PCGF1_HUMAN
ID PCGF1_HUMAN Reviewed; 259 AA.
AC Q9BSM1; Q7Z506;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Polycomb group RING finger protein 1;
DE AltName: Full=Nervous system Polycomb-1;
DE Short=NSPc1;
DE AltName: Full=RING finger protein 68;
GN Name=PCGF1; Synonyms=NSPC1, RNF68;
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] (ISOFORM 2).
RA Ding J.B., Yu L., Chu J.H., Ge H.P., Wang X.K., Zhao S.Y.;
RT "Cloning of a new human cDNA homology to human RNF3A mRNA.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
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 [LARGE SCALE MRNA] OF 4-259 (ISOFORM 1).
RC TISSUE=Uterus;
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 TISSUE SPECIFICITY.
RX PubMed=11287196; DOI=10.1016/s0925-4773(01)00288-x;
RA Nunes M., Blanc I., Maes J., Fellous M., Robert B., McElreavey K.;
RT "NSPc1, a novel mammalian Polycomb gene, is expressed in neural crest-
RT derived structures of the peripheral nervous system.";
RL Mech. Dev. 102:219-222(2001).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, REGION, AND MUTAGENESIS OF TYR-109 AND
RP SER-195.
RX PubMed=15620699; DOI=10.1016/j.febslet.2004.11.056;
RA Gong Y., Wang X., Liu J., Shi L., Yin B., Peng X., Qiang B., Yuan J.;
RT "NSPc1, a mainly nuclear localized protein of novel PcG family members, has
RT a transcription repression activity related to its PKC phosphorylation site
RT at S183.";
RL FEBS Lett. 579:115-121(2005).
RN [6]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH RNF2; BCOR AND RING1.
RX PubMed=16943429; DOI=10.1128/mcb.00630-06;
RA Gearhart M.D., Corcoran C.M., Wamstad J.A., Bardwell V.J.;
RT "Polycomb group and SCF ubiquitin ligases are found in a novel BCOR complex
RT that is recruited to BCL6 targets.";
RL Mol. Cell. Biol. 26:6880-6889(2006).
RN [7]
RP FUNCTION.
RX PubMed=17088287; DOI=10.1093/nar/gkl834;
RA Gong Y., Yue J., Wu X., Wang X., Wen J., Lu L., Peng X., Qiang B., Yuan J.;
RT "NSPc1 is a cell growth regulator that acts as a transcriptional repressor
RT of p21Waf1/Cip1 via the RARE element.";
RL Nucleic Acids Res. 34:6158-6169(2006).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-3, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], 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 [9]
RP IDENTIFICATION IN A PRC1-LIKE COMPLEX, INTERACTION WITH CBX6; CBX7 AND
RP CBX8, AND SUBCELLULAR LOCATION.
RX PubMed=21282530; DOI=10.1074/mcp.m110.002642;
RA Vandamme J., Volkel P., Rosnoblet C., Le Faou P., Angrand P.O.;
RT "Interaction proteomics analysis of polycomb proteins defines distinct PRC1
RT Complexes in mammalian cells.";
RL Mol. Cell. Proteomics 0:0-0(2011).
RN [10]
RP FUNCTION, AND SUBUNIT.
RX PubMed=26151332; DOI=10.1038/ncomms8621;
RA Taherbhoy A.M., Huang O.W., Cochran A.G.;
RT "BMI1-RING1B is an autoinhibited RING E3 ubiquitin ligase.";
RL Nat. Commun. 6:7621-7621(2015).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND INTERACTION WITH DPPA4;
RP BCOR; NANOG; POU5F1; RNF2 AND RYBP.
RX PubMed=26687479; DOI=10.1038/srep18388;
RA Oliviero G., Munawar N., Watson A., Streubel G., Manning G., Bardwell V.,
RA Bracken A.P., Cagney G.;
RT "The variant Polycomb Repressor Complex 1 component PCGF1 interacts with a
RT pluripotency sub-network that includes DPPA4, a regulator of
RT embryogenesis.";
RL Sci. Rep. 5:18388-18388(2015).
