MOAP1_HUMAN
ID MOAP1_HUMAN Reviewed; 351 AA.
AC Q96BY2; B2RDF6; Q9H833; Q9HAS1;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Modulator of apoptosis 1 {ECO:0000303|PubMed:11060313};
DE Short=MAP-1 {ECO:0000303|PubMed:11060313};
DE Short=MAP1 {ECO:0000303|PubMed:11060313};
DE AltName: Full=Paraneoplastic antigen Ma4 {ECO:0000303|PubMed:19366867};
GN Name=MOAP1 {ECO:0000303|PubMed:19366867, ECO:0000312|HGNC:HGNC:16658};
GN Synonyms=PNMA4 {ECO:0000303|PubMed:19366867};
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], FUNCTION, DOMAIN, INTERACTION WITH BAX, AND
RP MUTAGENESIS OF LEU-120; 120-LEU--ARG-127 AND 125-GLY--GLU-127.
RC TISSUE=Cerebellum;
RX PubMed=11060313; DOI=10.1074/jbc.m008955200;
RA Tan K.O., Tan K.M.L., Chan S.-L., Yee K.S.Y., Bevort M., Ang K.C., Yu V.C.;
RT "MAP-1, a novel proapoptotic protein containing a BH3-like motif that
RT associates with Bax through its Bcl-2 homology domains.";
RL J. Biol. Chem. 276:2802-2807(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Retinoblastoma, and Tongue;
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 GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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 [5]
RP INTERACTION WITH RASSF1, INTRAMOLECULAR INTERACTION, MUTAGENESIS OF
RP 161-LYS--ARG-166; 178-GLU--ALA-181 AND 202-LYS--ARG-205, AND FUNCTION.
RX PubMed=15949439; DOI=10.1016/j.molcel.2005.05.010;
RA Baksh S., Tommasi S., Fenton S., Yu V.C., Martins L.M., Pfeifer G.P.,
RA Latif F., Downward J., Neel B.G.;
RT "The tumor suppressor RASSF1A and MAP-1 link death receptor signaling to
RT Bax conformational change and cell death.";
RL Mol. Cell 18:637-650(2005).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH BAX.
RX PubMed=16199525; DOI=10.1073/pnas.0503524102;
RA Tan K.O., Fu N.Y., Sukumaran S.K., Chan S.L., Kang J.H., Poon K.L.,
RA Chen B.S., Yu V.C.;
RT "MAP-1 is a mitochondrial effector of Bax.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:14623-14628(2005).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=19366867; DOI=10.1093/cercor/bhp062;
RA Takaji M., Komatsu Y., Watakabe A., Hashikawa T., Yamamori T.;
RT "Paraneoplastic antigen-like 5 gene (PNMA5) is preferentially expressed in
RT the association areas in a primate specific manner.";
RL Cereb. Cortex 19:2865-2879(2009).
RN [8]
RP INTERACTION WITH TRIM39.
RX PubMed=19100260; DOI=10.1016/j.yexcr.2008.11.021;
RA Lee S.S., Fu N.Y., Sukumaran S.K., Wan K.F., Wan Q., Yu V.C.;
RT "TRIM39 is a MOAP-1-binding protein that stabilizes MOAP-1 through
RT inhibition of its poly-ubiquitination process.";
RL Exp. Cell Res. 315:1313-1325(2009).
RN [9]
RP UBIQUITINATION BY APC/C-CDH1.
RX PubMed=22529100; DOI=10.1083/jcb.201111141;
RA Huang N.J., Zhang L., Tang W., Chen C., Yang C.S., Kornbluth S.;
RT "The Trim39 ubiquitin ligase inhibits APC/CCdh1-mediated degradation of the
RT Bax activator MOAP-1.";
RL J. Cell Biol. 197:361-367(2012).
