H2AV_HUMAN
ID H2AV_HUMAN Reviewed; 128 AA.
AC Q71UI9; A6NFA8; A6NKY0; A6NN01; A8MQC5; Q59GV8; Q6PK98;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Histone H2A.V;
DE AltName: Full=H2A.F/Z;
DE AltName: Full=H2A.Z variant histone 2 {ECO:0000312|HGNC:HGNC:20664};
GN Name=H2AZ2 {ECO:0000312|HGNC:HGNC:20664};
GN Synonyms=H2AFV {ECO:0000312|HGNC:HGNC:20664}, H2AV;
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 1).
RA Groitl P., Wolf H., Niller H.H.;
RT "Novel human member of the variant histone family.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC TISSUE=Kidney, Ovarian adenocarcinoma, Prostatic carcinoma, Skin, and
RC 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 [7]
RP MASS SPECTROMETRY.
RX PubMed=16457589; DOI=10.1021/pr050269n;
RA Boyne M.T. II, Pesavento J.J., Mizzen C.A., Kelleher N.L.;
RT "Precise characterization of human histones in the H2A gene family by top
RT down mass spectrometry.";
RL J. Proteome Res. 5:248-253(2006).
CC -!- FUNCTION: Variant histone H2A which replaces conventional H2A in a
CC subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin,
CC limiting DNA accessibility to the cellular machineries which require
CC DNA as a template. Histones thereby play a central role in
CC transcription regulation, DNA repair, DNA replication and chromosomal
CC stability. DNA accessibility is regulated via a complex set of post-
CC translational modifications of histones, also called histone code, and
CC nucleosome remodeling. May be involved in the formation of constitutive
CC heterochromatin. May be required for chromosome segregation during cell
CC division (By similarity). {ECO:0000250}.
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. H2A or its variant H2AZ2 forms a heterodimer with H2B (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q71UI9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q71UI9-2; Sequence=VSP_042855;
CC Name=3;
CC IsoId=Q71UI9-3; Sequence=VSP_044633;
CC Name=4;
CC IsoId=Q71UI9-4; Sequence=VSP_045232;
CC Name=5;
CC IsoId=Q71UI9-5; Sequence=VSP_046783;
CC -!- PTM: Monoubiquitination of Lys-122 gives a specific tag for epigenetic
CC transcriptional repression. {ECO:0000250}.
CC -!- PTM: Acetylated on Lys-5, Lys-8 and Lys-12 during interphase.
CC Acetylation disappears at mitosis (By similarity). {ECO:0000250}.
CC -!- MASS SPECTROMETRY: Mass=13369.4; Method=Electrospray;
CC Note=Monoisotopic, not modified.;
CC Evidence={ECO:0000269|PubMed:16457589};
CC -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92238.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF081192; AAC31938.1; -; mRNA.
DR EMBL; AK023973; BAG51243.1; -; mRNA.
DR EMBL; AB209001; BAD92238.1; ALT_INIT; mRNA.
DR EMBL; AC004854; AAS00365.1; -; Genomic_DNA.
DR EMBL; CH471128; EAW61075.1; -; Genomic_DNA.
DR EMBL; CH471128; EAW61077.1; -; Genomic_DNA.
DR EMBL; BC000098; AAH00098.1; -; mRNA.
DR EMBL; BC004274; AAH04274.3; -; mRNA.
DR EMBL; BC014885; AAH14885.1; -; mRNA.
DR EMBL; BC070169; AAH70169.1; -; mRNA.
DR EMBL; BE742590; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BU543626; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS47581.1; -. [Q71UI9-5]
DR CCDS; CCDS5495.1; -. [Q71UI9-2]
DR CCDS; CCDS5496.1; -. [Q71UI9-1]
DR CCDS; CCDS5497.1; -. [Q71UI9-4]
DR CCDS; CCDS5498.1; -. [Q71UI9-3]
DR RefSeq; NP_036544.1; NM_012412.4. [Q71UI9-1]
DR RefSeq; NP_619541.1; NM_138635.3. [Q71UI9-2]
DR RefSeq; NP_958844.1; NM_201436.2. [Q71UI9-4]
DR RefSeq; NP_958924.1; NM_201516.2. [Q71UI9-5]
DR RefSeq; NP_958925.1; NM_201517.2. [Q71UI9-3]
DR PDB; 3WAA; X-ray; 3.20 A; C/G=1-128.
