ID   ATP5J_HUMAN             Reviewed;         108 AA.
AC   P18859; J3KQ83;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   27-MAR-2024, entry version 215.
DE   RecName: Full=ATP synthase-coupling factor 6, mitochondrial {ECO:0000305};
DE            Short=ATPase subunit F6;
DE   AltName: Full=ATP synthase peripheral stalk subunit F6 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=ATP5PF {ECO:0000312|HGNC:HGNC:847}; Synonyms=ATP5A, ATP5J, ATPM;
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).
RX   PubMed=1825642; DOI=10.1016/0378-1119(91)90068-m;
RA   Javed A.A., Ogata K., Sanadi D.R.;
RT   "Human mitochondrial ATP synthase: cloning cDNA for the nuclear-encoded
RT   precursor of coupling factor 6.";
RL   Gene 97:307-310(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=1830479; DOI=10.1016/0006-291x(91)90178-a;
RA   Higuti T., Tsurumi C., Kawamura Y., Tsujita H., Osaka F., Yoshihara Y.,
RA   Tani I., Tanaka K., Ichihara A.;
RT   "Molecular cloning of cDNA for the import precursor of human coupling
RT   factor 6 of H(+)-ATP synthase in mitochondria.";
RL   Biochem. Biophys. Res. Commun. 178:793-799(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Kidney;
RX   PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA   Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA   Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA   Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA   Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA   Klein M., Poustka A.;
RT   "Towards a catalog of human genes and proteins: sequencing and analysis of
RT   500 novel complete protein coding human cDNAs.";
RL   Genome Res. 11:422-435(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX   PubMed=17213182; DOI=10.1093/dnares/dsl016;
RA   Kim J.M., Lee K.H., Jeon Y.J., Oh J.H., Jeong S.Y., Song I.S., Kim J.M.,
RA   Lee D.S., Kim N.S.;
RT   "Identification of genes related to Parkinson's disease using expressed
RT   sequence tags.";
RL   DNA Res. 13:275-286(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10830953; DOI=10.1038/35012518;
RA   Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA   Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA   Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA   Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA   Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA   Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA   Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA   Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA   Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA   Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA   Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT   "The DNA sequence of human chromosome 21.";
RL   Nature 405:311-319(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Eye;
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   [8]
RP   PROTEIN SEQUENCE OF 33-43.
RC   TISSUE=Liver;
RX   PubMed=1286669; DOI=10.1002/elps.11501301201;
RA   Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F.,
RA   Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R.,
RA   Appel R.D., Hughes G.J.;
RT   "Human liver protein map: a reference database established by
RT   microsequencing and gel comparison.";
RL   Electrophoresis 13:992-1001(1992).
RN   [9]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-41; LYS-46; LYS-99 AND LYS-105,
RP   AND 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   [10]
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   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and 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].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [13]
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   [14]
RP   VARIANT THR-39.
RX   PubMed=29961568; DOI=10.1016/j.ajhg.2018.06.001;
RG   NIHR BioResource;
RG   Care4Rare Canada Consortium;
RA   Ito Y., Carss K.J., Duarte S.T., Hartley T., Keren B., Kurian M.A.,
RA   Marey I., Charles P., Mendonca C., Nava C., Pfundt R., Sanchis-Juan A.,
RA   van Bokhoven H., van Essen A., van Ravenswaaij-Arts C., Boycott K.M.,
RA   Kernohan K.D., Dyack S., Raymond F.L.;
RT   "De Novo Truncating Mutations in WASF1 Cause Intellectual Disability with
RT   Seizures.";
RL   Am. J. Hum. Genet. 103:144-153(2018).
CC   -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or
CC       Complex V) produces ATP from ADP in the presence of a proton gradient
CC       across the membrane which is generated by electron transport complexes
CC       of the respiratory chain. F-type ATPases consist of two structural
CC       domains, F(1) - containing the extramembraneous catalytic core and F(0)
CC       - containing the membrane proton channel, linked together by a central
CC       stalk and a peripheral stalk. During catalysis, ATP synthesis in the
CC       catalytic domain of F(1) is coupled via a rotary mechanism of the
CC       central stalk subunits to proton translocation. Part of the complex
CC       F(0) domain and the peripheric stalk, which acts as a stator to hold
CC       the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static
CC       relative to the rotary elements. Also involved in the restoration of
CC       oligomycin-sensitive ATPase activity to depleted F1-F0 complexes.
