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Apoptosis regulator BAX (Bcl-2-like protein 4) (Bcl2-L-4)

 BAX_HUMAN               Reviewed;         192 AA.
Q07812; A8K4W1; P55269; Q07814; Q07815; Q8WZ49; Q9NR76; Q9NYG7;
Q9UCZ6; Q9UCZ7; Q9UQD6;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
25-OCT-2017, entry version 194.
RecName: Full=Apoptosis regulator BAX;
AltName: Full=Bcl-2-like protein 4;
Short=Bcl2-L-4;
Name=BAX; Synonyms=BCL2L4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA; BETA AND GAMMA), FUNCTION,
SUBUNIT, AND SUBCELLULAR LOCATION.
TISSUE=B-cell;
PubMed=8358790; DOI=10.1016/0092-8674(93)90509-O;
Oltvai Z.N., Milliman C.L., Korsmeyer S.J.;
"Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that
accelerates programmed cell death.";
Cell 74:609-619(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DELTA).
PubMed=7607685; DOI=10.1016/0888-7543(95)80180-T;
Apte S.S., Mattei M.-G., Olsen B.R.;
"Mapping of the human BAX gene to chromosome 19q13.3-q13.4 and
isolation of a novel alternatively spliced transcript, BAX delta.";
Genomics 26:592-594(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM EPSILON).
TISSUE=Brain;
PubMed=9920818; DOI=10.1006/bbrc.1998.0130;
Shi B., Triebe D., Kajiji S., Iwata K.K., Bruskin A., Mahajna J.;
"Identification and characterization of baxepsilon, a novel bax
variant missing the BH2 and the transmembrane domains.";
Biochem. Biophys. Res. Commun. 254:779-785(1999).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND SIGMA), FUNCTION,
INTERACTION WITH BCL2A1 AND BCL2L1, AND TISSUE SPECIFICITY.
PubMed=10772918; DOI=10.1006/bbrc.2000.2537;
Schmitt E., Paquet C., Beauchemin M., Dever-Bertrand J., Bertrand R.;
"Characterization of Bax-sigma, a cell death-inducing isoform of
Bax.";
Biochem. Biophys. Res. Commun. 270:868-879(2000).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PSI), AND TISSUE SPECIFICITY.
PubMed=11912183; DOI=10.1093/hmg/11.6.675;
Cartron P.F., Oliver L., Martin S., Moreau C., LeCabellec M.T.,
Jezequel P., Meflah K., Vallette F.M.;
"The expression of a new variant of the pro-apoptotic molecule Bax,
Baxpsi, is correlated with an increased survival of glioblastoma
multiforme patients.";
Hum. Mol. Genet. 11:675-687(2002).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ZETA).
TISSUE=Ovarian carcinoma;
Perez R.P., Sanville H.;
"Bax mRNA splice variant lacking exons 2 and 3.";
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 63-77 AND 98-118, AND VARIANTS ARG-67
AND VAL-108.
PubMed=7475270;
Meijerink J.P.P., Smetsers T.F.C.M., Sloetjes A.W., Linders E.H.P.,
Mensink E.J.B.M.;
"Bax mutations in cell lines derived from hematological
malignancies.";
Leukemia 9:1828-1832(1995).
[12]
MUTAGENESIS, AND FUNCTION OF BH3 MOTIF.
PubMed=8521816;
Chittenden T., Flemington C., Houghton A.B., Ebb R.G., Gallo G.J.,
Elangovan B., Chinnadurai G., Lutz R.J.;
"A conserved domain in Bak, distinct from BH1 and BH2, mediates cell
death and protein binding functions.";
EMBO J. 14:5589-5596(1995).
[13]
SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-184.
PubMed=10228148; DOI=10.1093/emboj/18.9.2330;
Nechushtan A., Smith C.L., Hsu Y.-T., Youle R.J.;
"Conformation of the Bax C-terminus regulates subcellular location and
cell death.";
EMBO J. 18:2330-2341(1999).
[14]
INTERACTION WITH SH3GLB1.
PubMed=11259440; DOI=10.1074/jbc.M101527200;
Cuddeback S.M., Yamaguchi H., Komatsu K., Miyashita T., Yamada M.,
Wu C., Singh S., Wang H.-G.;
"Molecular cloning and characterization of Bif-1. A novel Src homology
3 domain-containing protein that associates with Bax.";
J. Biol. Chem. 276:20559-20565(2001).
[15]
INTERACTION WITH HN.
PubMed=12732850; DOI=10.1038/nature01627;
Guo B., Zhai D., Cabezas E., Welsh K., Nouraini S., Satterthwait A.C.,
Reed J.C.;
"Humanin peptide suppresses apoptosis by interfering with Bax
activation.";
Nature 423:456-461(2003).
[16]
INTERACTION WITH SFN AND YWHAZ, AND SUBCELLULAR LOCATION.
