UACA_HUMAN
ID UACA_HUMAN Reviewed; 1416 AA.
AC Q9BZF9; G3XAG2; Q14DD3; Q8N3B8; Q96NH6; Q9HCL1; Q9NWC6;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Uveal autoantigen with coiled-coil domains and ankyrin repeats;
GN Name=UACA; Synonyms=KIAA1561;
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 TISSUE SPECIFICITY.
RX PubMed=11162650; DOI=10.1006/bbrc.2001.4189;
RA Yamada K., Senju S., Nakatsura T., Murata Y., Ishihara M., Nakamura S.,
RA Ohno S., Negi A., Nishimura Y.;
RT "Identification of a novel autoantigen UACA in patients with panuveitis.";
RL Biochem. Biophys. Res. Commun. 280:1169-1176(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:273-281(2000).
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=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [LARGE SCALE MRNA] OF 646-1187 (ISOFORM 1/2), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-634 (ISOFORM 2).
RC TISSUE=Brain, and Embryo;
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1181-1416 (ISOFORM 1/2).
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [9]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=15358194; DOI=10.1016/j.bbrc.2004.06.162;
RA Ohkura T., Taniguchi S., Yamada K., Nishio N., Okamura T., Yoshida A.,
RA Kamijou K., Fukata S., Kuma K., Inoue Y., Hisatome I., Senju S.,
RA Nishimura Y., Shigemasa C.;
RT "Detection of the novel autoantibody (anti-UACA antibody) in patients with
RT Graves' disease.";
RL Biochem. Biophys. Res. Commun. 321:432-440(2004).
RN [10]
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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1035, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
CC -!- FUNCTION: Regulates APAF1 expression and plays an important role in the
CC regulation of stress-induced apoptosis. Promotes apoptosis by
CC regulating three pathways, apoptosome up-regulation, LGALS3/galectin-3
CC down-regulation and NF-kappa-B inactivation. Regulates the
CC redistribution of APAF1 into the nucleus after proapoptotic stress.
CC Down-regulates the expression of LGALS3 by inhibiting NFKB1 (By
CC similarity). {ECO:0000250}.
CC -!- FUNCTION: Modulates isoactin dynamics to regulate the morphological
CC alterations required for cell growth and motility. Interaction with
CC ARF6 may modulate cell shape and motility after injury. May be involved
CC in multiple neurite formation (By similarity).
CC {ECO:0000250|UniProtKB:Q8CGB3, ECO:0000250|UniProtKB:Q8HYY4}.
CC -!- SUBUNIT: Component of the apoptosome complex, composed of APAF1, pro-
CC caspase-9 and UACA. In the complex, it probably interacts directly with
CC APAF1. Interacts with LGALS3, ARF6 and ACTB. Interacts with RAB39A (By
CC similarity). {ECO:0000250|UniProtKB:Q8CGB3,
CC ECO:0000250|UniProtKB:Q8HYY4}.
CC -!- INTERACTION:
CC Q9BZF9; O43865: AHCYL1; NbExp=3; IntAct=EBI-350510, EBI-2371423;
CC Q9BZF9; Q86Z20: CCDC125; NbExp=3; IntAct=EBI-350510, EBI-11977221;
CC Q9BZF9; Q9NWT6: HIF1AN; NbExp=2; IntAct=EBI-350510, EBI-745632;
CC Q9BZF9; Q15323: KRT31; NbExp=3; IntAct=EBI-350510, EBI-948001;
CC Q9BZF9; Q6A162: KRT40; NbExp=3; IntAct=EBI-350510, EBI-10171697;
CC Q9BZF9; P31321: PRKAR1B; NbExp=3; IntAct=EBI-350510, EBI-2805516;
CC Q9BZF9; Q5QGT7: RTP2; NbExp=3; IntAct=EBI-350510, EBI-10244780;
CC Q9BZF9; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-350510, EBI-947187;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15358194}. Cytoplasm
CC {ECO:0000269|PubMed:15358194}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:15358194}. Note=Expressed diffusely in cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BZF9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BZF9-2; Sequence=VSP_047199;
CC -!- TISSUE SPECIFICITY: Highly expressed in skeletal muscle, heart, kidney
CC and pancreas. Expressed in choroid, retina and epidermal melanocytes.
CC Expressed in eye muscles and thyroid follicular cells.
CC {ECO:0000269|PubMed:11162650, ECO:0000269|PubMed:15358194}.
CC -!- INDUCTION: Up-regulated after TSH stimulation.
CC {ECO:0000269|PubMed:15358194}.
CC -!- MISCELLANEOUS: UACA is a possible target autoantigen in Vogt-Koyanagi-
CC Harada (VKH), Behcet disease (BD) and sarcoidosis that cause different
CC types of panuevitis.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91457.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF322916; AAG49577.1; -; mRNA.
