CNDG2_HUMAN
ID CNDG2_HUMAN Reviewed; 1143 AA.
AC Q86XI2; A4D228; Q7Z3J9; Q8WUG8; Q9BRX6; Q9H8S2; Q9H9K6;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Condensin-2 complex subunit G2;
DE AltName: Full=Chromosome-associated protein G2;
DE Short=CAP-G2;
DE Short=hCAP-G2;
DE AltName: Full=Leucine zipper protein 5;
DE AltName: Full=Non-SMC condensin II complex subunit G2;
GN Name=NCAPG2; Synonyms=LUZP5;
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] (ISOFORM 2).
RC TISSUE=Endometrium;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 352-1143.
RC TISSUE=Ovary;
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 IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE CONDENSIN-II
RP COMPLEX, FUNCTION, 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND IDENTIFICATION BY
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-805 AND THR-1119, AND
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30 AND THR-805, AND
RP 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 [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-805, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [11]
RP INVOLVEMENT IN 3KS, VARIANTS 3KS GLU-609; MET-693 AND PRO-850,
RP CHARACTERIZATION OF VARIANTS 3KS GLU-609 AND MET-693, AND FUNCTION.
RX PubMed=30609410; DOI=10.1016/j.ajhg.2018.11.017;
RG Task Force for Neonatal Genomics;
RA Khan T.N., Khan K., Sadeghpour A., Reynolds H., Perilla Y., McDonald M.T.,
RA Gallentine W.B., Baig S.M., Davis E.E., Katsanis N.;
RT "Mutations in NCAPG2 Cause a Severe Neurodevelopmental Syndrome that
RT Expands the Phenotypic Spectrum of Condensinopathies.";
RL Am. J. Hum. Genet. 104:94-111(2019).
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. {ECO:0000269|PubMed:14532007,
CC ECO:0000269|PubMed:30609410}.
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. {ECO:0000269|PubMed:14532007}.
CC -!- INTERACTION:
CC Q86XI2; Q6IBW4: NCAPH2; NbExp=2; IntAct=EBI-1047404, EBI-2548296;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14532007}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q86XI2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86XI2-2; Sequence=VSP_021311;
CC -!- DISEASE: Khan-Khan-Katsanis syndrome (3KS) [MIM:618460]: An autosomal
CC recessive neurodevelopmental disorder characterized by multiple
CC congenital anomalies affecting the ocular, renal, skeletal, and
CC sometimes cardiac systems, defects in urogenital and limb
CC morphogenesis, poor overall growth, microcephaly, and global
CC developmental delay. {ECO:0000269|PubMed:30609410}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH20560.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB14219.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB14534.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX537845; CAD97854.1; -; mRNA.
DR EMBL; CH236954; EAL23929.1; -; Genomic_DNA.
DR EMBL; BC005878; AAH05878.2; -; mRNA.
DR EMBL; BC020560; AAH20560.1; ALT_INIT; mRNA.
DR EMBL; BC043404; AAH43404.1; -; mRNA.
DR EMBL; AK022744; BAB14219.1; ALT_INIT; mRNA.
DR EMBL; AK023347; BAB14534.1; ALT_INIT; mRNA.
DR CCDS; CCDS43686.1; -. [Q86XI2-1]
DR CCDS; CCDS64816.1; -. [Q86XI2-2]
DR RefSeq; NP_001268861.1; NM_001281932.1. [Q86XI2-1]
DR RefSeq; NP_001268862.1; NM_001281933.1. [Q86XI2-2]
DR RefSeq; NP_060230.5; NM_017760.6. [Q86XI2-1]
DR RefSeq; XP_011514658.1; XM_011516356.2. [Q86XI2-2]
DR RefSeq; XP_011514659.1; XM_011516357.2. [Q86XI2-2]
DR AlphaFoldDB; Q86XI2; -.
DR BioGRID; 120239; 110.
DR ComplexPortal; CPX-985; Condensin II complex.
DR CORUM; Q86XI2; -.
DR DIP; DIP-43902N; -.
DR IntAct; Q86XI2; 14.
DR MINT; Q86XI2; -.
DR STRING; 9606.ENSP00000387007; -.
DR iPTMnet; Q86XI2; -.
DR PhosphoSitePlus; Q86XI2; -.