PubMed=15071501; DOI=10.1038/sj.emboj.7600194;
Tsuruta F., Sunayama J., Mori Y., Hattori S., Shimizu S.,
Tsujimoto Y., Yoshioka K., Masuyama N., Gotoh Y.;
"JNK promotes Bax translocation to mitochondria through
phosphorylation of 14-3-3 proteins.";
EMBO J. 23:1889-1899(2004).
[17]
INTERACTION WITH NOL3.
PubMed=15004034; DOI=10.1074/jbc.M400695200;
Gustafsson A.B., Tsai J.G., Logue S.E., Crow M.T., Gottlieb R.A.;
"Apoptosis repressor with caspase recruitment domain protects against
cell death by interfering with Bax activation.";
J. Biol. Chem. 279:21233-21238(2004).
[18]
INTERACTION WITH HHV-5 PROTEIN UL37.
PubMed=15004026; DOI=10.1074/jbc.M308408200;
Poncet D., Larochette N., Pauleau A.L., Boya P., Jalil A.A.,
Cartron P.F., Vallette F., Schnebelen C., Bartle L.M., Skaletskaya A.,
Boutolleau D., Martinou J.C., Goldmacher V.S., Kroemer G., Zamzami N.;
"An anti-apoptotic viral protein that recruits Bax to mitochondria.";
J. Biol. Chem. 279:22605-22614(2004).
[19]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CLU.
PubMed=16113678; DOI=10.1038/ncb1291;
Zhang H., Kim J.K., Edwards C.A., Xu Z., Taichman R., Wang C.Y.;
"Clusterin inhibits apoptosis by interacting with activated Bax.";
Nat. Cell Biol. 7:909-915(2005).
[20]
INTERACTION WITH FAIM2/LFG2.
PubMed=16964429;
Reimers K., Choi C.Y., Mau-Thek E., Vogt P.M.;
"Sequence analysis shows that Lifeguard belongs to a new
evolutionarily conserved cytoprotective family.";
Int. J. Mol. Med. 18:729-734(2006).
[21]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[22]
INTERACTION WITH RNF144B.
PubMed=20300062; DOI=10.1038/emboj.2010.39;
Benard G., Neutzner A., Peng G., Wang C., Livak F., Youle R.J.,
Karbowski M.;
"IBRDC2, an IBR-type E3 ubiquitin ligase, is a regulatory factor for
Bax and apoptosis activation.";
EMBO J. 29:1458-1471(2010).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[24]
INTERACTION WITH RTL10/BOP.
PubMed=23055042; DOI=10.1007/s13238-012-2069-7;
Zhang X., Weng C., Li Y., Wang X., Jiang C., Li X., Xu Y., Chen Q.,
Pan L., Tang H.;
"Human Bop is a novel BH3-only member of the Bcl-2 protein family.";
Protein Cell 3:790-801(2012).
[25]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[26]
STRUCTURE BY NMR, SUBCELLULAR LOCATION, AND SUBUNIT.
PubMed=11106734; DOI=10.1016/S0092-8674(00)00167-7;
Suzuki M., Youle R.J., Tjandra N.;
"Structure of Bax: coregulation of dimer formation and intracellular
localization.";
Cell 103:645-654(2000).
[27]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 13-19 IN COMPLEX WITH
ANTIBODY FRAGMENT.
PubMed=16946732; DOI=10.1038/sj.cdd.4402025;
Peyerl F.W., Dai S., Murphy G.A., Crawford F., White J., Marrack P.,
Kappler J.W.;
"Elucidation of some Bax conformational changes through
crystallization of an antibody-peptide complex.";
Cell Death Differ. 14:447-452(2007).
[28]
STRUCTURE BY NMR IN COMPLEX WITH BCL2L11, FUNCTION, SUBUNIT,
MUTAGENESIS OF LYS-21, AND INTERACTION WITH BCL2L11.
PubMed=18948948; DOI=10.1038/nature07396;
Gavathiotis E., Suzuki M., Davis M.L., Pitter K., Bird G.H.,
Katz S.G., Tu H.C., Kim H., Cheng E.H., Tjandra N., Walensky L.D.;
"BAX activation is initiated at a novel interaction site.";
Nature 455:1076-1081(2008).
[29]
X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) OF 48-81 IN COMPLEXES WITH
BCL2L1 AND MCL1, INTERACTION WITH MCL1; BCL2; BCL2L1 AND BCL2L2,
FUNCTION, AND MUTAGENESIS OF MET-74.
PubMed=21199865; DOI=10.1074/jbc.M110.161281;
Czabotar P.E., Lee E.F., Thompson G.V., Wardak A.Z., Fairlie W.D.,
Colman P.M.;
"Mutation to Bax beyond the BH3 domain disrupts interactions with pro-
survival proteins and promotes apoptosis.";
J. Biol. Chem. 286:7123-7131(2011).
[30]
VARIANTS GLU-11; ARG-67 AND VAL-108.
PubMed=9531611;
Meijerink J.P.P., Mensink E.J.B.M., Wang K., Sedlak T.W.,
Sloetjes A.W., de Witte T., Waksman G., Korsmeyer S.J.;
"Hematopoietic malignancies demonstrate loss-of-function mutations of
BAX.";
Blood 91:2991-2997(1998).
