SAP30_HUMAN
ID SAP30_HUMAN Reviewed; 220 AA.
AC O75446; D3DP38;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Histone deacetylase complex subunit SAP30;
DE AltName: Full=30 kDa Sin3-associated polypeptide;
DE AltName: Full=Sin3 corepressor complex subunit SAP30;
DE AltName: Full=Sin3-associated polypeptide p30;
GN Name=SAP30 {ECO:0000312|HGNC:HGNC:10532};
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] {ECO:0000305, ECO:0000312|EMBL:AAC33316.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH HDAC1.
RC TISSUE=Cervix carcinoma;
RX PubMed=9651585; DOI=10.1016/s1097-2765(00)80102-1;
RA Zhang Y., Sun Z.-W., Iratni R., Erdjument-Bromage H., Tempst P.,
RA Hampsey M., Reinberg D.;
RT "SAP30, a novel protein conserved between human and yeast, is a component
RT of a histone deacetylase complex.";
RL Mol. Cell 1:1021-1031(1998).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=9702189; DOI=10.1016/s1097-2765(00)80111-2;
RA Laherty C.D., Billin A.N., Lavinsky R.M., Yochum G.S., Bush A.C.,
RA Sun J.-M., Mullen T.-M., Davie J.R., Rose D.W., Glass C.K., Rosenfeld M.G.,
RA Ayer D.E., Eisenman R.N.;
RT "SAP30, a component of the mSin3 corepressor complex involved in N-CoR-
RT mediated repression by specific transcription factors.";
RL Mol. Cell 2:33-42(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000312|EMBL:AAH16757.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain {ECO:0000312|EMBL:AAH16757.1};
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 [5] {ECO:0000305}
RP INTERACTION WITH HCFC1.
RX PubMed=12670868; DOI=10.1101/gad.252103;
RA Wysocka J., Myers M.P., Laherty C.D., Eisenman R.N., Herr W.;
RT "Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4
RT methyltransferase are tethered together selectively by the cell-
RT proliferation factor HCF-1.";
RL Genes Dev. 17:896-911(2003).
RN [6]
RP INTERACTION WITH SAP30BP.
RX PubMed=15496587; DOI=10.1093/jb/mvh108;
RA Li J.-F., Liu L.-D., Ma S.-H., Che Y.-C., Wang L.-C., Dong C.-H.,
RA Zhao H.-L., Liao Y., Li Q.-H.;
RT "HTRP -- an immediate-early gene product induced by HSV1 infection in human
RT embryo fibroblasts, is involved in cellular co-repressors.";
RL J. Biochem. 136:169-176(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131 AND SER-138, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131; SER-138 AND THR-145, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131 AND SER-138, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, AND IDENTIFICATION BY
RP 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 [11]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=21221920; DOI=10.1007/s12250-010-3147-8;
RA Chen J., Li Y.M., Li J.F., Liu L.D., Liao Y., Na R.X., Wang J.J.,
RA Wang L.C., Li Q.H.;
RT "Transcriptional regulation by HSV-1 induced HTRP via acetylation system.";
RL Virol. Sin. 25:417-424(2010).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131 AND SER-138, 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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-5, AND IDENTIFICATION BY MASS
RP 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 [15]
RP IDENTIFICATION BY 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 [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-214, AND IDENTIFICATION BY MASS
RP 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 [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-87; LYS-194; LYS-205 AND LYS-214,
RP 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).
RN [18]
RP STRUCTURE BY NMR OF 64-131, DNA-BINDING, ZINC-FINGER, AND MUTAGENESIS OF
RP CYS-67; CYS-68; HIS-108 AND CYS-112.
RX PubMed=19223330; DOI=10.1093/nar/gkp051;
RA He Y., Imhoff R., Sahu A., Radhakrishnan I.;
RT "Solution structure of a novel zinc finger motif in the SAP30 polypeptide
RT of the Sin3 corepressor complex and its potential role in nucleic acid
RT recognition.";
RL Nucleic Acids Res. 37:2142-2152(2009).
CC -!- FUNCTION: Involved in the functional recruitment of the Sin3-histone
CC deacetylase complex (HDAC) to a specific subset of N-CoR corepressor
CC complexes. Capable of transcription repression by N-CoR. Active in
CC deacetylating core histone octamers (when in a complex) but inactive in
CC deacetylating nucleosomal histones. {ECO:0000250|UniProtKB:O88574,
CC ECO:0000269|PubMed:9651585}.
