H33_XENLA
ID H33_XENLA Reviewed; 136 AA.
AC Q6PI79; Q05AX9;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Histone H3.3;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP METHYLATION AT LYS-5; LYS-10 AND ARG-18, PHOSPHORYLATION AT SER-11, AND
RP ACETYLATION AT LYS-15.
RX PubMed=12138181; DOI=10.1128/mcb.22.16.5688-5697.2002;
RA Li J., Lin Q., Yoon H.-G., Huang Z.-Q., Strahl B.D., Allis C.D., Wong J.;
RT "Involvement of histone methylation and phosphorylation in regulation of
RT transcription by thyroid hormone receptor.";
RL Mol. Cell. Biol. 22:5688-5697(2002).
CC -!- FUNCTION: Variant histone H3 which replaces conventional H3 in a wide
CC range of nucleosomes in active genes. Constitutes the predominant form
CC of histone H3 in non-dividing cells and is incorporated into chromatin
CC independently of DNA synthesis. Deposited at sites of nucleosomal
CC displacement throughout transcribed genes, suggesting that it
CC represents an epigenetic imprint of transcriptionally active chromatin.
CC Nucleosomes wrap and compact DNA into chromatin, limiting DNA
CC accessibility to the cellular machineries which require DNA as a
CC template. Histones thereby play a central role in transcription
CC regulation, DNA repair, DNA replication and chromosomal stability. DNA
CC accessibility is regulated via a complex set of post-translational
CC modifications of histones, also called histone code, and nucleosome
CC remodeling. {ECO:0000250|UniProtKB:P84243}.
CC -!- SUBUNIT: The nucleosome is a histone octamer containing two molecules
CC each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and
CC two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of
CC DNA. Interacts with zmynd11; when trimethylated at 'Lys-36'
CC (H3.3K36me3). {ECO:0000250|UniProtKB:P84243}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC -!- DEVELOPMENTAL STAGE: Expressed during S phase, then expression strongly
CC decreases as cell division slows down during the process of
CC differentiation.
CC -!- DOMAIN: Specific interaction of trimethylated form at 'Lys-36'
CC (H3.3K36me3) with zmynd11 is mediated by the encapsulation of Ser-32
CC residue with a composite pocket formed by the tandem bromo-PWWP
CC domains. {ECO:0000250|UniProtKB:P84243}.
CC -!- PTM: Acetylation is generally linked to gene activation. Acetylation on
CC Lys-19 (H3K18ac) and Lys-24 (H3K24ac) favors methylation at Arg-18
CC (H3R17me). Acetylation at Lys-123 (H3K122ac) by EP300/p300 plays a
CC central role in chromatin structure: localizes at the surface of the
CC histone octamer and stimulates transcription, possibly by promoting
CC nucleosome instability. {ECO:0000269|PubMed:12138181}.
CC -!- PTM: Asymmetric dimethylation at Arg-18 (H3R17me2a) is linked to gene
CC activation. Asymmetric dimethylation at Arg-3 (H3R2me2a) by PRMT6 is
CC linked to gene repression and is mutually exclusive with H3 Lys-5
CC methylation (H3K4me2 and H3K4me3). H3R2me2a is present at the 3' of
CC genes regardless of their transcription state and is enriched on
CC inactive promoters, while it is absent on active promoters (By
CC similarity). {ECO:0000250|UniProtKB:P84243}.
CC -!- PTM: Specifically enriched in modifications associated with active
CC chromatin such as methylation at Lys-5 (H3K4me), Lys-37 (H3K36me) and
CC Lys-80 (H3K79me) are linked to gene activation. Methylation at Lys-5
CC (H3K4me) facilitates subsequent acetylation of H3 and H4. Methylation
CC at Lys-80 (H3K79me) is associated with DNA double-strand break (DSB)
CC responses and is a specific target for tp53bp1. Methylation at Lys-10
CC (H3K9me) and Lys-28 (H3K27me) are linked to gene repression.