-!- FUNCTION: Accelerates programmed cell death by binding to, and
antagonizing the apoptosis repressor BCL2 or its adenovirus
homolog E1B 19k protein. Under stress conditions, undergoes a
conformation change that causes translocation to the mitochondrion
membrane, leading to the release of cytochrome c that then
triggers apoptosis. Promotes activation of CASP3, and thereby
apoptosis. {ECO:0000269|PubMed:10772918,
ECO:0000269|PubMed:16113678, ECO:0000269|PubMed:18948948,
ECO:0000269|PubMed:21199865, ECO:0000269|PubMed:8358790,
ECO:0000269|PubMed:8521816}.
-!- SUBUNIT: Homodimer. Forms higher oligomers under stress
conditions. Interacts with BCL2L11. Interaction with BCL2L11
promotes BAX oligomerization and association with mitochondrial
membranes, with subsequent release of cytochrome c. Forms
heterodimers with BCL2, E1B 19K protein, BCL2L1 isoform Bcl-X(L),
BCL2L2, MCL1 and A1. Interacts with SH3GLB1 and HN. Interacts with
SFN and YWHAZ; the interaction occurs in the cytoplasm. Under
stress conditions, JNK-mediated phosphorylation of SFN and YWHAZ,
releases BAX to mitochondria. Isoform Sigma interacts with BCL2A1
and BCL2L1 isoform Bcl-X(L). Interacts with RNF144B, which
regulates the ubiquitin-dependent stability of BAX. Interacts with
CLU under stress conditions that cause a conformation change
leading to BAX oligomerization and association with mitochondria.
Does not interact with CLU in unstressed cells. Interacts with
FAIM2/LFG2. Interacts with human cytomegalovirus/HHV-5 protein
vMIA/UL37. Interacts with RTL10/BOP. Interacts (via a C-terminal
33 residues) with NOL3 (via CARD domain); inhibits BAX activation
and translocation and consequently cytochrome c release from
mitochondria. {ECO:0000269|PubMed:10772918,
ECO:0000269|PubMed:11106734, ECO:0000269|PubMed:11259440,
ECO:0000269|PubMed:12732850, ECO:0000269|PubMed:15004026,
ECO:0000269|PubMed:15004034, ECO:0000269|PubMed:15071501,
ECO:0000269|PubMed:16113678, ECO:0000269|PubMed:16946732,
ECO:0000269|PubMed:16964429, ECO:0000269|PubMed:18948948,
ECO:0000269|PubMed:20300062, ECO:0000269|PubMed:21199865,
ECO:0000269|PubMed:23055042, ECO:0000269|PubMed:8358790}.
-!- INTERACTION:
Self; NbExp=28; IntAct=EBI-516580, EBI-516580;
P26662:- (xeno); NbExp=3; IntAct=EBI-516580, EBI-9099462;
Q16611:BAK1; NbExp=5; IntAct=EBI-516580, EBI-519866;
P10415:BCL2; NbExp=13; IntAct=EBI-516580, EBI-77694;
Q07817:BCL2L1; NbExp=3; IntAct=EBI-516580, EBI-78035;
Q07817-1:BCL2L1; NbExp=20; IntAct=EBI-516580, EBI-287195;
Q9HD36:BCL2L10; NbExp=2; IntAct=EBI-516580, EBI-2126349;
O43521:BCL2L11; NbExp=22; IntAct=EBI-516580, EBI-526406;
Q92843:BCL2L2; NbExp=5; IntAct=EBI-516580, EBI-707714;
P55957:BID; NbExp=17; IntAct=EBI-516580, EBI-519672;
P70444:Bid (xeno); NbExp=2; IntAct=EBI-516580, EBI-783400;
O75460:ERN1; NbExp=2; IntAct=EBI-516580, EBI-371750;
Q99MI6:Gimap3 (xeno); NbExp=2; IntAct=EBI-516580, EBI-15572304;
Q8BWF2:Gimap5 (xeno); NbExp=2; IntAct=EBI-516580, EBI-15572348;
P22001:KCNA3; NbExp=2; IntAct=EBI-516580, EBI-8627664;
Q07820:MCL1; NbExp=8; IntAct=EBI-516580, EBI-1003422;
P97287:Mcl1 (xeno); NbExp=2; IntAct=EBI-516580, EBI-707292;
Q811U4:Mfn1 (xeno); NbExp=2; IntAct=EBI-516580, EBI-9029118;
Q80U63:Mfn2 (xeno); NbExp=2; IntAct=EBI-516580, EBI-8437663;
Q9ULZ3:PYCARD; NbExp=7; IntAct=EBI-516580, EBI-751215;
Q7Z419:RNF144B; NbExp=5; IntAct=EBI-516580, EBI-2129982;
Q7L3V2:RTL10; NbExp=2; IntAct=EBI-516580, EBI-10697720;
Q9Y371-1:SH3GLB1; NbExp=2; IntAct=EBI-516580, EBI-5291808;
P49334:TOM22 (xeno); NbExp=3; IntAct=EBI-516580, EBI-12527;
P23644:TOM40 (xeno); NbExp=2; IntAct=EBI-516580, EBI-12539;
P24391:tom40 (xeno); NbExp=2; IntAct=EBI-516580, EBI-1791540;
P07213:TOM70 (xeno); NbExp=2; IntAct=EBI-516580, EBI-12551;
P16778:UL37 (xeno); NbExp=2; IntAct=EBI-516580, EBI-16026491;
Q9P2Y5:UVRAG; NbExp=6; IntAct=EBI-516580, EBI-2952704;
P17361:VACWR028 (xeno); NbExp=3; IntAct=EBI-516580, EBI-7115640;
P12956:XRCC6; NbExp=2; IntAct=EBI-516580, EBI-353208;
-!- SUBCELLULAR LOCATION: Isoform Alpha: Mitochondrion membrane;
Single-pass membrane protein. Cytoplasm. Note=Colocalizes with 14-
3-3 proteins in the cytoplasm. Under stress conditions, undergoes
a conformation change that causes release from JNK-phosphorylated
14-3-3 proteins and translocation to the mitochondrion membrane.
