BAK_MOUSE
ID BAK_MOUSE Reviewed; 209 AA.
AC O08734; E9QM21; Q8C264;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-2015, sequence version 3.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Bcl-2 homologous antagonist/killer;
DE AltName: Full=Apoptosis regulator BAK;
GN Name=Bak1; Synonyms=Bak;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=SWR/J; TISSUE=Liver;
RX PubMed=9299236; DOI=10.1006/geno.1997.4858;
RA Ulrich E., Kauffmann-Zeh A., Hueber A.O., Williamson J., Chittenden T.,
RA Ma A., Evan G.I.;
RT "Gene structure, cDNA sequence, and expression of murine Bak, a
RT proapoptotic Bcl-2 family member.";
RL Genomics 44:195-200(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP INTERACTION WITH GIMAP3 AND GIMAP5.
RX PubMed=16509771; DOI=10.1371/journal.pbio.0040103;
RA Nitta T., Nasreen M., Seike T., Goji A., Ohigashi I., Miyazaki T., Ohta T.,
RA Kanno M., Takahama Y.;
RT "IAN family critically regulates survival and development of T
RT lymphocytes.";
RL PLoS Biol. 4:593-605(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP INTERACTION WITH MURINE GAMMAHERPESVIRUS 68 PROTEIN VBCL2.
RX PubMed=18248095; DOI=10.1371/journal.ppat.0040025;
RA Ku B., Woo J.S., Liang C., Lee K.H., Hong H.S., E X., Kim K.S., Jung J.U.,
RA Oh B.H.;
RT "Structural and biochemical bases for the inhibition of autophagy and
RT apoptosis by viral BCL-2 of murine gamma-herpesvirus 68.";
RL PLoS Pathog. 4:E25-E25(2008).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 65-90 IN COMPLEX WITH BCL2A1.
RX PubMed=18462686; DOI=10.1016/j.str.2008.02.009;
RA Smits C., Czabotar P.E., Hinds M.G., Day C.L.;
RT "Structural plasticity underpins promiscuous binding of the prosurvival
RT protein A1.";
RL Structure 16:818-829(2008).
CC -!- FUNCTION: In the presence of an appropriate stimulus, accelerates
CC programmed cell death by binding to, and antagonizing the anti-
CC apoptotic action of BCL2. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Formation of the homodimer is zinc-dependent. Forms
CC heterodimers with BCL2 and BCL2L1 isoform Bcl-X(L). Forms
CC heterooligomers with BAX (By similarity). Interacts with BCL2A1
CC (PubMed:18462686). Interacts withRTL10/BOP (PubMed:18462686). Interacts
CC with VDAC1 (By similarity). Interacts with GIMAP3/IAN4 and GIMAP5/IAN5
CC (PubMed:16509771). {ECO:0000250|UniProtKB:Q16611,
CC ECO:0000269|PubMed:16509771, ECO:0000269|PubMed:18462686}.
CC -!- SUBUNIT: (Microbial infection) Interacts with gamma-herpesvirus 68
CC protein vBCL2. {ECO:0000269|PubMed:18248095}.
CC -!- INTERACTION:
CC O08734; Q07440: Bcl2a1; NbExp=2; IntAct=EBI-822441, EBI-707754;
CC O08734; P97287: Mcl1; NbExp=2; IntAct=EBI-822441, EBI-707292;
CC O08734; Q80U63: Mfn2; NbExp=2; IntAct=EBI-822441, EBI-8437663;
CC O08734; Q60930: Vdac2; NbExp=3; IntAct=EBI-822441, EBI-444578;
CC O08734; O75460: ERN1; Xeno; NbExp=2; IntAct=EBI-822441, EBI-371750;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q16611}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- DOMAIN: Intact BH3 motif is required by BIK, BID, BAK, BAD and BAX for
CC their pro-apoptotic activity and for their interaction with anti-
CC apoptotic members of the Bcl-2 family. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Bcl-2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA73684.1; Type=Frameshift;
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DR EMBL; Y13231; CAA73684.1; ALT_FRAME; mRNA.
DR EMBL; AK089220; BAC40796.1; -; mRNA.
DR EMBL; AC132404; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS28558.1; -.
DR RefSeq; NP_031549.2; NM_007523.2.
DR PDB; 2VOH; X-ray; 1.90 A; B=65-90.
DR PDB; 5FMJ; X-ray; 2.43 A; B=61-94.
DR PDB; 5KTG; X-ray; 2.80 A; A/B=66-144.
DR PDB; 6MCY; X-ray; 1.75 A; A/B/C/D=21-184.
DR PDBsum; 2VOH; -.
DR PDBsum; 5FMJ; -.
DR PDBsum; 5KTG; -.
