PGAM5_HUMAN
ID PGAM5_HUMAN Reviewed; 289 AA.
AC Q96HS1; A9LN06; C9IZY7; Q96JB0;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Serine/threonine-protein phosphatase PGAM5, mitochondrial;
DE EC=3.1.3.16 {ECO:0000269|PubMed:19590015};
DE AltName: Full=Bcl-XL-binding protein v68;
DE AltName: Full=Phosphoglycerate mutase family member 5;
GN Name=PGAM5;
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], IDENTIFICATION BY MASS SPECTROMETRY,
RP ALTERNATIVE SPLICING, SUBUNIT, INTERACTION WITH BCL2L1 AND KEAP1, AND
RP MUTAGENESIS OF GLU-79 AND SER-80.
RX PubMed=17046835; DOI=10.1074/jbc.m606539200;
RA Lo S.-C., Hannink M.;
RT "PGAM5, a Bcl-XL-interacting protein, is a novel substrate for the redox-
RT regulated Keap1-dependent ubiquitin ligase complex.";
RL J. Biol. Chem. 281:37893-37903(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Cervix;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 124-157.
RC TISSUE=Kidney;
RX PubMed=11283018; DOI=10.1074/jbc.m011641200;
RA Hammond P.W., Alpin J., Rise C.E., Wright M., Kreider B.L.;
RT "In vitro selection and characterization of Bcl-X(L)-binding proteins from
RT a mix of tissue-specific mRNA display libraries.";
RL J. Biol. Chem. 276:20898-20906(2001).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, INTERACTION WITH NFE2L2 AND
RP KEAP1, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18387606; DOI=10.1016/j.yexcr.2008.02.014;
RA Lo S.-C., Hannink M.;
RT "PGAM5 tethers a ternary complex containing Keap1 and Nrf2 to
RT mitochondria.";
RL Exp. Cell Res. 314:1789-1803(2008).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH MAP3K5, AND MUTAGENESIS OF
RP HIS-105.
RX PubMed=19590015; DOI=10.1073/pnas.0901823106;
RA Takeda K., Komuro Y., Hayakawa T., Oguchi H., Ishida Y., Murakami S.,
RA Noguchi T., Kinoshita H., Sekine Y., Iemura S., Natsume T., Ichijo H.;
RT "Mitochondrial phosphoglycerate mutase 5 uses alternate catalytic activity
RT as a protein serine/threonine phosphatase to activate ASK1.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:12301-12305(2009).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-116; LYS-144 AND LYS-191, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [10]
RP FUNCTION, IDENTIFICATION IN COMPLEX WITH RIPK1; RIPK3 AND MLKL, AND
RP INTERACTION WITH DNM1L.
RX PubMed=22265414; DOI=10.1016/j.cell.2011.11.030;
RA Wang Z., Jiang H., Chen S., Du F., Wang X.;
RT "The mitochondrial phosphatase PGAM5 functions at the convergence point of
RT multiple necrotic death pathways.";
RL Cell 148:228-243(2012).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-87, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 90-289.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human phosphoglycerate mutase family member 5
RT (PGAM5).";
RL Submitted (SEP-2010) to the PDB data bank.
CC -!- FUNCTION: Displays phosphatase activity for serine/threonine residues,
CC and, dephosphorylates and activates MAP3K5 kinase. Has apparently no
CC phosphoglycerate mutase activity. May be regulator of mitochondrial
CC dynamics. Substrate for a KEAP1-dependent ubiquitin ligase complex.
CC Contributes to the repression of NFE2L2-dependent gene expression. Acts
CC as a central mediator for programmed necrosis induced by TNF, by
CC reactive oxygen species and by calcium ionophore.
CC {ECO:0000269|PubMed:18387606, ECO:0000269|PubMed:19590015,
CC ECO:0000269|PubMed:22265414}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC Evidence={ECO:0000269|PubMed:19590015};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC Evidence={ECO:0000269|PubMed:19590015};
CC -!- SUBUNIT: Dimer. Forms a ternary complex with NFE2L2 and KEAP1.
CC Interacts with BCL2L1 and MAP3K5. Upon TNF-induced necrosis, forms in
CC complex with RIPK1, RIPK3 and MLKL; the formation of this complex leads
CC to PGAM5 phosphorylation. Isoform 2, but not isoform 1, interacts with
CC DNM1L; this interaction leads to DNM1L dephosphorylation and activation
CC and eventually to mitochondria fragmentation.
CC {ECO:0000269|PubMed:17046835, ECO:0000269|PubMed:18387606,
CC ECO:0000269|PubMed:19590015, ECO:0000269|PubMed:22265414}.