-!- SUBCELLULAR LOCATION: Isoform Beta: Cytoplasm.
-!- SUBCELLULAR LOCATION: Isoform Gamma: Cytoplasm.
-!- SUBCELLULAR LOCATION: Isoform Delta: Cytoplasm {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=8;
Name=Alpha;
IsoId=Q07812-1; Sequence=Displayed;
Name=Beta;
IsoId=Q07812-2, Q07814-1;
Sequence=VSP_031237;
Name=Gamma;
IsoId=Q07812-3, Q07815-1;
Sequence=VSP_031234, VSP_031236;
Name=Delta;
IsoId=Q07812-4, P55269-1;
Sequence=VSP_031235;
Name=Epsilon;
IsoId=Q07812-5; Sequence=VSP_031240;
Name=Zeta;
IsoId=Q07812-6; Sequence=VSP_031239;
Name=Psi;
IsoId=Q07812-7; Sequence=VSP_031238;
Name=Sigma;
IsoId=Q07812-8; Sequence=VSP_037475;
-!- TISSUE SPECIFICITY: Expressed in a wide variety of tissues.
Isoform Psi is found in glial tumors. Isoform Alpha is expressed
in spleen, breast, ovary, testis, colon and brain, and at low
levels in skin and lung. Isoform Sigma is expressed in spleen,
breast, ovary, testis, lung, colon, brain and at low levels in
skin. Isoform Alpha and isoform Sigma are expressed in pro-
myelocytic leukemia, histiocytic lymphoma, Burkitt's lymphoma, T-
cell lymphoma, lymphoblastic leukemia, breast adenocarcinoma,
ovary adenocarcinoma, prostate carcinoma, prostate adenocarcinoma,
lung carcinoma, epidermoid carcinoma, small cell lung carcinoma
and colon adenocarcinoma cell lines. {ECO:0000269|PubMed:10772918,
ECO:0000269|PubMed:11912183}.
-!- DOMAIN: Intact BH3 motif is required by BIK, BID, BAK, BAD and BAX
for their pro-apoptotic activity and for their interaction with
anti-apoptotic members of the Bcl-2 family. {ECO:0000250}.
-!- SIMILARITY: Belongs to the Bcl-2 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/bax/";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/BAXID128ch19q13.html";
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EMBL; L22473; AAA03619.1; -; mRNA.
EMBL; L22474; AAA03620.1; -; mRNA.
EMBL; L22475; AAA03621.1; -; mRNA.
EMBL; U19599; AAC50142.1; -; mRNA.
EMBL; AF007826; AAD22706.1; -; mRNA.
EMBL; AF247393; AAF71267.1; -; mRNA.
EMBL; AJ417988; CAD10744.1; -; mRNA.
EMBL; AF250190; AAF82094.1; -; mRNA.
EMBL; AK291076; BAF83765.1; -; mRNA.
EMBL; AY217036; AAO22992.1; -; Genomic_DNA.
EMBL; CH471177; EAW52418.1; -; Genomic_DNA.
EMBL; CH471177; EAW52417.1; -; Genomic_DNA.
EMBL; BC014175; AAH14175.1; -; mRNA.
CCDS; CCDS12742.1; -. [Q07812-1]
CCDS; CCDS12743.1; -. [Q07812-4]
CCDS; CCDS12744.1; -. [Q07812-2]
CCDS; CCDS12745.2; -. [Q07812-8]
PIR; A47538; A47538.
PIR; B47538; B47538.
PIR; C47538; C47538.
PIR; I38921; I38921.
PIR; JC7255; JC7255.
RefSeq; NP_001278357.1; NM_001291428.1.