CC Methylation at Lys-10 (H3K9me) is a specific target for HP1 proteins
CC (cbx1, cbx3 and cbx5) and prevents subsequent phosphorylation at Ser-11
CC (H3S10ph) and acetylation of H3 and H4. Methylation at Lys-5 (H3K4me)
CC and Lys-80 (H3K79me) require preliminary monoubiquitination of H2B at
CC 'Lys-120' (By similarity). {ECO:0000250|UniProtKB:P84243}.
CC -!- PTM: Phosphorylated at Thr-4 (H3T3ph) by HASPIN during prophase and
CC dephosphorylated during anaphase. Phosphorylation at Ser-11 (H3S10ph)
CC by aurkb is crucial for chromosome condensation and cell-cycle
CC progression during mitosis and meiosis. In addition phosphorylation at
CC Ser-11 (H3S10ph) by rps6ka4 and rps6ka5 is important during interphase
CC because it enables the transcription of genes following external
CC stimulation, like mitogens, stress, growth factors or UV irradiation
CC and result in the activation of genes, such as c-fos and c-jun.
CC Phosphorylation at Ser-11 (H3S10ph), which is linked to gene
CC activation, prevents methylation at Lys-10 (H3K9me) but facilitates
CC acetylation of H3 and H4. Phosphorylation at Ser-11 (H3S10ph) by aurkb
CC mediates the dissociation of HP1 proteins (cbx1, cbx3 and cbx5) from
CC heterochromatin. Phosphorylation at Ser-11 (H3S10ph) is also an
CC essential regulatory mechanism for neoplastic cell transformation.
CC Phosphorylated at Ser-29 (H3S28ph) by map3k20 isoform 1, rps6ka5 or
CC aurkb during mitosis or upon ultraviolet B irradiation. Phosphorylation
CC at Thr-7 (H3T6ph) by prkcb is a specific tag for epigenetic
CC transcriptional activation that prevents demethylation of Lys-5
CC (H3K4me) by lsd1/kdm1a. At centromeres, specifically phosphorylated at
CC Thr-12 (H3T11ph) from prophase to early anaphase, by DAPK3 and PKN1.
CC Phosphorylation at Thr-12 (H3T11ph) by PKN1 or isoform M2 of PKM (PKM2)
CC is a specific tag for epigenetic transcriptional activation that
CC promotes demethylation of Lys-10 (H3K9me) by kdm4c/jmjd2c.
CC Phosphorylation at Tyr-42 (H3Y41ph) by jak2 promotes exclusion of cbx5
CC (HP1 alpha) from chromatin. Phosphorylation on Ser-32 (H3S31ph) is
CC specific to regions bordering centromeres in metaphase chromosomes.
CC {ECO:0000250|UniProtKB:P84243}.
CC -!- PTM: Monoubiquitinated by rag1 in lymphoid cells, monoubiquitination is
CC required for V(D)J recombination. {ECO:0000250|UniProtKB:P84243}.
CC -!- PTM: Lysine deamination at Lys-5 (H3K4all) to form allysine only takes
CC place on H3K4me3 and results in gene repression.
CC {ECO:0000250|UniProtKB:P84243}.
CC -!- PTM: Butyrylation of histones marks active promoters and competes with
CC histone acetylation. It is present during late spermatogenesis.
CC {ECO:0000250|UniProtKB:P68433}.
CC -!- PTM: Succinylation at Lys-80 (H3K79succ) by KAT2A takes place with a
CC maximum frequency around the transcription start sites of genes. It
CC gives a specific tag for epigenetic transcription activation.
CC Desuccinylation at Lys-123 (H3K122succ) by SIRT7 in response to DNA
CC damage promotes chromatin condensation and double-strand breaks (DSBs)
CC repair. {ECO:0000250|UniProtKB:P84243}.