RN [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-24 AND LYS-88, AND IDENTIFICATION
RP 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 [13]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 167-255 IN COMPLEXES WITH BCOR
RP AND BCORL1, INTERACTION WITH BCOR AND BCORL1, AND MUTAGENESIS OF TYR-191;
RP ARG-193 AND VAL-206.
RX PubMed=23523425; DOI=10.1016/j.str.2013.02.013;
RA Junco S.E., Wang R., Gaipa J.C., Taylor A.B., Schirf V., Gearhart M.D.,
RA Bardwell V.J., Demeler B., Hart P.J., Kim C.A.;
RT "Structure of the polycomb group protein PCGF1 in complex with BCOR reveals
RT basis for binding selectivity of PCGF homologs.";
RL Structure 21:665-671(2013).
RN [14] {ECO:0007744|PDB:5JH5}
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 150-255, AND SUBUNIT.
RX PubMed=27568929; DOI=10.1016/j.str.2016.07.011;
RA Wong S.J., Gearhart M.D., Taylor A.B., Nanyes D.R., Ha D.J., Robinson A.K.,
RA Artigas J.A., Lee O.J., Demeler B., Hart P.J., Bardwell V.J., Kim C.A.;
RT "KDM2B Recruitment of the Polycomb Group Complex, PRC1.1, Requires
RT Cooperation between PCGF1 and BCORL1.";
RL Structure 24:1795-1801(2016).
CC -!- FUNCTION: Component of the Polycomb group (PcG) multiprotein BCOR
CC complex, a complex required to maintain the transcriptionally
CC repressive state of some genes, such as BCL6 and the cyclin-dependent
CC kinase inhibitor, CDKN1A. Transcriptional repressor that may be
CC targeted to the DNA by BCL6; this transcription repressor activity may
CC be related to PKC signaling pathway. Represses CDKN1A expression by
CC binding to its promoter, and this repression is dependent on the
CC retinoic acid response element (RARE element). Promotes cell cycle
CC progression and enhances cell proliferation as well. May have a
CC positive role in tumor cell growth by down-regulating CDKN1A. Component
CC of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex
CC class required to maintain the transcriptionally repressive state of
CC many genes, including Hox genes, throughout development. PcG PRC1
CC complex acts via chromatin remodeling and modification of histones; it
CC mediates monoubiquitination of histone H2A 'Lys-119', rendering
CC chromatin heritably changed in its expressibility (PubMed:26151332).
CC Within the PRC1-like complex, regulates RNF2 ubiquitin ligase activity
CC (PubMed:26151332). Regulates the expression of DPPA4 and NANOG in the
CC NT2 embryonic carcinoma cells (PubMed:26687479).
CC {ECO:0000269|PubMed:15620699, ECO:0000269|PubMed:16943429,
CC ECO:0000269|PubMed:17088287, ECO:0000269|PubMed:26151332,
CC ECO:0000269|PubMed:26687479}.
CC -!- SUBUNIT: Interacts with BCORL1, forming heterodimers (PubMed:23523425,
CC PubMed:27568929). The PCGF1-BCORL1 heterodimeric complex interacts with
CC the KDM2B-SKP1 heterodimeric complex to form a homotetrameric polycomb
CC repression complex 1 (PRC1.1) (PubMed:27568929). Component of the
CC repressive BCOR complex containing a Polycomb group subcomplex at least
CC composed of RYBP, RING1 and RNF2/RING2 (PubMed:16943429). Specifically
CC interacts with BCOR, RING1 and RNF2/RING2 (PubMed:16943429,
CC PubMed:26687479, PubMed:23523425). Component of a PRC1-like complex
CC (PubMed:21282530, PubMed:26151332). Interacts with CBX6, CBX7 and CBX8
CC (PubMed:21282530). Interacts with DPPA4, NANOG, POU5F1 and RYBP
CC (PubMed:26687479). {ECO:0000269|PubMed:16943429,
CC ECO:0000269|PubMed:21282530, ECO:0000269|PubMed:23523425,
CC ECO:0000269|PubMed:26151332, ECO:0000269|PubMed:26687479,
CC ECO:0000269|PubMed:27568929}.