RefSeq; NP_001278360.1; NM_001291431.1. [Q07812-6]
RefSeq; NP_004315.1; NM_004324.3. [Q07812-2]
RefSeq; NP_620116.1; NM_138761.3. [Q07812-1]
RefSeq; NP_620118.1; NM_138763.3. [Q07812-4]
RefSeq; NP_620119.2; NM_138764.4. [Q07812-8]
RefSeq; XP_016882566.1; XM_017027077.1. [Q07812-7]
UniGene; Hs.624291; -.
PDB; 1F16; NMR; -; A=1-192.
PDB; 2G5B; X-ray; 2.30 A; I/J/K/L=13-19.
PDB; 2K7W; NMR; -; A=1-192.
PDB; 2LR1; NMR; -; A=1-192.
PDB; 3PK1; X-ray; 2.49 A; B/D=48-81.
PDB; 3PL7; X-ray; 2.61 A; C=48-81.
PDB; 4BD2; X-ray; 2.21 A; A=1-171.
PDB; 4BD6; X-ray; 2.49 A; A=1-171, C=48-81.
PDB; 4BD7; X-ray; 2.80 A; A/B/C/D=1-171.
PDB; 4BD8; X-ray; 2.22 A; A/B/C/D=1-171.
PDB; 4BDU; X-ray; 3.00 A; A/B/C/D=53-128.
PDB; 4S0O; X-ray; 1.90 A; A/B=1-192.
PDB; 4S0P; X-ray; 3.25 A; A/B=1-192.
PDB; 4UF2; X-ray; 3.00 A; B=50-77.
PDB; 4ZIE; X-ray; 1.80 A; A=1-166.
PDB; 4ZIF; X-ray; 2.40 A; A=1-166.
PDB; 4ZIG; X-ray; 2.20 A; A=1-166.
PDB; 4ZIH; X-ray; 2.50 A; A=1-164.
PDB; 4ZII; X-ray; 2.19 A; A=1-170.
PDBsum; 1F16; -.
PDBsum; 2G5B; -.
PDBsum; 2K7W; -.
PDBsum; 2LR1; -.
PDBsum; 3PK1; -.
PDBsum; 3PL7; -.
PDBsum; 4BD2; -.
PDBsum; 4BD6; -.
PDBsum; 4BD7; -.
PDBsum; 4BD8; -.
PDBsum; 4BDU; -.
PDBsum; 4S0O; -.
PDBsum; 4S0P; -.
PDBsum; 4UF2; -.
PDBsum; 4ZIE; -.
PDBsum; 4ZIF; -.
PDBsum; 4ZIG; -.
PDBsum; 4ZIH; -.
PDBsum; 4ZII; -.
ProteinModelPortal; Q07812; -.
SMR; Q07812; -.
BioGrid; 107057; 78.
CORUM; Q07812; -.
DIP; DIP-232N; -.
IntAct; Q07812; 68.
MINT; MINT-134330; -.
STRING; 9606.ENSP00000293288; -.
BindingDB; Q07812; -.
ChEMBL; CHEMBL5318; -.
TCDB; 1.A.21.1.2; the bcl-2 (bcl-2) family.
iPTMnet; Q07812; -.
PhosphoSitePlus; Q07812; -.
SwissPalm; Q07812; -.
BioMuta; BAX; -.
DMDM; 728945; -.
EPD; Q07812; -.
MaxQB; Q07812; -.
PaxDb; Q07812; -.
PeptideAtlas; Q07812; -.
PRIDE; Q07812; -.
TopDownProteomics; Q07812-1; -. [Q07812-1]
TopDownProteomics; Q07812-2; -. [Q07812-2]
TopDownProteomics; Q07812-5; -. [Q07812-5]
TopDownProteomics; Q07812-6; -. [Q07812-6]
TopDownProteomics; Q07812-8; -. [Q07812-8]
DNASU; 581; -.
Ensembl; ENST00000293288; ENSP00000293288; ENSG00000087088. [Q07812-2]
Ensembl; ENST00000345358; ENSP00000263262; ENSG00000087088. [Q07812-1]
Ensembl; ENST00000354470; ENSP00000346461; ENSG00000087088. [Q07812-4]
Ensembl; ENST00000356483; ENSP00000348871; ENSG00000087088. [Q07812-5]
Ensembl; ENST00000415969; ENSP00000389971; ENSG00000087088. [Q07812-8]
Ensembl; ENST00000515540; ENSP00000426328; ENSG00000087088. [Q07812-3]
GeneID; 581; -.
KEGG; hsa:581; -.
UCSC; uc002plf.2; human. [Q07812-1]
CTD; 581; -.
DisGeNET; 581; -.
EuPathDB; HostDB:ENSG00000087088.19; -.
GeneCards; BAX; -.
HGNC; HGNC:959; BAX.
HPA; CAB004206; -.
HPA; HPA027878; -.
MalaCards; BAX; -.
MIM; 600040; gene.
neXtProt; NX_Q07812; -.
OpenTargets; ENSG00000087088; -.