CC -!- INTERACTION:
CC Q96HS1; Q99683: MAP3K5; NbExp=2; IntAct=EBI-713608, EBI-476263;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:18387606}; Single-pass membrane protein
CC {ECO:0000269|PubMed:18387606}. Note=Isoform 2 overexpression results in
CC the formation of disconnected punctuate mitochondria distributed
CC throughout the cytoplasm. Isoform 1 overexpression results in the
CC clustering of mitochondria around the nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=PGAM5-L;
CC IsoId=Q96HS1-1; Sequence=Displayed;
CC Name=2; Synonyms=PGAM5-S;
CC IsoId=Q96HS1-2; Sequence=VSP_025761;
CC -!- DOMAIN: The N-terminal 35 amino acids, including the potential
CC transmembrane alpha-helix, function as a non-cleaved mitochondrial
CC targeting sequence that targets the protein to the cytosolic side of
CC the outer mitochondrial membrane. {ECO:0000269|PubMed:18387606}.
CC -!- PTM: Both isoform 1 and isoform 2 are phosphorylated by the RIPK1/RIPK3
CC complex under necrotic conditions. This phosphorylation increases PGAM5
CC phosphatase activity.
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC dependent PGAM subfamily. {ECO:0000305}.
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DR EMBL; EU249757; ABX39494.1; -; mRNA.
DR EMBL; AC135586; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC008196; AAH08196.1; -; mRNA.
DR EMBL; AF357523; AAK60627.1; -; mRNA.
DR CCDS; CCDS53845.1; -. [Q96HS1-1]
DR CCDS; CCDS9280.1; -. [Q96HS1-2]
DR RefSeq; NP_001164014.1; NM_001170543.1. [Q96HS1-1]
DR RefSeq; NP_612642.2; NM_138575.3. [Q96HS1-2]
DR PDB; 3MXO; X-ray; 1.70 A; A/B=90-289.
DR PDB; 3O0T; X-ray; 1.90 A; A/B=90-289.
DR PDB; 5MUF; X-ray; 3.10 A; A/B/C=54-289.
DR PDB; 6CNI; X-ray; 1.70 A; A/B=90-289.
DR PDB; 6CNL; X-ray; 2.60 A; A/B/C/D/E/F/G/H/I/J/K/L=90-289.
DR PDBsum; 3MXO; -.
DR PDBsum; 3O0T; -.
DR PDBsum; 5MUF; -.
DR PDBsum; 6CNI; -.
DR PDBsum; 6CNL; -.
DR AlphaFoldDB; Q96HS1; -.
DR SMR; Q96HS1; -.
DR BioGRID; 128154; 226.
DR CORUM; Q96HS1; -.
DR DIP; DIP-50735N; -.
DR ELM; Q96HS1; -.
DR IntAct; Q96HS1; 87.
DR MINT; Q96HS1; -.
DR STRING; 9606.ENSP00000438465; -.
DR ChEMBL; CHEMBL4802013; -.
DR DEPOD; PGAM5; -.
DR GlyGen; Q96HS1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96HS1; -.
DR PhosphoSitePlus; Q96HS1; -.
DR SwissPalm; Q96HS1; -.
DR BioMuta; PGAM5; -.
DR DMDM; 150417955; -.
DR EPD; Q96HS1; -.
DR jPOST; Q96HS1; -.
DR MassIVE; Q96HS1; -.
DR MaxQB; Q96HS1; -.
DR PaxDb; Q96HS1; -.
DR PeptideAtlas; Q96HS1; -.
DR PRIDE; Q96HS1; -.
DR ProteomicsDB; 76781; -. [Q96HS1-1]
DR ProteomicsDB; 76782; -. [Q96HS1-2]
DR TopDownProteomics; Q96HS1-1; -. [Q96HS1-1]
DR TopDownProteomics; Q96HS1-2; -. [Q96HS1-2]
DR Antibodypedia; 49123; 61 antibodies from 15 providers.
DR DNASU; 192111; -.
DR Ensembl; ENST00000317555.6; ENSP00000321503.2; ENSG00000247077.7. [Q96HS1-2]
DR Ensembl; ENST00000498926.7; ENSP00000438465.1; ENSG00000247077.7. [Q96HS1-1]
DR GeneID; 192111; -.
DR KEGG; hsa:192111; -.
DR MANE-Select; ENST00000498926.7; ENSP00000438465.1; NM_001170543.2; NP_001164014.1.
DR UCSC; uc001uku.4; human. [Q96HS1-1]
DR CTD; 192111; -.
DR DisGeNET; 192111; -.
DR GeneCards; PGAM5; -.
DR HGNC; HGNC:28763; PGAM5.
DR HPA; ENSG00000247077; Low tissue specificity.
DR MIM; 614939; gene.
DR neXtProt; NX_Q96HS1; -.
DR OpenTargets; ENSG00000247077; -.
DR PharmGKB; PA143485574; -.
DR VEuPathDB; HostDB:ENSG00000247077; -.
