AKA11_HUMAN
ID AKA11_HUMAN Reviewed; 1901 AA.
AC Q9UKA4; O75124; Q9NUK7;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=A-kinase anchor protein 11;
DE Short=AKAP-11;
DE AltName: Full=A-kinase anchor protein 220 kDa;
DE Short=AKAP 220;
DE Short=hAKAP220;
DE AltName: Full=Protein kinase A-anchoring protein 11;
DE Short=PRKA11;
GN Name=AKAP11; Synonyms=AKAP220, KIAA0629;
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].
RX PubMed=10864471; DOI=10.1006/dbio.2000.9725;
RA Reinton N., Collas P., Haugen T.B., Skalhegg B.S., Hansson V., Jahnsen T.,
RA Tasken K.;
RT "Localization of a novel human A-kinase-anchoring protein, hAKAP220, during
RT spermatogenesis.";
RL Dev. Biol. 223:194-204(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 630-1901.
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1121-1469.
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-422; SER-433; SER-448;
RP THR-1100 AND SER-1337, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448 AND THR-1100, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-433; THR-1100 AND
RP SER-1242, AND 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-444; SER-448;
RP THR-981; THR-1100; SER-1171; SER-1242; THR-1485 AND SER-1580, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [13]
RP IDENTIFICATION BY 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).
CC -!- FUNCTION: Binds to type II regulatory subunits of protein kinase A and
CC anchors/targets them.
CC -!- INTERACTION:
CC Q9UKA4; Q99732: LITAF; NbExp=3; IntAct=EBI-1049491, EBI-725647;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome. Note=Cytoplasmic in premeiotic pachytene
CC spermatocytes and in the centrosome of developing postmeiotic germ
CC cells, while a midpiece/centrosome localization was found in elongating
CC spermatocytes and mature sperm.
CC -!- TISSUE SPECIFICITY: Expressed in heart, brain, lung, liver, kidney,
CC testis and ovary. Weakly expressed in skeletal muscle, pancreas and
CC spleen.
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 -!- SIMILARITY: Belongs to the AKAP110 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA92117.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF176555; AAF07045.1; -; mRNA.
DR EMBL; AL136527; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB014529; BAA31604.2; -; mRNA.
DR EMBL; AK002166; BAA92117.1; ALT_INIT; mRNA.
DR CCDS; CCDS9383.1; -.
DR PIR; T00384; T00384.
DR RefSeq; NP_057332.1; NM_016248.3.
DR RefSeq; XP_011533205.1; XM_011534903.2.
DR RefSeq; XP_011533206.1; XM_011534904.1.
DR RefSeq; XP_011533207.1; XM_011534905.1.
DR RefSeq; XP_011533208.1; XM_011534906.2.
DR RefSeq; XP_016875870.1; XM_017020381.1.
DR AlphaFoldDB; Q9UKA4; -.
DR BioGRID; 116384; 87.
DR IntAct; Q9UKA4; 43.
DR MINT; Q9UKA4; -.
DR STRING; 9606.ENSP00000025301; -.
DR GlyConnect; 999; 1 N-Linked glycan (1 site).
DR GlyGen; Q9UKA4; 20 sites, 1 N-linked glycan (1 site), 2 O-linked glycans (19 sites).
DR iPTMnet; Q9UKA4; -.
DR PhosphoSitePlus; Q9UKA4; -.
DR BioMuta; AKAP11; -.
DR DMDM; 13431310; -.
DR EPD; Q9UKA4; -.
DR jPOST; Q9UKA4; -.
DR MassIVE; Q9UKA4; -.
DR MaxQB; Q9UKA4; -.
DR PaxDb; Q9UKA4; -.
DR PeptideAtlas; Q9UKA4; -.
DR PRIDE; Q9UKA4; -.
DR ProteomicsDB; 84751; -.
DR Antibodypedia; 23478; 59 antibodies from 19 providers.
DR DNASU; 11215; -.
DR Ensembl; ENST00000025301.4; ENSP00000025301.2; ENSG00000023516.9.
DR GeneID; 11215; -.
DR KEGG; hsa:11215; -.
