319 (ISOFORM 1).
RC TISSUE=Hippocampus;
RX PubMed=7721854; DOI=10.1074/jbc.270.16.9327;
RA McCartney S., Little B.M., Langeberg L.K., Scott J.D.;
RT "Cloning and characterization of A-kinase anchor protein 100 (AKAP100). A
RT protein that targets A-kinase to the sarcoplasmic reticulum.";
RL J. Biol. Chem. 270:9327-9333(1995).
RN [8]
RP INTERACTION WITH SYNPO2.
RX PubMed=17923693; DOI=10.1128/mcb.00950-07;
RA Faul C., Dhume A., Schecter A.D., Mundel P.;
RT "Protein kinase A, Ca2+/calmodulin-dependent kinase II, and calcineurin
RT regulate the intracellular trafficking of myopodin between the Z-disc and
RT the nucleus of cardiac myocytes.";
RL Mol. Cell. Biol. 27:8215-8227(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP VARIANTS [LARGE SCALE ANALYSIS] MET-910; ILE-1192; GLN-1702 AND THR-1839.
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).
CC -!- FUNCTION: Binds to type II regulatory subunits of protein kinase A and
CC anchors/targets them to the nuclear membrane or sarcoplasmic reticulum.
CC May act as an adapter for assembling multiprotein complexes.
CC -!- SUBUNIT: Interacts with RII subunit of PKA, phosphatase 2B
CC (calcineurin) and AKAP79. Interacts with SYNPO2.
CC {ECO:0000269|PubMed:17923693}.
CC -!- SUBCELLULAR LOCATION: Sarcoplasmic reticulum. Nucleus membrane. Note=In
CC heart muscle. Participation of multiple targeting signals allow correct
CC intracellular targeting. These may be repeated motifs rich in basic and
CC hydrophobic amino acids, palmitoylated/myristoylated motifs or
CC alternatively splice targeting sequences.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q13023-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13023-2; Sequence=VSP_054497, VSP_054498;
CC -!- TISSUE SPECIFICITY: Highly expressed in cardiac and skeletal muscle,
CC followed by brain.
CC -!- DOMAIN: RII-alpha binding site, predicted to form an amphipathic helix,
CC could participate in protein-protein interactions with a complementary
CC surface on the R-subunit dimer.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA20770.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U17195; AAA92354.2; -; mRNA.
DR EMBL; AB002309; BAA20770.2; ALT_INIT; mRNA.
DR EMBL; AL049781; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL117672; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL132988; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL136298; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471078; EAW65931.1; -; Genomic_DNA.
DR EMBL; BC150185; AAI50186.1; -; mRNA.
DR EMBL; BC150288; AAI50289.1; -; mRNA.
DR EMBL; BC154413; AAI54414.1; -; mRNA.
DR CCDS; CCDS9644.1; -. [Q13023-1]
DR RefSeq; NP_004265.3; NM_004274.4. [Q13023-1]
DR AlphaFoldDB; Q13023; -.
DR BioGRID; 114857; 15.
DR ELM; Q13023; -.
DR IntAct; Q13023; 16.
DR MINT; Q13023; -.
DR STRING; 9606.ENSP00000280979; -.
DR GlyGen; Q13023; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q13023; -.
DR PhosphoSitePlus; Q13023; -.
DR BioMuta; AKAP6; -.
DR DMDM; 116241243; -.
DR EPD; Q13023; -.
DR jPOST; Q13023; -.
DR MassIVE; Q13023; -.
DR MaxQB; Q13023; -.
DR PaxDb; Q13023; -.
DR PeptideAtlas; Q13023; -.
DR PRIDE; Q13023; -.
DR ProteomicsDB; 1788; -.
DR ProteomicsDB; 59109; -. [Q13023-1]
DR Antibodypedia; 23117; 147 antibodies from 29 providers.
DR DNASU; 9472; -.
DR Ensembl; ENST00000280979.9; ENSP00000280979.4; ENSG00000151320.11. [Q13023-1]
DR Ensembl; ENST00000557354.5; ENSP00000450531.1; ENSG00000151320.11. [Q13023-2]
DR GeneID; 9472; -.
DR KEGG; hsa:9472; -.