DR eggNOG; KOG4609; Eukaryota.
DR GeneTree; ENSGT00390000004796; -.
DR HOGENOM; CLU_063130_0_1_1; -.
DR InParanoid; Q96HS1; -.
DR OMA; WHSPLPR; -.
DR OrthoDB; 1112626at2759; -.
DR PhylomeDB; Q96HS1; -.
DR TreeFam; TF314977; -.
DR BRENDA; 3.1.3.16; 2681.
DR PathwayCommons; Q96HS1; -.
DR Reactome; R-HSA-8934903; Receptor Mediated Mitophagy. [Q96HS1-2]
DR SignaLink; Q96HS1; -.
DR BioGRID-ORCS; 192111; 12 hits in 1075 CRISPR screens.
DR ChiTaRS; PGAM5; human.
DR EvolutionaryTrace; Q96HS1; -.
DR GenomeRNAi; 192111; -.
DR Pharos; Q96HS1; Tbio.
DR PRO; PR:Q96HS1; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q96HS1; protein.
DR Bgee; ENSG00000247077; Expressed in gastrocnemius and 101 other tissues.
DR ExpressionAtlas; Q96HS1; baseline and differential.
DR Genevisible; Q96HS1; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005096; F:GTPase activator activity; IMP:UniProtKB.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016791; F:phosphatase activity; IMP:UniProtKB.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:CACAO.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB.
DR GO; GO:0016236; P:macroautophagy; TAS:Reactome.
DR GO; GO:0070266; P:necroptotic process; IMP:UniProtKB.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0035970; P:peptidyl-threonine dephosphorylation; IBA:GO_Central.
DR GO; GO:0090141; P:positive regulation of mitochondrial fission; IBA:GO_Central.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.1240; -; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR Pfam; PF00300; His_Phos_1; 1.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Hydrolase; Membrane;
KW Mitochondrion; Mitochondrion outer membrane; Necrosis; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..289
FT /note="Serine/threonine-protein phosphatase PGAM5,
FT mitochondrial"
FT /id="PRO_0000288782"
FT TRANSMEM 7..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 32..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 77..82
FT /note="Interaction with KEAP1"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 116
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 144
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 191
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 240..289
FT /note="RALQFPPEGWLRLSLNNGSITHLVIRPNGRVALRTLGDTGFMPPDKITRS
FT -> SIPPLLSAGDFVLLGS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025761"
FT MUTAGEN 79
FT /note="E->A: Loss of interaction with KEAP1; when
FT associated with A-80."
FT /evidence="ECO:0000269|PubMed:17046835"
FT MUTAGEN 80
FT /note="S->A: Loss of interaction with KEAP1; when
FT associated with A-79."
FT /evidence="ECO:0000269|PubMed:17046835"
FT MUTAGEN 105
FT /note="H->A: Loss of phosphatase activity."
FT /evidence="ECO:0000269|PubMed:19590015"
FT CONFLICT 124
FT /note="G -> C (in Ref. 3; AAK60627)"
FT /evidence="ECO:0000305"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:3MXO"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:3MXO"
FT HELIX 122..136
FT /evidence="ECO:0007829|PDB:3MXO"
FT STRAND 143..150
FT /evidence="ECO:0007829|PDB:3MXO"
FT HELIX 151..162
FT /evidence="ECO:0007829|PDB:3MXO"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:3MXO"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:3MXO"
FT HELIX 197..211
FT /evidence="ECO:0007829|PDB:3MXO"
FT STRAND 223..229
FT /evidence="ECO:0007829|PDB:3MXO"
FT HELIX 231..241
FT /evidence="ECO:0007829|PDB:3MXO"
FT HELIX 246..251
FT /evidence="ECO:0007829|PDB:3MXO"
FT STRAND 259..264
FT /evidence="ECO:0007829|PDB:3MXO"
FT STRAND 270..277
FT /evidence="ECO:0007829|PDB:3MXO"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:3MXO"
FT CONFLICT Q96HS1-2:252
FT /note="L -> V (in Ref. 2; AAH08196)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 289 AA; 32004 MW; EE20D2F0A99FCD83 CRC64;
MAFRQALQLA ACGLAGGSAA VLFSAVAVGK PRAGGDAEPR PAEPPAWAGG ARPGPGVWDP
NWDRREPLSL INVRKRNVES GEEELASKLD HYKAKATRHI FLIRHSQYHV DGSLEKDRTL
TPLGREQAEL TGLRLASLGL KFNKIVHSSM TRAIETTDII SRHLPGVCKV STDLLREGAP
IEPDPPVSHW KPEAVQYYED GARIEAAFRN YIHRADARQE EDSYEIFICH ANVIRYIVCR
ALQFPPEGWL RLSLNNGSIT HLVIRPNGRV ALRTLGDTGF MPPDKITRS