DR MANE-Select; ENST00000025301.4; ENSP00000025301.2; NM_016248.4; NP_057332.1.
DR UCSC; uc001uys.2; human.
DR CTD; 11215; -.
DR DisGeNET; 11215; -.
DR GeneCards; AKAP11; -.
DR HGNC; HGNC:369; AKAP11.
DR HPA; ENSG00000023516; Low tissue specificity.
DR MIM; 604696; gene.
DR neXtProt; NX_Q9UKA4; -.
DR OpenTargets; ENSG00000023516; -.
DR PharmGKB; PA24663; -.
DR VEuPathDB; HostDB:ENSG00000023516; -.
DR eggNOG; ENOG502QRN4; Eukaryota.
DR GeneTree; ENSGT00940000153313; -.
DR HOGENOM; CLU_002178_0_0_1; -.
DR InParanoid; Q9UKA4; -.
DR OMA; KFKFDCP; -.
DR OrthoDB; 43913at2759; -.
DR PhylomeDB; Q9UKA4; -.
DR TreeFam; TF343800; -.
DR PathwayCommons; Q9UKA4; -.
DR SignaLink; Q9UKA4; -.
DR SIGNOR; Q9UKA4; -.
DR BioGRID-ORCS; 11215; 4 hits in 1087 CRISPR screens.
DR ChiTaRS; AKAP11; human.
DR GeneWiki; AKAP11; -.
DR GenomeRNAi; 11215; -.
DR Pharos; Q9UKA4; Tbio.
DR PRO; PR:Q9UKA4; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q9UKA4; protein.
DR Bgee; ENSG00000023516; Expressed in Brodmann (1909) area 46 and 209 other tissues.
DR Genevisible; Q9UKA4; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0051018; F:protein kinase A binding; IBA:GO_Central.
DR GO; GO:0034237; F:protein kinase A regulatory subunit binding; IEA:Ensembl.
DR GO; GO:0008157; F:protein phosphatase 1 binding; TAS:ProtInc.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0035556; P:intracellular signal transduction; TAS:ProtInc.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0036010; P:protein localization to endosome; IEA:Ensembl.
DR GO; GO:0003091; P:renal water homeostasis; IEA:Ensembl.
DR InterPro; IPR008382; SPHK1-interactor_AKAP_110.
DR PANTHER; PTHR10226; PTHR10226; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome.
FT CHAIN 1..1901
FT /note="A-kinase anchor protein 11"
FT /id="PRO_0000064517"
FT REGION 407..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 843..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 971..993
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1131..1153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1650..1663
FT /note="PKA-RII subunit binding domain"
FT REGION 1708..1805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 974..993
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1137..1153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1708..1740
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1753..1769
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 444
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163"
FT MOD_RES 981
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1100
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1171
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1176
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62924"
FT MOD_RES 1177
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62924"
