ID   ZN202_HUMAN             Reviewed;         648 AA.
AC   O95125; B0LPH9; Q4JG21; Q9H1B9; Q9NSM4;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 4.
DT   27-MAR-2024, entry version 209.
DE   RecName: Full=Zinc finger protein 202;
DE   AltName: Full=Zinc finger protein with KRAB and SCAN domains 10;
GN   Name=ZNF202; Synonyms=ZKSCAN10;
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] (ISOFORMS ALPHA AND BETA), AND VARIANT ALA-154.
RC   TISSUE=Testis;
RX   PubMed=9790754; DOI=10.1006/geno.1998.5419;
RA   Monaco C., Helmer Citterich M., Caprini E., Vorechovsky I., Russo G.,
RA   Croce C.M., Barbanti-Brodano G., Negrini M.;
RT   "Molecular cloning and characterization of ZNF202: a new gene at 11q23.3
RT   encoding testis-specific zinc finger proteins.";
RL   Genomics 52:358-362(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-154.
RA   Langmann T., Porsch-Oezcueruemez M., Heimerl S., Andrikovics H.,
RA   Schmitz G.;
RT   "Genomic sequence analysis of the ZNF202 gene: relevance for lipid
RT   parameters.";
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ALA-154 AND ALA-533.
RG   SeattleSNPs variation discovery resource;
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-154.
RG   NHLBI resequencing and genotyping service (RS&G);
RL   Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA), AND VARIANT ALA-154.
RC   TISSUE=Brain;
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 [LARGE SCALE MRNA] OF 15-648 (ISOFORM BETA).
RC   TISSUE=Mammary cancer;
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   [7]
RP   CHARACTERIZATION.
RX   PubMed=10748193; DOI=10.1074/jbc.m910152199;
RA   Wagner S., Hess M.A., Ormonde-Hanson P., Malandro J., Hu H., Chen M.,
RA   Kehrer R., Frodsham M., Schumacher C., Beluch M., Honer C., Skolnick M.,
RA   Ballinger D., Bowen B.R.;
RT   "A broad role for the zinc finger protein ZNF202 in human lipid
RT   metabolism.";
RL   J. Biol. Chem. 275:15685-15690(2000).
RN   [8]
RP   POSSIBLE FUNCTION.
RX   PubMed=11279031; DOI=10.1074/jbc.m100218200;
RA   Porsch-Oezcueruemez M., Langmann T., Heimerl S., Borsukova H.,
RA   Kaminski W.E., Drobnik W., Honer C., Schumacher C., Schmitz G.;
RT   "The zinc finger protein 202 (ZNF202) is a transcriptional repressor of ATP
RT   binding cassette transporter A1 (ABCA1) and ABCG1 gene expression and a
RT   modulator of cellular lipid efflux.";
RL   J. Biol. Chem. 276:12427-12433(2001).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466, 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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466, AND IDENTIFICATION BY
RP   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   [11]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-22; LYS-454; LYS-460; LYS-507 AND
RP   LYS-521, 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: Transcriptional repressor that binds to elements found
CC       predominantly in genes that participate in lipid metabolism. Among its
CC       targets are structural components of lipoprotein particles
CC       (apolipoproteins AIV, CIII, and E), enzymes involved in lipid
CC       processing (lipoprotein lipase, lecithin cholesteryl ester
CC       transferase), transporters involved in lipid homeostasis (ABCA1,
CC       ABCG1), and several genes involved in processes related to energy
CC       metabolism and vascular disease.
CC   -!- SUBUNIT: Interacts with SDP1.