CC -!- FUNCTION: (Microbial infection) Involved in transcriptional repression
CC of HHV-1 genes TK and gC. {ECO:0000269|PubMed:21221920}.
CC -!- SUBUNIT: Component of the histone deacetylase complex that includes at
CC least SIN3A, HDAC1 and HDAC2 (By similarity). Found in a complex
CC composed of at least SINHCAF, SIN3A, HDAC1, SAP30, RBBP4, OGT and TET1
CC (By similarity). Interacts with HDAC1 (PubMed:9651585). Interacts with
CC SIN3A, SIN3B, HDAC2, RBBP4 and NCOR1 (By similarity). Interacts with
CC SAMSN1 (By similarity). Interacts with HCFC1 (PubMed:12670868).
CC Interacts with SAP30BP (PubMed:15496587).
CC {ECO:0000250|UniProtKB:O88574, ECO:0000269|PubMed:12670868,
CC ECO:0000269|PubMed:15496587, ECO:0000269|PubMed:9651585}.
CC -!- INTERACTION:
CC O75446; Q92870-2: APBB2; NbExp=3; IntAct=EBI-632609, EBI-21535880;
CC O75446; O95817: BAG3; NbExp=3; IntAct=EBI-632609, EBI-747185;
CC O75446; Q01658: DR1; NbExp=3; IntAct=EBI-632609, EBI-750300;
CC O75446; P26378-2: ELAVL4; NbExp=3; IntAct=EBI-632609, EBI-21603100;
CC O75446; Q00403: GTF2B; NbExp=3; IntAct=EBI-632609, EBI-389564;
CC O75446; Q9Y5Q9: GTF3C3; NbExp=3; IntAct=EBI-632609, EBI-1054873;
CC O75446; P42858: HTT; NbExp=3; IntAct=EBI-632609, EBI-466029;
CC O75446; Q92597: NDRG1; NbExp=3; IntAct=EBI-632609, EBI-716486;
CC O75446; Q8N2W9: PIAS4; NbExp=3; IntAct=EBI-632609, EBI-473160;
CC O75446; P37840: SNCA; NbExp=3; IntAct=EBI-632609, EBI-985879;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested with highest levels
CC in pancreas, ovary, PBL, spleen and thymus; lowest levels in brain,
CC placenta, lung and kidney. {ECO:0000269|PubMed:9702189}.
CC -!- SIMILARITY: Belongs to the SAP30 family. {ECO:0000305}.
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DR EMBL; AF055993; AAC33316.1; -; mRNA.
DR EMBL; CH471056; EAX04755.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX04756.1; -; Genomic_DNA.
DR EMBL; BC016757; AAH16757.1; -; mRNA.
DR CCDS; CCDS3817.1; -.
DR RefSeq; NP_003855.1; NM_003864.3.
DR PDB; 2KDP; NMR; -; A=64-131.
DR PDBsum; 2KDP; -.
DR AlphaFoldDB; O75446; -.
DR SMR; O75446; -.
DR BioGRID; 114346; 122.
DR ComplexPortal; CPX-3321; SIN3A histone deacetylase complex.
DR ComplexPortal; CPX-3322; SIN3B histone deacetylase complex.
DR ComplexPortal; CPX-3323; SIN3A histone deacetylase complex, ES cell-specific variant.
DR CORUM; O75446; -.
DR DIP; DIP-33328N; -.
DR IntAct; O75446; 52.
DR MINT; O75446; -.
DR STRING; 9606.ENSP00000296504; -.
DR CarbonylDB; O75446; -.
DR GlyConnect; 787; 2 N-Linked glycans (2 sites).
DR GlyGen; O75446; 2 sites, 3 N-linked glycans (2 sites).
DR iPTMnet; O75446; -.
DR PhosphoSitePlus; O75446; -.
DR BioMuta; SAP30; -.
DR EPD; O75446; -.
DR jPOST; O75446; -.
DR MassIVE; O75446; -.
DR MaxQB; O75446; -.
DR PaxDb; O75446; -.
DR PeptideAtlas; O75446; -.
DR PRIDE; O75446; -.
DR ProteomicsDB; 50014; -.
DR Antibodypedia; 17174; 186 antibodies from 28 providers.
DR DNASU; 8819; -.
DR Ensembl; ENST00000296504.4; ENSP00000296504.3; ENSG00000164105.4.
DR GeneID; 8819; -.
DR KEGG; hsa:8819; -.
DR MANE-Select; ENST00000296504.4; ENSP00000296504.3; NM_003864.4; NP_003855.1.
DR UCSC; uc003itd.4; human.
DR CTD; 8819; -.