DR MANE-Select; ENST00000280979.9; ENSP00000280979.4; NM_004274.5; NP_004265.3.
DR UCSC; uc001wrq.4; human. [Q13023-1]
DR CTD; 9472; -.
DR DisGeNET; 9472; -.
DR GeneCards; AKAP6; -.
DR HGNC; HGNC:376; AKAP6.
DR HPA; ENSG00000151320; Tissue enhanced (brain, heart muscle, skeletal muscle, tongue).
DR MIM; 604691; gene.
DR neXtProt; NX_Q13023; -.
DR OpenTargets; ENSG00000151320; -.
DR PharmGKB; PA24670; -.
DR VEuPathDB; HostDB:ENSG00000151320; -.
DR eggNOG; ENOG502QSMH; Eukaryota.
DR GeneTree; ENSGT00810000125473; -.
DR HOGENOM; CLU_231193_0_0_1; -.
DR InParanoid; Q13023; -.
DR OMA; EPQPVMP; -.
DR PhylomeDB; Q13023; -.
DR TreeFam; TF105405; -.
DR PathwayCommons; Q13023; -.
DR SignaLink; Q13023; -.
DR BioGRID-ORCS; 9472; 13 hits in 1076 CRISPR screens.
DR ChiTaRS; AKAP6; human.
DR GeneWiki; AKAP6; -.
DR GenomeRNAi; 9472; -.
DR Pharos; Q13023; Tbio.
DR PRO; PR:Q13023; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q13023; protein.
DR Bgee; ENSG00000151320; Expressed in cortical plate and 149 other tissues.
DR ExpressionAtlas; Q13023; baseline and differential.
DR Genevisible; Q13023; HS.
DR GO; GO:0034704; C:calcium channel complex; IDA:BHF-UCL.
DR GO; GO:0005901; C:caveola; ISS:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; ISS:BHF-UCL.
DR GO; GO:0014704; C:intercalated disc; ISS:BHF-UCL.
DR GO; GO:0014701; C:junctional sarcoplasmic reticulum membrane; ISS:BHF-UCL.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0030315; C:T-tubule; ISS:BHF-UCL.
DR GO; GO:0008179; F:adenylate cyclase binding; ISS:BHF-UCL.
DR GO; GO:0060090; F:molecular adaptor activity; ISS:BHF-UCL.
DR GO; GO:0051018; F:protein kinase A binding; IBA:GO_Central.
DR GO; GO:0034237; F:protein kinase A regulatory subunit binding; ISS:BHF-UCL.
DR GO; GO:0043495; F:protein-membrane adaptor activity; ISS:BHF-UCL.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:BHF-UCL.
DR GO; GO:0001508; P:action potential; IC:BHF-UCL.
DR GO; GO:0019933; P:cAMP-mediated signaling; NAS:BHF-UCL.
DR GO; GO:0071320; P:cellular response to cAMP; IDA:BHF-UCL.
DR GO; GO:0071345; P:cellular response to cytokine stimulus; ISS:BHF-UCL.
DR GO; GO:0070886; P:positive regulation of calcineurin-NFAT signaling cascade; ISS:BHF-UCL.
DR GO; GO:0030307; P:positive regulation of cell growth; ISS:BHF-UCL.
DR GO; GO:0061051; P:positive regulation of cell growth involved in cardiac muscle cell development; ISS:BHF-UCL.
DR GO; GO:1902261; P:positive regulation of delayed rectifier potassium channel activity; IDA:BHF-UCL.
DR GO; GO:1901381; P:positive regulation of potassium ion transmembrane transport; IDA:BHF-UCL.
DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; ISS:BHF-UCL.
DR GO; GO:0060316; P:positive regulation of ryanodine-sensitive calcium-release channel activity; ISS:BHF-UCL.
DR GO; GO:0006605; P:protein targeting; NAS:UniProtKB.
DR GO; GO:0060306; P:regulation of membrane repolarization; IDA:BHF-UCL.
DR GO; GO:0010738; P:regulation of protein kinase A signaling; ISS:BHF-UCL.
DR GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IC:BHF-UCL.
DR CDD; cd00176; SPEC; 1.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR SMART; SM00150; SPEC; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Sarcoplasmic reticulum.
