KAT7_RAT
ID KAT7_RAT Reviewed; 612 AA.
AC Q810T5; Q80YN5;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Histone acetyltransferase KAT7 {ECO:0000305};
DE EC=2.3.1.48 {ECO:0000250|UniProtKB:O95251};
DE AltName: Full=Histone acetyltransferase binding to ORC1 {ECO:0000303|Ref.1};
DE AltName: Full=Lysine acetyltransferase 7;
DE AltName: Full=MOZ, YBF2/SAS3, SAS2 and TIP60 protein 2;
DE Short=MYST-2;
GN Name=Kat7 {ECO:0000312|RGD:727966};
GN Synonyms=Hbo1 {ECO:0000303|Ref.1}, Myst2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=Fischer 344; TISSUE=Testis;
RA Inaguma S., Ogawa K., Cho Y.-M., Ohnishi H., Asamoto M., Shirai T.;
RT "Identification of cDNA and expression of the gene encoding rat homolog of
RT HBO1.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58 AND SER-103, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Catalytic subunit of histone acetyltransferase HBO1
CC complexes, which specifically mediate acetylation of histone H3 at
CC 'Lys-14' (H3K14ac), thereby regulating various processes, such as gene
CC transcription, protein ubiquitination, immune regulation, stem cell
CC pluripotent and self-renewal maintenance and embryonic development.
CC Some complexes also catalyze acetylation of histone H4 at 'Lys-5',
CC 'Lys-8' and 'Lys-12' (H4K5ac, H4K8ac and H4K12ac, respectively),
CC regulating DNA replication initiation, regulating DNA replication
CC initiation. Specificity of the HBO1 complexes is determined by the
CC scaffold subunit: complexes containing BRPF scaffold (BRPF1, BRD1/BRPF2
CC or BRPF3) direct KAT7/HBO1 specificity towards H3K14ac, while complexes
CC containing JADE (JADE1, JADE2 and JADE3) scaffold direct KAT7/HBO1
CC specificity towards histone H4. H3K14ac promotes transcriptional
CC elongation by facilitating the processivity of RNA polymerase II. Acts
CC as a key regulator of hematopoiesis by forming a complex with
CC BRD1/BRPF2, directing KAT7/HBO1 specificity towards H3K14ac and
CC promoting erythroid differentiation (By similarity). H3K14ac is also
CC required for T-cell development (By similarity). KAT7/HBO1-mediated
CC acetylation facilitates two consecutive steps, licensing and
CC activation, in DNA replication initiation: H3K14ac facilitates the
CC activation of replication origins, and histone H4 acetylation (H4K5ac,
CC H4K8ac and H4K12ac) facilitates chromatin loading of MCM complexes,
CC promoting DNA replication licensing. Acts as a positive regulator of
CC centromeric CENPA assembly: recruited to centromeres and mediates
CC histone acetylation, thereby preventing centromere inactivation
CC mediated by SUV39H1, possibly by increasing histone turnover/exchange.
CC Involved in nucleotide excision repair: phosphorylation by ATR in
CC response to ultraviolet irradiation promotes its localization to DNA
CC damage sites, where it mediates histone acetylation to facilitate
CC recruitment of XPC at the damaged DNA sites. Acts as an inhibitor of
CC NF-kappa-B independently of its histone acetyltransferase activity (By
CC similarity). {ECO:0000250|UniProtKB:O95251,
CC ECO:0000250|UniProtKB:Q5SVQ0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[histone] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[histone]; Xref=Rhea:RHEA:21992, Rhea:RHEA-COMP:9845,
CC Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC Evidence={ECO:0000250|UniProtKB:O95251};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21993;
CC Evidence={ECO:0000250|UniProtKB:O95251};
CC -!- ACTIVITY REGULATION: Histone acetyltransferase activity is inhibited by
CC GMNN in the context of a complex with CDT1, inhibiting histone H4
CC acetylation and DNA replication licensing.
CC {ECO:0000250|UniProtKB:O95251}.
CC -!- PATHWAY: Protein degradation; proteasomal ubiquitin-dependent pathway.
CC {ECO:0000250|UniProtKB:Q5SVQ0}.
CC -!- SUBUNIT: Component of the HBO1 complex composed of KAT7/HBO1, MEAF6,
CC ING4 or ING5, and one scaffold subunit: complexes containing BRPF
CC scaffold (BRPF1, BRD1/BRPF2 or BRPF3) direct KAT7/HBO1 specificity
CC towards H3K14ac, while complexes containing JADE scaffold (JADE1, JADE2
CC and JADE3) mediate acetylation of histone H4. Interacts with MCM2 and
CC ORC1. Interacts with the androgen receptor (AR); in the presence of
CC dihydrotestosterone. Interacts with CDT1 (By similarity). Interacts
CC with MAP2K1 and CUL1 (By similarity). Interacts with p53/TP53; leading
CC to inhibit histone acetyltransferase activity. Interacts with MIS18BP1
CC (By similarity). {ECO:0000250|UniProtKB:O95251,
CC ECO:0000250|UniProtKB:Q5SVQ0}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O95251}.
