HOGA1_HUMAN
ID HOGA1_HUMAN Reviewed; 327 AA.
AC Q86XE5; A8K075; Q5T680; Q5T684; Q711P0; Q8N9F2; Q96EV5;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=4-hydroxy-2-oxoglutarate aldolase, mitochondrial;
DE EC=4.1.3.16;
DE AltName: Full=Dihydrodipicolinate synthase-like;
DE Short=DHDPS-like protein;
DE AltName: Full=Probable 2-keto-4-hydroxyglutarate aldolase;
DE Short=Probable KHG-aldolase;
DE AltName: Full=Protein 569272;
DE Flags: Precursor;
GN Name=HOGA1; Synonyms=C10orf65, DHDPSL;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Urinary bladder;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Hippocampus, and Kidney;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-279 (ISOFORM 1).
RA Moschonas N.K.;
RT "Homo sapiens gene 569272.";
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, AND VARIANTS HP3 GLY-257; VAL-287 AND GLU-315 DEL.
RX PubMed=20797690; DOI=10.1016/j.ajhg.2010.07.023;
RA Belostotsky R., Seboun E., Idelson G.H., Milliner D.S., Becker-Cohen R.,
RA Rinat C., Monico C.G., Feinstein S., Ben-Shalom E., Magen D., Weissman I.,
RA Charon C., Frishberg Y.;
RT "Mutations in DHDPSL are responsible for primary hyperoxaluria type III.";
RL Am. J. Hum. Genet. 87:392-399(2010).
RN [7]
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 [8]
RP X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) OF 26-327 IN COMPLEX WITH PYRUVATE,
RP SUBUNIT, ACTIVE SITE, MUTAGENESIS OF SER-77; ASN-78; TYR-140; TYR-168;
RP LYS-196 AND SER-198, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=21998747; DOI=10.1371/journal.pone.0026021;
RA Riedel T.J., Johnson L.C., Knight J., Hantgan R.R., Holmes R.P.,
RA Lowther W.T.;
RT "Structural and biochemical studies of human 4-hydroxy-2-oxoglutarate
RT aldolase: implications for hydroxyproline metabolism in primary
RT hyperoxaluria.";
RL PLoS ONE 6:E26021-E26021(2011).
CC -!- FUNCTION: Catalyzes the final step in the metabolic pathway of
CC hydroxyproline. {ECO:0000269|PubMed:20797690,
CC ECO:0000269|PubMed:21998747}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4S)-4-hydroxy-2-oxoglutarate = glyoxylate + pyruvate;
CC Xref=Rhea:RHEA:35639, ChEBI:CHEBI:15361, ChEBI:CHEBI:36655,
CC ChEBI:CHEBI:71685; EC=4.1.3.16;
CC Evidence={ECO:0000269|PubMed:21998747};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4R)-4-hydroxy-2-oxoglutarate = glyoxylate + pyruvate;
CC Xref=Rhea:RHEA:30687, ChEBI:CHEBI:15361, ChEBI:CHEBI:36655,
CC ChEBI:CHEBI:62213; EC=4.1.3.16;
CC Evidence={ECO:0000269|PubMed:21998747};
CC -!- ACTIVITY REGULATION: Inhibited by divalent cations. {ECO:0000250}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- INTERACTION:
CC Q86XE5; Q96PU9: ODF3; NbExp=3; IntAct=EBI-9658477, EBI-12002088;
CC Q86XE5; Q9NQZ5: STARD7; NbExp=2; IntAct=EBI-9658477, EBI-4402938;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q0P5I5}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q86XE5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86XE5-3; Sequence=VSP_022515;
CC -!- DISEASE: Hyperoxaluria primary 3 (HP3) [MIM:613616]: A disorder
CC phenotypically similar to hyperoxaluria type 1 and type 2. It is
CC characterized by increase in urinary oxalate excretion and mild
CC glycolic aciduria. Clinical manifestations include calcium oxalate
CC urolithiasis, hematuria, pain, and/or urinary tract infection.
CC {ECO:0000269|PubMed:20797690}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the DapA family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC84901.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AK289440; BAF82129.1; -; mRNA.
DR EMBL; AL355315; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW49912.1; -; Genomic_DNA.
DR EMBL; BC011916; AAH11916.1; -; mRNA.
DR EMBL; BC045550; AAH45550.1; -; mRNA.
DR EMBL; BC057821; AAH57821.1; -; mRNA.
DR EMBL; AJ312051; CAC84901.1; ALT_SEQ; Genomic_DNA.
DR CCDS; CCDS44469.1; -. [Q86XE5-3]
DR CCDS; CCDS7467.1; -. [Q86XE5-1]
DR RefSeq; NP_001128142.1; NM_001134670.1. [Q86XE5-3]
DR RefSeq; NP_612422.2; NM_138413.3. [Q86XE5-1]
DR PDB; 3S5N; X-ray; 2.50 A; A=26-327.
DR PDB; 3S5O; X-ray; 1.97 A; A=26-327.
DR PDBsum; 3S5N; -.
