CNDD3_HUMAN
ID CNDD3_HUMAN Reviewed; 1498 AA.
AC P42695; A6NFS2; Q4KMQ9;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Condensin-2 complex subunit D3;
DE AltName: Full=Non-SMC condensin II complex subunit D3;
DE Short=hCAP-D3;
GN Name=NCAPD3 {ECO:0000303|PubMed:27737959, ECO:0000312|HGNC:HGNC:28952};
GN Synonyms=CAPD3, KIAA0056;
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 [LARGE SCALE MRNA].
RC TISSUE=Bone marrow;
RX PubMed=7584044; DOI=10.1093/dnares/1.5.223;
RA Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N.,
RA Kawarabayasi Y., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. II. The
RT coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 1:223-229(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1162-1498.
RC TISSUE=Brain;
RA Yu W., Gibbs R.A.;
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=14532007; DOI=10.1016/s0092-8674(03)00724-4;
RA Ono T., Losada A., Hirano M., Myers M.P., Neuwald A.F., Hirano T.;
RT "Differential contributions of condensin I and condensin II to mitotic
RT chromosome architecture in vertebrate cells.";
RL Cell 115:109-121(2003).
RN [7]
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1329; THR-1331; SER-1348;
RP SER-1357 AND SER-1384, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1384, AND IDENTIFICATION BY
RP 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-567; THR-1379; SER-1382 AND
RP SER-1384, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1384, 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1348; SER-1357; SER-1372 AND
RP SER-1384, AND 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 [16]
RP INTERACTION WITH BRD4.
RX PubMed=23728299; DOI=10.1038/nature12147;
RA Floyd S.R., Pacold M.E., Huang Q., Clarke S.M., Lam F.C., Cannell I.G.,
RA Bryson B.D., Rameseder J., Lee M.J., Blake E.J., Fydrych A., Ho R.,
RA Greenberger B.A., Chen G.C., Maffa A., Del Rosario A.M., Root D.E.,
RA Carpenter A.E., Hahn W.C., Sabatini D.M., Chen C.C., White F.M.,
RA Bradner J.E., Yaffe M.B.;
RT "The bromodomain protein Brd4 insulates chromatin from DNA damage
RT signalling.";
RL Nature 498:246-250(2013).
RN [17]
RP INVOLVEMENT IN MCPH22, VARIANT MCPH22 ALA-1153, CHARACTERIZATION OF VARIANT
RP MCPH22 ALA-1153, AND FUNCTION.
RX PubMed=27737959; DOI=10.1101/gad.286351.116;
RG Deciphering Developmental Disorders Study;
RA Martin C.A., Murray J.E., Carroll P., Leitch A., Mackenzie K.J.,
RA Halachev M., Fetit A.E., Keith C., Bicknell L.S., Fluteau A., Gautier P.,
RA Hall E.A., Joss S., Soares G., Silva J., Bober M.B., Duker A., Wise C.A.,
RA Quigley A.J., Phadke S.R., Wood A.J., Vagnarelli P., Jackson A.P.;
RT "Mutations in genes encoding condensin complex proteins cause microcephaly
RT through decatenation failure at mitosis.";
RL Genes Dev. 30:2158-2172(2016).
CC -!- FUNCTION: Regulatory subunit of the condensin-2 complex, a complex
CC which establishes mitotic chromosome architecture and is involved in
CC physical rigidity of the chromatid axis (PubMed:14532007). May promote
CC the resolution of double-strand DNA catenanes (intertwines) between
CC sister chromatids. Condensin-mediated compaction likely increases
CC tension in catenated sister chromatids, providing directionality for
CC type II topoisomerase-mediated strand exchanges toward chromatid
CC decatenation. Specifically required for decatenation of centromeric
CC ultrafine DNA bridges during anaphase. Early in neurogenesis, may play
CC an essential role to ensure accurate mitotic chromosome condensation in
CC neuron stem cells, ultimately affecting neuron pool and cortex size
CC (PubMed:27737959). {ECO:0000269|PubMed:14532007,
CC ECO:0000269|PubMed:27737959}.
CC -!- SUBUNIT: Component of the condensin-2 complex, which contains the SMC2
CC and SMC4 heterodimer, and 3 non SMC subunits that probably regulate the
CC complex: NCAPH2, NCAPD3 and NCAPG2. Interacts with BRD4 (isoform B),
CC leading to insulate chromatin from DNA damage response pathway.
CC {ECO:0000269|PubMed:14532007, ECO:0000269|PubMed:23728299}.
CC -!- INTERACTION:
CC P42695; P07814: EPRS1; NbExp=4; IntAct=EBI-722805, EBI-355315;
CC P42695; P04406: GAPDH; NbExp=2; IntAct=EBI-722805, EBI-354056;
CC P42695; Q6IBW4: NCAPH2; NbExp=3; IntAct=EBI-722805, EBI-2548296;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14532007}.
