ID   ATPD_HUMAN              Reviewed;         168 AA.
AC   P30049; D6W5Y3; Q6FG90;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 2.
DT   27-MAR-2024, entry version 213.
DE   RecName: Full=ATP synthase subunit delta, mitochondrial {ECO:0000305};
DE   AltName: Full=ATP synthase F1 subunit delta {ECO:0000312|HGNC:HGNC:837};
DE   AltName: Full=F-ATPase delta subunit;
DE   Flags: Precursor;
GN   Name=ATP5F1D {ECO:0000312|HGNC:HGNC:837};
GN   Synonyms=ATP5D {ECO:0000312|HGNC:HGNC:837};
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], AND FUNCTION.
RX   PubMed=1531933; DOI=10.1016/0167-4781(92)90477-h;
RA   Jordan E.M., Breen G.A.M.;
RT   "Molecular cloning of an import precursor of the delta-subunit of the human
RT   mitochondrial ATP synthase complex.";
RL   Biochim. Biophys. Acta 1130:123-126(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA   Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA   LaBaer J.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA   Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA   Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA   Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA   Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA   Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA   Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA   Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA   Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA   McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA   Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA   Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA   She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA   Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, and Lung;
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   [6]
RP   PROTEIN SEQUENCE OF 23-38.
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   [7]
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   [8]
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   [9]
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   [10]
RP   FUNCTION, INVOLVEMENT IN MC5DN5, VARIANTS MC5DN5 LEU-82 AND GLY-106, AND
RP   CHARACTERIZATION OF VARIANTS MC5DN5 LEU-82 AND GLY-106.
RX   PubMed=29478781; DOI=10.1016/j.ajhg.2018.01.020;
RG   Undiagnosed Diseases Network;
RA   Olahova M., Yoon W.H., Thompson K., Jangam S., Fernandez L., Davidson J.M.,
RA   Kyle J.E., Grove M.E., Fisk D.G., Kohler J.N., Holmes M., Dries A.M.,
RA   Huang Y., Zhao C., Contrepois K., Zappala Z., Fresard L., Waggott D.,
RA   Zink E.M., Kim Y.M., Heyman H.M., Stratton K.G., Webb-Robertson B.M.,
RA   Snyder M., Merker J.D., Montgomery S.B., Fisher P.G., Feichtinger R.G.,
RA   Mayr J.A., Hall J., Barbosa I.A., Simpson M.A., Deshpande C., Waters K.M.,
RA   Koeller D.M., Metz T.O., Morris A.A., Schelley S., Cowan T.,
RA   Friederich M.W., McFarland R., Van Hove J.L.K., Enns G.M., Yamamoto S.,
RA   Ashley E.A., Wangler M.F., Taylor R.W., Bellen H.J., Bernstein J.A.,
RA   Wheeler M.T.;
RT   "Biallelic Mutations in ATP5F1D, which Encodes a Subunit of ATP Synthase,
RT   Cause a Metabolic Disorder.";
RL   Am. J. Hum. Genet. 102:494-504(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 (PubMed:29478781). F-type ATPases consist of
CC       two structural domains, F(1) - containing the extramembraneous
CC       catalytic core, and F(0) - containing the membrane proton channel,
CC       linked together by a central stalk and a peripheral stalk. During
CC       catalysis, ATP turnover in the catalytic domain of F(1) is coupled via
CC       a rotary mechanism of the central stalk subunits to proton
CC       translocation. Part of the complex F(1) domain and of the central stalk
CC       which is part of the complex rotary element. Rotation of the central
CC       stalk against the surrounding alpha(3)beta(3) subunits leads to
CC       hydrolysis of ATP in three separate catalytic sites on the beta
CC       subunits (PubMed:1531933). {ECO:0000269|PubMed:29478781,
CC       ECO:0000303|PubMed:1531933}.
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC       - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC       alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) seems to have
CC       nine subunits: a, b, c, d, e, f, g, F6 and 8 (or A6L). Component of an
CC       ATP synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD,
CC       ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D,
CC       ATP5F1C, ATP5PO, ATP5MG, ATP5MK and ATP5MJ (By similarity).
CC       {ECO:0000250}.