RN [10]
RP FUNCTION, INTERACTION WITH MAP1LC3A; MAP1LC3B AND MAP1LC3C, DOMAIN, AND
RP MUTAGENESIS OF 49-TYR--LEU-52; 89-TRP--ILE-92 AND 162-TYR--LEU-165.
RX PubMed=33783314; DOI=10.1080/15548627.2021.1896157;
RA Chang H.C., Tao R.N., Tan C.T., Wu Y.J., Bay B.H., Yu V.C.;
RT "The BAX-binding protein MOAP1 associates with LC3 and promotes closure of
RT the phagophore.";
RL Autophagy 17:3725-3739(2021).
RN [11]
RP FUNCTION, AND INTERACTION WITH SQSTM1.
RX PubMed=33393215; DOI=10.15252/embr.202050854;
RA Tan C.T., Chang H.C., Zhou Q., Yu C., Fu N.Y., Sabapathy K., Yu V.C.;
RT "MOAP-1-mediated dissociation of p62/SQSTM1 bodies releases Keap1 and
RT suppresses Nrf2 signaling.";
RL EMBO Rep. 22:e50854-e50854(2021).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 246-351, AND DOMAIN.
RX PubMed=34357660; DOI=10.1002/prot.26204;
RA Zurowska K., Alam A., Ganser-Pornillos B.K., Pornillos O.;
RT "Structural evidence that MOAP1 and PEG10 are derived from
RT retrovirus/retrotransposon Gag proteins.";
RL Proteins 90:309-313(2022).
CC -!- FUNCTION: Retrotransposon-derived protein that forms virion-like
CC capsids (By similarity). Acts as an effector of BAX during apoptosis:
CC enriched at outer mitochondria membrane and associates with BAX upon
CC induction of apoptosis, facilitating BAX-dependent mitochondrial outer
CC membrane permeabilization and apoptosis (PubMed:11060313,
CC PubMed:16199525). Required for death receptor-dependent apoptosis
CC (PubMed:11060313). When associated with RASSF1, promotes BAX
CC conformational change and translocation to mitochondrial membranes in
CC response to TNF and TNFSF10 stimulation (PubMed:15949439). Also
CC promotes autophagy: promotes phagophore closure via association with
CC ATG8 proteins (PubMed:33783314). Acts as an inhibitor of the
CC NFE2L2/NRF2 pathway via interaction with SQSTM1: interaction promotes
CC dissociation of SQSTM1 inclusion bodies that sequester KEAP1, relieving
CC inactivation of the BCR(KEAP1) complex (PubMed:33393215).
CC {ECO:0000250|UniProtKB:Q9ERH6, ECO:0000269|PubMed:11060313,
CC ECO:0000269|PubMed:15949439, ECO:0000269|PubMed:16199525,
CC ECO:0000269|PubMed:33393215, ECO:0000269|PubMed:33783314}.
CC -!- SUBUNIT: Homodimer (PubMed:15949439). Under normal circumstances, held
CC in an inactive conformation by an intramolecular interaction
CC (PubMed:15949439). Interacts with BAX (PubMed:11060313,
CC PubMed:16199525). Binding to RASSF1 isoform A (RASSF1A) relieves this
CC inhibitory interaction and allows further binding to BAX
CC (PubMed:15949439). Binds also to BCL2 and BCLX (PubMed:11060313).
CC Recruited to the TNFRSF1A and TNFRSF10A complexes in response to their
CC respective cognate ligand, after internalization (PubMed:15949439).
CC Interacts with TRIM39 (PubMed:19100260). Interacts with RASSF6 (By
CC similarity). Interacts with ATG8 proteins MAP1LC3A, MAP1LC3B and
CC MAP1LC3C (PubMed:33783314). Does not interact with ATG8 proteins
CC GABARAPL1, GABARAPL2 and GABARAP (PubMed:33783314). Interacts with
CC SQSTM1; promoting dissociation of SQSTM1 inclusion bodies that
CC sequester KEAP1 (PubMed:33393215). {ECO:0000250|UniProtKB:Q9ERH6,
CC ECO:0000269|PubMed:11060313, ECO:0000269|PubMed:15949439,
CC ECO:0000269|PubMed:16199525, ECO:0000269|PubMed:19100260,
CC ECO:0000269|PubMed:33393215, ECO:0000269|PubMed:33783314}.