CC -!- DISEASE: Microcephaly 22, primary, autosomal recessive (MCPH22)
CC [MIM:617984]: A form of microcephaly, a disease defined as a head
CC circumference more than 3 standard deviations below the age, sex and
CC ethnically matched mean. Brain weight is markedly reduced and the
CC cerebral cortex is disproportionately small.
CC {ECO:0000269|PubMed:27737959}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
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DR EMBL; D29954; BAA06224.1; -; mRNA.
DR EMBL; AP001775; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471065; EAW67824.1; -; Genomic_DNA.
DR EMBL; BC098398; AAH98398.1; -; mRNA.
DR EMBL; AF070553; AAC28639.1; -; mRNA.
DR CCDS; CCDS31723.1; -.
DR RefSeq; NP_056076.1; NM_015261.2.
DR AlphaFoldDB; P42695; -.
DR BioGRID; 116902; 139.
DR ComplexPortal; CPX-985; Condensin II complex.
DR CORUM; P42695; -.
DR DIP; DIP-43903N; -.
DR IntAct; P42695; 216.
DR MINT; P42695; -.
DR STRING; 9606.ENSP00000433681; -.
DR iPTMnet; P42695; -.
DR PhosphoSitePlus; P42695; -.
DR SwissPalm; P42695; -.
DR BioMuta; NCAPD3; -.
DR DMDM; 82654946; -.
DR EPD; P42695; -.
DR jPOST; P42695; -.
DR MassIVE; P42695; -.
DR MaxQB; P42695; -.
DR PaxDb; P42695; -.
DR PeptideAtlas; P42695; -.
DR PRIDE; P42695; -.
DR ProteomicsDB; 55540; -.
DR Antibodypedia; 33156; 187 antibodies from 30 providers.
DR DNASU; 23310; -.
DR Ensembl; ENST00000534548.7; ENSP00000433681.3; ENSG00000151503.14.
DR Ensembl; ENST00000685324.1; ENSP00000508707.1; ENSG00000151503.14.
DR Ensembl; ENST00000688672.1; ENSP00000510391.1; ENSG00000151503.14.
DR GeneID; 23310; -.
DR KEGG; hsa:23310; -.
DR MANE-Select; ENST00000534548.7; ENSP00000433681.3; NM_015261.3; NP_056076.1.
DR UCSC; uc001qhd.2; human.
DR CTD; 23310; -.
DR DisGeNET; 23310; -.
DR GeneCards; NCAPD3; -.
DR HGNC; HGNC:28952; NCAPD3.
DR HPA; ENSG00000151503; Tissue enriched (prostate).
DR MalaCards; NCAPD3; -.
DR MIM; 609276; gene.
DR MIM; 617984; phenotype.
DR MIM; 617985; phenotype.
DR neXtProt; NX_P42695; -.
DR OpenTargets; ENSG00000151503; -.
DR Orphanet; 2512; Autosomal recessive primary microcephaly.
DR PharmGKB; PA162397090; -.
DR VEuPathDB; HostDB:ENSG00000151503; -.
DR eggNOG; KOG0413; Eukaryota.
DR GeneTree; ENSGT00940000153566; -.
DR InParanoid; P42695; -.
DR OMA; RIHPNIC; -.
DR OrthoDB; 60751at2759; -.
DR PhylomeDB; P42695; -.
DR TreeFam; TF101162; -.
DR PathwayCommons; P42695; -.
DR Reactome; R-HSA-2299718; Condensation of Prophase Chromosomes.
DR SignaLink; P42695; -.
DR SIGNOR; P42695; -.
DR BioGRID-ORCS; 23310; 594 hits in 1085 CRISPR screens.
DR ChiTaRS; NCAPD3; human.
DR GeneWiki; NCAPD3; -.
DR GenomeRNAi; 23310; -.
DR Pharos; P42695; Tbio.
DR PRO; PR:P42695; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P42695; protein.
DR Bgee; ENSG00000151503; Expressed in sural nerve and 146 other tissues.
DR ExpressionAtlas; P42695; baseline and differential.
DR Genevisible; P42695; HS.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; IBA:GO_Central.
DR GO; GO:0000796; C:condensin complex; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005721; C:pericentric heterochromatin; IDA:BHF-UCL.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0010032; P:meiotic chromosome condensation; IBA:GO_Central.
DR GO; GO:0007076; P:mitotic chromosome condensation; IDA:UniProtKB.
DR Gene3D; 1.25.10.10; -; 3.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR026971; CND1/NCAPD3.
DR InterPro; IPR032682; Cnd1_C.
DR InterPro; IPR012371; NCAPD3.
DR PANTHER; PTHR14222; PTHR14222; 1.
DR Pfam; PF12717; Cnd1; 1.
DR PIRSF; PIRSF036508; Condns_HCP-6; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Coiled coil; Disease variant; DNA condensation;
KW Mitosis; Nucleus; Phosphoprotein; Primary microcephaly; Reference proteome;
KW Repeat.
