CAZA2_HUMAN
ID CAZA2_HUMAN Reviewed; 286 AA.
AC P47755; B4DG50;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=F-actin-capping protein subunit alpha-2;
DE AltName: Full=CapZ alpha-2;
GN Name=CAPZA2;
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).
RC TISSUE=Retina;
RX PubMed=7665558; DOI=10.1074/jbc.270.37.21472;
RA Barron-Casella E.A., Torres M.A., Scherer S.W., Heng H.H.Q., Tsui L.-C.,
RA Casella J.F.;
RT "Sequence analysis and chromosomal localization of human Cap Z. Conserved
RT residues within the actin-binding domain may link Cap Z to gelsolin/severin
RT and profilin protein families.";
RL J. Biol. Chem. 270:21472-21479(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Amygdala;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 3-286 (ISOFORM 1).
RC TISSUE=Pancreas;
RX PubMed=9331217;
RX DOI=10.1002/(sici)1097-0169(1997)38:2<120::aid-cm2>3.0.co;2-b;
RA Hart M.C., Korshunova Y.O., Cooper J.A.;
RT "Vertebrates have conserved capping protein alpha isoforms with specific
RT expression patterns.";
RL Cell Motil. Cytoskeleton 38:120-132(1997).
RN [7]
RP PROTEIN SEQUENCE OF 2-15.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [8]
RP PROTEIN SEQUENCE OF 2-15; 20-66; 122-129 AND 179-210, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma, and Mammary carcinoma;
RA Bienvenut W.V., Calvo F., Matallanas D., Cooper W.N., Kolch W.;
RL Submitted (MAR-2008) to UniProtKB.
RN [9]
RP PROTEIN SEQUENCE OF 20-86; 147-166 AND 179-226, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [10]
RP INTERACTION WITH RCSD1/CAPZIP, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15850461; DOI=10.1042/bj20050387;
RA Eyers C.E., McNeill H., Knebel A., Morrice N., Arthur S.J.C., Cuenda A.,
RA Cohen P.;
RT "The phosphorylation of CapZ-interacting protein (CapZIP) by stress-
RT activated protein kinases triggers its dissociation from CapZ.";
RL Biochem. J. 389:127-135(2005).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP IDENTIFICATION IN THE WASH COMPLEX.
RX PubMed=19922875; DOI=10.1016/j.devcel.2009.09.010;
RA Derivery E., Sousa C., Gautier J.J., Lombard B., Loew D., Gautreau A.;
RT "The Arp2/3 activator WASH controls the fission of endosomes through a
RT large multiprotein complex.";
RL Dev. Cell 17:712-723(2009).
RN [13]
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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND IDENTIFICATION BY MASS
RP 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 [17]
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).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [19]
RP INTERACTION WITH CRACD.
RX PubMed=30361697; DOI=10.1038/s41556-018-0215-z;
RA Jung Y.S., Wang W., Jun S., Zhang J., Srivastava M., Kim M.J., Lien E.M.,
RA Shang J., Chen J., McCrea P.D., Zhang S., Park J.I.;
RT "Deregulation of CRAD-controlled cytoskeleton initiates mucinous colorectal
RT cancer via beta-catenin.";
RL Nat. Cell Biol. 20:1303-1314(2018).
CC -!- FUNCTION: F-actin-capping proteins bind in a Ca(2+)-independent manner
CC to the fast growing ends of actin filaments (barbed end) thereby
CC blocking the exchange of subunits at these ends. Unlike other capping
CC proteins (such as gelsolin and severin), these proteins do not sever
CC actin filaments.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Component of the
CC WASH complex, composed of F-actin-capping protein subunit alpha
CC (CAPZA1, CAPZA2 or CAPZA3), F-actin-capping protein subunit beta
CC (CAPZB), WASH (WASHC1, WASH2P, WASH3P, WASH4P, WASH5P or WASH6P),
CC WASHC2 (WASHC2A or WASHC2C), WASHC3, WASHC4 and WASHC5. Interacts with
CC RCSD1/CAPZIP. Directly interacts with CRACD; this interaction decreases
CC binding to actin (PubMed:30361697). {ECO:0000269|PubMed:15850461,
CC ECO:0000269|PubMed:19922875, ECO:0000269|PubMed:30361697}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P47755-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P47755-2; Sequence=VSP_053871, VSP_053872;
CC -!- SIMILARITY: Belongs to the F-actin-capping protein alpha subunit
CC family. {ECO:0000305}.
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DR EMBL; U03269; AAA88848.1; -; mRNA.
DR EMBL; BT006735; AAP35381.1; -; mRNA.
DR EMBL; AK294409; BAG57661.1; -; mRNA.
DR EMBL; AC002543; AAC60382.1; -; Genomic_DNA.
DR EMBL; BC005338; AAH05338.1; -; mRNA.
DR EMBL; U03851; AAC00534.1; -; mRNA.
DR CCDS; CCDS5768.1; -. [P47755-1]
DR PIR; G01229; G01229.
DR RefSeq; NP_006127.1; NM_006136.2. [P47755-1]
DR AlphaFoldDB; P47755; -.
DR SMR; P47755; -.
DR BioGRID; 107280; 369.
DR IntAct; P47755; 281.
DR MINT; P47755; -.
DR STRING; 9606.ENSP00000354947; -.
DR iPTMnet; P47755; -.
DR MetOSite; P47755; -.
DR PhosphoSitePlus; P47755; -.