DR SwissPalm; Q86XI2; -.
DR BioMuta; NCAPG2; -.
DR DMDM; 74727834; -.
DR EPD; Q86XI2; -.
DR jPOST; Q86XI2; -.
DR MassIVE; Q86XI2; -.
DR MaxQB; Q86XI2; -.
DR PaxDb; Q86XI2; -.
DR PeptideAtlas; Q86XI2; -.
DR PRIDE; Q86XI2; -.
DR ProteomicsDB; 70279; -. [Q86XI2-1]
DR ProteomicsDB; 70280; -. [Q86XI2-2]
DR Antibodypedia; 10695; 146 antibodies from 22 providers.
DR DNASU; 54892; -.
DR Ensembl; ENST00000356309.8; ENSP00000348657.3; ENSG00000146918.20. [Q86XI2-1]
DR Ensembl; ENST00000409339.3; ENSP00000387007.3; ENSG00000146918.20. [Q86XI2-2]
DR Ensembl; ENST00000409423.5; ENSP00000386569.1; ENSG00000146918.20. [Q86XI2-1]
DR GeneID; 54892; -.
DR KEGG; hsa:54892; -.
DR MANE-Select; ENST00000356309.8; ENSP00000348657.3; NM_017760.7; NP_060230.5.
DR UCSC; uc003wnv.3; human. [Q86XI2-1]
DR CTD; 54892; -.
DR DisGeNET; 54892; -.
DR GeneCards; NCAPG2; -.
DR HGNC; HGNC:21904; NCAPG2.
DR HPA; ENSG00000146918; Tissue enhanced (bone marrow, lymphoid tissue).
DR MalaCards; NCAPG2; -.
DR MIM; 608532; gene.
DR MIM; 618460; phenotype.
DR neXtProt; NX_Q86XI2; -.
DR OpenTargets; ENSG00000146918; -.
DR PharmGKB; PA162397212; -.
DR VEuPathDB; HostDB:ENSG00000146918; -.
DR eggNOG; KOG1949; Eukaryota.
DR GeneTree; ENSGT00490000043432; -.
DR InParanoid; Q86XI2; -.
DR OMA; SMRTLGE; -.
DR OrthoDB; 79594at2759; -.
DR PhylomeDB; Q86XI2; -.
DR TreeFam; TF101163; -.
DR PathwayCommons; Q86XI2; -.
DR Reactome; R-HSA-2299718; Condensation of Prophase Chromosomes.
DR SignaLink; Q86XI2; -.
DR SIGNOR; Q86XI2; -.
DR BioGRID-ORCS; 54892; 657 hits in 1087 CRISPR screens.
DR ChiTaRS; NCAPG2; human.
DR GeneWiki; NCAPG2; -.
DR GenomeRNAi; 54892; -.
DR Pharos; Q86XI2; Tbio.
DR PRO; PR:Q86XI2; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q86XI2; protein.
DR Bgee; ENSG00000146918; Expressed in ventricular zone and 139 other tissues.
DR ExpressionAtlas; Q86XI2; baseline and differential.
DR Genevisible; Q86XI2; HS.
DR GO; GO:0000794; C:condensed nuclear chromosome; IEA:Ensembl.
DR GO; GO:0000796; C:condensin complex; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0043425; F:bHLH transcription factor binding; IEA:Ensembl.
DR GO; GO:0008047; F:enzyme activator activity; IEA:Ensembl.
DR GO; GO:0035033; F:histone deacetylase regulator activity; IEA:Ensembl.
DR GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
DR GO; GO:0030293; F:transmembrane receptor protein tyrosine kinase inhibitor activity; IEA:Ensembl.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0030261; P:chromosome condensation; IEA:UniProtKB-KW.
DR GO; GO:0030218; P:erythrocyte differentiation; IEA:Ensembl.
DR GO; GO:0001833; P:inner cell mass cell proliferation; IEA:Ensembl.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central.
DR GO; GO:0051984; P:positive regulation of chromosome segregation; IEA:Ensembl.
DR GO; GO:1905820; P:positive regulation of chromosome separation; IEA:Ensembl.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR024741; Condensin2_G2.