DR EMBL; AB046781; BAB13387.2; -; mRNA.
DR EMBL; AC009269; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC087699; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471082; EAW77855.1; -; Genomic_DNA.
DR EMBL; BC113407; AAI13408.1; -; mRNA.
DR EMBL; BC113409; AAI13410.1; -; mRNA.
DR EMBL; AK000990; BAA91457.1; ALT_INIT; mRNA.
DR EMBL; AK055435; BAB70922.1; -; mRNA.
DR EMBL; AL834464; CAD39123.1; -; mRNA.
DR CCDS; CCDS10235.1; -. [Q9BZF9-1]
DR CCDS; CCDS32280.1; -. [Q9BZF9-2]
DR RefSeq; NP_001008225.1; NM_001008224.1. [Q9BZF9-2]
DR RefSeq; NP_060473.2; NM_018003.2. [Q9BZF9-1]
DR AlphaFoldDB; Q9BZF9; -.
DR SMR; Q9BZF9; -.
DR BioGRID; 120392; 129.
DR DIP; DIP-33117N; -.
DR IntAct; Q9BZF9; 69.
DR MINT; Q9BZF9; -.
DR STRING; 9606.ENSP00000314556; -.
DR GlyGen; Q9BZF9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BZF9; -.
DR PhosphoSitePlus; Q9BZF9; -.
DR BioMuta; UACA; -.
DR DMDM; 91207950; -.
DR EPD; Q9BZF9; -.
DR jPOST; Q9BZF9; -.
DR MassIVE; Q9BZF9; -.
DR MaxQB; Q9BZF9; -.
DR PaxDb; Q9BZF9; -.
DR PeptideAtlas; Q9BZF9; -.
DR PRIDE; Q9BZF9; -.
DR ProteomicsDB; 33739; -.
DR ProteomicsDB; 77515; -.
DR ProteomicsDB; 79836; -. [Q9BZF9-1]
DR Antibodypedia; 26467; 314 antibodies from 26 providers.
DR DNASU; 55075; -.
DR Ensembl; ENST00000322954.11; ENSP00000314556.6; ENSG00000137831.15. [Q9BZF9-1]
DR Ensembl; ENST00000379983.6; ENSP00000369319.2; ENSG00000137831.15. [Q9BZF9-2]
DR GeneID; 55075; -.
DR KEGG; hsa:55075; -.
DR MANE-Select; ENST00000322954.11; ENSP00000314556.6; NM_018003.4; NP_060473.2.
DR UCSC; uc002asq.4; human. [Q9BZF9-1]
DR CTD; 55075; -.
DR DisGeNET; 55075; -.
DR GeneCards; UACA; -.
DR HGNC; HGNC:15947; UACA.
DR HPA; ENSG00000137831; Tissue enhanced (skeletal).
DR MIM; 612516; gene.
DR neXtProt; NX_Q9BZF9; -.
DR OpenTargets; ENSG00000137831; -.
DR PharmGKB; PA38062; -.
DR VEuPathDB; HostDB:ENSG00000137831; -.
DR eggNOG; ENOG502QPYN; Eukaryota.
DR GeneTree; ENSGT00940000157475; -.
DR HOGENOM; CLU_005323_1_0_1; -.
DR InParanoid; Q9BZF9; -.
DR OMA; NQMKAEY; -.
DR OrthoDB; 876605at2759; -.
DR PhylomeDB; Q9BZF9; -.
DR TreeFam; TF331274; -.
DR PathwayCommons; Q9BZF9; -.
DR Reactome; R-HSA-9013407; RHOH GTPase cycle.
DR Reactome; R-HSA-9627069; Regulation of the apoptosome activity.
DR SignaLink; Q9BZF9; -.
DR BioGRID-ORCS; 55075; 14 hits in 1079 CRISPR screens.
DR ChiTaRS; UACA; human.
DR GeneWiki; UACA; -.
DR GenomeRNAi; 55075; -.
DR Pharos; Q9BZF9; Tbio.
DR PRO; PR:Q9BZF9; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q9BZF9; protein.
DR Bgee; ENSG00000137831; Expressed in calcaneal tendon and 188 other tissues.
DR ExpressionAtlas; Q9BZF9; baseline and differential.
DR Genevisible; Q9BZF9; HS.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0097190; P:apoptotic signaling pathway; IEA:InterPro.
DR GO; GO:1901223; P:negative regulation of NIK/NF-kappaB signaling; IBA:GO_Central.
DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
DR Gene3D; 1.25.40.20; -; 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR000727; T_SNARE_dom.
DR InterPro; IPR030227; UACA.
DR PANTHER; PTHR24173:SF23; PTHR24173:SF23; 1.
DR Pfam; PF12796; Ank_2; 2.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 6.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 5.