PharmGKB; PA25269; -.
eggNOG; ENOG410IWQJ; Eukaryota.
eggNOG; ENOG4112738; LUCA.
GeneTree; ENSGT00730000111112; -.
HOVERGEN; HBG003606; -.
InParanoid; Q07812; -.
KO; K02159; -.
OMA; VINWIRE; -.
OrthoDB; EOG091G0YWR; -.
PhylomeDB; Q07812; -.
TreeFam; TF315834; -.
Reactome; R-HSA-114294; Activation, translocation and oligomerization of BAX.
Reactome; R-HSA-6803204; TP53 Regulates Transcription of Genes Involved in Cytochrome C Release.
Reactome; R-HSA-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
SIGNOR; Q07812; -.
ChiTaRS; BAX; human.
EvolutionaryTrace; Q07812; -.
GeneWiki; Bcl-2-associated_X_protein; -.
GenomeRNAi; 581; -.
PMAP-CutDB; Q07812; -.
PRO; PR:Q07812; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000087088; -.
CleanEx; HS_BAX; -.
ExpressionAtlas; Q07812; baseline and differential.
Genevisible; Q07812; HS.
GO; GO:0097144; C:BAX complex; IDA:UniProtKB.
GO; GO:0097136; C:Bcl-2 family protein complex; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IDA:HGNC.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:HGNC.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005741; C:mitochondrial outer membrane; IBA:GO_Central.
GO; GO:0005757; C:mitochondrial permeability transition pore complex; IDA:HGNC.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0005635; C:nuclear envelope; IDA:AgBase.
GO; GO:0005634; C:nucleus; IDA:AgBase.
GO; GO:0046930; C:pore complex; IDA:BHF-UCL.
GO; GO:0051434; F:BH3 domain binding; IDA:UniProtKB.
GO; GO:0015267; F:channel activity; IDA:BHF-UCL.
GO; GO:0051087; F:chaperone binding; IEA:Ensembl.
GO; GO:0030544; F:Hsp70 protein binding; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0008289; F:lipid binding; IDA:HGNC.
GO; GO:0046982; F:protein heterodimerization activity; IPI:HGNC.
GO; GO:0042803; F:protein homodimerization activity; IDA:HGNC.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:HGNC.
GO; GO:0008635; P:activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c; IDA:HGNC.
GO; GO:0097296; P:activation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0006987; P:activation of signaling protein activity involved in unfolded protein response; TAS:ParkinsonsUK-UCL.
GO; GO:0008637; P:apoptotic mitochondrial changes; IDA:HGNC.
GO; GO:0006915; P:apoptotic process; IDA:ParkinsonsUK-UCL.
GO; GO:1902262; P:apoptotic process involved in blood vessel morphogenesis; IEA:Ensembl.
GO; GO:1902263; P:apoptotic process involved in embryonic digit morphogenesis; IEA:Ensembl.
GO; GO:0097190; P:apoptotic signaling pathway; IDA:HGNC.
GO; GO:0001783; P:B cell apoptotic process; IDA:HGNC.
GO; GO:0001782; P:B cell homeostasis; IEA:Ensembl.
GO; GO:0002358; P:B cell homeostatic proliferation; IEA:Ensembl.
GO; GO:0002352; P:B cell negative selection; IEA:Ensembl.
GO; GO:1990117; P:B cell receptor apoptotic signaling pathway; IDA:BHF-UCL.
GO; GO:0001974; P:blood vessel remodeling; IEA:Ensembl.
GO; GO:0034644; P:cellular response to UV; IEA:Ensembl.
GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
GO; GO:0045136; P:development of secondary sexual characteristics; IEA:Ensembl.
GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
GO; GO:0035234; P:ectopic germ cell programmed cell death; IEA:Ensembl.
GO; GO:0032469; P:endoplasmic reticulum calcium ion homeostasis; TAS:UniProtKB.
GO; GO:0010248; P:establishment or maintenance of transmembrane electrochemical gradient; IDA:HGNC.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IDA:BHF-UCL.
GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IBA:GO_Central.
GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IC:BHF-UCL.
GO; GO:0009566; P:fertilization; IEA:Ensembl.
GO; GO:0007281; P:germ cell development; IEA:Ensembl.
GO; GO:0006687; P:glycosphingolipid metabolic process; IEA:Ensembl.
GO; GO:0048873; P:homeostasis of number of cells within a tissue; IEA:Ensembl.
GO; GO:0021854; P:hypothalamus development; IEA:Ensembl.
GO; GO:0097193; P:intrinsic apoptotic signaling pathway; IDA:HGNC.
GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; IEA:Ensembl.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IBA:GO_Central.
GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IMP:UniProtKB.
GO; GO:0001822; P:kidney development; IEA:Ensembl.
GO; GO:0043653; P:mitochondrial fragmentation involved in apoptotic process; IDA:HGNC.
GO; GO:0008053; P:mitochondrial fusion; IDA:HGNC.
GO; GO:0070584; P:mitochondrion morphogenesis; IEA:Ensembl.