DR Pfam; PF12422; Condensin2nSMC; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Disease variant;
KW DNA condensation; Mitosis; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..1143
FT /note="Condensin-2 complex subunit G2"
FT /id="PRO_0000255942"
FT REPEAT 460..498
FT /note="HEAT"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 805
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 1119
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 1128..1143
FT /note="FLYESSSRTLGELLNS -> YEDLLCCPGWALTPGLLDSIYPSASVPIG
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_021311"
FT VARIANT 609
FT /note="K -> E (in 3KS; leads to defects in mitotic
FT chromosome compaction and organization; increases the
FT number of micronuclei; increases cell death;
FT dbSNP:rs1299537743)"
FT /evidence="ECO:0000269|PubMed:30609410"
FT /id="VAR_083028"
FT VARIANT 693
FT /note="T -> M (in 3KS; leads to defects in mitotic
FT chromosome compaction and organization; increases the
FT number of micronuclei; increases cell death;
FT dbSNP:rs772209292)"
FT /evidence="ECO:0000269|PubMed:30609410"
FT /id="VAR_083029"
FT VARIANT 794
FT /note="T -> M (in dbSNP:rs10248318)"
FT /id="VAR_053046"
FT VARIANT 850
FT /note="T -> P (in 3KS; dbSNP:rs1563515856)"
FT /evidence="ECO:0000269|PubMed:30609410"
FT /id="VAR_083030"
FT VARIANT 867
FT /note="E -> D (in dbSNP:rs3214000)"
FT /id="VAR_053047"
FT CONFLICT 369
FT /note="E -> G (in Ref. 4; BAB14219)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1143 AA; 130960 MW; 7C7B7FA2A7F0683C CRC64;
MEKRETFVQA VSKELVGEFL QFVQLDKEAS DPFSLNELLD ELSRKQKEEL WQRLKNLLTD
VLLESPVDGW QVVEAQGEDN METEHGSKMR KSIEIIYAIT SVILASVSVI NESENYEALL
ECVIILNGIL YALPESERKL QSSIQDLCVT WWEKGLPAKE DTGKTAFVML LRRSLETKTG
ADVCRLWRIH QALYCFDYDL EESGEIKDML LECFININYI KKEEGRRFLS CLFNWNINFI
KMIHGTIKNQ LQGLQKSLMV YIAEIYFRAW KKASGKILEA IENDCIQDFM FHGIHLPRRS
PVHSKVREVL SYFHHQKKVR QGVEEMLYRL YKPILWRGLK ARNSEVRSNA ALLFVEAFPI
RDPNLHAIEM DSEIQKQFEE LYSLLEDPYP MVRSTGILGV CKITSKYWEM MPPTILIDLL
KKVTGELAFD TSSADVRCSV FKCLPMILDN KLSHPLLEQL LPALRYSLHD NSEKVRVAFV
DMLLKIKAVR AAKFWKICPM EHILVRLETD SRPVSRRLVS LIFNSFLPVN QPEEVWCERC
VTLVQMNHAA ARRFYQYAHE HTACTNIAKL IHVIRHCLNA CIQRAVREPP EDEEEEDGRE
KENVTVLDKT LSVNDVACMA GLLEIIVILW KSIDRSMENN KEAKLYTINK FASVLPEYLK
VFKDDRCKIP LFMLMSFMPA SAVPPFSCGV ISTLRSREEG AVDKSYCTLL DCLCSWGQVG
HILELVDNWL PTEHAQAKSN TASKGRVQIH DTRPVKPELA LVYIEYLLTH PKNRECLLSA
PRKKLNHLLK ALETSKADLE SLLQTPGGKP RGFSEAAAPR AFGLHCRLSI HLQHKFCSEG
KVYLSMLEDT GFWLESKILS FIQDQEEDYL KLHRVIYQQI IQTYLTVCKD VVMVGLGDHQ
FQMQLLQRSL GIMQTVKGFF YVSLLLDILK EITGSSLIQK TDSDEEVAML LDTVQKVFQK
MLECIARSFR KQPEEGLRLL YSVQRPLHEF ITAVQSRHTD TPVHRGVLST LIAGPVVEIS
HQLRKVSDVE ELTPPEHLSD LPPFSRCLIG IIIKSSNVVR SFLDELKACV ASNDIEGIVC
LTAAVHIILV INAGKHKSSK VREVAATVHR KLKTFMEITL EEDSIERFLY ESSSRTLGEL
LNS