CC Chromosome {ECO:0000250|UniProtKB:O95251}. Chromosome, centromere
CC {ECO:0000250|UniProtKB:O95251}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q5SVQ0}. Note=Associates with replication
CC origins specifically during the G1 phase of the cell cycle. Localizes
CC to transcription start sites. Localizes to ultraviolet-induced DNA
CC damage sites following phosphorylation by ATR. Localizes to centromeres
CC in G1 phase. {ECO:0000250|UniProtKB:O95251}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q810T5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q810T5-2; Sequence=VSP_014585;
CC -!- DOMAIN: The C2HC MYST-type zinc finger is required for interaction with
CC MCM2 and ORC1. {ECO:0000250|UniProtKB:O95251}.
CC -!- DOMAIN: The N-terminus is involved in transcriptional repression, while
CC the C-terminus mediates AR-interaction. {ECO:0000250|UniProtKB:O95251}.
CC -!- PTM: Phosphorylated at Ser-51 and Ser-54 by ATR in response to DNA
CC damage, promoting its ubiquitination by the CRL4(DDB2) complex and
CC subsequent degradation. Phosphorylation at Ser-51 and Ser-54 by ATR in
CC response to ultraviolet-induced DNA, promotes localization to DNA
CC damage sites. Phosphorylation at Ser-58 by PLK1 during mitosis seems
CC important for prereplicative complex formation and DNA replication
CC licensing, and requires prior phosphorylation at Thr-86 and Thr-89 by
CC CDK1 (By similarity). Phosphorylated by MAP2K1, which accelerates its
CC degradation (By similarity). {ECO:0000250|UniProtKB:O95251,
CC ECO:0000250|UniProtKB:Q5SVQ0}.
CC -!- PTM: Ubiquitinated at Lys-339, leading to proteasomal degradation.
CC Ubiquitinated by the CRL4(DDB2) complex following phosphorylation by
CC ATR, leading to its subsequent degradation.
CC {ECO:0000250|UniProtKB:O95251}.
CC -!- PTM: Autoacetylation at Lys-433 is required for proper function.
CC {ECO:0000250|UniProtKB:Q9H7Z6}.
CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family. {ECO:0000305}.
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DR EMBL; AY236854; AAO84914.1; -; mRNA.
DR EMBL; AY241457; AAO86770.1; -; mRNA.
DR RefSeq; NP_851595.1; NM_181081.2. [Q810T5-1]
DR AlphaFoldDB; Q810T5; -.
DR SMR; Q810T5; -.
DR iPTMnet; Q810T5; -.
DR PhosphoSitePlus; Q810T5; -.
DR jPOST; Q810T5; -.
DR Ensembl; ENSRNOT00000109616; ENSRNOP00000090504; ENSRNOG00000022664. [Q810T5-1]
DR GeneID; 303470; -.
DR KEGG; rno:303470; -.
DR UCSC; RGD:727966; rat. [Q810T5-1]
DR CTD; 11143; -.
DR RGD; 727966; Kat7.
DR GeneTree; ENSGT00940000157744; -.
DR InParanoid; Q810T5; -.
DR OrthoDB; 629545at2759; -.
DR PhylomeDB; Q810T5; -.
DR Reactome; R-RNO-3214847; HATs acetylate histones.
DR UniPathway; UPA00144; -.
DR PRO; PR:Q810T5; -.
DR Proteomes; UP000002494; Chromosome 10.
DR GO; GO:0005694; C:chromosome; ISO:RGD.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0000123; C:histone acetyltransferase complex; ISS:UniProtKB.
DR GO; GO:0036409; C:histone H3-K14 acetyltransferase complex; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0090734; C:site of DNA damage; ISS:UniProtKB.
DR GO; GO:0003688; F:DNA replication origin binding; ISO:RGD.
DR GO; GO:0004402; F:histone acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; ISS:UniProtKB.
DR GO; GO:0043966; P:histone H3 acetylation; ISS:UniProtKB.
DR GO; GO:0044154; P:histone H3-K14 acetylation; ISS:UniProtKB.
DR GO; GO:0043967; P:histone H4 acetylation; ISS:UniProtKB.
DR GO; GO:0043983; P:histone H4-K12 acetylation; ISS:UniProtKB.
DR GO; GO:0043981; P:histone H4-K5 acetylation; ISS:UniProtKB.
DR GO; GO:0043982; P:histone H4-K8 acetylation; ISS:UniProtKB.
DR GO; GO:0016570; P:histone modification; ISO:RGD.
DR GO; GO:0018393; P:internal peptidyl-lysine acetylation; ISS:UniProtKB.
DR GO; GO:0001779; P:natural killer cell differentiation; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0045740; P:positive regulation of DNA replication; ISS:UniProtKB.