FT CHAIN 1..1498
FT /note="Condensin-2 complex subunit D3"
FT /id="PRO_0000050716"
FT REPEAT 441..475
FT /note="HEAT 1"
FT REPEAT 537..572
FT /note="HEAT 2"
FT REPEAT 579..610
FT /note="HEAT 3"
FT REPEAT 973..1009
FT /note="HEAT 4"
FT REGION 155..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 889..911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1306..1339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1429..1498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1219..1275
FT /evidence="ECO:0000255"
FT COMPBIAS 155..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 889..906
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 567
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1329
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1331
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1348
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1357
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1372
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1379
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1382
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1384
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT VARIANT 622
FT /note="R -> Q (in dbSNP:rs12292394)"
FT /id="VAR_053043"
FT VARIANT 907
FT /note="P -> T (in dbSNP:rs34739733)"
FT /id="VAR_053044"
FT VARIANT 1034
FT /note="S -> R (in dbSNP:rs7927108)"
FT /id="VAR_053045"
FT VARIANT 1153
FT /note="E -> A (in MCPH22; impairs mitotic chromosome
FT compaction; dbSNP:rs1350194762)"
FT /evidence="ECO:0000269|PubMed:27737959"
FT /id="VAR_080955"
SQ SEQUENCE 1498 AA; 168891 MW; 038033DA393E4310 CRC64;
MVALRGLGSG LQPWCPLDLR LEWVDTVWEL DFTETEPLDP SIEAEIIETG LAAFTKLYES
LLPFATGEHG SMESIWTFFI ENNVSHSTLV ALFYHFVQIV HKKNVSVQYR EYGLHAAGLY
FLLLEVPGSV ANQVFHPVMF DKCIQTLKKS WPQESNLNRK RKKEQPKSSQ ANPGRHRKRG
KPPRREDIEM DEIIEEQEDE NICFSARDLS QIRNAIFHLL KNFLRLLPKF SLKEKPQCVQ
NCIEVFVSLT NFEPVLHECH VTQARALNQA KYIPELAYYG LYLLCSPIHG EGDKVISCVF
HQMLSVILML EVGEGSHRAP LAVTSQVINC RNQAVQFISA LVDELKESIF PVVRILLQHI
CAKVVDKSEY RTFAAQSLVQ LLSKLPCGEY AMFIAWLYKY SRSSKIPHRV FTLDVVLALL
ELPEREVDNT LSLEHQKFLK HKFLVQEIMF DRCLDKAPTV RSKALSSFAH CLELTVTSAS
ESILELLINS PTFSVIESHP GTLLRNSSAF SYQRQTSNRS EPSGEINIDS SGETVGSGER
CVMAMLRRRI RDEKTNVRKS ALQVLVSILK HCDVSGMKED LWILQDQCRD PAVSVRKQAL
QSLTELLMAQ PRCVQIQKAW LRGVVPVVMD CESTVQEKAL EFLDQLLLQN IRHHSHFHSG
DDSQVLAWAL LTLLTTESQE LSRYLNKAFH IWSKKEKFSP TFINNVISHT GTEHSAPAWM
LLSKIAGSSP RLDYSRIIQS WEKISSQQNP NSNTLGHILC VIGHIAKHLP KSTRDKVTDA
VKCKLNGFQW SLEVISSAVD ALQRLCRASA ETPAEEQELL TQVCGDVLST CEHRLSNIVL
KENGTGNMDE DLLVKYIFTL GDIAQLCPAR VEKRIFLLIQ SVLASSADAD HSPSSQGSSE
APASQPPPQV RGSVMPSVIR AHAIITLGKL CLQHEDLAKK SIPALVRELE VCEDVAVRNN
VIIVMCDLCI RYTIMVDKYI PNISMCLKDS DPFIRKQTLI LLTNLLQEEF VKWKGSLFFR
FVSTLIDSHP DIASFGEFCL AHLLLKRNPV MFFQHFIECI FHFNNYEKHE KYNKFPQSER
EKRLFSLKGK SNKERRMKIY KFLLEHFTDE QRFNITSKIC LSILACFADG ILPLDLDASE
LLSDTFEVLS SKEIKLLAMR SKPDKDLLME EDDMALANVV MQEAQKKLIS QVQKRNFIEN
IIPIIISLKT VLEKNKIPAL RELMHYLREV MQDYRDELKD FFAVDKQLAS ELEYDMKKYQ
EQLVQEQELA KHADVAGTAG GAEVAPVAQV ALCLETVPVP AGQENPAMSP AVSQPCTPRA
SAGHVAVSSP TPETGPLQRL LPKARPMSLS TIAILNSVKK AVESKSRHRS RSLGVLPFTL
NSGSPEKTCS QVSSYSLEQE SNGEIEHVTK RAISTPEKSI SDVTFGAGVS YIGTPRTPSS
AKEKIEGRSQ GNDILCLSLP DKPPPQPQQW NVRSPARNKD TPACSRRSLR KTPLKTAN