GO; GO:0002262; P:myeloid cell homeostasis; IEA:Ensembl.
GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0032471; P:negative regulation of endoplasmic reticulum calcium ion concentration; IEA:Ensembl.
GO; GO:0048147; P:negative regulation of fibroblast proliferation; IEA:Ensembl.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
GO; GO:0032091; P:negative regulation of protein binding; IDA:UniProtKB.
GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
GO; GO:0001764; P:neuron migration; IEA:Ensembl.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl.
GO; GO:0001541; P:ovarian follicle development; IEA:Ensembl.
GO; GO:1902512; P:positive regulation of apoptotic DNA fragmentation; IMP:BHF-UCL.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0060058; P:positive regulation of apoptotic process involved in mammary gland involution; IEA:Ensembl.
GO; GO:0002904; P:positive regulation of B cell apoptotic process; IEA:Ensembl.
GO; GO:0048087; P:positive regulation of developmental pigmentation; IEA:Ensembl.
GO; GO:1900103; P:positive regulation of endoplasmic reticulum unfolded protein response; IMP:UniProtKB.
GO; GO:2001241; P:positive regulation of extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IMP:UniProtKB.
GO; GO:1903896; P:positive regulation of IRE1-mediated unfolded protein response; TAS:ParkinsonsUK-UCL.
GO; GO:1901030; P:positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; TAS:Reactome.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IDA:HGNC.
GO; GO:0032461; P:positive regulation of protein oligomerization; IDA:UniProtKB.
GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; IDA:UniProtKB.
GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; IEA:Ensembl.
GO; GO:0048597; P:post-embryonic camera-type eye morphogenesis; IEA:Ensembl.
GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
GO; GO:0001844; P:protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; TAS:Reactome.
GO; GO:0051259; P:protein oligomerization; IDA:UniProtKB.
GO; GO:0042981; P:regulation of apoptotic process; TAS:Reactome.
GO; GO:0033599; P:regulation of mammary gland epithelial cell proliferation; IEA:Ensembl.
GO; GO:1902445; P:regulation of mitochondrial membrane permeability involved in programmed necrotic cell death; IEA:Ensembl.
GO; GO:0051881; P:regulation of mitochondrial membrane potential; IDA:HGNC.
GO; GO:0006808; P:regulation of nitrogen utilization; IEA:Ensembl.
GO; GO:0043497; P:regulation of protein heterodimerization activity; IPI:HGNC.
GO; GO:0043496; P:regulation of protein homodimerization activity; IDA:HGNC.
GO; GO:0001836; P:release of cytochrome c from mitochondria; IDA:BHF-UCL.
GO; GO:0032976; P:release of matrix enzymes from mitochondria; IDA:HGNC.
GO; GO:0048678; P:response to axon injury; IEA:Ensembl.
GO; GO:0010332; P:response to gamma radiation; IEA:Ensembl.
GO; GO:0009651; P:response to salt stress; IEA:Ensembl.
GO; GO:0009636; P:response to toxic substance; IDA:HGNC.
GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
GO; GO:0046666; P:retinal cell programmed cell death; IEA:Ensembl.
GO; GO:0060011; P:Sertoli cell proliferation; IEA:Ensembl.
GO; GO:0048515; P:spermatid differentiation; IEA:Ensembl.
GO; GO:0001777; P:T cell homeostatic proliferation; IEA:Ensembl.
GO; GO:0070242; P:thymocyte apoptotic process; IEA:Ensembl.
GO; GO:0060068; P:vagina development; IEA:Ensembl.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
Gene3D; 1.10.437.10; -; 1.
InterPro; IPR026304; BAX.
InterPro; IPR002475; Bcl2-like.
InterPro; IPR020717; Bcl2_BH1_motif_CS.
InterPro; IPR020726; Bcl2_BH2_motif_CS.
InterPro; IPR020728; Bcl2_BH3_motif_CS.
InterPro; IPR036834; Blc2-like_sf.
InterPro; IPR026298; Blc2_fam.
PANTHER; PTHR11256; PTHR11256; 1.
PANTHER; PTHR11256:SF42; PTHR11256:SF42; 1.
Pfam; PF00452; Bcl-2; 1.
PRINTS; PR01862; BCL2FAMILY.
SUPFAM; SSF56854; SSF56854; 1.
PROSITE; PS50062; BCL2_FAMILY; 1.
PROSITE; PS01080; BH1; 1.
PROSITE; PS01258; BH2; 1.
PROSITE; PS01259; BH3; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Apoptosis;
Complete proteome; Cytoplasm; Host-virus interaction; Membrane;
Mitochondrion; Polymorphism; Reference proteome; Transmembrane;
Transmembrane helix; Tumor suppressor.
CHAIN 1 192 Apoptosis regulator BAX.
/FTId=PRO_0000143053.
TRANSMEM 172 192 Helical. {ECO:0000255}.
MOTIF 59 73 BH3.
MOTIF 98 118 BH1.
MOTIF 150 165 BH2.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:25944712}.
