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ZN142_HUMAN
ID   ZN142_HUMAN             Reviewed;        1687 AA.
AC   P52746; Q92510;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 4.
DT   03-AUG-2022, entry version 182.
DE   RecName: Full=Zinc finger protein 142 {ECO:0000305};
GN   Name=ZNF142 {ECO:0000303|PubMed:7557990, ECO:0000312|HGNC:HGNC:12927};
GN   Synonyms=KIAA0236 {ECO:0000303|PubMed:9039502};
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], AND VARIANT GLY-751.
RC   TISSUE=Bone marrow;
RX   PubMed=9039502; DOI=10.1093/dnares/3.5.321;
RA   Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
RA   Tanaka A., Kotani H., Miyajima N., Nomura N.;
RT   "Prediction of the coding sequences of unidentified human genes. VI. The
RT   coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of
RT   cDNA clones from cell line KG-1 and brain.";
RL   DNA Res. 3:321-329(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 460-632.
RC   TISSUE=Insulinoma;
RX   PubMed=7557990; DOI=10.1006/geno.1995.1040;
RA   Tommerup N., Vissing H.;
RT   "Isolation and fine mapping of 16 novel human zinc finger-encoding cDNAs
RT   identify putative candidate genes for developmental and malignant
RT   disorders.";
RL   Genomics 27:259-264(1995).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154, 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   [5]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-594, 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).
RN   [6]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1193; LYS-1242 AND LYS-1591, AND
RP   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).
RN   [7]
RP   INVOLVEMENT IN NEDISHM, AND VARIANTS NEDISHM 1059-ARG--GLY-1687 DEL;
RP   PHE-1233; 1395-LEU--GLY-1687 DEL AND THR-1500.
RX   PubMed=31036918; DOI=10.1038/s41436-019-0523-0;
RA   Khan K., Zech M., Morgan A.T., Amor D.J., Skorvanek M., Khan T.N.,
RA   Hildebrand M.S., Jackson V.E., Scerri T.S., Coleman M., Rigbye K.A.,
RA   Scheffer I.E., Bahlo M., Wagner M., Lam D.D., Berutti R., Havrankova P.,
RA   Fecikova A., Strom T.M., Han V., Dosekova P., Gdovinova Z., Laccone F.,
RA   Jameel M., Mooney M.R., Baig S.M., Jech R., Davis E.E., Katsanis N.,
RA   Winkelmann J.;
RT   "Recessive variants in ZNF142 cause a complex neurodevelopmental disorder
RT   with intellectual disability, speech impairment, seizures, and dystonia.";
RL   Genet. Med. 21:2532-2542(2019).
CC   -!- FUNCTION: May be involved in transcriptional regulation. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- DISEASE: Neurodevelopmental disorder with impaired speech and
CC       hyperkinetic movements (NEDISHM) [MIM:618425]: An autosomal recessive
CC       disorder characterized by global developmental delay, impaired
CC       intellectual development, delayed walking, poor or absent speech, and a
CC       hyperkinetic movement disorder with dystonia, tremor, ataxia, or
CC       chorea. Some patients develop seizures. {ECO:0000269|PubMed:31036918}.
CC       Note=The disease is caused by variants affecting the gene represented
CC       in this entry.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA13242.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; D87073; BAA13242.2; ALT_INIT; mRNA.
DR   EMBL; AC012510; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; U09849; AAC50265.1; -; mRNA.
DR   CCDS; CCDS42817.1; -.
DR   PIR; I38617; I38617.
DR   RefSeq; NP_001099007.1; NM_001105537.2.
DR   RefSeq; XP_011510091.1; XM_011511789.2.
DR   RefSeq; XP_016860361.1; XM_017004872.1.
DR   AlphaFoldDB; P52746; -.
DR   BioGRID; 113495; 19.
DR   IntAct; P52746; 7.
DR   STRING; 9606.ENSP00000398798; -.
DR   iPTMnet; P52746; -.
DR   PhosphoSitePlus; P52746; -.
DR   BioMuta; ZNF142; -.
DR   DMDM; 313104298; -.
DR   jPOST; P52746; -.
DR   MassIVE; P52746; -.
DR   MaxQB; P52746; -.
DR   PaxDb; P52746; -.
DR   PeptideAtlas; P52746; -.
DR   PRIDE; P52746; -.
DR   ProteomicsDB; 56521; -.
DR   Antibodypedia; 56468; 26 antibodies from 10 providers.
DR   DNASU; 7701; -.
DR   Ensembl; ENST00000449707.5; ENSP00000408643.1; ENSG00000115568.16.
DR   GeneID; 7701; -.
DR   KEGG; hsa:7701; -.