CC   -!- INTERACTION:
CC       P30049; P56381: ATP5F1E; NbExp=4; IntAct=EBI-1049505, EBI-3904845;
CC       P30049; P54253: ATXN1; NbExp=3; IntAct=EBI-1049505, EBI-930964;
CC       P30049; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-1049505, EBI-10171774;
CC       P30049; Q99750: MDFI; NbExp=3; IntAct=EBI-1049505, EBI-724076;
CC       P30049; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-1049505, EBI-22310682;
CC       P30049; Q05519-2: SRSF11; NbExp=3; IntAct=EBI-1049505, EBI-11975029;
CC       P30049; Q63HR2: TNS2; NbExp=3; IntAct=EBI-1049505, EBI-949753;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC   -!- DISEASE: Mitochondrial complex V deficiency, nuclear type 5 (MC5DN5)
CC       [MIM:618120]: A mitochondrial disorder characterized by childhood onset
CC       of episodic metabolic decompensation featuring lactic acidosis and
CC       hyperammonemia accompanied by ketoacidosis or hypoglycemia. Chronic
CC       manifestations include developmental delay, easy fatiguability, and 3-
CC       methylglutaconic aciduria. The transmission pattern of MC5DN5 is
CC       consistent with autosomal recessive inheritance.
CC       {ECO:0000269|PubMed:29478781}. Note=Disease susceptibility is
CC       associated with variants affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the ATPase epsilon chain family. {ECO:0000305}.
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DR   EMBL; S87916; AAA08055.1; -; mRNA.
DR   EMBL; S87918; ABB76284.1; -; mRNA.
DR   EMBL; X63422; CAA45016.1; -; mRNA.
DR   EMBL; X63423; CAA45017.1; -; mRNA.
DR   EMBL; CR542218; CAG47014.1; -; mRNA.
DR   EMBL; AC004221; AAC04304.1; -; Genomic_DNA.
DR   EMBL; CH471139; EAW69532.1; -; Genomic_DNA.
DR   EMBL; CH471139; EAW69533.1; -; Genomic_DNA.
DR   EMBL; CH471139; EAW69534.1; -; Genomic_DNA.
DR   EMBL; BC002389; AAH02389.1; -; mRNA.
DR   EMBL; BC004426; AAH04426.1; -; mRNA.
DR   EMBL; BC018079; AAH18079.1; -; mRNA.
DR   CCDS; CCDS12058.1; -.
DR   PIR; S22348; S22348.
DR   RefSeq; NP_001001975.1; NM_001001975.1.
DR   RefSeq; NP_001678.1; NM_001687.4.
DR   PDB; 8H9F; EM; 2.69 A; H=23-168.
DR   PDB; 8H9J; EM; 3.26 A; H=23-168.
DR   PDB; 8H9M; EM; 3.00 A; H=23-168.
DR   PDB; 8H9Q; EM; 3.47 A; H=23-168.
DR   PDB; 8H9S; EM; 2.53 A; H=23-168.
DR   PDB; 8H9T; EM; 2.77 A; H=23-168.
DR   PDB; 8H9U; EM; 2.61 A; H=23-168.
DR   PDB; 8H9V; EM; 3.02 A; H=23-168.
DR   PDBsum; 8H9F; -.
DR   PDBsum; 8H9J; -.
DR   PDBsum; 8H9M; -.
DR   PDBsum; 8H9Q; -.
DR   PDBsum; 8H9S; -.
DR   PDBsum; 8H9T; -.
DR   PDBsum; 8H9U; -.
DR   PDBsum; 8H9V; -.
DR   AlphaFoldDB; P30049; -.
DR   EMDB; EMD-34565; -.
DR   EMDB; EMD-34569; -.
DR   EMDB; EMD-34573; -.
DR   EMDB; EMD-34577; -.
DR   EMDB; EMD-34580; -.
DR   EMDB; EMD-34581; -.
DR   EMDB; EMD-34582; -.
DR   EMDB; EMD-34583; -.
DR   SMR; P30049; -.
DR   BioGRID; 106998; 149.
DR   ComplexPortal; CPX-6151; Mitochondrial proton-transporting ATP synthase complex.
DR   CORUM; P30049; -.
DR   IntAct; P30049; 66.
DR   MINT; P30049; -.
DR   STRING; 9606.ENSP00000215375; -.
DR   DrugBank; DB01189; Desflurane.
DR   DrugBank; DB00753; Isoflurane.
DR   DrugBank; DB13749; Magnesium gluconate.
DR   TCDB; 3.A.2.1.15; the h+- or na+-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR   GlyGen; P30049; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P30049; -.