FT CHAIN 1..2319
FT /note="A-kinase anchor protein 6"
FT /id="PRO_0000064530"
FT REPEAT 762..848
FT /note="Spectrin 1"
FT REPEAT 1036..1150
FT /note="Spectrin 2"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 566..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1250..1272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1821..1842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1900..1925
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1963..1983
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2063..2076
FT /note="PKA-RII subunit binding domain"
FT REGION 2198..2319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..507
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..532
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..750
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2198..2222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2246..2261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1073
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WVC7"
FT MOD_RES 1570
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WVC7"
FT MOD_RES 1595
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WVC7"
FT VAR_SEQ 1050..1075
FT /note="KTLGEKIQDTMAGHSGSSPRDLLSPE -> VFAFLLLFVGYVYIFCVVKYSV
FT RFLI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054497"
FT VAR_SEQ 1076..2319
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054498"
FT VARIANT 337
FT /note="A -> V (in dbSNP:rs3742926)"
FT /id="VAR_028171"
FT VARIANT 408
FT /note="N -> S (in dbSNP:rs17099240)"
FT /id="VAR_028172"
FT VARIANT 558
FT /note="N -> D (in dbSNP:rs35210906)"
FT /id="VAR_050653"
FT VARIANT 892
FT /note="E -> K (in dbSNP:rs34572259)"
FT /id="VAR_050654"
FT VARIANT 910
FT /note="K -> M (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035781"
FT VARIANT 1192
FT /note="M -> I (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035782"
FT VARIANT 1492
FT /note="A -> V (in dbSNP:rs11845640)"
FT /evidence="ECO:0000269|PubMed:10413680"
FT /id="VAR_028173"
FT VARIANT 1516
FT /note="T -> A (in dbSNP:rs17099587)"
FT /id="VAR_050655"
FT VARIANT 1522
FT /note="V -> I (in dbSNP:rs34711402)"
FT /id="VAR_050656"
FT VARIANT 1702
FT /note="E -> Q (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035783"
FT VARIANT 1839
FT /note="P -> T (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs745389246)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035784"
FT VARIANT 2035
FT /note="N -> D (in dbSNP:rs1051695)"
FT /id="VAR_028174"
FT VARIANT 2171
FT /note="F -> Y (in dbSNP:rs4647899)"
FT /id="VAR_028175"
FT VARIANT 2209
FT /note="D -> H (in dbSNP:rs4402458)"
FT /id="VAR_028176"
FT VARIANT 2267
FT /note="E -> D (in dbSNP:rs35977369)"
FT /id="VAR_050657"
