ZN608_HUMAN
ID ZN608_HUMAN Reviewed; 1512 AA.
AC Q9ULD9; A7E2W9; Q3SYM6; Q68D12; Q8IY05; Q9Y5A1;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 4.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Zinc finger protein 608;
DE AltName: Full=Renal carcinoma antigen NY-REN-36;
GN Name=ZNF608; Synonyms=KIAA1281;
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 1), AND VARIANT ASN-721.
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ASN-721.
RC TISSUE=Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ASN-721.
RC TISSUE=PNS, and Skin;
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 584-810, IDENTIFICATION AS A RENAL CANCER
RP ANTIGEN, AND VARIANT ASN-721.
RC TISSUE=Renal cell carcinoma;
RX PubMed=10508479;
RX DOI=10.1002/(sici)1097-0215(19991112)83:4<456::aid-ijc4>3.0.co;2-5;
RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
RA Old L.J.;
RT "Antigens recognized by autologous antibody in patients with renal-cell
RT carcinoma.";
RL Int. J. Cancer 83:456-464(1999).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-782 AND SER-964, AND
RP IDENTIFICATION BY 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-627; SER-895; SER-964 AND
RP SER-1098, AND IDENTIFICATION BY 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).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-627, AND IDENTIFICATION BY
RP 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 [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-880 AND LYS-1292, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-283; LYS-880; LYS-1118; LYS-1176;
RP LYS-1182; LYS-1199; LYS-1216; LYS-1234; LYS-1250; LYS-1292; LYS-1310 AND
RP LYS-1414, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Transcription factor, which represses ZNF609 transcription.
CC {ECO:0000250|UniProtKB:Q56A10}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9ULD9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ULD9-2; Sequence=VSP_023664;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA86595.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB033107; BAA86595.2; ALT_INIT; mRNA.
DR EMBL; CR749624; CAH18418.1; -; mRNA.
DR EMBL; AC112196; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC113398; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC038370; AAH38370.1; -; mRNA.
DR EMBL; BC103742; AAI03743.1; -; mRNA.
DR EMBL; BC151226; AAI51227.1; -; mRNA.
DR EMBL; AF155106; AAD42872.1; -; mRNA.
DR CCDS; CCDS34219.1; -. [Q9ULD9-1]
DR RefSeq; NP_065798.2; NM_020747.2. [Q9ULD9-1]
DR RefSeq; XP_005272094.1; XM_005272037.2. [Q9ULD9-1]
DR RefSeq; XP_005272095.1; XM_005272038.1. [Q9ULD9-1]
DR AlphaFoldDB; Q9ULD9; -.
DR SMR; Q9ULD9; -.
DR BioGRID; 121571; 77.
DR DIP; DIP-29419N; -.
DR IntAct; Q9ULD9; 46.
DR MINT; Q9ULD9; -.
DR STRING; 9606.ENSP00000307746; -.
DR iPTMnet; Q9ULD9; -.
DR PhosphoSitePlus; Q9ULD9; -.
DR BioMuta; ZNF608; -.
DR DMDM; 296453083; -.
DR EPD; Q9ULD9; -.
DR jPOST; Q9ULD9; -.
DR MassIVE; Q9ULD9; -.
DR PaxDb; Q9ULD9; -.
DR PeptideAtlas; Q9ULD9; -.
DR PRIDE; Q9ULD9; -.
DR ProteomicsDB; 85004; -. [Q9ULD9-1]
DR ProteomicsDB; 85005; -. [Q9ULD9-2]
DR Antibodypedia; 1014; 90 antibodies from 25 providers.
DR DNASU; 57507; -.
DR Ensembl; ENST00000306315.9; ENSP00000307746.5; ENSG00000168916.16. [Q9ULD9-1]
DR Ensembl; ENST00000504926.5; ENSP00000427657.1; ENSG00000168916.16. [Q9ULD9-2]
DR Ensembl; ENST00000513986.2; ENSP00000421899.2; ENSG00000168916.16. [Q9ULD9-1]
DR GeneID; 57507; -.
DR KEGG; hsa:57507; -.
DR MANE-Select; ENST00000513986.2; ENSP00000421899.2; NM_020747.3; NP_065798.2.
DR UCSC; uc003ktq.2; human. [Q9ULD9-1]
DR CTD; 57507; -.
DR DisGeNET; 57507; -.
DR GeneCards; ZNF608; -.
DR HGNC; HGNC:29238; ZNF608.
DR HPA; ENSG00000168916; Low tissue specificity.
DR neXtProt; NX_Q9ULD9; -.
DR OpenTargets; ENSG00000168916; -.
DR PharmGKB; PA134945727; -.
DR VEuPathDB; HostDB:ENSG00000168916; -.
DR eggNOG; ENOG502QSUK; Eukaryota.
DR GeneTree; ENSGT00390000008748; -.
DR HOGENOM; CLU_004142_1_0_1; -.
DR InParanoid; Q9ULD9; -.
DR OMA; PSGHLYG; -.
DR PhylomeDB; Q9ULD9; -.
DR TreeFam; TF329775; -.
DR PathwayCommons; Q9ULD9; -.
DR SignaLink; Q9ULD9; -.
DR BioGRID-ORCS; 57507; 11 hits in 1078 CRISPR screens.
DR ChiTaRS; ZNF608; human.
DR GenomeRNAi; 57507; -.