CC -!- INTERACTION:
CC Q9BSM1; Q6W2J9: BCOR; NbExp=13; IntAct=EBI-749901, EBI-950027;
CC Q9BSM1; O95931: CBX7; NbExp=2; IntAct=EBI-749901, EBI-3923843;
CC Q9BSM1; Q9HC52: CBX8; NbExp=7; IntAct=EBI-749901, EBI-712912;
CC Q9BSM1; A0A0C3SFZ9: FCHO1; NbExp=3; IntAct=EBI-749901, EBI-11977403;
CC Q9BSM1; Q06587: RING1; NbExp=9; IntAct=EBI-749901, EBI-752313;
CC Q9BSM1; Q99496: RNF2; NbExp=15; IntAct=EBI-749901, EBI-722416;
CC Q9BSM1-1; Q6W2J9-1: BCOR; NbExp=7; IntAct=EBI-16041863, EBI-16028932;
CC Q9BSM1-1; Q5H9F3-1: BCORL1; NbExp=6; IntAct=EBI-16041863, EBI-16041827;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15620699,
CC ECO:0000269|PubMed:21282530}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BSM1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BSM1-3; Sequence=VSP_036393;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11287196}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH04952.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAP97183.1; Type=Erroneous initiation; Note=Extended N-terminus.; 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; AF087884; AAP97183.1; ALT_INIT; mRNA.
DR EMBL; AC005041; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004952; AAH04952.1; ALT_INIT; mRNA.
DR CCDS; CCDS1946.2; -. [Q9BSM1-1]
DR RefSeq; NP_116062.2; NM_032673.2. [Q9BSM1-1]
DR PDB; 4HPL; X-ray; 2.00 A; B=167-255.
DR PDB; 4HPM; X-ray; 1.85 A; B/D=167-255.
DR PDB; 5JH5; X-ray; 2.55 A; C=150-255.
DR PDBsum; 4HPL; -.
DR PDBsum; 4HPM; -.
DR PDBsum; 5JH5; -.
DR AlphaFoldDB; Q9BSM1; -.
DR SMR; Q9BSM1; -.
DR BioGRID; 124243; 204.
DR CORUM; Q9BSM1; -.
DR DIP; DIP-52708N; -.
DR IntAct; Q9BSM1; 89.
DR MINT; Q9BSM1; -.
DR STRING; 9606.ENSP00000233630; -.
DR iPTMnet; Q9BSM1; -.
DR PhosphoSitePlus; Q9BSM1; -.
DR BioMuta; PCGF1; -.
DR DMDM; 223590124; -.
DR EPD; Q9BSM1; -.
DR jPOST; Q9BSM1; -.
DR MassIVE; Q9BSM1; -.
DR MaxQB; Q9BSM1; -.
DR PaxDb; Q9BSM1; -.
DR PeptideAtlas; Q9BSM1; -.
DR PRIDE; Q9BSM1; -.
DR ProteomicsDB; 78914; -. [Q9BSM1-1]
DR ProteomicsDB; 78915; -. [Q9BSM1-3]
DR Antibodypedia; 1867; 166 antibodies from 24 providers.
DR DNASU; 84759; -.
DR Ensembl; ENST00000233630.11; ENSP00000233630.6; ENSG00000115289.14. [Q9BSM1-1]
DR GeneID; 84759; -.
DR KEGG; hsa:84759; -.
DR MANE-Select; ENST00000233630.11; ENSP00000233630.6; NM_032673.3; NP_116062.2.
DR UCSC; uc002slz.4; human. [Q9BSM1-1]
DR CTD; 84759; -.
DR DisGeNET; 84759; -.
DR GeneCards; PCGF1; -.
DR HGNC; HGNC:17615; PCGF1.
DR HPA; ENSG00000115289; Low tissue specificity.
DR MIM; 610231; gene.
DR neXtProt; NX_Q9BSM1; -.
DR OpenTargets; ENSG00000115289; -.
DR PharmGKB; PA134976631; -.
DR VEuPathDB; HostDB:ENSG00000115289; -.
DR eggNOG; KOG2660; Eukaryota.
DR GeneTree; ENSGT00940000159651; -.
DR HOGENOM; CLU_046427_4_2_1; -.
DR InParanoid; Q9BSM1; -.
DR OMA; ISECSHT; -.
DR OrthoDB; 1203951at2759; -.
DR PhylomeDB; Q9BSM1; -.