DR PDBsum; 3S5O; -.
DR AlphaFoldDB; Q86XE5; -.
DR SMR; Q86XE5; -.
DR BioGRID; 125207; 31.
DR IntAct; Q86XE5; 16.
DR STRING; 9606.ENSP00000359680; -.
DR BindingDB; Q86XE5; -.
DR ChEMBL; CHEMBL5996; -.
DR PhosphoSitePlus; Q86XE5; -.
DR BioMuta; HOGA1; -.
DR DMDM; 74750531; -.
DR MassIVE; Q86XE5; -.
DR MaxQB; Q86XE5; -.
DR PaxDb; Q86XE5; -.
DR PeptideAtlas; Q86XE5; -.
DR PRIDE; Q86XE5; -.
DR ProteomicsDB; 70271; -. [Q86XE5-1]
DR ProteomicsDB; 70272; -. [Q86XE5-3]
DR Antibodypedia; 55095; 24 antibodies from 9 providers.
DR DNASU; 112817; -.
DR Ensembl; ENST00000370646.9; ENSP00000359680.4; ENSG00000241935.9. [Q86XE5-1]
DR Ensembl; ENST00000370647.8; ENSP00000359681.4; ENSG00000241935.9. [Q86XE5-3]
DR GeneID; 112817; -.
DR KEGG; hsa:112817; -.
DR MANE-Select; ENST00000370646.9; ENSP00000359680.4; NM_138413.4; NP_612422.2.
DR UCSC; uc001kny.4; human. [Q86XE5-1]
DR CTD; 112817; -.
DR DisGeNET; 112817; -.
DR GeneCards; HOGA1; -.
DR GeneReviews; HOGA1; -.
DR HGNC; HGNC:25155; HOGA1.
DR HPA; ENSG00000241935; Tissue enhanced (kidney, liver).
DR MalaCards; HOGA1; -.
DR MIM; 613597; gene.
DR MIM; 613616; phenotype.
DR neXtProt; NX_Q86XE5; -.
DR OpenTargets; ENSG00000241935; -.
DR Orphanet; 93600; Primary hyperoxaluria type 3.
DR PharmGKB; PA165548441; -.
DR VEuPathDB; HostDB:ENSG00000241935; -.
DR eggNOG; ENOG502QWNS; Eukaryota.
DR GeneTree; ENSGT00530000063604; -.
DR HOGENOM; CLU_1668837_0_0_1; -.
DR InParanoid; Q86XE5; -.
DR OMA; GMDACVP; -.
DR OrthoDB; 1238597at2759; -.
DR PhylomeDB; Q86XE5; -.
DR TreeFam; TF324600; -.
DR BioCyc; MetaCyc:G66-31234-MON; -.
DR BRENDA; 4.1.3.16; 2681.
DR PathwayCommons; Q86XE5; -.
DR Reactome; R-HSA-389661; Glyoxylate metabolism and glycine degradation.
DR SignaLink; Q86XE5; -.
DR BioGRID-ORCS; 112817; 6 hits in 1067 CRISPR screens.
DR ChiTaRS; HOGA1; human.
DR GenomeRNAi; 112817; -.
DR Pharos; Q86XE5; Tbio.
DR PRO; PR:Q86XE5; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q86XE5; protein.
DR Bgee; ENSG00000241935; Expressed in kidney epithelium and 104 other tissues.
DR ExpressionAtlas; Q86XE5; baseline and differential.
DR Genevisible; Q86XE5; HS.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; ISS:BHF-UCL.
DR GO; GO:0106009; F:(4S)-4-hydroxy-2-oxoglutarate aldolase activity; IEA:RHEA.
DR GO; GO:0008700; F:4-hydroxy-2-oxoglutarate aldolase activity; IDA:BHF-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL.
DR GO; GO:0019470; P:4-hydroxyproline catabolic process; IDA:BHF-UCL.
DR GO; GO:0009436; P:glyoxylate catabolic process; IMP:UniProtKB.
DR GO; GO:0046487; P:glyoxylate metabolic process; IDA:BHF-UCL.
DR GO; GO:0033609; P:oxalate metabolic process; IMP:BHF-UCL.
DR GO; GO:0042866; P:pyruvate biosynthetic process; IDA:BHF-UCL.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002220; DapA-like.
DR InterPro; IPR020625; Schiff_base-form_aldolases_AS.
DR PANTHER; PTHR12128; PTHR12128; 1.
DR Pfam; PF00701; DHDPS; 1.
DR PIRSF; PIRSF001365; DHDPS; 1.
DR PRINTS; PR00146; DHPICSNTHASE.
DR SMART; SM01130; DHDPS; 1.
DR PROSITE; PS00666; DHDPS_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Disease variant; Lyase; Mitochondrion;
KW Reference proteome; Schiff base; Transit peptide.