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC       - and CF(0) - the membrane proton channel. CF(0) seems to have nine
CC       subunits: a, b, c, d, e, f, g, F6 and 8 (or A6L). Component of an ATP
CC       synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME,
CC       ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C,
CC       ATP5PO, ATP5MG, ATP5MK and MP68 (By similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       P18859; O95870: ABHD16A; NbExp=3; IntAct=EBI-2606700, EBI-348517;
CC       P18859; P25705: ATP5F1A; NbExp=4; IntAct=EBI-2606700, EBI-351437;
CC       P18859; Q92843: BCL2L2; NbExp=3; IntAct=EBI-2606700, EBI-707714;
CC       P18859; Q9BT40: INPP5K; NbExp=3; IntAct=EBI-2606700, EBI-749162;
CC       P18859; O95279: KCNK5; NbExp=3; IntAct=EBI-2606700, EBI-3934936;
CC       P18859; Q13021: MALL; NbExp=3; IntAct=EBI-2606700, EBI-750078;
CC       P18859; Q9NQG6: MIEF1; NbExp=3; IntAct=EBI-2606700, EBI-740987;
CC       P18859; Q96C03-3: MIEF2; NbExp=3; IntAct=EBI-2606700, EBI-11988931;
CC       P18859; O75425: MOSPD3; NbExp=3; IntAct=EBI-2606700, EBI-12179105;
CC       P18859; Q9ULP0-2: NDRG4; NbExp=3; IntAct=EBI-2606700, EBI-11978907;
CC       P18859; Q8TCD6: PHOSPHO2; NbExp=5; IntAct=EBI-2606700, EBI-2861380;
CC       P18859; Q04941: PLP2; NbExp=3; IntAct=EBI-2606700, EBI-608347;
CC       P18859; P43378: PTPN9; NbExp=3; IntAct=EBI-2606700, EBI-742898;
CC       P18859; Q96HR9-2: REEP6; NbExp=3; IntAct=EBI-2606700, EBI-14065960;
CC       P18859; O95562: SFT2D2; NbExp=3; IntAct=EBI-2606700, EBI-4402330;
CC       P18859; Q96PQ1: SIGLEC12; NbExp=3; IntAct=EBI-2606700, EBI-17640454;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P18859-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P18859-2; Sequence=VSP_046187;
CC   -!- SIMILARITY: Belongs to the eukaryotic ATPase subunit F6 family.
CC       {ECO:0000305}.
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DR   EMBL; M37104; AAA51807.1; -; mRNA.
DR   EMBL; M73031; AAA58630.1; -; mRNA.
DR   EMBL; AL110183; CAB53667.1; -; mRNA.
DR   EMBL; BT007244; AAP35908.1; -; mRNA.
DR   EMBL; DT217787; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AP001694; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC001178; AAH01178.1; -; mRNA.
DR   CCDS; CCDS13574.1; -. [P18859-1]
DR   CCDS; CCDS46637.1; -. [P18859-2]
DR   PIR; JT0563; JT0563.
DR   RefSeq; NP_001003696.1; NM_001003696.1. [P18859-1]
DR   RefSeq; NP_001003697.1; NM_001003697.1. [P18859-1]
DR   RefSeq; NP_001003701.1; NM_001003701.1. [P18859-2]
DR   RefSeq; NP_001003703.1; NM_001003703.1. [P18859-1]
DR   RefSeq; NP_001307195.1; NM_001320266.1. [P18859-1]
DR   RefSeq; NP_001307196.1; NM_001320267.1. [P18859-1]
DR   RefSeq; NP_001676.2; NM_001685.4. [P18859-1]
DR   PDB; 8H9G; EM; 2.95 A; L=1-108.
DR   PDB; 8H9K; EM; 3.51 A; L=1-108.
DR   PDB; 8H9N; EM; 3.56 A; L=1-108.