DR PDBsum; 6MCY; -.
DR AlphaFoldDB; O08734; -.
DR SMR; O08734; -.
DR ComplexPortal; CPX-2033; BAK1 oligomer.
DR CORUM; O08734; -.
DR DIP; DIP-29807N; -.
DR IntAct; O08734; 11.
DR MINT; O08734; -.
DR STRING; 10090.ENSMUSP00000077757; -.
DR iPTMnet; O08734; -.
DR PhosphoSitePlus; O08734; -.
DR SwissPalm; O08734; -.
DR EPD; O08734; -.
DR jPOST; O08734; -.
DR MaxQB; O08734; -.
DR PaxDb; O08734; -.
DR PeptideAtlas; O08734; -.
DR PRIDE; O08734; -.
DR ProteomicsDB; 273535; -.
DR TopDownProteomics; O08734; -.
DR Antibodypedia; 3556; 762 antibodies from 46 providers.
DR DNASU; 12018; -.
DR Ensembl; ENSMUST00000078691; ENSMUSP00000077757; ENSMUSG00000057789.
DR GeneID; 12018; -.
DR KEGG; mmu:12018; -.
DR UCSC; uc008bff.1; mouse.
DR CTD; 578; -.
DR MGI; MGI:1097161; Bak1.
DR VEuPathDB; HostDB:ENSMUSG00000057789; -.
DR eggNOG; KOG4728; Eukaryota.
DR GeneTree; ENSGT01050000244872; -.
DR HOGENOM; CLU_085401_1_1_1; -.
DR InParanoid; O08734; -.
DR OMA; NGGWVAA; -.
DR PhylomeDB; O08734; -.
DR TreeFam; TF315834; -.
DR Reactome; R-MMU-111452; Activation and oligomerization of BAK protein.
DR Reactome; R-MMU-111457; Release of apoptotic factors from the mitochondria.
DR Reactome; R-MMU-5620971; Pyroptosis.
DR BioGRID-ORCS; 12018; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Bak1; mouse.
DR EvolutionaryTrace; O08734; -.
DR PRO; PR:O08734; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; O08734; protein.
DR Bgee; ENSMUSG00000057789; Expressed in ear vesicle and 201 other tissues.
DR ExpressionAtlas; O08734; baseline and differential.
DR Genevisible; O08734; MM.
DR GO; GO:0097145; C:BAK complex; IDA:ARUK-UCL.
DR GO; GO:0097136; C:Bcl-2 family protein complex; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; IDA:BHF-UCL.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:ComplexPortal.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0046930; C:pore complex; ISS:HGNC-UCL.
DR GO; GO:0051400; F:BH domain binding; ISO:MGI.
DR GO; GO:0051087; F:chaperone binding; ISO:MGI.
DR GO; GO:0031072; F:heat shock protein binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:ARUK-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR GO; GO:0097202; P:activation of cysteine-type endopeptidase activity; ISO:MGI.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:MGI.
DR GO; GO:0008635; P:activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c; IMP:MGI.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
DR GO; GO:0006915; P:apoptotic process; ISO:MGI.
DR GO; GO:1902262; P:apoptotic process involved in blood vessel morphogenesis; IGI:MGI.
DR GO; GO:0097190; P:apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0001783; P:B cell apoptotic process; IGI:MGI.
DR GO; GO:0001782; P:B cell homeostasis; IMP:MGI.
DR GO; GO:0002352; P:B cell negative selection; IGI:MGI.
DR GO; GO:0001974; P:blood vessel remodeling; IGI:MGI.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0060402; P:calcium ion transport into cytosol; IGI:MGI.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0034644; P:cellular response to UV; IMP:UniProtKB.
DR GO; GO:0031018; P:endocrine pancreas development; IEA:Ensembl.
DR GO; GO:0050673; P:epithelial cell proliferation; IDA:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IGI:MGI.
DR GO; GO:0010248; P:establishment or maintenance of transmembrane electrochemical gradient; ISS:HGNC-UCL.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IGI:MGI.
DR GO; GO:0044346; P:fibroblast apoptotic process; IMP:MGI.
DR GO; GO:0048872; P:homeostasis of number of cells; IGI:MGI.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IMP:MGI.
DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IGI:MGI.
DR GO; GO:0001776; P:leukocyte homeostasis; IGI:MGI.
DR GO; GO:0035108; P:limb morphogenesis; IGI:MGI.
DR GO; GO:0008053; P:mitochondrial fusion; IGI:MGI.
DR GO; GO:0002262; P:myeloid cell homeostasis; IGI:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0032471; P:negative regulation of endoplasmic reticulum calcium ion concentration; IGI:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:1901029; P:negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IGI:MGI.