CC -!- INTERACTION:
CC Q96BY2; Q13557: CAMK2D; NbExp=3; IntAct=EBI-739825, EBI-351018;
CC Q96BY2; Q6PJG3: LATS1; NbExp=3; IntAct=EBI-739825, EBI-10253976;
CC Q96BY2; Q9NS73-5: MBIP; NbExp=3; IntAct=EBI-739825, EBI-10182361;
CC Q96BY2; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-739825, EBI-16439278;
CC Q96BY2; Q96PV4: PNMA5; NbExp=3; IntAct=EBI-739825, EBI-10171633;
CC Q96BY2; Q969Q6: PPP2R3C; NbExp=3; IntAct=EBI-739825, EBI-2561661;
CC Q96BY2; Q9BVN2: RUSC1; NbExp=3; IntAct=EBI-739825, EBI-6257312;
CC Q96BY2; Q96FV9: THOC1; NbExp=7; IntAct=EBI-739825, EBI-1765605;
CC Q96BY2; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-739825, EBI-947187;
CC Q96BY2; Q9H0C1: ZMYND12; NbExp=5; IntAct=EBI-739825, EBI-12030590;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:19100260}.
CC Mitochondrion outer membrane {ECO:0000269|PubMed:16199525}.
CC Extracellular vesicle membrane {ECO:0000250|UniProtKB:Q9ERH6}.
CC Note=Forms virion-like extracellular vesicles that are released from
CC cells. {ECO:0000250|UniProtKB:Q9ERH6}.
CC -!- TISSUE SPECIFICITY: Widely expressed, with high levels in heart and
CC brain. {ECO:0000269|PubMed:19366867}.
CC -!- DOMAIN: The protein is evolutionarily related to retrotransposon Gag
CC proteins: it contains the capsid (CA)subdomain of gag.
CC {ECO:0000269|PubMed:34357660}.
CC -!- DOMAIN: The BH3-like domain is required for association with BAX and
CC for mediating apoptosis (PubMed:11060313). The three BH domains (BH1,
CC BH2, and BH3) of BAX are all required for mediating protein-protein
CC interaction (PubMed:11060313). {ECO:0000269|PubMed:11060313}.
CC -!- DOMAIN: The LIR motif (LC3-interacting region) is required for the
CC interaction with the ATG8 family proteins MAP1LC3A, MAP1LC3B and
CC MAP1LC3C. {ECO:0000269|PubMed:33783314}.
CC -!- PTM: Ubiquitinated and degraded during mitotic exit by APC/C-Cdh1, this
CC modification is inhibited by TRIM39. {ECO:0000269|PubMed:22529100}.
CC -!- SIMILARITY: Belongs to the PNMA family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14788.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF305550; AAG31786.1; -; mRNA.
DR EMBL; AK024029; BAB14788.1; ALT_SEQ; mRNA.
DR EMBL; AK315522; BAG37903.1; -; mRNA.
DR EMBL; CH471061; EAW81516.1; -; Genomic_DNA.
DR EMBL; BC015044; AAH15044.1; -; mRNA.
DR CCDS; CCDS9908.1; -.
DR RefSeq; NP_071434.2; NM_022151.4.
DR PDB; 7LGC; X-ray; 1.85 A; A/B=242-351.
DR PDBsum; 7LGC; -.
DR AlphaFoldDB; Q96BY2; -.
DR SMR; Q96BY2; -.
DR BioGRID; 122069; 40.
DR DIP; DIP-49959N; -.