DR Pharos; Q9ULD9; Tdark.
DR PRO; PR:Q9ULD9; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9ULD9; protein.
DR Bgee; ENSG00000168916; Expressed in cardiac muscle of right atrium and 163 other tissues.
DR ExpressionAtlas; Q9ULD9; baseline and differential.
DR Genevisible; Q9ULD9; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR040010; ZN608/ZN609.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR21564; PTHR21564; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Isopeptide bond; Metal-binding;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1512
FT /note="Zinc finger protein 608"
FT /id="PRO_0000280420"
FT ZN_FING 553..578
FT /note="C2H2-type"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 46..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 622..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 713..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 777..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 925..996
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1011..1066
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1117..1192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1220..1335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1423..1459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 278..304
FT /evidence="ECO:0000255"
FT COMPBIAS 50..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..295
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..545
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..731
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..858
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 925..941
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 956..994
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1029..1052
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1122..1144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1145..1192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1254..1275
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1292..1323
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1434..1455
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 421
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q56A10"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q56A10"
FT MOD_RES 481
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q56A10"
FT MOD_RES 493
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q56A10"
FT MOD_RES 627
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 782
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 895
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 964
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1098
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 283
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 880
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 1118
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1176
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1182
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1199
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1216
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1234
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1250
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1292
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 1310
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1414
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..427
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_023664"
FT VARIANT 721
FT /note="T -> N (in dbSNP:rs6862252)"
FT /evidence="ECO:0000269|PubMed:10508479,
FT ECO:0000269|PubMed:10574462, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_031148"
FT CONFLICT 1512
FT /note="E -> G (in Ref. 3; CAH18418)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1512 AA; 162208 MW; 46A41B939FEBD054 CRC64;
MSVNISTAGK GVDPNTVDTY DSGDDWEIGV GNLIIDLDAD LEKDRQKFEM NNSTTTTSSS
NSKDCGGPAS SGAGATAALA DGLKFASVQA SAPQGNSHKE TSKSKVKRSK TSKDANKSLP
SAALYGIPEI SSTGKRQEVQ GRPGEATGMN SALGQSVSSG GSGNPNSNST STSTSAATAG
AGSCGKSKEE KPGKSQSSRG AKRDKDAGKS RKDKHDLLQG HQNGSGSQAP SGGHLYGFGA
KSNGGGASPF HCGGTGSGSV AAAGEVSKSA PDSGLMGNSM LVKKEEEEEE SHRRIKKLKT
EKVDPLFTVP APPPPISSSL TPQILPSYFS PSSSNIAAPV EQLLVRTRSV GVNTCEVGVV
TEPECLGPCE PGTSVNLEGI VWHETEEGVL VVNVTWRNKT YVGTLLDCTK HDWAPPRFCE
SPTSDLEMRG GRGRGKRARS AAAAPGSEAS FTESRGLQNK NRGGANGKGR RGSLNASGRR
TPPNCAAEDI KASPSSTNKR KNKPPMELDL NSSSEDNKPG KRVRTNSRST PTTPQGKPET
TFLDQGCSSP VLIDCPHPNC NKKYKHINGL RYHQAHAHLD PENKLEFEPD SEDKISDCEE
GLSNVALECS EPSTSVSAYD QLKAPASPGA GNPPGTPKGK RELMSNGPGS IIGAKAGKNS
GKKKGLNNEL NNLPVISNMT AALDSCSAAD GSLAAEMPKL EAEGLIDKKN LGDKEKGKKA
TNCKTDKNLS KLKSARPIAP APAPTPPQLI AIPTATFTTT TTGTIPGLPS LTTTVVQATP
KSPPLKPIQP KPTIMGEPIT VNPALVSLKD KKKKEKRKLK DKEGKETGSP KMDAKLGKLE
DSKGASKDLP GHFLKDHLNK NEGLANGLSE SQESRMASIK AEADKVYTFT DNAPSPSIGS
ASRLECSTLV NGQAPMAPLH VLTQNGAESS AAKTSSPAYS DISDAADDGG SDSRSEGMRS
KASSPSDIIS SKDSVVKGHS STTAQSSQLK ESHSPYYHSY DPYYSPSYMH PGQVGAPAAG
NSGSTQGMKI KKESEEDAEK KDKAEQLDSK KVDHNSASLQ PQHQSVITQR HPALAQSLYY
GQYAYGLYMD QKSLMATSPA YRQQYEKYYE DQRLAEQKMA QTGRGDCERK SELPLKELGK
EETKQKNMPS ATISKAPSTP EPNKNHSKLG PSVPNKTEET GKSQLLSNHQ QQLQADSFKA
KQMENHQLIK EAVEMKSVMD SMKQTGVDPT SRFKQDPDSR TWHHYVYQPK YLDQQKSEEL
DREKKLKEDS PRKTPNKESG VPSLPVSLTS IKEEPKEAKH PDSQSMEESK LKNDDRKTPV
NWKDSRGTRV AVSSPMSQHQ SYIQYLHAYP YPQMYDPSHP AYRAVSPVLM HSYPGAYLSP
GFHYPVYGKM SGREETEKVN TSPSVNTKTT TESKALDLLQ QHANQYRSKS PAPVEKATAE
REREAERERD RHSPFGQRHL HTHHHTHVGM GYPLIPGQYD PFQGLTSAAL VASQQVAAQA
SASGMFPGQR RE