CC   -!- INTERACTION:
CC       O95125; Q9BWT7: CARD10; NbExp=3; IntAct=EBI-751960, EBI-3866279;
CC       O95125; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-751960, EBI-739624;
CC       O95125; Q96JC9: EAF1; NbExp=3; IntAct=EBI-751960, EBI-769261;
CC       O95125; Q6A162: KRT40; NbExp=6; IntAct=EBI-751960, EBI-10171697;
CC       O95125; P61968: LMO4; NbExp=4; IntAct=EBI-751960, EBI-2798728;
CC       O95125; Q15013: MAD2L1BP; NbExp=3; IntAct=EBI-751960, EBI-712181;
CC       O95125; P23508: MCC; NbExp=3; IntAct=EBI-751960, EBI-307531;
CC       O95125; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-751960, EBI-16439278;
CC       O95125; Q9H2K0: MTIF3; NbExp=3; IntAct=EBI-751960, EBI-3923617;
CC       O95125; P41227: NAA10; NbExp=3; IntAct=EBI-751960, EBI-747693;
CC       O95125; Q9BSU3: NAA11; NbExp=3; IntAct=EBI-751960, EBI-2585120;
CC       O95125; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-751960, EBI-748391;
CC       O95125; P49903: SEPHS1; NbExp=5; IntAct=EBI-751960, EBI-714091;
CC       O95125; Q9Y2D8: SSX2IP; NbExp=3; IntAct=EBI-751960, EBI-2212028;
CC       O95125; P15622-3: ZNF250; NbExp=3; IntAct=EBI-751960, EBI-10177272;
CC       O95125; Q7Z4V0: ZNF438; NbExp=3; IntAct=EBI-751960, EBI-11962468;
CC       O95125; Q9Y2P0: ZNF835; NbExp=3; IntAct=EBI-751960, EBI-5667516;
CC       O95125; Q96EG3: ZNF837; NbExp=3; IntAct=EBI-751960, EBI-11962574;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Beta; Synonyms=2;
CC         IsoId=O95125-1; Sequence=Displayed;
CC       Name=Alpha; Synonyms=1;
CC         IsoId=O95125-2; Sequence=VSP_006902;
CC   -!- TISSUE SPECIFICITY: Highly expressed in testis. Also expressed in
CC       breast carcinoma cell lines.
CC   -!- WEB RESOURCE: Name=SeattleSNPs;
CC       URL="http://pga.gs.washington.edu/data/znf202/";
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; AF027219; AAC79941.1; -; mRNA.
DR   EMBL; AF027218; AAC79940.1; -; mRNA.
DR   EMBL; AJ276177; CAC21447.1; -; Genomic_DNA.
DR   EMBL; AJ276178; CAC21447.1; JOINED; Genomic_DNA.
DR   EMBL; AJ276179; CAC21447.1; JOINED; Genomic_DNA.
DR   EMBL; AJ276180; CAC21447.1; JOINED; Genomic_DNA.
DR   EMBL; AJ276181; CAC21447.1; JOINED; Genomic_DNA.
DR   EMBL; AJ276182; CAC21447.1; JOINED; Genomic_DNA.
DR   EMBL; DQ093962; AAY88738.1; -; Genomic_DNA.
DR   EMBL; EU332869; ABY87558.1; -; Genomic_DNA.
DR   EMBL; BC013382; AAH13382.1; -; mRNA.
DR   EMBL; AL162031; CAB82384.1; -; mRNA.
DR   CCDS; CCDS8443.1; -. [O95125-1]
DR   PIR; T47156; T47156.
DR   RefSeq; NP_001288708.1; NM_001301779.1. [O95125-1]
DR   RefSeq; NP_001288709.1; NM_001301780.1. [O95125-1]
DR   RefSeq; NP_001288748.1; NM_001301819.1. [O95125-2]
DR   RefSeq; NP_003446.2; NM_003455.3. [O95125-1]
DR   RefSeq; XP_005271716.1; XM_005271659.1. [O95125-1]
DR   RefSeq; XP_005271717.1; XM_005271660.1. [O95125-1]
DR   RefSeq; XP_005271718.1; XM_005271661.1. [O95125-1]
DR   RefSeq; XP_005271721.1; XM_005271664.1.
DR   RefSeq; XP_006718964.1; XM_006718901.2. [O95125-1]
DR   RefSeq; XP_011541274.1; XM_011542972.1. [O95125-1]
DR   RefSeq; XP_011541275.1; XM_011542973.1. [O95125-1]
DR   RefSeq; XP_011541277.1; XM_011542975.1. [O95125-1]
DR   RefSeq; XP_011541278.1; XM_011542976.1.