DR   PDB; 8H9R; EM; 3.97 A; L=1-108.
DR   PDB; 8H9S; EM; 2.53 A; L=1-108.
DR   PDB; 8H9T; EM; 2.77 A; L=1-108.
DR   PDB; 8H9U; EM; 2.61 A; L=1-108.
DR   PDB; 8H9V; EM; 3.02 A; L=1-108.
DR   PDBsum; 8H9G; -.
DR   PDBsum; 8H9K; -.
DR   PDBsum; 8H9N; -.
DR   PDBsum; 8H9R; -.
DR   PDBsum; 8H9S; -.
DR   PDBsum; 8H9T; -.
DR   PDBsum; 8H9U; -.
DR   PDBsum; 8H9V; -.
DR   AlphaFoldDB; P18859; -.
DR   EMDB; EMD-34566; -.
DR   EMDB; EMD-34570; -.
DR   EMDB; EMD-34574; -.
DR   EMDB; EMD-34578; -.
DR   EMDB; EMD-34580; -.
DR   EMDB; EMD-34581; -.
DR   EMDB; EMD-34582; -.
DR   EMDB; EMD-34583; -.
DR   SMR; P18859; -.
DR   BioGRID; 107006; 213.
DR   ComplexPortal; CPX-6151; Mitochondrial proton-transporting ATP synthase complex.
DR   CORUM; P18859; -.
DR   IntAct; P18859; 81.
DR   MINT; P18859; -.
DR   STRING; 9606.ENSP00000389649; -.
DR   TCDB; 3.A.2.1.15; the h+- or na+-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR   iPTMnet; P18859; -.
DR   PhosphoSitePlus; P18859; -.
DR   BioMuta; ATP5J; -.
DR   DMDM; 114688; -.
DR   EPD; P18859; -.
DR   jPOST; P18859; -.
DR   MassIVE; P18859; -.
DR   MaxQB; P18859; -.
DR   PaxDb; 9606-ENSP00000389649; -.
DR   PeptideAtlas; P18859; -.
DR   ProteomicsDB; 53618; -. [P18859-1]
DR   Pumba; P18859; -.
DR   TopDownProteomics; P18859-1; -. [P18859-1]
DR   Antibodypedia; 22308; 225 antibodies from 29 providers.
DR   DNASU; 522; -.
DR   Ensembl; ENST00000284971.8; ENSP00000284971.3; ENSG00000154723.13. [P18859-1]
DR   Ensembl; ENST00000400087.7; ENSP00000382959.3; ENSG00000154723.13. [P18859-1]
DR   Ensembl; ENST00000400090.7; ENSP00000382962.3; ENSG00000154723.13. [P18859-1]
DR   Ensembl; ENST00000400093.3; ENSP00000382965.3; ENSG00000154723.13. [P18859-1]
DR   Ensembl; ENST00000400094.5; ENSP00000382966.1; ENSG00000154723.13. [P18859-1]
DR   Ensembl; ENST00000457143.6; ENSP00000389649.2; ENSG00000154723.13. [P18859-2]
DR   GeneID; 522; -.
DR   KEGG; hsa:522; -.
DR   MANE-Select; ENST00000284971.8; ENSP00000284971.3; NM_001003703.2; NP_001003703.1.
DR   UCSC; uc002ylv.4; human. [P18859-1]
DR   AGR; HGNC:847; -.
DR   CTD; 522; -.
DR   DisGeNET; 522; -.
DR   GeneCards; ATP5PF; -.
DR   HGNC; HGNC:847; ATP5PF.
DR   HPA; ENSG00000154723; Tissue enhanced (tongue).
DR   MIM; 603152; gene.
DR   neXtProt; NX_P18859; -.
DR   OpenTargets; ENSG00000154723; -.
DR   PharmGKB; PA25137; -.
DR   VEuPathDB; HostDB:ENSG00000154723; -.
DR   eggNOG; KOG4634; Eukaryota.
DR   GeneTree; ENSGT00390000008902; -.
DR   HOGENOM; CLU_145649_1_0_1; -.
DR   InParanoid; P18859; -.