DR TreeFam; TF324206; -.
DR PathwayCommons; Q9BSM1; -.
DR SignaLink; Q9BSM1; -.
DR SIGNOR; Q9BSM1; -.
DR BioGRID-ORCS; 84759; 69 hits in 1137 CRISPR screens.
DR ChiTaRS; PCGF1; human.
DR GeneWiki; PCGF1; -.
DR GenomeRNAi; 84759; -.
DR Pharos; Q9BSM1; Tbio.
DR PRO; PR:Q9BSM1; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9BSM1; protein.
DR Bgee; ENSG00000115289; Expressed in oocyte and 187 other tissues.
DR Genevisible; Q9BSM1; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0031519; C:PcG protein complex; IDA:UniProtKB.
DR GO; GO:0035102; C:PRC1 complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IBA:GO_Central.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0035518; P:histone H2A monoubiquitination; IDA:UniProtKB.
DR GO; GO:0036353; P:histone H2A-K119 monoubiquitination; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR IDEAL; IID00621; -.
DR InterPro; IPR032443; RAWUL.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF16207; RAWUL; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CHAIN 2..259
FT /note="Polycomb group RING finger protein 1"
FT /id="PRO_0000277855"
FT ZN_FING 47..86
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 86..247
FT /note="Required for repressor activity"
FT REGION 150..255
FT /note="Required for the interaction with the KDM2B-SKP1
FT heterodimeric complex"
FT /evidence="ECO:0000269|PubMed:27568929"
FT REGION 167..255
FT /note="RING-finger and WD40-associated ubiquitin-like
FT domain (RAWUL); sufficient for interaction with BCOR and
FT BCORL1"
FT /evidence="ECO:0000269|PubMed:23523425,
FT ECO:0000269|PubMed:27568929"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CROSSLNK 24
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 88
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..83
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_036393"
FT MUTAGEN 109
FT /note="Y->F: Marked decrease of repressor activity. May be
FT a kinase phosphorylation site."
FT /evidence="ECO:0000269|PubMed:15620699"
FT MUTAGEN 191
FT /note="Y->A: Abolishes interaction with BCOR and BCORL1."
FT /evidence="ECO:0000269|PubMed:23523425"
FT MUTAGEN 193
FT /note="R->A: Abolishes interaction with BCOR and BCORL1."
FT /evidence="ECO:0000269|PubMed:23523425"
FT MUTAGEN 195
FT /note="S->F: Abolishes repressor activity. May be a PKC
FT phosphorylation site."
FT /evidence="ECO:0000269|PubMed:15620699"
FT MUTAGEN 206
FT /note="V->D: Abolishes interaction with BCOR and BCORL1."
FT /evidence="ECO:0000269|PubMed:23523425"
FT TURN 158..161
FT /evidence="ECO:0007829|PDB:5JH5"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:5JH5"
FT STRAND 168..176
FT /evidence="ECO:0007829|PDB:4HPM"
FT STRAND 191..195
FT /evidence="ECO:0007829|PDB:4HPM"
FT HELIX 200..211
FT /evidence="ECO:0007829|PDB:4HPM"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:4HPM"
FT STRAND 219..222
FT /evidence="ECO:0007829|PDB:4HPM"
FT HELIX 233..240
FT /evidence="ECO:0007829|PDB:4HPM"
FT TURN 241..243
FT /evidence="ECO:0007829|PDB:4HPL"
FT STRAND 246..253
FT /evidence="ECO:0007829|PDB:4HPM"
SQ SEQUENCE 259 AA; 30346 MW; 456C9417E53A01B6 CRC64;
MASPQGGQIA IAMRLRNQLQ SVYKMDPLRN EEEVRVKIKD LNEHIVCCLC AGYFVDATTI
TECLHTFCKS CIVKYLQTSK YCPMCNIKIH ETQPLLNLKL DRVMQDIVYK LVPGLQDSEE
KRIREFYQSR GLDRVTQPTG EEPALSNLGL PFSSFDHSKA HYYRYDEQLN LCLERLSSGK
DKNKSVLQNK YVRCSVRAEV RHLRRVLCHR LMLNPQHVQL LFDNEVLPDH MTMKQIWLSR
WFGKPSPLLL QYSVKEKRR