VAR_SEQ 1 78 Missing (in isoform Zeta).
{ECO:0000303|Ref.6}.
/FTId=VSP_031239.
VAR_SEQ 1 19 Missing (in isoform Psi).
{ECO:0000303|PubMed:11912183}.
/FTId=VSP_031238.
VAR_SEQ 12 41 GPTSSEQIMKTGALLLQGFIQDRAGRMGGE -> VSSRIEQ
GEWGGRHPSWPWTRCLRMRPPRS (in isoform
Gamma). {ECO:0000303|PubMed:8358790}.
/FTId=VSP_031234.
VAR_SEQ 30 78 Missing (in isoform Delta).
{ECO:0000303|PubMed:7607685}.
/FTId=VSP_031235.
VAR_SEQ 42 192 Missing (in isoform Gamma).
{ECO:0000303|PubMed:8358790}.
/FTId=VSP_031236.
VAR_SEQ 125 192 LCTKVPELIRTIMGWTLDFLRERLLGWIQDQGGWDGLLSYF
GTPTWQTVTIFVAGVLTASLTIWKKMG -> GVKWRDLGSL
QPLPPGFKRFTCLSIPRSWDYRPCAPRCRN (in
isoform Epsilon).
{ECO:0000303|PubMed:9920818}.
/FTId=VSP_031240.
VAR_SEQ 159 192 DGLLSYFGTPTWQTVTIFVAGVLTASLTIWKKMG -> VRL
LKPPHPHHRALTTAPAPPSLPPATPLGPWAFWSRSQWCPLP
IFRSSDVVYNAFSLRV (in isoform Beta).
{ECO:0000303|PubMed:8358790}.
/FTId=VSP_031237.
VAR_SEQ 159 171 Missing (in isoform Sigma).
{ECO:0000303|PubMed:10772918}.
/FTId=VSP_037475.
VARIANT 11 11 G -> E (in a plasmacytoma cell line;
dbSNP:rs555248599).
{ECO:0000269|PubMed:9531611}.
/FTId=VAR_013575.
VARIANT 39 39 G -> R (in dbSNP:rs36017265).
/FTId=VAR_047053.
VARIANT 67 67 G -> R (in a T-cell acute lymphoblastic
leukemia cell line; loss of
heterodimerization with Bcl-2 or Bcl-
X(L); dbSNP:rs398122513).
{ECO:0000269|PubMed:7475270,
ECO:0000269|PubMed:9531611}.
/FTId=VAR_007809.
VARIANT 108 108 G -> V (in a Burkitt lymphoma; loss of
homodimerization).
{ECO:0000269|PubMed:7475270,
ECO:0000269|PubMed:9531611}.
/FTId=VAR_013576.
MUTAGEN 21 21 K->E: Reduces interaction with BCL2L11,
homooligomerization and triggering of
apoptosis. {ECO:0000269|PubMed:18948948}.
MUTAGEN 74 74 M->D,E: Strongly reduced interaction with
MCL1, BCL2, BCL2L1 and BCL2L2. No effect
on cytochrome c release and subsequent
apoptosis triggered by etoposide.
{ECO:0000269|PubMed:21199865}.
MUTAGEN 184 184 S->D,E,H,K: Constitutive cytoplasmic
location. {ECO:0000269|PubMed:10228148}.
MUTAGEN 184 184 S->V: Constitutive mitochondrial
location. {ECO:0000269|PubMed:10228148}.
TURN 2 4 {ECO:0000244|PDB:2K7W}.
STRAND 10 14 {ECO:0000244|PDB:1F16}.
HELIX 16 34 {ECO:0000244|PDB:4ZIE}.
HELIX 36 38 {ECO:0000244|PDB:2K7W}.
HELIX 43 45 {ECO:0000244|PDB:4S0O}.
HELIX 54 71 {ECO:0000244|PDB:4ZIE}.
HELIX 74 82 {ECO:0000244|PDB:4ZIE}.
HELIX 88 99 {ECO:0000244|PDB:4ZIE}.
TURN 100 102 {ECO:0000244|PDB:4ZIE}.
HELIX 107 147 {ECO:0000244|PDB:4ZIE}.
HELIX 149 154 {ECO:0000244|PDB:4ZIE}.
TURN 155 158 {ECO:0000244|PDB:4ZIE}.
HELIX 159 164 {ECO:0000244|PDB:4ZIE}.
HELIX 170 191 {ECO:0000244|PDB:4S0O}.
SEQUENCE 192 AA; 21184 MW; 6C0CDB0A7DEE4994 CRC64;
MDGSGEQPRG GGPTSSEQIM KTGALLLQGF IQDRAGRMGG EAPELALDPV PQDASTKKLS
ECLKRIGDEL DSNMELQRMI AAVDTDSPRE VFFRVAADMF SDGNFNWGRV VALFYFASKL
VLKALCTKVP ELIRTIMGWT LDFLRERLLG WIQDQGGWDG LLSYFGTPTW QTVTIFVAGV
LTASLTIWKK MG


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