ID   ANR28_HUMAN             Reviewed;        1053 AA.
AC   O15084; B4DES5; Q1WWL4; Q29RW6; Q3B857; Q6ULS0; Q6ZT57;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 5.
DT   27-MAR-2024, entry version 202.
DE   RecName: Full=Serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit A;
DE            Short=PP6-ARS-A;
DE            Short=Serine/threonine-protein phosphatase 6 regulatory subunit ARS-A;
DE   AltName: Full=Ankyrin repeat domain-containing protein 28;
DE   AltName: Full=Phosphatase interactor targeting protein hnRNP K;
DE            Short=PITK;
GN   Name=ANKRD28; Synonyms=KIAA0379;
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 2).
RC   TISSUE=Testis;
RA   Lu L., Huang X.Y., Yin L.L., Xu M., Li J.M., Zhou Z.M., Sha J.H.;
RT   "Cloning a new transcript of KIAA0379 protein in testis.";
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
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 MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 1-767 (ISOFORM 3).
RC   TISSUE=Amygdala, and Cerebellum;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-752 (ISOFORMS 3 AND 4).
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   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PPP1C AND HNRPK,
RP   PHOSPHORYLATION AT SER-1007 AND SER-1011, AND MUTAGENESIS OF
RP   1007-SER--SER-1011.
RX   PubMed=16564677; DOI=10.1016/j.cellsig.2006.01.019;
RA   Kwiek N.C., Thacker D.F., Datto M.B., Megosh H.B., Haystead T.A.J.;
RT   "PITK, a PP1 targeting subunit that modulates the phosphorylation of the
RT   transcriptional regulator hnRNP K.";
RL   Cell. Signal. 18:1769-1778(2006).
RN   [7]
RP   FUNCTION, AND INTERACTION WITH PPP6C; PPP6R1 AND PPP6R3.
RX   PubMed=18186651; DOI=10.1021/bi7022877;
RA   Stefansson B., Ohama T., Daugherty A.E., Brautigan D.L.;
RT   "Protein phosphatase 6 regulatory subunits composed of ankyrin repeat
RT   domains.";
RL   Biochemistry 47:1442-1451(2008).
RN   [8]
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   [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   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   [11]
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   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1011, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=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).
CC   -!- FUNCTION: Putative regulatory subunit of protein phosphatase 6 (PP6)
CC       that may be involved in the recognition of phosphoprotein substrates.
CC       Involved in the PP6-mediated dephosphorylation of NFKBIE opposing its
CC       degradation in response to TNF-alpha. Selectively inhibits the
CC       phosphatase activity of PPP1C. Targets PPP1C to modulate HNRPK
CC       phosphorylation. {ECO:0000269|PubMed:16564677,
CC       ECO:0000269|PubMed:18186651}.
CC   -!- SUBUNIT: Protein phosphatase 6 (PP6) holoenzyme is proposed to be a
CC       heterotrimeric complex formed by the catalytic subunit, a SAPS domain-
CC       containing subunit (PP6R) and an ankyrin repeat-domain containing
CC       regulatory subunit (ARS). Interacts with PPP1C and HNRPK. Interacts
CC       with PPP6C, PPP6R1 and PPP6R3. {ECO:0000269|PubMed:16564677,
CC       ECO:0000269|PubMed:18186651}.