CC -!- PTM: Serine ADP-ribosylation constitutes the primary form of ADP-
CC ribosylation of proteins in response to DNA damage. Serine ADP-
CC ribosylation at Ser-11 (H3S10ADPr) is mutually exclusive with
CC phosphorylation at Ser-11 (H3S10ph) and impairs acetylation at Lys-10
CC (H3K9ac). {ECO:0000250|UniProtKB:P68431}.
CC -!- PTM: Serotonylated by TGM2 at Gln-6 (H3Q5ser) during serotonergic
CC neuron differentiation (By similarity). H3Q5ser is associated with
CC trimethylation of Lys-5 (H3K4me3) and enhances general transcription
CC factor IID (TFIID) complex-binding to H3K4me3, thereby facilitating
CC transcription (By similarity). {ECO:0000250|UniProtKB:P84243}.
CC -!- PTM: Dopaminylated by TGM2 at Gln-6 (H3Q5dop) in ventral tegmental area
CC (VTA) neurons (By similarity). H3Q5dop mediates neurotransmission-
CC independent role of nuclear dopamine by regulating relapse-related
CC transcriptional plasticity in the reward system (By similarity).
CC {ECO:0000250|UniProtKB:P84243, ECO:0000250|UniProtKB:P84245}.
CC -!- PTM: Lactylated in macrophages by EP300/P300 by using lactoyl-CoA
CC directly derived from endogenous or exogenous lactate, leading to
CC stimulates gene transcription. {ECO:0000250|UniProtKB:P84243}.
CC -!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}.
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DR EMBL; BC041218; AAH41218.1; -; mRNA.
DR EMBL; BC042290; AAH42290.1; -; mRNA.
DR EMBL; BC042309; AAH42309.1; -; mRNA.
DR EMBL; BC070966; AAH70966.1; -; mRNA.
DR EMBL; BC074158; AAH74158.1; -; mRNA.
DR EMBL; BC106302; AAI06303.1; -; mRNA.
DR EMBL; BC123120; AAI23121.1; -; mRNA.
DR RefSeq; NP_001079375.1; NM_001085906.1.
DR RefSeq; NP_001080065.1; NM_001086596.1.
DR RefSeq; NP_001085048.1; NM_001091579.1.
DR RefSeq; NP_001086074.1; NM_001092605.1.
DR RefSeq; NP_001091902.1; NM_001098432.1.
DR RefSeq; XP_018091870.1; XM_018236381.1.
DR RefSeq; XP_018118148.1; XM_018262659.1.
DR RefSeq; XP_018119714.1; XM_018264225.1.
DR PDB; 6LTJ; EM; 3.70 A; A/E=1-136.
DR PDB; 7EA8; EM; 3.10 A; A/E=34-134.
DR PDBsum; 6LTJ; -.
DR PDBsum; 7EA8; -.
DR AlphaFoldDB; Q6PI79; -.
DR SASBDB; Q6PI79; -.
DR SMR; Q6PI79; -.
DR BioGRID; 102666; 1.
DR iPTMnet; Q6PI79; -.
DR DNASU; 108701569; -.
DR DNASU; 108716488; -.
DR DNASU; 379062; -.
DR DNASU; 379757; -.
DR DNASU; 399418; -.
DR DNASU; 432115; -.
DR DNASU; 444503; -.
DR GeneID; 108701569; -.
DR GeneID; 108716488; -.
DR GeneID; 379062; -.
DR GeneID; 379757; -.
DR GeneID; 399418; -.
DR GeneID; 432115; -.
DR GeneID; 444503; -.
DR KEGG; xla:108716488; -.
DR KEGG; xla:379062; -.
DR KEGG; xla:379757; -.
DR KEGG; xla:444503; -.
DR CTD; 379062; -.
DR CTD; 379757; -.
DR CTD; 399418; -.
DR CTD; 432115; -.
DR CTD; 444503; -.
DR Xenbase; XB-GENE-6253904; h3-3a.L.
DR Xenbase; XB-GENE-17337112; h3-3b.L.
DR Xenbase; XB-GENE-488762; h3-3b.S.
DR Xenbase; XB-GENE-6251829; h3-5.L.