FT CONFLICT 974
FT /note="W -> C (in Ref. 1; AAA92354)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2319 AA; 256720 MW; 7607B71AD2140727 CRC64;
MLTMSVTLSP LRSQDLDPMA TDASPMAINM TPTVEQGEGE EAMKDMDSDQ QYEKPPPLHT
GADWKIVLHL PEIETWLRMT SERVRDLTYS VQQDSDSKHV DVHLVQLKDI CEDISDHVEQ
IHALLETEFS LKLLSYSVNV IVDIHAVQLL WHQLRVSVLV LRERILQGLQ DANGNYTRQT
DILQAFSEET KEGRLDSLTE VDDSGQLTIK CSQNYLSLDC GITAFELSDY SPSEDLLSGL
GDMTSSQVKT KPFDSWSYSE MEKEFPELIR SVGLLTVAAD SISTNGSEAV TEEVSQVSLS
VDDKGGCEED NASAVEEQPG LTLGVSSSSG EALTNAAQPS SETVQQESSS SSHHDAKNQQ
PVPCENATPK RTIRDCFNYN EDSPTQPTLP KRGLFLKEET FKNDLKGNGG KRQMVDLKPE
MSRSTPSLVD PPDRSKLCLV LQSSYPNSPS AASQSYECLH KVGNGNLENT VKFHIKEISS
SLGRLNDCYK EKSRLKKPHK TSEEVPPCRT PKRGTGSGKQ AKNTKSSAVP NGELSYTSKA
IEGPQTNSAS TSSLEPCNQR SWNAKLQLQS ETSSSPAFTQ SSESSVGSDN IMSPVPLLSK
HKSKKGQASS PSHVTRNGEV VEAWYGSDEY LALPSHLKQT EVLALKLENL TKLLPQKPRG
ETIQNIDDWE LSEMNSDSEI YPTYHVKKKH TRLGRVSPSS SSDIASSLGE SIESGPLSDI
LSDEESSMPL AGMKKYADEK SERASSSEKN ESHSATKSAL IQKLMQDIQH QDNYEAIWEK
IEGFVNKLDE FIQWLNEAME TTENWTPPKA EMDDLKLYLE THLSFKLNVD SHCALKEAVE
EEGHQLLELI ASHKAGLKDM LRMIASQWKE LQRQIKRQHS WILRALDTIK AEILATDVSV
EDEEGTGSPK AEVQLCYLEA QRDAVEQMSL KLYSEQYTSS SKRKEEFADM SKVHSVGSNG
LLDFDSEYQE LWDWLIDMES LVMDSHDLMM SEEQQQHLYK RYSVEMSIRH LKKTELLSKV
EALKKGGVLL PNDLLEKVDS INEKWELLGK TLGEKIQDTM AGHSGSSPRD LLSPESGSLV
RQLEVRIKEL KGWLRDTELF IFNSCLRQEK EGTMNTEKQL QYFKSLCREI KQRRRGVASI
LRLCQHLLDD RETCNLNADH QPMQLIIVNL ERRWEAIVMQ AVQWQTRLQK KMGKESETLN
VIDPGLMDLN GMSEDALEWD EMDISNKLIS LNEESNDLDQ ELQPVIPSLK LGETSNEDPG
YDEEADNHGG SQYASNITAP SSPHIYQVYS LHNVELYEDN HMPFLKNNPK VTGMTQPNVL
TKSLSKDSSF SSTKSLPDLL GGSNLVKPCA CHGGDMSQNS GSESGIVSEG DTETTTNSEM
CLLNAVDGSP SNLETEHLDP QMGDAVNVLK QKFTDEGESI KLPNSSQSSI SPVGCVNGKV
GDLNSITKHT PDCLGEELQG KHDVFTFYDY SYLQGSKLKL PMIMKQSQSE KAHVEDPLLR
GFYFDKKSCK SKHQTTELQP DVPPHERILA SASHEMDRIS YKSGNIEKTF TGMQNAKQLS
LLSHSSSIES LSPGGDLFGL GIFKNGSDSL QRSTSLESWL TSYKSNEDLF SCHSSGDISV
SSGSVGELSK RTLDLLNRLE NIQSPSEQKI KRSVSDITLQ SSSQKMSFTG QMSLDIASSI
NEDSAASLTE LSSSDELSLC SEDIVLHKNK IPESNASFRK RLTRSVADES DVNVSMIVNV
SCTSACTDDE DDSDLLSSST LTLTEEELCI KDEDDDSSIA TDDEIYEDCT LMSGLDYIKN
ELQTWIRPKL SLTRDKKRCN VSDEMKGSKD ISSSEMTNPS DTLNIETLLN GSVKRVSENN
GNGKNSSHTH ELGTKRENKK TIFKVNKDPY VADMENGNIE GIPERQKGKP NVTSKVSENL
GSHGKEISES EHCKCKALMD SLDDSNTAGK EFVSQDVRHL PKKCPNHHHF ENQSTASTPT
EKSFSELALE TRFNNRQDSD ALKSSDDAPS MAGKSAGCCL ALEQNGTEEN ASISNISCCN
CEPDVFHQKD AEDCSVHNFV KEIIDMASTA LKSKSQPENE VAAPTSLTQI KEKVLEHSHR
PIQLRKGDFY SYLSLSSHDS DCGEVTNYIE EKSSTPLPLD TTDSGLDDKE DIECFFEACV
EGDSDGEEPC FSSAPPNESA VPSEAAMPLQ ATACSSEFSD SSLSADDADT VALSSPSSQE
RAEVGKEVNG LPQTSSGCAE NLEFTPSKLD SEKESSGKPG ESGMPEEHNA ASAKSKVQDL
SLKANQPTDK AALHPSPKTL TCEENLLNLH EKRHRNMHR