DR   RefSeq; XP_016873757.1; XM_017018268.1. [O95125-1]
DR   AlphaFoldDB; O95125; -.
DR   SMR; O95125; -.
DR   BioGRID; 113537; 31.
DR   IntAct; O95125; 28.
DR   STRING; 9606.ENSP00000432504; -.
DR   iPTMnet; O95125; -.
DR   PhosphoSitePlus; O95125; -.
DR   BioMuta; ZNF202; -.
DR   EPD; O95125; -.
DR   jPOST; O95125; -.
DR   MassIVE; O95125; -.
DR   MaxQB; O95125; -.
DR   PaxDb; 9606-ENSP00000337724; -.
DR   PeptideAtlas; O95125; -.
DR   ProteomicsDB; 50655; -. [O95125-1]
DR   ProteomicsDB; 50656; -. [O95125-2]
DR   Antibodypedia; 32833; 189 antibodies from 19 providers.
DR   DNASU; 7753; -.
DR   Ensembl; ENST00000336139.8; ENSP00000337724.4; ENSG00000166261.11. [O95125-1]
DR   Ensembl; ENST00000529691.1; ENSP00000433881.1; ENSG00000166261.11. [O95125-1]
DR   Ensembl; ENST00000530393.6; ENSP00000432504.1; ENSG00000166261.11. [O95125-1]
DR   GeneID; 7753; -.
DR   KEGG; hsa:7753; -.
DR   MANE-Select; ENST00000530393.6; ENSP00000432504.1; NM_003455.4; NP_003446.2.
DR   UCSC; uc001pzd.2; human. [O95125-1]
DR   AGR; HGNC:12994; -.
DR   CTD; 7753; -.
DR   DisGeNET; 7753; -.
DR   GeneCards; ZNF202; -.
DR   HGNC; HGNC:12994; ZNF202.
DR   HPA; ENSG00000166261; Low tissue specificity.
DR   MIM; 603430; gene.
DR   neXtProt; NX_O95125; -.
DR   OpenTargets; ENSG00000166261; -.
DR   PharmGKB; PA37574; -.
DR   VEuPathDB; HostDB:ENSG00000166261; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000161189; -.
DR   HOGENOM; CLU_002678_49_8_1; -.
DR   InParanoid; O95125; -.
DR   OMA; ELYLCNE; -.
DR   OrthoDB; 5249345at2759; -.
DR   PhylomeDB; O95125; -.
DR   TreeFam; TF350829; -.
DR   PathwayCommons; O95125; -.
DR   Reactome; R-HSA-212436; Generic Transcription Pathway.
DR   SignaLink; O95125; -.
DR   SIGNOR; O95125; -.
DR   BioGRID-ORCS; 7753; 24 hits in 1180 CRISPR screens.
DR   ChiTaRS; ZNF202; human.
DR   GeneWiki; ZNF202; -.
DR   GenomeRNAi; 7753; -.
DR   Pharos; O95125; Tbio.
DR   PRO; PR:O95125; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; O95125; Protein.
DR   Bgee; ENSG00000166261; Expressed in secondary oocyte and 136 other cell types or tissues.
DR   ExpressionAtlas; O95125; baseline and differential.
DR   GO; GO:0005694; C:chromosome; IDA:HPA.
DR   GO; GO:0016604; C:nuclear body; IDA:HPA.
DR   GO; GO:0005730; C:nucleolus; IDA:HPA.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR   GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd07765; KRAB_A-box; 1.
DR   CDD; cd07936; SCAN; 1.
DR   Gene3D; 6.10.140.140; -; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 8.
DR   Gene3D; 1.10.4020.10; DNA breaking-rejoining enzymes; 1.
DR   InterPro; IPR001909; KRAB.
DR   InterPro; IPR036051; KRAB_dom_sf.
DR   InterPro; IPR003309; SCAN_dom.
