ANR28_HUMAN
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 03-AUG-2022, entry version 193.
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 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; 216.
DR CORUM; O15084; -.
DR DIP; DIP-27583N; -.
DR IntAct; O15084; 123.
DR MINT; O15084; -.
DR STRING; 9606.ENSP00000382379; -.
DR ChEMBL; CHEMBL4105921; -.
DR GlyGen; O15084; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O15084; -.
DR PhosphoSitePlus; O15084; -.
DR BioMuta; ANKRD28; -.
DR EPD; O15084; -.
DR jPOST; O15084; -.
DR MassIVE; O15084; -.
DR MaxQB; O15084; -.
DR PaxDb; O15084; -.
DR PeptideAtlas; O15084; -.
DR PRIDE; O15084; -.
DR ProteomicsDB; 48437; -. [O15084-3]
DR ProteomicsDB; 48438; -. [O15084-1]
DR ProteomicsDB; 48439; -. [O15084-2]
DR ProteomicsDB; 48440; -. [O15084-4]
DR Antibodypedia; 26857; 113 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 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; YNGHLEM; -.
DR OrthoDB; 1115202at2759; -.
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; 13 hits in 1083 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 205 other tissues.
DR ExpressionAtlas; O15084; baseline and differential.
DR Genevisible; O15084; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR Gene3D; 1.25.40.20; -; 12.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR Pfam; PF00023; Ank; 3.
DR Pfam; PF12796; Ank_2; 8.
DR Pfam; PF13637; Ank_4; 2.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 28.
DR SUPFAM; SSF48403; SSF48403; 4.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 24.
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