DR   UCSC; uc002vin.6; human.
DR   CTD; 7701; -.
DR   DisGeNET; 7701; -.
DR   GeneCards; ZNF142; -.
DR   HGNC; HGNC:12927; ZNF142.
DR   HPA; ENSG00000115568; Low tissue specificity.
DR   MalaCards; ZNF142; -.
DR   MIM; 604083; gene.
DR   MIM; 618425; phenotype.
DR   neXtProt; NX_P52746; -.
DR   OpenTargets; ENSG00000115568; -.
DR   PharmGKB; PA37514; -.
DR   VEuPathDB; HostDB:ENSG00000115568; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000163074; -.
DR   HOGENOM; CLU_001774_0_0_1; -.
DR   InParanoid; P52746; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; P52746; -.
DR   TreeFam; TF327469; -.
DR   PathwayCommons; P52746; -.
DR   SignaLink; P52746; -.
DR   BioGRID-ORCS; 7701; 10 hits in 1098 CRISPR screens.
DR   ChiTaRS; ZNF142; human.
DR   GenomeRNAi; 7701; -.
DR   Pharos; P52746; Tdark.
DR   PRO; PR:P52746; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; P52746; protein.
DR   Bgee; ENSG00000115568; Expressed in cortical plate and 159 other tissues.
DR   ExpressionAtlas; P52746; baseline and differential.
DR   Genevisible; P52746; HS.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF00096; zf-C2H2; 3.
DR   SMART; SM00355; ZnF_C2H2; 36.
DR   SUPFAM; SSF57667; SSF57667; 12.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 17.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 18.
PE   1: Evidence at protein level;
KW   Disease variant; DNA-binding; Intellectual disability; Isopeptide bond;
KW   Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW   Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..1687
FT                   /note="Zinc finger protein 142"
FT                   /id="PRO_0000047425"
FT   ZN_FING         163..185
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         219..242
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         253..275
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         286..311
FT                   /note="C2H2-type 4; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         316..340
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         343..366
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         372..395
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         401..423
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         429..451
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         457..479
FT                   /note="C2H2-type 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         485..507
FT                   /note="C2H2-type 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         512..536
FT                   /note="C2H2-type 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         544..567
FT                   /note="C2H2-type 13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         573..596
FT                   /note="C2H2-type 14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1135..1158
FT                   /note="C2H2-type 15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1171..1194
FT                   /note="C2H2-type 16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1200..1222
FT                   /note="C2H2-type 17"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1228..1251
FT                   /note="C2H2-type 18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1257..1280
FT                   /note="C2H2-type 19"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1286..1309
FT                   /note="C2H2-type 20"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1328..1351
FT                   /note="C2H2-type 21"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1354..1377
FT                   /note="C2H2-type 22"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1380..1403
FT                   /note="C2H2-type 23"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1424..1446
FT                   /note="C2H2-type 24"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1452..1474
FT                   /note="C2H2-type 25"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1480..1502
FT                   /note="C2H2-type 26"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1508..1530
FT                   /note="C2H2-type 27"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1536..1559
FT                   /note="C2H2-type 28"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1565..1587
FT                   /note="C2H2-type 29"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1593..1615
FT                   /note="C2H2-type 30"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1621..1643