DR   InterPro; IPR038269; SCAN_sf.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR23232; KRAB DOMAIN C2H2 ZINC FINGER; 1.
DR   PANTHER; PTHR23232:SF136; KRAB DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01352; KRAB; 1.
DR   Pfam; PF02023; SCAN; 1.
DR   Pfam; PF00096; zf-C2H2; 7.
DR   SMART; SM00349; KRAB; 1.
DR   SMART; SM00431; SCAN; 1.
DR   SMART; SM00355; ZnF_C2H2; 8.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 4.
DR   SUPFAM; SSF109640; KRAB domain (Kruppel-associated box); 1.
DR   SUPFAM; SSF47353; Retrovirus capsid dimerization domain-like; 1.
DR   PROSITE; PS50805; KRAB; 1.
DR   PROSITE; PS50804; SCAN_BOX; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 8.
DR   Genevisible; O95125; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW   Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..648
FT                   /note="Zinc finger protein 202"
FT                   /id="PRO_0000047450"
FT   DOMAIN          46..127
FT                   /note="SCAN box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT   DOMAIN          237..308
FT                   /note="KRAB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT   ZN_FING         397..419
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         425..447
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         481..503
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         509..531
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         537..559
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         565..587
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         593..615
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         621..643
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          146..221
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        161..185
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         466
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163"
FT   CROSSLNK        22
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        454
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        460
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        507
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        521
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   VAR_SEQ         1..224
FT                   /note="Missing (in isoform Alpha)"
FT                   /evidence="ECO:0000303|PubMed:9790754"
FT                   /id="VSP_006902"
FT   VARIANT         154
FT                   /note="V -> A (in dbSNP:rs1144507)"
FT                   /evidence="ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:9790754, ECO:0000269|Ref.2,
FT                   ECO:0000269|Ref.3, ECO:0000269|Ref.4"
FT                   /id="VAR_007818"
FT   VARIANT         533
FT                   /note="G -> A (in dbSNP:rs34111365)"
FT                   /evidence="ECO:0000269|Ref.3"
FT                   /id="VAR_023975"
FT   CONFLICT        15
FT                   /note="E -> P (in Ref. 6; CAB82384)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        205
FT                   /note="Missing (in Ref. 2; CAC21447)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        278
FT                   /note="S -> AA (in Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   648 AA;  74720 MW;  E738506D71DAFAE9 CRC64;
     MATAVEPEDQ DLWEEEGILM VKLEDDFTCR PESVLQRDDP VLETSHQNFR RFRYQEAASP
     REALIRLREL CHQWLRPERR TKEQILELLV LEQFLTVLPG ELQSWVRGQR PESGEEAVTL
     VEGLQKQPRR PRRWVTVHVH GQEVLSEETV HLGVEPESPN ELQDPVQSST PEQSPEETTQ
     SPDLGAPAEQ RPHQEEELQT LQESEVPVPE DPDLPAERSS GDSEMVALLT ALSQGLVTFK
     DVAVCFSQDQ WSDLDPTQKE FYGEYVLEED CGIVVSLSFP IPRPDEISQV REEEPWVPDI
     QEPQETQEPE ILSFTYTGDR SKDEEECLEQ EDLSLEDIHR PVLGEPEIHQ TPDWEIVFED
     NPGRLNERRF GTNISQVNSF VNLRETTPVH PLLGRHHDCS VCGKSFTCNS HLVRHLRTHT
     GEKPYKCMEC GKSYTRSSHL ARHQKVHKMN APYKYPLNRK NLEETSPVTQ AERTPSVEKP
     YRCDDCGKHF RWTSDLVRHQ RTHTGEKPFF CTICGKSFSQ KSVLTTHQRI HLGGKPYLCG
     ECGEDFSEHR RYLAHRKTHA AEELYLCSEC GRCFTHSAAF AKHLRGHASV RPCRCNECGK
     SFSRRDHLVR HQRTHTGEKP FTCPTCGKSF SRGYHLIRHQ RTHSEKTS
//