DR PDB; 6M4D; EM; 4.40 A; C/G=1-108.
DR PDBsum; 3WAA; -.
DR PDBsum; 6M4D; -.
DR AlphaFoldDB; Q71UI9; -.
DR SMR; Q71UI9; -.
DR BioGRID; 125150; 98.
DR ComplexPortal; CPX-5671; Nucleosome, variant H3.1-H2A.V-H2B.1.
DR IntAct; Q71UI9; 32.
DR MINT; Q71UI9; -.
DR STRING; 9606.ENSP00000308405; -.
DR GlyGen; Q71UI9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q71UI9; -.
DR PhosphoSitePlus; Q71UI9; -.
DR SwissPalm; Q71UI9; -.
DR BioMuta; H2AFV; -.
DR DMDM; 74749787; -.
DR EPD; Q71UI9; -.
DR jPOST; Q71UI9; -.
DR MassIVE; Q71UI9; -.
DR MaxQB; Q71UI9; -.
DR PaxDb; Q71UI9; -.
DR PeptideAtlas; Q71UI9; -.
DR PRIDE; Q71UI9; -.
DR ProteomicsDB; 1035; -.
DR ProteomicsDB; 1437; -.
DR ProteomicsDB; 1947; -.
DR ProteomicsDB; 68632; -. [Q71UI9-1]
DR ProteomicsDB; 68633; -. [Q71UI9-2]
DR TopDownProteomics; Q71UI9-1; -. [Q71UI9-1]
DR TopDownProteomics; Q71UI9-3; -. [Q71UI9-3]
DR TopDownProteomics; Q71UI9-4; -. [Q71UI9-4]
DR Antibodypedia; 27370; 100 antibodies from 16 providers.
DR DNASU; 94239; -.
DR Ensembl; ENST00000222690.10; ENSP00000222690.6; ENSG00000105968.19. [Q71UI9-2]
DR Ensembl; ENST00000308153.9; ENSP00000308405.5; ENSG00000105968.19. [Q71UI9-1]
DR Ensembl; ENST00000349299.7; ENSP00000342714.3; ENSG00000105968.19. [Q71UI9-3]
DR Ensembl; ENST00000350771.7; ENSP00000340708.3; ENSG00000105968.19. [Q71UI9-4]
DR Ensembl; ENST00000381124.9; ENSP00000370516.5; ENSG00000105968.19. [Q71UI9-5]
DR GeneID; 94239; -.
DR KEGG; hsa:94239; -.
DR MANE-Select; ENST00000308153.9; ENSP00000308405.5; NM_012412.5; NP_036544.1.
DR UCSC; uc003tlz.3; human. [Q71UI9-1]
DR CTD; 94239; -.
DR DisGeNET; 94239; -.
DR GeneCards; H2AZ2; -.
DR HGNC; HGNC:20664; H2AZ2.
DR HPA; ENSG00000105968; Low tissue specificity.
DR neXtProt; NX_Q71UI9; -.
DR OpenTargets; ENSG00000105968; -.
DR VEuPathDB; HostDB:ENSG00000105968; -.
DR eggNOG; KOG1757; Eukaryota.
DR GeneTree; ENSGT00900000140979; -.
DR HOGENOM; CLU_062828_2_4_1; -.
DR InParanoid; Q71UI9; -.
DR OMA; FPCGRIK; -.
DR OrthoDB; 1504122at2759; -.
DR PhylomeDB; Q71UI9; -.
DR TreeFam; TF354232; -.
DR PathwayCommons; Q71UI9; -.
DR Reactome; R-HSA-110328; Recognition and association of DNA glycosylase with site containing an affected pyrimidine.
DR Reactome; R-HSA-110329; Cleavage of the damaged pyrimidine.
DR Reactome; R-HSA-110330; Recognition and association of DNA glycosylase with site containing an affected purine.
DR Reactome; R-HSA-110331; Cleavage of the damaged purine.
DR Reactome; R-HSA-1221632; Meiotic synapsis.
DR Reactome; R-HSA-171306; Packaging Of Telomere Ends.
DR Reactome; R-HSA-1912408; Pre-NOTCH Transcription and Translation.
DR Reactome; R-HSA-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-HSA-212300; PRC2 methylates histones and DNA.
DR Reactome; R-HSA-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR Reactome; R-HSA-2559586; DNA Damage/Telomere Stress Induced Senescence.
DR Reactome; R-HSA-3214858; RMTs methylate histone arginines.