DR GeneCards; SAP30; -.
DR HGNC; HGNC:10532; SAP30.
DR HPA; ENSG00000164105; Low tissue specificity.
DR MIM; 603378; gene.
DR neXtProt; NX_O75446; -.
DR OpenTargets; ENSG00000164105; -.
DR PharmGKB; PA34941; -.
DR VEuPathDB; HostDB:ENSG00000164105; -.
DR eggNOG; ENOG502QWFH; Eukaryota.
DR GeneTree; ENSGT00390000006633; -.
DR HOGENOM; CLU_097961_0_0_1; -.
DR InParanoid; O75446; -.
DR OMA; MNGFAPE; -.
DR OrthoDB; 1520155at2759; -.
DR PhylomeDB; O75446; -.
DR TreeFam; TF324135; -.
DR PathwayCommons; O75446; -.
DR Reactome; R-HSA-3214815; HDACs deacetylate histones.
DR Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
DR Reactome; R-HSA-9679191; Potential therapeutics for SARS.
DR SignaLink; O75446; -.
DR BioGRID-ORCS; 8819; 15 hits in 1087 CRISPR screens.
DR EvolutionaryTrace; O75446; -.
DR GeneWiki; SAP30; -.
DR GenomeRNAi; 8819; -.
DR Pharos; O75446; Tbio.
DR PRO; PR:O75446; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; O75446; protein.
DR Bgee; ENSG00000164105; Expressed in secondary oocyte and 181 other tissues.
DR Genevisible; O75446; HS.
DR GO; GO:0000118; C:histone deacetylase complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0016580; C:Sin3 complex; IC:ComplexPortal.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
DR GO; GO:0052472; P:modulation by host of symbiont transcription; IDA:UniProtKB.
DR GO; GO:0030336; P:negative regulation of cell migration; IC:ComplexPortal.
DR GO; GO:1902455; P:negative regulation of stem cell population maintenance; IC:ComplexPortal.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IC:ComplexPortal.
DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; IC:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IEA:Ensembl.
DR Gene3D; 6.10.160.20; -; 1.
DR InterPro; IPR024145; His_deAcase_SAP30/SAP30L.
DR InterPro; IPR038291; SAP30_C_sf.
DR InterPro; IPR025718; SAP30_Sin3-bd.
DR InterPro; IPR025717; SAP30_zn-finger.
DR PANTHER; PTHR13286; PTHR13286; 1.
DR Pfam; PF13867; SAP30_Sin3_bdg; 1.
DR Pfam; PF13866; zf-SAP30; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..220
FT /note="Histone deacetylase complex subunit SAP30"
FT /id="PRO_0000097582"
FT ZN_FING 67..115
FT /note="Atypical"
FT REGION 1..129
FT /note="Interaction with NCOR1"
FT /evidence="ECO:0000250"
FT REGION 123..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..220
FT /note="Interaction with SIN3A"
FT /evidence="ECO:0000250"
FT MOD_RES 5
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 145
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CROSSLNK 87
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 194
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 205
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 214
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 MUTAGEN 67
FT /note="C->A: Abolishes zinc-binding."
FT /evidence="ECO:0000269|PubMed:19223330"
FT MUTAGEN 68
FT /note="C->A: Retains zinc-binding."
FT /evidence="ECO:0000269|PubMed:19223330"
FT MUTAGEN 108
FT /note="H->A: Retains zinc-binding."
FT /evidence="ECO:0000269|PubMed:19223330"
FT MUTAGEN 112
FT /note="C->A: Abolishes zinc-binding."
FT /evidence="ECO:0000269|PubMed:19223330"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:2KDP"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:2KDP"
FT HELIX 87..96
FT /evidence="ECO:0007829|PDB:2KDP"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:2KDP"
FT HELIX 113..120
FT /evidence="ECO:0007829|PDB:2KDP"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:2KDP"
SQ SEQUENCE 220 AA; 23306 MW; FF84E06B17AFCAC2 CRC64;
MNGFTPDEMS RGGDAAAAVA AVVAAAAAAA SAGNGTGAGT GAEVPGAGAV SAAGPPGAAG
PGPGQLCCLR EDGERCGRAA GNASFSKRIQ KSISQKKVKI ELDKSARHLY ICDYHKNLIQ
SVRNRRKRKG SDDDGGDSPV QDIDTPEVDL YQLQVNTLRR YKRHFKLPTR PGLNKAQLVE
IVGCHFRSIP VNEKDTLTYF IYSVKNDKNK SDLKVDSGVH