CC   -!- INTERACTION:
CC       O15084; Q14185: DOCK1; NbExp=4; IntAct=EBI-359567, EBI-446740;
CC       O15084; O15371: EIF3D; NbExp=3; IntAct=EBI-359567, EBI-353818;
CC       O15084; Q8TAE8: GADD45GIP1; NbExp=3; IntAct=EBI-359567, EBI-372506;
CC       O15084; Q0VD86: INCA1; NbExp=3; IntAct=EBI-359567, EBI-6509505;
CC       O15084; Q8TDN2: KCNV2; NbExp=3; IntAct=EBI-359567, EBI-12014650;
CC       O15084; Q8IVT4: MGC50722; NbExp=3; IntAct=EBI-359567, EBI-14086479;
CC       O15084; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-359567, EBI-14066006;
CC       O15084; O00743: PPP6C; NbExp=10; IntAct=EBI-359567, EBI-359751;
CC       O15084; Q9UPN7: PPP6R1; NbExp=10; IntAct=EBI-359567, EBI-359745;
CC       O15084; O75170: PPP6R2; NbExp=7; IntAct=EBI-359567, EBI-359739;
CC       O15084; Q5H9R7: PPP6R3; NbExp=5; IntAct=EBI-359567, EBI-355498;
CC       O15084; Q86Y79: PTRH1; NbExp=3; IntAct=EBI-359567, EBI-2602515;
CC       O15084; Q9BT49: THAP7; NbExp=3; IntAct=EBI-359567, EBI-741350;
CC       O15084; Q9H2K2: TNKS2; NbExp=3; IntAct=EBI-359567, EBI-4398527;
CC       O15084; Q96MU7: YTHDC1; NbExp=3; IntAct=EBI-359567, EBI-2849854;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC       {ECO:0000269|PubMed:16564677}. Note=Seems to be excluded from nucleoli.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative promoter usage, Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=O15084-3; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O15084-2; Sequence=VSP_012433;
CC       Name=3;
CC         IsoId=O15084-1; Sequence=VSP_041013;
CC       Name=4;
CC         IsoId=O15084-4; Sequence=VSP_041014;
CC   -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative promoter usage.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAQ72374.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAA20833.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAC86737.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR   EMBL; AY367056; AAQ72374.1; ALT_FRAME; mRNA.
DR   EMBL; AB002377; BAA20833.2; ALT_INIT; mRNA.
DR   EMBL; AK126888; BAC86737.1; ALT_SEQ; mRNA.
DR   EMBL; AK293770; BAG57186.1; -; mRNA.
DR   EMBL; BC106948; AAI06949.2; -; mRNA.
DR   EMBL; BC113868; AAI13869.1; -; mRNA.
DR   EMBL; BC114476; AAI14477.1; -; mRNA.
DR   CCDS; CCDS46769.1; -. [O15084-3]
DR   CCDS; CCDS74908.1; -. [O15084-2]
DR   CCDS; CCDS93222.1; -. [O15084-4]
DR   RefSeq; NP_001182027.1; NM_001195098.1. [O15084-2]
DR   RefSeq; NP_001182028.1; NM_001195099.1. [O15084-2]
DR   RefSeq; NP_056014.2; NM_015199.3. [O15084-3]
DR   RefSeq; XP_005265053.1; XM_005264996.3.
DR   RefSeq; XP_011531842.1; XM_011533540.2.
DR   RefSeq; XP_016861515.1; XM_017006026.1.
DR   RefSeq; XP_016861516.1; XM_017006027.1.
DR   AlphaFoldDB; O15084; -.
DR   SMR; O15084; -.
DR   BioGRID; 116847; 256.
DR   CORUM; O15084; -.
DR   DIP; DIP-27583N; -.
DR   IntAct; O15084; 127.
DR   MINT; O15084; -.
DR   STRING; 9606.ENSP00000382379; -.
DR   ChEMBL; CHEMBL4105921; -.
DR   GlyCosmos; O15084; 1 site, 1 glycan.
DR   GlyGen; O15084; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; O15084; -.
DR   PhosphoSitePlus; O15084; -.
DR   SwissPalm; O15084; -.
DR   BioMuta; ANKRD28; -.
DR   EPD; O15084; -.
DR   jPOST; O15084; -.
DR   MassIVE; O15084; -.
DR   MaxQB; O15084; -.
DR   PaxDb; 9606-ENSP00000382379; -.
DR   PeptideAtlas; O15084; -.
DR   ProteomicsDB; 48437; -. [O15084-3]
DR   ProteomicsDB; 48438; -. [O15084-1]
DR   ProteomicsDB; 48439; -. [O15084-2]
DR   ProteomicsDB; 48440; -. [O15084-4]
DR   Pumba; O15084; -.
DR   Antibodypedia; 26857; 125 antibodies from 22 providers.
DR   DNASU; 23243; -.
DR   Ensembl; ENST00000399451.6; ENSP00000382379.2; ENSG00000206560.12. [O15084-3]
DR   Ensembl; ENST00000412318.5; ENSP00000397341.1; ENSG00000206560.12. [O15084-3]
DR   Ensembl; ENST00000624145.3; ENSP00000485421.1; ENSG00000206560.12. [O15084-2]
DR   Ensembl; ENST00000683139.1; ENSP00000508086.1; ENSG00000206560.12. [O15084-4]
DR   GeneID; 23243; -.