DR GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; ISO:MGI.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IGI:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0010524; P:positive regulation of calcium ion transport into cytosol; IGI:MGI.
DR GO; GO:1900103; P:positive regulation of endoplasmic reticulum unfolded protein response; ISO:MGI.
DR GO; GO:1901030; P:positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; IC:ComplexPortal.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISO:MGI.
DR GO; GO:0045862; P:positive regulation of proteolysis; ISO:MGI.
DR GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; ISO:MGI.
DR GO; GO:0048597; P:post-embryonic camera-type eye morphogenesis; IGI:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; IGI:MGI.
DR GO; GO:0046902; P:regulation of mitochondrial membrane permeability; ISS:HGNC-UCL.
DR GO; GO:0051881; P:regulation of mitochondrial membrane potential; ISS:HGNC-UCL.
DR GO; GO:0001836; P:release of cytochrome c from mitochondria; IMP:BHF-UCL.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0009620; P:response to fungus; IMP:MGI.
DR GO; GO:0010332; P:response to gamma radiation; IMP:MGI.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
DR GO; GO:0010046; P:response to mycotoxin; IMP:MGI.
DR GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
DR GO; GO:0010225; P:response to UV-C; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0070242; P:thymocyte apoptotic process; IGI:MGI.
DR GO; GO:0060068; P:vagina development; IGI:MGI.
DR CDD; cd06845; Bcl-2_like; 1.
DR Gene3D; 1.10.437.10; -; 1.
DR InterPro; IPR026308; BAK.
DR InterPro; IPR036834; Bcl-2-like_sf.
DR InterPro; IPR046371; Bcl-2_BH1-3.
DR InterPro; IPR026298; Bcl-2_fam.
DR InterPro; IPR002475; Bcl2-like.
DR InterPro; IPR020717; Bcl2_BH1_motif_CS.
DR InterPro; IPR020726; Bcl2_BH2_motif_CS.
DR InterPro; IPR020728; Bcl2_BH3_motif_CS.
DR PANTHER; PTHR11256; PTHR11256; 1.
DR PANTHER; PTHR11256:SF41; PTHR11256:SF41; 1.
DR Pfam; PF00452; Bcl-2; 1.
DR PRINTS; PR01862; BCL2FAMILY.
DR SMART; SM00337; BCL; 1.
DR SUPFAM; SSF56854; SSF56854; 1.
DR PROSITE; PS50062; BCL2_FAMILY; 1.
DR PROSITE; PS01080; BH1; 1.
DR PROSITE; PS01258; BH2; 1.
DR PROSITE; PS01259; BH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Apoptosis; Host-virus interaction; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion outer membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q16611"
FT CHAIN 2..209
FT /note="Bcl-2 homologous antagonist/killer"
FT /id="PRO_0000143060"
FT TRANSMEM 186..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 72..86
FT /note="BH3"
FT MOTIF 115..134
FT /note="BH1"
FT MOTIF 167..182
FT /note="BH2"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q16611"
FT CONFLICT 50..52
FT /note="AAA -> RP (in Ref. 1; CAA73684)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="Y -> H (in Ref. 2; BAC40796)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="F -> L (in Ref. 1; CAA73684 and 2; BAC40796)"
FT /evidence="ECO:0000305"
FT HELIX 21..48
FT /evidence="ECO:0007829|PDB:6MCY"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:6MCY"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:6MCY"
FT HELIX 68..83
FT /evidence="ECO:0007829|PDB:6MCY"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:6MCY"
FT HELIX 88..95
FT /evidence="ECO:0007829|PDB:6MCY"
FT HELIX 105..116
FT /evidence="ECO:0007829|PDB:6MCY"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:6MCY"
FT HELIX 123..142
FT /evidence="ECO:0007829|PDB:6MCY"
FT HELIX 149..162
FT /evidence="ECO:0007829|PDB:6MCY"
FT HELIX 165..171
FT /evidence="ECO:0007829|PDB:6MCY"
FT HELIX 175..181
FT /evidence="ECO:0007829|PDB:6MCY"
SQ SEQUENCE 209 AA; 23295 MW; 49972D3CA21F4218 CRC64;
MASGQGPGPP KVGCDESPSP SEQQVAQDTE EVFRSYVFYL HQQEQETQGA AAPANPEMDN
LPLEPNSILG QVGRQLALIG DDINRRYDTE FQNLLEQLQP TAGNAYELFT KIASSLFKSG
ISWGRVVALL GFGYRLALYV YQRGLTGFLG QVTCFLADII LHHYIARWIA QRGGWVAALN
FRRDPILTVM VIFGVVLLGQ FVVHRFFRS