DR   PhosphoSitePlus; P30049; -.
DR   BioMuta; ATP5D; -.
DR   DMDM; 584812; -.
DR   OGP; P30049; -.
DR   EPD; P30049; -.
DR   jPOST; P30049; -.
DR   MassIVE; P30049; -.
DR   MaxQB; P30049; -.
DR   PaxDb; 9606-ENSP00000215375; -.
DR   PeptideAtlas; P30049; -.
DR   ProteomicsDB; 54629; -.
DR   Pumba; P30049; -.
DR   TopDownProteomics; P30049; -.
DR   Antibodypedia; 1258; 348 antibodies from 29 providers.
DR   DNASU; 513; -.
DR   Ensembl; ENST00000215375.7; ENSP00000215375.1; ENSG00000099624.8.
DR   Ensembl; ENST00000395633.5; ENSP00000378995.1; ENSG00000099624.8.
DR   Ensembl; ENST00000591660.5; ENSP00000464863.1; ENSG00000099624.8.
DR   GeneID; 513; -.
DR   KEGG; hsa:513; -.
DR   MANE-Select; ENST00000215375.7; ENSP00000215375.1; NM_001687.5; NP_001678.1.
DR   UCSC; uc002lrn.4; human.
DR   AGR; HGNC:837; -.
DR   CTD; 513; -.
DR   DisGeNET; 513; -.
DR   GeneCards; ATP5F1D; -.
DR   HGNC; HGNC:837; ATP5F1D.
DR   HPA; ENSG00000099624; Tissue enhanced (skeletal).
DR   MalaCards; ATP5F1D; -.
DR   MIM; 603150; gene.
DR   MIM; 618120; phenotype.
DR   neXtProt; NX_P30049; -.
DR   OpenTargets; ENSG00000099624; -.
DR   Orphanet; 254913; Isolated ATP synthase deficiency.
DR   PharmGKB; PA25127; -.
DR   VEuPathDB; HostDB:ENSG00000099624; -.
DR   eggNOG; KOG1758; Eukaryota.
DR   GeneTree; ENSGT00390000017576; -.
DR   HOGENOM; CLU_084338_0_1_1; -.
DR   InParanoid; P30049; -.
DR   OMA; PHQTIYR; -.
DR   OrthoDB; 5394300at2759; -.
DR   PhylomeDB; P30049; -.
DR   TreeFam; TF313029; -.
DR   BioCyc; MetaCyc:HS01900-MONOMER; -.
DR   PathwayCommons; P30049; -.
DR   Reactome; R-HSA-163210; Formation of ATP by chemiosmotic coupling.
DR   Reactome; R-HSA-8949613; Cristae formation.
DR   SignaLink; P30049; -.
DR   SIGNOR; P30049; -.
DR   BioGRID-ORCS; 513; 662 hits in 1152 CRISPR screens.
DR   ChiTaRS; ATP5D; human.
DR   GeneWiki; ATP5D; -.
DR   GenomeRNAi; 513; -.
DR   Pharos; P30049; Tbio.
DR   PRO; PR:P30049; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; P30049; Protein.
DR   Bgee; ENSG00000099624; Expressed in apex of heart and 203 other cell types or tissues.
DR   ExpressionAtlas; P30049; baseline and differential.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR   GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IDA:UniProtKB.
DR   GO; GO:0000275; C:mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1); IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; NAS:UniProtKB.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0009060; P:aerobic respiration; IMP:UniProtKB.
DR   GO; GO:0033615; P:mitochondrial proton-transporting ATP synthase complex assembly; IMP:UniProtKB.
DR   GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
DR   GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IDA:UniProtKB.
DR   GO; GO:0046688; P:response to copper ion; NAS:UniProtKB.
DR   CDD; cd12152; F1-ATPase_delta; 1.
DR   Gene3D; 1.20.5.440; ATP synthase delta/epsilon subunit, C-terminal domain; 1.
DR   Gene3D; 2.60.15.10; F0F1 ATP synthase delta/epsilon subunit, N-terminal; 1.
DR   HAMAP; MF_00530; ATP_synth_epsil_bac; 1.
DR   InterPro; IPR036794; ATP_F1_dsu/esu_C_sf.
DR   InterPro; IPR001469; ATP_synth_F1_dsu/esu.