DR Reactome; R-HSA-427359; SIRT1 negatively regulates rRNA expression.
DR Reactome; R-HSA-427389; ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.
DR Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
DR Reactome; R-HSA-5250924; B-WICH complex positively regulates rRNA expression.
DR Reactome; R-HSA-5334118; DNA methylation.
DR Reactome; R-HSA-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
DR Reactome; R-HSA-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
DR Reactome; R-HSA-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR Reactome; R-HSA-68616; Assembly of the ORC complex at the origin of replication.
DR Reactome; R-HSA-73728; RNA Polymerase I Promoter Opening.
DR Reactome; R-HSA-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-HSA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR Reactome; R-HSA-912446; Meiotic recombination.
DR Reactome; R-HSA-9616222; Transcriptional regulation of granulopoiesis.
DR Reactome; R-HSA-9670095; Inhibition of DNA recombination at telomere.
DR Reactome; R-HSA-9710421; Defective pyroptosis.
DR SignaLink; Q71UI9; -.
DR SIGNOR; Q71UI9; -.
DR BioGRID-ORCS; 94239; 11 hits in 1087 CRISPR screens.
DR ChiTaRS; H2AFV; human.
DR GeneWiki; H2AFV; -.
DR GenomeRNAi; 94239; -.
DR Pharos; Q71UI9; Tbio.
DR PRO; PR:Q71UI9; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q71UI9; protein.
DR Bgee; ENSG00000105968; Expressed in ventricular zone and 205 other tissues.
DR ExpressionAtlas; Q71UI9; baseline and differential.
DR Genevisible; Q71UI9; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0000786; C:nucleosome; IPI:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR CDD; cd00074; H2A; 1.
DR DisProt; DP02301; -.
DR Gene3D; 1.10.20.10; -; 1.
DR IDEAL; IID00614; -.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR002119; Histone_H2A.
DR InterPro; IPR007125; Histone_H2A/H2B/H3.
DR InterPro; IPR032454; Histone_H2A_C.
DR InterPro; IPR032458; Histone_H2A_CS.
DR PANTHER; PTHR23430; PTHR23430; 1.
DR Pfam; PF00125; Histone; 1.
DR Pfam; PF16211; Histone_H2A_C; 1.
DR PRINTS; PR00620; HISTONEH2A.
DR SMART; SM00414; H2A; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
DR PROSITE; PS00046; HISTONE_H2A; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Chromosome; DNA-binding;
KW Nucleosome core; Nucleus; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT CHAIN 2..128
FT /note="Histone H2A.V"
FT /id="PRO_0000239068"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 5
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q3THW5"
FT MOD_RES 8
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q3THW5"
FT MOD_RES 12
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q3THW5"
FT MOD_RES 12
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0C0S5"
FT MOD_RES 14
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0C0S5"
FT MOD_RES 116
FT /note="N6-lactoyllysine"
FT /evidence="ECO:0000250|UniProtKB:P0C0S5"
FT VAR_SEQ 1..27
FT /note="MAGGKAGKDSGKAKAKAVSRSQRAGLQ -> M (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045232"
FT VAR_SEQ 28..65
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_044633"
FT VAR_SEQ 67..128
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_046783"
FT VAR_SEQ 109..128
FT /note="GVIPHIHKSLIGKKGQQKTA -> EKRRCS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042855"
FT VARIANT 125
FT /note="Q -> R (in dbSNP:rs1802437)"
FT /id="VAR_059312"
FT HELIX 20..23
FT /evidence="ECO:0007829|PDB:3WAA"
FT HELIX 30..38
FT /evidence="ECO:0007829|PDB:3WAA"
FT HELIX 49..75
FT /evidence="ECO:0007829|PDB:3WAA"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:3WAA"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:3WAA"
FT HELIX 84..93
FT /evidence="ECO:0007829|PDB:3WAA"
FT HELIX 95..100
FT /evidence="ECO:0007829|PDB:3WAA"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:3WAA"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:3WAA"
SQ SEQUENCE 128 AA; 13509 MW; 1F3C388F6854041C CRC64;
MAGGKAGKDS GKAKAKAVSR SQRAGLQFPV GRIHRHLKTR TTSHGRVGAT AAVYSAAILE
YLTAEVLELA GNASKDLKVK RITPRHLQLA IRGDEELDSL IKATIAGGGV IPHIHKSLIG
KKGQQKTA