FT                   /note="C2H2-type 31"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          83..150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          613..690
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          704..798
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          897..935
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          947..1014
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1052..1092
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1638..1687
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        118..137
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        761..785
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1062..1092
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         154
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   CROSSLNK        594
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25218447"
FT   CROSSLNK        1193
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        1242
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        1591
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   VARIANT         751
FT                   /note="S -> G (in dbSNP:rs3770214)"
FT                   /evidence="ECO:0000269|PubMed:9039502"
FT                   /id="VAR_047230"
FT   VARIANT         956
FT                   /note="L -> H (in dbSNP:rs3770213)"
FT                   /id="VAR_047231"
FT   VARIANT         1059..1687
FT                   /note="Missing (in NEDISHM)"
FT                   /evidence="ECO:0000269|PubMed:31036918"
FT                   /id="VAR_082094"
FT   VARIANT         1233
FT                   /note="C -> F (in NEDISHM; dbSNP:rs1275959058)"
FT                   /evidence="ECO:0000269|PubMed:31036918"
FT                   /id="VAR_082095"
FT   VARIANT         1313
FT                   /note="A -> T (in dbSNP:rs3821033)"
FT                   /id="VAR_047232"
FT   VARIANT         1395..1687
FT                   /note="Missing (in NEDISHM)"
FT                   /evidence="ECO:0000269|PubMed:31036918"
FT                   /id="VAR_082096"
FT   VARIANT         1500
FT                   /note="R -> T (in NEDISHM)"
FT                   /evidence="ECO:0000269|PubMed:31036918"
FT                   /id="VAR_082097"
FT   CONFLICT        460..463
FT                   /note="TECG -> LKGS (in Ref. 2; AAC50265)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        541
FT                   /note="A -> S (in Ref. 1; BAA13242)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1687 AA;  187880 MW;  91143EAF2481B6B3 CRC64;
     MTDPLLDSQP ASSTGEMDGL CPELLLIPPP LSNRGILGPV QSPCPSRDPA PIPTEPGCLL
     VEATATEEGP GNMEIIVETV AGTLTPGAPG ETPAPKLPPG EREPSQEAGT PLPGQETAEE
     ENVEKEEKSD TQKDSQKAVD KGQGAQRLEG DVVSGTESLF KTHMCPECKR CFKKRTHLVE
     HLHLHFPDPS LQCPNCQKFF TSKSKLKTHL LRELGEKAHH CPLCHYSAVE RNALNRHMAS
     MHEDISNFYS DTYACPVCRE EFRLSQALKE HLKSHTAAAA AEPLPLRCFQ EGCSYAAPDR
     KAFIKHLKET HGVRAVECRH HSCPMLFATA EAMEAHHKSH YAFHCPHCDF ACSNKHLFRK
     HKKQGHPGSE ELRCTFCPFA TFNPVAYQDH VGKMHAHEKI HQCPECNFAT AHKRVLIRHM
     LLHTGEKPHK CELCDFTCRD VSYLSKHMLT HSNTKDYMCT ECGYVTKWKH YLRVHMRKHA
     GDLRYQCNQC SYRCHRADQL SSHKLRHQGK SLMCEVCAFA CKRKYELQKH MASQHHPGTP
     APLYPCHYCS YQSRHKQAVL SHENCKHTRL REFHCALCDY RTFSNTTLLF HKRKAHGYVP
     GDQAWQLRYA SQEPEGAMQG PTPPPDSEPS NQLSARPEGP GHEPGTVVDP SLDQALPEMS
     EEVNTGRQEG SEAPHGGDLG GSPSPAEVEE GSCTLHLEAL GVELESVTEP PLEEVTETAP
     MEFRPLGLEG PDGLEGPELS SFEGIGTSDL SAEENPLLEK PVSEPSTNPP SLEEAPNNWV
     GTFKTTPPAE TAPLPPLPES ESLLKALRRQ DKEQAEALVL EGRVQMVVIQ GEGRAFRCPH
     CPFITRREKA LNLHSRTGCQ GRREPLLCPE CGASFKQQRG LSTHLLKKCP VLLRKNKGLP
     RPDSPIPLQP VLPGTQASED TESGKPPPAS QEAELLLPKD APLELPREPE ETEEPLATVS
     GSPVPPAGNS LPTEAPKKHC FDPVPPAGNS SPTEAPKKHH LDPVPPAGNS SPTEALKKHR
     FEQGKFHCNS CPFLCSRLSS ITSHVAEGCR GGRGGGGKRG TPQTQPDVSP LSNGDSAPPK
     NGSTESSSGD GDTVLVQKQK GARFSCPTCP FSCQQERALR THQIRGCPLE ESGELHCSLC
     PFTAPAATAL RLHQKRRHPT AAPARGPRPH LQCGDCGFTC KQSRCMQQHR RLKHEGVKPH
     QCPFCDFSTT RRYRLEAHQS RHTGIGRIPC SSCPQTFGTN SKLRLHRLRV HDKTPTHFCP
     LCDYSGYLRH DITRHVNSCH QGTPAFACSQ CEAQFSSETA LKQHALRRHP EPAQPAPGSP
     AETTEGPLHC SRCGLLCPSP ASLRGHTRKQ HPRLECGACQ EAFPSRLALD EHRRQQHFSH
     RCQLCDFAAR ERVGLVKHYL EQHEETSAAV AASDGDGDAG QPPLHCPFCD FTCRHQLVLD
     HHVKGHGGTR LYKCTDCAYS TKNRQKITWH SRIHTGEKPY HCHLCPYACA DPSRLKYHMR
     IHKEERKYLC PECGYKCKWV NQLKYHMTKH TGLKPYQCPE CEYCTNRADA LRVHQETRHR
     EARAFMCEQC GKAFKTRFLL RTHLRKHSEA KPYVCNVCHR AFRWAAGLRH HALTHTDRHP
     FFCRLCNYKA KQKFQVVKHV RRHHPDQADP NQGVGKDPTT PTVHLHDVQL EDPSPPAPAA
     PHTGPEG
 
 
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