FT TRANSIT 1..25
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:Q0P5I5"
FT CHAIN 26..327
FT /note="4-hydroxy-2-oxoglutarate aldolase, mitochondrial"
FT /id="PRO_0000273346"
FT ACT_SITE 196
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000269|PubMed:21998747"
FT BINDING 77..78
FT /ligand="substrate"
FT BINDING 198
FT /ligand="substrate"
FT BINDING 222
FT /ligand="substrate"
FT SITE 168
FT /note="Involved in proton transfer during cleavage"
FT VAR_SEQ 71..233
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022515"
FT VARIANT 257
FT /note="C -> G (in HP3; dbSNP:rs267606764)"
FT /evidence="ECO:0000269|PubMed:20797690"
FT /id="VAR_064035"
FT VARIANT 287
FT /note="G -> V (in HP3; dbSNP:rs138207257)"
FT /evidence="ECO:0000269|PubMed:20797690"
FT /id="VAR_064036"
FT VARIANT 315
FT /note="Missing (in HP3)"
FT /evidence="ECO:0000269|PubMed:20797690"
FT /id="VAR_064037"
FT MUTAGEN 77
FT /note="S->A: 2-fold decrease in kcat and a nearly 8-fold
FT increase in KM."
FT /evidence="ECO:0000269|PubMed:21998747"
FT MUTAGEN 77
FT /note="S->T: Significant loss of activity."
FT /evidence="ECO:0000269|PubMed:21998747"
FT MUTAGEN 78
FT /note="N->A: 6-fold increase in KM."
FT /evidence="ECO:0000269|PubMed:21998747"
FT MUTAGEN 78
FT /note="N->Q: 25-fold increase in KM."
FT /evidence="ECO:0000269|PubMed:21998747"
FT MUTAGEN 140
FT /note="Y->F: No change in activity."
FT /evidence="ECO:0000269|PubMed:21998747"
FT MUTAGEN 168
FT /note="Y->F: No enzymatic activity."
FT /evidence="ECO:0000269|PubMed:21998747"
FT MUTAGEN 196
FT /note="K->A: No enzymatic activity."
FT /evidence="ECO:0000269|PubMed:21998747"
FT MUTAGEN 198
FT /note="S->A: 2.5-fold decrease in kcat and 4.2 fold
FT increase in KM."
FT /evidence="ECO:0000269|PubMed:21998747"
FT MUTAGEN 198
FT /note="S->T: 7-fold increase in KM."
FT /evidence="ECO:0000269|PubMed:21998747"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:3S5O"
FT HELIX 54..64
FT /evidence="ECO:0007829|PDB:3S5O"
FT STRAND 70..76
FT /evidence="ECO:0007829|PDB:3S5O"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:3S5O"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:3S5O"
FT HELIX 86..98
FT /evidence="ECO:0007829|PDB:3S5O"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:3S5O"
FT HELIX 115..127
FT /evidence="ECO:0007829|PDB:3S5O"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:3S5O"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:3S5O"
FT HELIX 147..160
FT /evidence="ECO:0007829|PDB:3S5O"
FT STRAND 165..169
FT /evidence="ECO:0007829|PDB:3S5O"
FT HELIX 171..174
FT /evidence="ECO:0007829|PDB:3S5O"
FT HELIX 180..187
FT /evidence="ECO:0007829|PDB:3S5O"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:3S5O"
FT HELIX 202..211
FT /evidence="ECO:0007829|PDB:3S5O"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:3S5O"
FT STRAND 218..223
FT /evidence="ECO:0007829|PDB:3S5O"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:3S5O"
FT HELIX 227..233
FT /evidence="ECO:0007829|PDB:3S5O"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:3S5O"
FT HELIX 241..244
FT /evidence="ECO:0007829|PDB:3S5O"
FT HELIX 247..258
FT /evidence="ECO:0007829|PDB:3S5O"
FT HELIX 262..278
FT /evidence="ECO:0007829|PDB:3S5O"
FT TURN 279..283
FT /evidence="ECO:0007829|PDB:3S5O"
FT HELIX 284..295
FT /evidence="ECO:0007829|PDB:3S5O"
FT HELIX 311..322
FT /evidence="ECO:0007829|PDB:3S5O"
FT TURN 323..325
FT /evidence="ECO:0007829|PDB:3S5O"
SQ SEQUENCE 327 AA; 35249 MW; 2DC011E4F9FD32C9 CRC64;
MLGPQVWSSV RQGLSRSLSR NVGVWASGEG KKVDIAGIYP PVTTPFTATA EVDYGKLEEN
LHKLGTFPFR GFVVQGSNGE FPFLTSSERL EVVSRVRQAM PKNRLLLAGS GCESTQATVE
MTVSMAQVGA DAAMVVTPCY YRGRMSSAAL IHHYTKVADL SPIPVVLYSV PANTGLDLPV
DAVVTLSQHP NIVGMKDSGG DVTRIGLIVH KTRKQDFQVL AGSAGFLMAS YALGAVGGVC
ALANVLGAQV CQLERLCCTG QWEDAQKLQH RLIEPNAAVT RRFGIPGLKK IMDWFGYYGG
PCRAPLQELS PAEEEALRMD FTSNGWL