DR GO; GO:0032786; P:positive regulation of DNA-templated transcription, elongation; ISS:UniProtKB.
DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; ISS:UniProtKB.
DR GO; GO:1902035; P:positive regulation of hematopoietic stem cell proliferation; ISS:UniProtKB.
DR GO; GO:0090240; P:positive regulation of histone H4 acetylation; ISO:RGD.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:RGD.
DR GO; GO:0001558; P:regulation of cell growth; ISO:RGD.
DR GO; GO:2000278; P:regulation of DNA biosynthetic process; ISO:RGD.
DR GO; GO:0006275; P:regulation of DNA replication; ISO:RGD.
DR GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; ISS:UniProtKB.
DR GO; GO:2000819; P:regulation of nucleotide-excision repair; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0072716; P:response to actinomycin D; ISO:RGD.
DR GO; GO:0072739; P:response to anisomycin; ISO:RGD.
DR GO; GO:0072720; P:response to dithiothreitol; ISO:RGD.
DR GO; GO:0072710; P:response to hydroxyurea; ISO:RGD.
DR GO; GO:0072708; P:response to sorbitol; ISO:RGD.
DR GO; GO:0031098; P:stress-activated protein kinase signaling cascade; ISO:RGD.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR002717; HAT_MYST-type.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR040706; Zf-MYST.
DR InterPro; IPR002515; Znf_C2H2C.
DR InterPro; IPR036060; Znf_C2H2C_sf.
DR Pfam; PF01853; MOZ_SAS; 1.
DR Pfam; PF01530; zf-C2HC; 1.
DR Pfam; PF17772; zf-MYST; 1.
DR SUPFAM; SSF103637; SSF103637; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51726; MYST_HAT; 1.
DR PROSITE; PS51802; ZF_CCHHC; 1.
PE 1: Evidence at protein level;
KW Acetylation; Acyltransferase; Alternative splicing; Centromere;
KW Chromatin regulator; Chromosome; Cytoplasm; DNA damage; DNA repair;
KW DNA replication; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation; Transferase;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..612
FT /note="Histone acetyltransferase KAT7"
FT /id="PRO_0000051571"
FT DOMAIN 333..608
FT /note="MYST-type HAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT ZN_FING 177..220
FT /note="CCHHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT ZN_FING 366..391
FT /note="C2HC MYST-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT REGION 1..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 509
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 204
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 210
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 369
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O95251"
FT BINDING 372
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O95251"
FT BINDING 385
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O95251"
FT BINDING 389
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O95251"
FT BINDING 476..478
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:O95251"
FT BINDING 484..489
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:O95251"
FT BINDING 513
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:O95251"
FT BINDING 522
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:O95251"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95251"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95251"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95251"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95251"
FT MOD_RES 86
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:O95251"
FT MOD_RES 89
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:O95251"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 105
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5SVQ0"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95251"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95251"
FT MOD_RES 129
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5SVQ0"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95251"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95251"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95251"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95251"
FT MOD_RES 200
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O95251"
FT MOD_RES 278
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q5SVQ0"
FT MOD_RES 433
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT MOD_RES 507
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95251"
FT CROSSLNK 324
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O95251"
FT CROSSLNK 339
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:O95251"
FT VAR_SEQ 223..252
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_014585"
SQ SEQUENCE 612 AA; 70514 MW; A73190BCEBD975CD CRC64;
MAIGVKRNAG SSSDGTEDSD FSTDLEHTDS SESDGTSRRS ARVTRSSARL SQSSQDSSPV
RNLPSFGTEE PAYSTRRVTR SQQQPTPVTP KKYPLRQTRS SGSETEQAVD FSDRETKNTA
DHDESPPRTP TGNAPSSESD IDISSPNVSH DESIAKDMSL KDSGSDLSHR PKRRRFHESY
NFNMKCPTPG CNSLGHLTGK HERHFSISGC PLYHNLSADE CKVRAQSRDK QIEERMLSHR
QDDNNRHATR HQAPTERQLR YKEKVAELRK KRNSGLSKEQ KEKYMEHRQT YGNTREPLLE
NLTSEYDLDL FRRAQARASE DLEKLRLQGQ ITEGSNMIKT IAFGRYELDT WYHSPYPEEY
ARLGRLYMCE FCLKYMKSQT ILRRHMAKCV WKHPPGDEIY RKGSISVFEV DGKKNKIYCQ
NLCLLAKLFL DHKTLYYDVE PFLFYVMTEA DNTGCHLIGY FSKEKNSFLN YNVSCILTMP
QYMRQGYGKM LIDFSYLLSK VEEKVGSPER PLSDLGLISY RSYWKEVLLR YLHNFQGKEI
SIKEISQETA VNPVDIVSTL QALQMLKYWK GKHLVLKRQD LIDEWIAKEA KRSNSNKTMD
PSCLKWTPPK GT