DR   KEGG; hsa:23243; -.
DR   MANE-Select; ENST00000683139.1; ENSP00000508086.1; NM_001349278.2; NP_001336207.1. [O15084-4]
DR   UCSC; uc003cai.2; human. [O15084-3]
DR   AGR; HGNC:29024; -.
DR   CTD; 23243; -.
DR   DisGeNET; 23243; -.
DR   GeneCards; ANKRD28; -.
DR   HGNC; HGNC:29024; ANKRD28.
DR   HPA; ENSG00000206560; Low tissue specificity.
DR   MIM; 611122; gene.
DR   neXtProt; NX_O15084; -.
DR   OpenTargets; ENSG00000206560; -.
DR   PharmGKB; PA134880251; -.
DR   VEuPathDB; HostDB:ENSG00000206560; -.
DR   eggNOG; KOG0504; Eukaryota.
DR   GeneTree; ENSGT00950000182908; -.
DR   HOGENOM; CLU_000134_58_0_1; -.
DR   InParanoid; O15084; -.
DR   OMA; AEHSSYC; -.
DR   OrthoDB; 5474520at2759; -.
DR   TreeFam; TF312824; -.
DR   PathwayCommons; O15084; -.
DR   Reactome; R-HSA-171319; Telomere Extension By Telomerase.
DR   Reactome; R-HSA-204005; COPII-mediated vesicle transport.
DR   SignaLink; O15084; -.
DR   SIGNOR; O15084; -.
DR   BioGRID-ORCS; 23243; 15 hits in 1159 CRISPR screens.
DR   ChiTaRS; ANKRD28; human.
DR   GenomeRNAi; 23243; -.
DR   Pharos; O15084; Tbio.
DR   PRO; PR:O15084; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; O15084; Protein.
DR   Bgee; ENSG00000206560; Expressed in corpus epididymis and 207 other cell types or tissues.
DR   ExpressionAtlas; O15084; baseline and differential.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 12.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   PANTHER; PTHR24173; ANKYRIN REPEAT CONTAINING; 1.
DR   PANTHER; PTHR24173:SF74; UVEAL AUTOANTIGEN WITH COILED-COIL DOMAINS AND ANKYRIN REPEATS; 1.
DR   Pfam; PF00023; Ank; 3.
DR   Pfam; PF12796; Ank_2; 8.
DR   Pfam; PF13637; Ank_4; 1.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 28.
DR   SUPFAM; SSF48403; Ankyrin repeat; 4.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 24.
DR   Genevisible; O15084; HS.
PE   1: Evidence at protein level;
KW   Alternative promoter usage; Alternative splicing; ANK repeat; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           1..1053
FT                   /note="Serine/threonine-protein phosphatase 6 regulatory
FT                   ankyrin repeat subunit A"
FT                   /id="PRO_0000066919"
FT   REPEAT          40..69
FT                   /note="ANK 1"
FT   REPEAT          73..102
FT                   /note="ANK 2"
FT   REPEAT          106..135
FT                   /note="ANK 3"
FT   REPEAT          139..168
FT                   /note="ANK 4"
FT   REPEAT          172..201
FT                   /note="ANK 5"
FT   REPEAT          205..234
FT                   /note="ANK 6"
FT   REPEAT          238..267
FT                   /note="ANK 7"
FT   REPEAT          271..301
FT                   /note="ANK 8"
FT   REPEAT          305..334
FT                   /note="ANK 9"
FT   REPEAT          338..367
FT                   /note="ANK 10"
FT   REPEAT          371..400
FT                   /note="ANK 11"
FT   REPEAT          404..433
FT                   /note="ANK 12"
FT   REPEAT          437..466
FT                   /note="ANK 13"
FT   REPEAT          470..500
FT                   /note="ANK 14"
FT   REPEAT          504..534
FT                   /note="ANK 15"
FT   REPEAT          549..578
FT                   /note="ANK 16"
FT   REPEAT          582..611
FT                   /note="ANK 17"
FT   REPEAT          616..645
FT                   /note="ANK 18"
FT   REPEAT          652..681
FT                   /note="ANK 19"
FT   REPEAT          685..714
FT                   /note="ANK 20"
FT   REPEAT          718..747
FT                   /note="ANK 21"
FT   REPEAT          755..784
FT                   /note="ANK 22"
FT   REPEAT          787..817
FT                   /note="ANK 23"
FT   REPEAT          822..851
FT                   /note="ANK 24"
FT   REPEAT          855..885
FT                   /note="ANK 25"
FT   REPEAT          889..918
FT                   /note="ANK 26"
FT   REPEAT          925..954
FT                   /note="ANK 27"
FT   MOD_RES         1007
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:16564677"
FT   MOD_RES         1011
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:16564677,
FT                   ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         1..154
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.1"
FT                   /id="VSP_012433"
FT   VAR_SEQ         1..9
FT                   /note="MAFLKLRDQ -> MSRVCIVVLEEVEDESPAFISKLPQENKSLHSPPSGNVL
FT                   VRY (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_041013"
FT   VAR_SEQ         1..9
FT                   /note="MAFLKLRDQ -> MSRVCIVVLEEVEDESPAFISKLPQENKSLHSPPSGNVL
FT                   (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_041014"
FT   MUTAGEN         1007..1011
FT                   /note="SKTVS->AKTVA: Marked decrease in phosphorylation.