FT MOD_RES 1242
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1337
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1485
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1580
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 721
FT /note="S -> C (in dbSNP:rs2236364)"
FT /id="VAR_020131"
FT VARIANT 1070
FT /note="H -> R (in dbSNP:rs17063163)"
FT /id="VAR_048207"
FT VARIANT 1410
FT /note="L -> F (in dbSNP:rs17063167)"
FT /id="VAR_048208"
FT CONFLICT 1303
FT /note="K -> R (in Ref. 5; BAA92117)"
FT /evidence="ECO:0000305"
FT CONFLICT 1444..1469
FT /note="LDPYRNEVSQLYSFSTSLVHSITKDA -> CGPSVELSPWKWQTRCGREGNS
FT WKRE (in Ref. 5; BAA92117)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1901 AA; 210512 MW; 0893316C46A75672 CRC64;
MATFRNNHMK TKASVRKSFS EDVFQSVKSL LQSQKELCSV TAEDCLQQDE HANLTEVTFL
GFNEETDAAH IQDLAAVSLE LPDILNSLHF CSLNENEIIC MKNINKPLDI SSDPLNQSHP
SGMLCVMRVS PTSPRLRIDF IFSLLSKYAT GIRYTLDTFL HQKHQLETTD EDDDDTNQSV
SSIEDDFVTA FEHLEEEETS KPYNDGMNIT VLRSQCDAAS QTVTGHHLET HDLKILISSG
QQKSLAKPST SSVNVLGHKE LPSVKTSVTT SISEPWTQRS FYRSSNASDK DSDLQKTFFS
SSPAYSSESE CSSPSPVIFL DEEGYQKSLK AKLELPKIPV MKDDIEDSDS EVSEFFDSFD
QFDELEQTLE TCLFNKDPVI GKSSQRKGHK HGKSCMNPQK FKFDRPALPA NVRKPTPRKP
ESPYGNLCDA PDSPRPVKAS REDSGLFSPI RSSAFSPLGG CTPAECFCQT DIGGDRIHEN
HDSVYYTYED YAKSISCEVL GSVLRTHHTN TLSNINSIKH GENKTVTFKH GNLDQKNKSK
NKSLMIKDSI QKFAADLVEK SFGSAFKDLQ KGVSSCTNAL YHLAIKLTSS VLQMAFDELR
RQRAFSLKER AISGLANFLV SEALSNALKD LQYVKKQIFT NTVARFAADL AEELVFEGIM
EVCQFSYPQT PASPQCGSFD FEDKVVKLYA KDLSESVIQE AFIELSQVDV TFTTKAAVSV
STDNIKYVSA ESVVPSTQAV TFSPSFHNQA IMVTKPVQEY KKEYTVQQAL FCTSGIVTSI
PVPLAGSALL PYHISSTACQ AKAHLSSDDS NSNGDSAQVH IATKNREEKA ACLRNICLPS
EHNPGNQNDF KPTNDDIEMQ SSSKLPNDPA IISNFSAAVV HTIVNETLES MTSLEVTKMV
DERTDYLTKS LKEKTPPFSH CDQAVLQCSE ASSNKDMFAD RLSKSIIKHS IDKSKSVIPN
IDKNAVYKES LPVSGEESQL TPEKSPKFPD SQNQLTHCSL SAAKDCVPEC KVSMVHGSSL
ETLPSCPAVT GQKSDLKESA KDQPLKKHNL NSTSLEALSF GQENPFPHSH TFSSTALTCV
DGLHVEDKQK VRDRNVIPDT PPSTPLVPSR ASSEWDIKKL TKKLKGELAK EFAPATPPST
PHNSSVGSLS ENEQNTIEKE EFMLKLMRSL SEEVESSESG ELPEVDVKSE HSGKKVQFAE
ALATHILSLA TEMAASHLDN KIIQEPKVKN PCLNVQSQRS VSPTFLNPSD ENLKTLCNFA
GDLAAEVITE AEKIAKVRNC MLFKQKKNSC YADGDEDYKV EEKLDIEAVV HPREVDPFIL
SLPPSSCMSG LMYKYPSCES VTDEYAGHLI QILKQEGGNS ELIMDQYANR LAYRSVKSGL
QEAAKTTKVQ CNSRMFPVPS SQVKTNKELL MFSNKEHHQE ADKKRQSKRN EGYFCKNQTC
ERTLDPYRNE VSQLYSFSTS LVHSITKDAK EELTASLVGL PKSLTDSCLF EKSGYEEDNE
CHVTPELPKS LQPSSQNHRF YHSTGSLNGY GCGDNVVQAV EQYAKKVVDD TLELTLGSTV
FRVSETTKSA DRVTYAEKLS PLTGQACRYC DLKELHNCTG NSSQHFFRQG SLASSKPASN
PKFSSRYQKS RIFHLSVPQI HVNLDKKAVL AEKIVAEAIE KAERELSSTS LAADSGIGQE
GASFAESLAT ETMTAAVTNV GHAVSSSKEI EDFQSTESVS SQQMNLSIGD DSTGSWSNLS
FEDEHQDESS SFHHLSESNG NSSSWSSLGL EGDLYEDNLS FPTSDSDGPD DKDEEHEDEV
EGLGQDGKTL LITNIDMEPC TVDPQLRIIL QWLIASEAEV AELYFHDSAN KEFMLLSKQL
QEKGWKVGDL LQAVLQYYEV MEKASSEERC KSLFDWLLEN A