DR   InterPro; IPR020546; ATP_synth_F1_dsu/esu_N.
DR   InterPro; IPR048937; ATPD_C_metazoa.
DR   InterPro; IPR036771; ATPsynth_dsu/esu_N.
DR   NCBIfam; TIGR01216; ATP_synt_epsi; 1.
DR   PANTHER; PTHR13822; ATP SYNTHASE DELTA/EPSILON CHAIN; 1.
DR   PANTHER; PTHR13822:SF7; ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL; 1.
DR   Pfam; PF02823; ATP-synt_DE_N; 1.
DR   Pfam; PF21335; ATPD_C_metazoa; 1.
DR   SUPFAM; SSF46604; Epsilon subunit of F1F0-ATP synthase C-terminal domain; 1.
DR   SUPFAM; SSF51344; Epsilon subunit of F1F0-ATP synthase N-terminal domain; 1.
DR   SWISS-2DPAGE; P30049; -.
DR   UCD-2DPAGE; P30049; -.
DR   Genevisible; P30049; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; ATP synthesis; CF(1); Direct protein sequencing;
KW   Disease variant; Hydrogen ion transport; Ion transport; Membrane;
KW   Mitochondrion; Mitochondrion inner membrane; Primary mitochondrial disease;
KW   Reference proteome; Transit peptide; Transport.
FT   TRANSIT         1..22
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:1286669"
FT   CHAIN           23..168
FT                   /note="ATP synthase subunit delta, mitochondrial"
FT                   /id="PRO_0000002661"
FT   MOD_RES         136
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D3D9"
FT   MOD_RES         136
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D3D9"
FT   MOD_RES         165
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D3D9"
FT   MOD_RES         165
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D3D9"
FT   VARIANT         82
FT                   /note="P -> L (in MC5DN5; no effect on protein abundance;
FT                   decreased mitochondrial proton-transporting ATP synthase
FT                   complex assembly; decreased aerobic respiration in patient
FT                   cells homozygous for the mutation; partial loss of function
FT                   confirmed by complementation assays; dbSNP:rs867410737)"
FT                   /evidence="ECO:0000269|PubMed:29478781"
FT                   /id="VAR_081452"
FT   VARIANT         106
FT                   /note="V -> G (in MC5DN5; no effect on protein abundance;
FT                   decreased mitochondrial proton-transporting ATP synthase
FT                   complex assembly; decreased aerobic respiration in patient
FT                   cells homozygous for the mutation; partial loss of function
FT                   confirmed by complementation assays; dbSNP:rs1555745989)"
FT                   /evidence="ECO:0000269|PubMed:29478781"
FT                   /id="VAR_081453"
FT   STRAND          39..43
FT                   /evidence="ECO:0007829|PDB:8H9M"
FT   STRAND          47..49
FT                   /evidence="ECO:0007829|PDB:8H9V"
FT   STRAND          51..62
FT                   /evidence="ECO:0007829|PDB:8H9M"
FT   STRAND          65..69
FT                   /evidence="ECO:0007829|PDB:8H9M"
FT   STRAND          76..80
FT                   /evidence="ECO:0007829|PDB:8H9M"
FT   STRAND          82..89
FT                   /evidence="ECO:0007829|PDB:8H9M"
FT   STRAND          94..99
FT                   /evidence="ECO:0007829|PDB:8H9M"
FT   STRAND          101..106
FT                   /evidence="ECO:0007829|PDB:8H9M"
FT   STRAND          110..121
FT                   /evidence="ECO:0007829|PDB:8H9M"
FT   HELIX           122..124
FT                   /evidence="ECO:0007829|PDB:8H9M"
FT   HELIX           127..143
FT                   /evidence="ECO:0007829|PDB:8H9M"
FT   HELIX           147..167
FT                   /evidence="ECO:0007829|PDB:8H9M"
SQ   SEQUENCE   168 AA;  17490 MW;  B7F0D1D01ADFDFE7 CRC64;
     MLPAALLRRP GLGRLVRHAR AYAEAAAAPA AASGPNQMSF TFASPTQVFF NGANVRQVDV
     PTLTGAFGIL AAHVPTLQVL RPGLVVVHAE DGTTSKYFVS SGSIAVNADS SVQLLAEEAV
     TLDMLDLGAA KANLEKAQAE LVGTADEATR AEIQIRIEAN EALVKALE
//