FT                   Increased PPP1C-binding. No effect on HNRPK-binding."
FT                   /evidence="ECO:0000269|PubMed:16564677"
FT   CONFLICT        293
FT                   /note="V -> A (in Ref. 1; AAQ72374)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        500
FT                   /note="I -> V (in Ref. 1; AAQ72374 and 4; BAC86737)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1053 AA;  112966 MW;  BDB4855193364585 CRC64;
     MAFLKLRDQP SLVQAIFNGD PDEVRALIFK KEDVNFQDNE KRTPLHAAAY LGDAEIIELL
     ILSGARVNAK DSKWLTPLHR AVASCSEEAV QVLLKHSADV NARDKNWQTP LHIAAANKAV
     KCAEALVPLL SNVNVSDRAG RTALHHAAFS GHGEMVKLLL SRGANINAFD KKDRRAIHWA
     AYMGHIEVVK LLVSHGAEVT CKDKKSYTPL HAAASSGMIS VVKYLLDLGV DMNEPNAYGN
     TPLHVACYNG QDVVVNELID CGAIVNQKNE KGFTPLHFAA ASTHGALCLE LLVGNGADVN
     MKSKDGKTPL HMTALHGRFS RSQTIIQSGA VIDCEDKNGN TPLHIAARYG HELLINTLIT
     SGADTAKRGI HGMFPLHLAA LSGFSDCCRK LLSSGFDIDT PDDFGRTCLH AAAAGGNLEC
     LNLLLNTGAD FNKKDKFGRS PLHYAAANCN YQCLFALVGS GASVNDLDER GCTPLHYAAT
     SDTDGKCLEY LLRNDANPGI RDKQGYNAVH YSAAYGHRLC LQLIASETPL DVLMETSGTD
     MLSDSDNRAT ISPLHLAAYH GHHQALEVLV QSLLDLDVRN SSGRTPLDLA AFKGHVECVD
     VLINQGASIL VKDYILKRTP IHAAATNGHS ECLRLLIGNA EPQNAVDIQD GNGQTPLMLS
     VLNGHTDCVY SLLNKGANVD AKDKWGRTAL HRGAVTGHEE CVDALLQHGA KCLLRDSRGR
     TPIHLSAACG HIGVLGALLQ SAASMDANPA TADNHGYTAL HWACYNGHET CVELLLEQEV
     FQKTEGNAFS PLHCAVINDN EGAAEMLIDT LGASIVNATD SKGRTPLHAA AFTDHVECLQ
     LLLSHNAQVN SVDSTGKTPL MMAAENGQTN TVEMLVSSAS AELTLQDNSK NTALHLACSK
     GHETSALLIL EKITDRNLIN ATNAALQTPL HVAARNGLTM VVQELLGKGA SVLAVDENGY
     TPALACAPNK DVADCLALIL ATMMPVSSSS PLSSLTFNAI NRYTNTSKTV SFEALPIMRN
     EPSSYCSFNN IGGEQEYLYT DVDELNDSDS ETY
//