DR   OMA; FPTFEFK; -.
DR   OrthoDB; 4241537at2759; -.
DR   PhylomeDB; P18859; -.
DR   TreeFam; TF318998; -.
DR   BioCyc; MetaCyc:ENSG00000154723-MONOMER; -.
DR   PathwayCommons; P18859; -.
DR   Reactome; R-HSA-163210; Formation of ATP by chemiosmotic coupling.
DR   Reactome; R-HSA-8949613; Cristae formation.
DR   SignaLink; P18859; -.
DR   SIGNOR; P18859; -.
DR   BioGRID-ORCS; 522; 212 hits in 1112 CRISPR screens.
DR   ChiTaRS; ATP5J; human.
DR   GeneWiki; ATP5J; -.
DR   GenomeRNAi; 522; -.
DR   Pharos; P18859; Tbio.
DR   PRO; PR:P18859; -.
DR   Proteomes; UP000005640; Chromosome 21.
DR   RNAct; P18859; Protein.
DR   Bgee; ENSG00000154723; Expressed in left ventricle myocardium and 217 other cell types or tissues.
DR   ExpressionAtlas; P18859; baseline and differential.
DR   GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR   GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IDA:UniProtKB.
DR   GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IEA:InterPro.
DR   GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR   GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015986; P:proton motive force-driven ATP synthesis; NAS:ComplexPortal.
DR   GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IDA:UniProtKB.
DR   GO; GO:0021762; P:substantia nigra development; HEP:UniProtKB.
DR   Gene3D; 1.10.246.110; Mitochondrial ATP synthase-coupling factor 6; 1.
DR   InterPro; IPR008387; ATP_synth_f6_mt.
DR   InterPro; IPR036204; ATP_synth_f6_sf_mt.
DR   PANTHER; PTHR12441; ATP SYNTHASE COUPLING FACTOR 6, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR12441:SF10; ATP SYNTHASE-COUPLING FACTOR 6, MITOCHONDRIAL; 1.
DR   Pfam; PF05511; ATP-synt_F6; 1.
DR   PIRSF; PIRSF002455; ATP_synthase_coupling_factor_6; 1.
DR   SUPFAM; SSF111357; Mitochondrial ATP synthase coupling factor 6; 1.
DR   SWISS-2DPAGE; P18859; -.
DR   Genevisible; P18859; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; CF(0);
KW   Direct protein sequencing; Hydrogen ion transport; Ion transport; Membrane;
KW   Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
KW   Reference proteome; Transit peptide; Transport.
FT   TRANSIT         1..32
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:1286669"
FT   CHAIN           33..108
FT                   /note="ATP synthase-coupling factor 6, mitochondrial"
FT                   /id="PRO_0000002527"
FT   MOD_RES         41
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         46
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         65
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         79
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P97450"
FT   MOD_RES         94
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P97450"
FT   MOD_RES         94
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P97450"
FT   MOD_RES         99
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         99
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P97450"
FT   MOD_RES         105
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   VAR_SEQ         1
FT                   /note="M -> MHCDGGISM (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:17213182"
FT                   /id="VSP_046187"
FT   VARIANT         39
FT                   /note="I -> T"
FT                   /evidence="ECO:0000269|PubMed:29961568"
FT                   /id="VAR_083477"
FT   CONFLICT        68
FT                   /note="Q -> H (in Ref. 2; AAA58630)"
FT                   /evidence="ECO:0000305"
FT   HELIX           41..54
FT                   /evidence="ECO:0007829|PDB:8H9G"
FT   STRAND          60..63
FT                   /evidence="ECO:0007829|PDB:8H9G"
FT   HELIX           68..82
FT                   /evidence="ECO:0007829|PDB:8H9G"
SQ   SEQUENCE   108 AA;  12588 MW;  EDC1A14F01A10F17 CRC64;
     MILQRLFRFS SVIRSAVSVH LRRNIGVTAV AFNKELDPIQ KLFVDKIREY KSKRQTSGGP
     VDASSEYQQE LERELFKLKQ MFGNADMNTF PTFKFEDPKF EVIEKPQA
//