DR PROSITE; PS50192; T_SNARE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ANK repeat; Coiled coil; Cytoplasm;
KW Cytoskeleton; Isopeptide bond; Nucleus; Reference proteome; Repeat;
KW Ubl conjugation.
FT CHAIN 1..1416
FT /note="Uveal autoantigen with coiled-coil domains and
FT ankyrin repeats"
FT /id="PRO_0000231650"
FT REPEAT 38..66
FT /note="ANK 1"
FT REPEAT 67..96
FT /note="ANK 2"
FT REPEAT 100..129
FT /note="ANK 3"
FT REPEAT 133..162
FT /note="ANK 4"
FT REPEAT 166..195
FT /note="ANK 5"
FT REPEAT 199..228
FT /note="ANK 6"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 286..374
FT /evidence="ECO:0000255"
FT COILED 438..1386
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CROSSLNK 1035
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447"
FT VAR_SEQ 1..26
FT /note="MKSLKSRLRRQDVPGPASSGAAAASA -> MMNCWFSCTPKNR (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047199"
FT VARIANT 814
FT /note="I -> T (in dbSNP:rs3743315)"
FT /id="VAR_048313"
FT CONFLICT 139..141
FT /note="HDA -> QKK (in Ref. 1; AAG49577)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="D -> K (in Ref. 1; AAG49577)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1416 AA; 162505 MW; 92C1104445FB0009 CRC64;
MKSLKSRLRR QDVPGPASSG AAAASAHAAD WNKYDDRLMK AAERGDVEKV TSILAKKGVN
PGKLDVEGRS VFHVVTSKGN LECLNAILIH GVDITTSDTA GRNALHLAAK YGHALCLQKL
LQYNCPTEHA DLQGRTALHD AAMADCPSSI QLLCDHGASV NAKDVDGRTP LVLATQMSRP
TICQLLIDRG ADVNSRDKQN RTALMLGCEY GCRDAVEVLI KNGADISLLD ALGHDSSYYA
RIGDNLDILT LLKTASENTN KGRELWKKGP SLQQRNLTHM QDEVNVKSHQ REHQNIQDLE
IENEDLKERL RKIQQEQRIL LDKVNGLQLQ LNEEVMVADD LESEREKLKS LLAAKEKQHE
ESLRTIEALK NRFKYFESDH LGSGSHFSNR KEDMLLKQGQ MYMADSQCTS PGIPAHMQSR
SMLRPLELSL PSQTSYSENE ILKKELEAMR TFCESAKQDR LKLQNELAHK VAECKALALE
CERVKEDSDE QIKQLEDALK DVQKRMYESE GKVKQMQTHF LALKEHLTSE AASGNHRLTE
ELKDQLKDLK VKYEGASAEV GKLRNQIKQN EMIVEEFKRD EGKLIEENKR LQKELSMCEM
EREKKGRKVT EMEGQAKELS AKLALSIPAE KFENMKSSLS NEVNEKAKKL VEMEREHEKS
LSEIRQLKRE LENVKAKLAQ HVKPEEHEQV KSRLEQKSGE LGKKITELTL KNQTLQKEIE
KVYLDNKLLK EQAHNLTIEM KNHYVPLKVS EDMKKSHDAI IDDLNRKLLD VTQKYTEKKL
EMEKLLLEND SLSKDVSRLE TVFVPPEKHE KEIIALKSNI VELKKQLSEL KKKCGEDQEK
IHALTSENTN LKKMMSNQYV PVKTHEEVKM TLNDTLAKTN RELLDVKKKF EDINQEFVKI
KDKNEILKRN LENTQNQIKA EYISLAEHEA KMSSLSQSMR KVQDSNAEIL ANYRKGQEEI
VTLHAEIKAQ KKELDTIQEC IKVKYAPIVS FEECERKFKA TEKELKDQLS EQTQKYSVSE
EEVKKNKQEN DKLKKEIFTL QKDLRDKTVL IEKSHEMERA LSRKTDELNK QLKDLSQKYT
EVKNVKEKLV EENAKQTSEI LAVQNLLQKQ HVPLEQVEAL KKSLNGTIEN LKEELKSMQR
CYEKEQQTVT KLHQLLENQK NSSVPLAEHL QIKEAFEKEV GIIKASLREK EEESQNKMEE
VSKLQSEVQN TKQALKKLET REVVDLSKYK ATKSDLETQI SSLNEKLANL NRKYEEVCEE
VLHAKKKEIS AKDEKELLHF SIEQEIKDQK ERCDKSLTTI TELQRRIQES AKQIEAKDNK
ITELLNDVER LKQALNGLSQ LTYTSGNPTK RQSQLIDTLQ HQVKSLEQQL ADADRQHQEV
IAIYRTHLLS AAQGHMDEDV QEALLQIIQM RQGLVC