DR IntAct; Q96BY2; 31.
DR MINT; Q96BY2; -.
DR STRING; 9606.ENSP00000451594; -.
DR iPTMnet; Q96BY2; -.
DR PhosphoSitePlus; Q96BY2; -.
DR BioMuta; MOAP1; -.
DR DMDM; 37999755; -.
DR MassIVE; Q96BY2; -.
DR MaxQB; Q96BY2; -.
DR PaxDb; Q96BY2; -.
DR PeptideAtlas; Q96BY2; -.
DR PRIDE; Q96BY2; -.
DR ProteomicsDB; 76126; -.
DR Antibodypedia; 22; 319 antibodies from 32 providers.
DR DNASU; 64112; -.
DR Ensembl; ENST00000298894.5; ENSP00000298894.4; ENSG00000165943.5.
DR Ensembl; ENST00000556883.1; ENSP00000451594.1; ENSG00000165943.5.
DR Ensembl; ENST00000616515.2; ENSP00000482284.1; ENSG00000278268.2.
DR Ensembl; ENST00000627896.1; ENSP00000486260.1; ENSG00000278268.2.
DR GeneID; 64112; -.
DR KEGG; hsa:64112; -.
DR MANE-Select; ENST00000298894.5; ENSP00000298894.4; NM_022151.5; NP_071434.2.
DR UCSC; uc001ybj.4; human.
DR CTD; 64112; -.
DR DisGeNET; 64112; -.
DR GeneCards; MOAP1; -.
DR HGNC; HGNC:16658; MOAP1.
DR HPA; ENSG00000165943; Low tissue specificity.
DR MIM; 609485; gene.
DR neXtProt; NX_Q96BY2; -.
DR OpenTargets; ENSG00000165943; -.
DR PharmGKB; PA134908381; -.
DR VEuPathDB; HostDB:ENSG00000165943; -.
DR eggNOG; ENOG502SAVD; Eukaryota.
DR GeneTree; ENSGT01030000234522; -.
DR HOGENOM; CLU_014694_0_0_1; -.
DR InParanoid; Q96BY2; -.
DR OMA; GMIPEIR; -.
DR OrthoDB; 820525at2759; -.
DR PhylomeDB; Q96BY2; -.
DR TreeFam; TF335054; -.
DR PathwayCommons; Q96BY2; -.
DR SignaLink; Q96BY2; -.
DR BioGRID-ORCS; 64112; 14 hits in 1071 CRISPR screens.
DR ChiTaRS; MOAP1; human.
DR GeneWiki; MOAP1; -.
DR GenomeRNAi; 64112; -.
DR Pharos; Q96BY2; Tbio.
DR PRO; PR:Q96BY2; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q96BY2; protein.
DR Bgee; ENSG00000165943; Expressed in superior frontal gyrus and 104 other tissues.
DR Genevisible; Q96BY2; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
DR GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:BHF-UCL.
DR GO; GO:0005739; C:mitochondrion; IDA:BHF-UCL.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:BHF-UCL.
DR GO; GO:0097190; P:apoptotic signaling pathway; IDA:BHF-UCL.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IMP:BHF-UCL.
DR GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IMP:BHF-UCL.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IMP:BHF-UCL.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:2000786; P:positive regulation of autophagosome assembly; IMP:UniProtKB.
DR GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; IMP:BHF-UCL.
DR GO; GO:0001844; P:protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; IMP:BHF-UCL.
DR GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
DR InterPro; IPR026523; PNMA.
DR PANTHER; PTHR23095; PTHR23095; 1.
DR Pfam; PF14893; PNMA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; Autophagy; Cytoplasm; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Reference proteome; Ubl conjugation.