DR Xenbase; XB-GENE-17346492; h3-5.S.
DR Xenbase; XB-GENE-5890272; h3c13.S.
DR OrthoDB; 1564596at2759; -.
DR Proteomes; UP000186698; Chromosome 5L.
DR Proteomes; UP000186698; Chromosome 5S.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Proteomes; UP000186698; Chromosome 9_10S.
DR Bgee; 108701569; Expressed in gastrula and 19 other tissues.
DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR007125; Histone_H2A/H2B/H3.
DR InterPro; IPR000164; Histone_H3/CENP-A.
DR PANTHER; PTHR11426; PTHR11426; 1.
DR Pfam; PF00125; Histone; 1.
DR PRINTS; PR00622; HISTONEH3.
DR SMART; SM00428; H3; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
DR PROSITE; PS00322; HISTONE_H3_1; 1.
DR PROSITE; PS00959; HISTONE_H3_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ADP-ribosylation; Chromosome; DNA-binding;
KW Hydroxylation; Methylation; Nucleosome core; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT CHAIN 2..136
FT /note="Histone H3.3"
FT /id="PRO_0000253957"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 32
FT /note="Interaction with zmynd11"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 3
FT /note="Asymmetric dimethylarginine; by PRMT6"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 4
FT /note="Phosphothreonine; by HASPIN"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 5
FT /note="Allysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 5
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:12138181"
FT MOD_RES 5
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:12138181"
FT MOD_RES 5
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 5
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 5
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:12138181"
FT MOD_RES 6
FT /note="5-glutamyl dopamine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 6
FT /note="5-glutamyl serotonin; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 7
FT /note="Phosphothreonine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 10
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 10
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 10
FT /note="N6-methylated lysine"
FT /evidence="ECO:0000269|PubMed:12138181"
FT MOD_RES 11
FT /note="ADP-ribosylserine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 11
FT /note="Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3,
FT RPS6KA4 and RPS6KA5"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 12
FT /note="Phosphothreonine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 15
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 15
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:12138181"
FT MOD_RES 15
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 15
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84244"
FT MOD_RES 18
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:12138181"
FT MOD_RES 19
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 19
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 19
FT /note="N6-butyryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68433"
FT MOD_RES 19
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 19
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 19
FT /note="N6-methylated lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 24
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 24
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 24
FT /note="N6-butyryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68433"
FT MOD_RES 24
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 24
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 28
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 28
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 28
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 28
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 28
FT /note="N6-methylated lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 29
FT /note="ADP-ribosylserine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 29
FT /note="Phosphoserine; alternate; by AURKB, AURKC and
FT RPS6KA5"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 37
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 37
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 37
FT /note="N6-methylated lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 42
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 57
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 57
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 57
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84244"
FT MOD_RES 57
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84244"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 65
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 65
FT /note="N6-methylated lysine"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 80
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 80
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 80
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 80
FT /note="N6-methylated lysine"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 80
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84244"
FT MOD_RES 81
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 116
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 116
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 123
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P68431"
FT MOD_RES 123
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 123
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 123
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT MOD_RES 123
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84243"
FT HELIX 46..57
FT /evidence="ECO:0007829|PDB:7EA8"
FT HELIX 65..76
FT /evidence="ECO:0007829|PDB:7EA8"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:7EA8"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:7EA8"
FT HELIX 88..114
FT /evidence="ECO:0007829|PDB:7EA8"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:7EA8"
FT HELIX 122..132
FT /evidence="ECO:0007829|PDB:7EA8"
SQ SEQUENCE 136 AA; 15328 MW; 5158ED279E6F9E1C CRC64;
MARTKQTARK STGGKAPRKQ LATKAARKSA PSTGGVKKPH RYRPGTVALR EIRRYQKSTE
LLIRKLPFQR LVREIAQDFK TDLRFQSAAI GALQEASEAY LVGLFEDTNL CAIHAKRVTI
MPKDIQLARR IRGERA