DR BioMuta; CAPZA2; -.
DR DMDM; 1345695; -.
DR DOSAC-COBS-2DPAGE; P47755; -.
DR OGP; P47755; -.
DR REPRODUCTION-2DPAGE; P47755; -.
DR EPD; P47755; -.
DR jPOST; P47755; -.
DR MassIVE; P47755; -.
DR MaxQB; P47755; -.
DR PaxDb; P47755; -.
DR PeptideAtlas; P47755; -.
DR PRIDE; P47755; -.
DR ProteomicsDB; 4106; -.
DR ProteomicsDB; 55792; -. [P47755-1]
DR Antibodypedia; 2213; 208 antibodies from 26 providers.
DR DNASU; 830; -.
DR Ensembl; ENST00000361183.8; ENSP00000354947.2; ENSG00000198898.15. [P47755-1]
DR GeneID; 830; -.
DR KEGG; hsa:830; -.
DR MANE-Select; ENST00000361183.8; ENSP00000354947.2; NM_006136.3; NP_006127.1.
DR UCSC; uc003vil.4; human. [P47755-1]
DR CTD; 830; -.
DR DisGeNET; 830; -.
DR GeneCards; CAPZA2; -.
DR HGNC; HGNC:1490; CAPZA2.
DR HPA; ENSG00000198898; Low tissue specificity.
DR MalaCards; CAPZA2; -.
DR MIM; 601571; gene.
DR neXtProt; NX_P47755; -.
DR OpenTargets; ENSG00000198898; -.
DR PharmGKB; PA26071; -.
DR VEuPathDB; HostDB:ENSG00000198898; -.
DR eggNOG; KOG0836; Eukaryota.
DR GeneTree; ENSGT00950000183119; -.
DR HOGENOM; CLU_045161_0_0_1; -.
DR InParanoid; P47755; -.
DR OMA; HVHYYED; -.
DR PhylomeDB; P47755; -.
DR TreeFam; TF314822; -.
DR PathwayCommons; P47755; -.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR Reactome; R-HSA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
DR Reactome; R-HSA-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-HSA-879415; Advanced glycosylation endproduct receptor signaling.
DR Reactome; R-HSA-9662360; Sensory processing of sound by inner hair cells of the cochlea.
DR Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
DR SignaLink; P47755; -.
DR BioGRID-ORCS; 830; 26 hits in 1044 CRISPR screens.
DR ChiTaRS; CAPZA2; human.
DR GeneWiki; CAPZA2; -.
DR GenomeRNAi; 830; -.
DR Pharos; P47755; Tbio.
DR PRO; PR:P47755; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P47755; protein.
DR Bgee; ENSG00000198898; Expressed in jejunal mucosa and 214 other tissues.
DR ExpressionAtlas; P47755; baseline and differential.
DR Genevisible; P47755; HS.
DR GO; GO:0015629; C:actin cytoskeleton; TAS:ProtInc.
DR GO; GO:0005903; C:brush border; IEA:Ensembl.
DR GO; GO:0030863; C:cortical cytoskeleton; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0008290; C:F-actin capping protein complex; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:Ensembl.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0051016; P:barbed-end actin filament capping; IBA:GO_Central.
DR GO; GO:0065003; P:protein-containing complex assembly; TAS:ProtInc.
DR Gene3D; 3.30.1140.60; -; 1.
DR Gene3D; 3.90.1150.210; -; 1.
DR InterPro; IPR002189; CapZ_alpha.
DR InterPro; IPR037282; CapZ_alpha/beta.
DR InterPro; IPR042276; CapZ_alpha/beta_2.
DR InterPro; IPR042489; CapZ_alpha_1.
DR InterPro; IPR017865; F-actin_cap_asu_CS.
DR PANTHER; PTHR10653; PTHR10653; 1.
DR Pfam; PF01267; F-actin_cap_A; 1.
DR PRINTS; PR00191; FACTINCAPA.
DR SUPFAM; SSF90096; SSF90096; 1.
DR PROSITE; PS00748; F_ACTIN_CAPPING_A_1; 1.
DR PROSITE; PS00749; F_ACTIN_CAPPING_A_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin capping; Actin-binding; Alternative splicing;
KW Direct protein sequencing; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801, ECO:0000269|Ref.8,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..286
FT /note="F-actin-capping protein subunit alpha-2"
FT /id="PRO_0000208627"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 143..172
FT /note="VYGKKIDGQQTIIACIESHQFQAKNFWNGR -> EWSLEVRMEVYNHSFNHS
FT SGWHLENSGSLL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_053871"
FT VAR_SEQ 173..286
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_053872"
SQ SEQUENCE 286 AA; 32949 MW; B5E1B617A38E758B CRC64;
MADLEEQLSD EEKVRIAAKF IIHAPPGEFN EVFNDVRLLL NNDNLLREGA AHAFAQYNLD
QFTPVKIEGY EDQVLITEHG DLGNGKFLDP KNRICFKFDH LRKEATDPRP CEVENAVESW
RTSVETALRA YVKEHYPNGV CTVYGKKIDG QQTIIACIES HQFQAKNFWN GRWRSEWKFT
ITPSTTQVVG ILKIQVHYYE DGNVQLVSHK DIQDSLTVSN EVQTAKEFIK IVEAAENEYQ
TAISENYQTM SDTTFKALRR QLPVTRTKID WNKILSYKIG KEMQNA