FT CHAIN 1..351
FT /note="Modulator of apoptosis 1"
FT /id="PRO_0000155205"
FT REGION 120..127
FT /note="BH3-like"
FT /evidence="ECO:0000303|PubMed:11060313"
FT REGION 202..205
FT /note="RASSF1-binding"
FT /evidence="ECO:0000269|PubMed:15949439"
FT MOTIF 49..52
FT /note="LIR"
FT /evidence="ECO:0000269|PubMed:33783314"
FT MUTAGEN 49..52
FT /note="YRLL->ARLA: Abolished interaction with ATG8 proteins
FT MAP1LC3A, MAP1LC3B and MAP1LC3C."
FT /evidence="ECO:0000269|PubMed:33783314"
FT MUTAGEN 89..92
FT /note="WRVI->ARVA: Does not affect interaction with ATG8
FT proteins MAP1LC3A, MAP1LC3B and MAP1LC3C."
FT /evidence="ECO:0000269|PubMed:33783314"
FT MUTAGEN 120..127
FT /note="Missing: Abrogates interaction with BAX, resulting
FT in a nonapoptotic protein."
FT /evidence="ECO:0000269|PubMed:11060313"
FT MUTAGEN 120
FT /note="L->E: Weakened interaction with BAX, resulting in a
FT nonapoptotic protein."
FT /evidence="ECO:0000269|PubMed:11060313"
FT MUTAGEN 125..127
FT /note="GHE->VLA: Abrogates interaction with BAX, resulting
FT in a nonapoptotic protein."
FT /evidence="ECO:0000269|PubMed:11060313"
FT MUTAGEN 161..166
FT /note="KYKKLR->AYAALA: No effect on RASSF1-binding."
FT /evidence="ECO:0000269|PubMed:15949439"
FT MUTAGEN 162..165
FT /note="YKKL->AKKA: Does not affect interaction with ATG8
FT proteins MAP1LC3A, MAP1LC3B and MAP1LC3C."
FT /evidence="ECO:0000269|PubMed:33783314"
FT MUTAGEN 178..180
FT /note="EEE->AAA: No effect on RASSF1-binding; interacts
FT with BAX in the absence of RASSF1."
FT MUTAGEN 202..205
FT /note="KRRR->AAAA: Loss of RASSF1-binding; interacts with
FT BAX in the absence of RASSF1."
FT /evidence="ECO:0000269|PubMed:15949439"
FT CONFLICT 244
FT /note="T -> A (in Ref. 2; BAB14788)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="Y -> H (in Ref. 2; BAB14788)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="Q -> H (in Ref. 1; AAG31786)"
FT /evidence="ECO:0000305"
FT HELIX 247..255
FT /evidence="ECO:0007829|PDB:7LGC"
FT HELIX 265..281
FT /evidence="ECO:0007829|PDB:7LGC"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:7LGC"
FT HELIX 290..301
FT /evidence="ECO:0007829|PDB:7LGC"
FT HELIX 307..310
FT /evidence="ECO:0007829|PDB:7LGC"
FT HELIX 322..346
FT /evidence="ECO:0007829|PDB:7LGC"
SQ SEQUENCE 351 AA; 39513 MW; 5310142AC02B563C CRC64;
MTLRLLEDWC RGMDMNPRKA LLIAGISQSC SVAEIEEALQ AGLAPLGEYR LLGRMFRRDE
NRKVALVGLT AETSHALVPK EIPGKGGIWR VIFKPPDPDN TFLSRLNEFL AGEGMTVGEL
SRALGHENGS LDPEQGMIPE MWAPMLAQAL EALQPALQCL KYKKLRVFSG RESPEPGEEE
FGRWMFHTTQ MIKAWQVPDV EKRRRLLESL RGPALDVIRV LKINNPLITV DECLQALEEV
FGVTDNPREL QVKYLTTYQK DEEKLSAYVL RLEPLLQKLV QRGAIERDAV NQARLDQVIA
GAVHKTIRRE LNLPEDGPAP GFLQLLVLIK DYEAAEEEEA LLQAILEGNF T
