ALDOC_HUMAN
ID ALDOC_HUMAN Reviewed; 364 AA.
AC P09972; B2R5R3; Q3SYL3; Q6FH94; Q6P0L5;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 212.
DE RecName: Full=Fructose-bisphosphate aldolase C;
DE EC=4.1.2.13;
DE AltName: Full=Brain-type aldolase;
GN Name=ALDOC; Synonyms=ALDC;
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 [GENOMIC DNA].
RX PubMed=3105602; DOI=10.1016/0300-9084(87)90246-x;
RA Rottmann W.H., Deselms K.R., Niclas J., Camerato T., Holman P.S.,
RA Green C.J., Tolan D.R.;
RT "The complete amino acid sequence of the human aldolase C isozyme derived
RT from genomic clones.";
RL Biochimie 69:137-145(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3267224; DOI=10.1093/nar/16.10.4733;
RA Buono P., Paolella G., Mancini F.P., Izzo P., Salvatore F.;
RT "The complete nucleotide sequence of the gene coding for the human aldolase
RT C.";
RL Nucleic Acids Res. 16:4733-4733(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2209624; DOI=10.1111/j.1432-1033.1990.tb19294.x;
RA Buono P., Mancini F.P., Izzo P., Salvatore F.;
RT "Characterization of the transcription-initiation site and of the promoter
RT region within the 5' flanking region of the human aldolase C gene.";
RL Eur. J. Biochem. 192:805-811(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Yu W., Gibbs R.A.;
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
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 [8]
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon, Eye, and Uterus;
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 [10]
RP INTERACTION WITH ATP6V1E1.
RX PubMed=11399750; DOI=10.1074/jbc.m008768200;
RA Lu M., Holliday L.S., Zhang L., Dunn W.A. Jr., Gluck S.L.;
RT "Interaction between aldolase and vacuolar H+-ATPase: evidence for direct
RT coupling of glycolysis to the ATP-hydrolyzing proton pump.";
RL J. Biol. Chem. 276:30407-30413(2001).
RN [11]
RP INTERACTION WITH PLD2.
RX PubMed=11876650; DOI=10.1021/bi015700a;
RA Kim J.H., Lee S., Kim J.H., Lee T.G., Hirata M., Suh P.-G., Ryu S.H.;
RT "Phospholipase D2 directly interacts with aldolase via its PH domain.";
RL Biochemistry 41:3414-3421(2002).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-111, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND IDENTIFICATION BY
RP 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; SER-39 AND SER-45, AND
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 [16]
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 [17]
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 1-364, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15537755; DOI=10.1110/ps.04915904;
RA Arakaki T.L., Pezza J.A., Cronin M.A., Hopkins C.E., Zimmer D.B.,
RA Tolan D.R., Allen K.N.;
RT "Structure of human brain fructose 1,6-(bis)phosphate aldolase: linking
RT isozyme structure with function.";
RL Protein Sci. 13:3077-3084(2004).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-
CC phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729,
CC ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13;
CC Evidence={ECO:0000269|PubMed:15537755};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10.7 uM for fructose 1,6-bisphosphate
CC {ECO:0000269|PubMed:15537755};
CC KM=16 mM for fructose 1-phosphate {ECO:0000269|PubMed:15537755};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 4/4.
CC -!- SUBUNIT: Homotetramer. Interacts with ATP6V1E1. May interact with PLD2.
CC {ECO:0000269|PubMed:11399750, ECO:0000269|PubMed:11876650}.
CC -!- INTERACTION:
CC P09972; P04075: ALDOA; NbExp=3; IntAct=EBI-2952751, EBI-709613;
CC P09972; P04075-2: ALDOA; NbExp=6; IntAct=EBI-2952751, EBI-10194102;
CC P09972; Q49AR9: ANKS1A; NbExp=3; IntAct=EBI-2952751, EBI-11954519;
CC P09972; Q8TBB1: LNX1; NbExp=6; IntAct=EBI-2952751, EBI-739832;
CC -!- MISCELLANEOUS: In vertebrates, three forms of this ubiquitous
CC glycolytic enzyme are found, aldolase A in muscle, aldolase B in liver
CC and aldolase C in brain.
CC -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI03761.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X05196; CAA28825.1; -; Genomic_DNA.
DR EMBL; X07292; CAA30270.1; -; Genomic_DNA.
DR EMBL; AF054987; AAC09348.1; -; mRNA.
DR EMBL; BT007006; AAP35652.1; -; mRNA.
DR EMBL; CR541862; CAG46660.1; -; mRNA.
DR EMBL; CR541881; CAG46679.1; -; mRNA.
DR EMBL; AK312281; BAG35210.1; -; mRNA.
DR EMBL; CH471159; EAW51104.1; -; Genomic_DNA.
DR EMBL; BC003613; AAH03613.3; -; mRNA.
DR EMBL; BC103760; AAI03761.1; ALT_INIT; mRNA.
DR EMBL; BC065565; AAH65565.2; -; mRNA.
DR EMBL; BC106925; AAI06926.1; -; mRNA.
DR EMBL; BC106926; AAI06927.1; -; mRNA.
DR CCDS; CCDS11236.1; -.
DR PIR; A25861; ADHUC.
DR RefSeq; NP_005156.1; NM_005165.2.
DR RefSeq; XP_005258006.1; XM_005257949.2.
DR RefSeq; XP_011522858.1; XM_011524556.1.
DR PDB; 1XFB; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J/K/L=1-364.
DR PDBsum; 1XFB; -.
DR AlphaFoldDB; P09972; -.
DR SMR; P09972; -.
DR BioGRID; 106731; 92.
DR IntAct; P09972; 18.
DR MINT; P09972; -.
DR STRING; 9606.ENSP00000226253; -.
DR ChEMBL; CHEMBL4295709; -.
DR GlyGen; P09972; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P09972; -.
DR PhosphoSitePlus; P09972; -.
DR SwissPalm; P09972; -.
DR BioMuta; ALDOC; -.
DR DMDM; 113613; -.
DR UCD-2DPAGE; P09972; -.
DR CPTAC; CPTAC-1372; -.
DR CPTAC; CPTAC-1373; -.
DR CPTAC; CPTAC-1374; -.
DR CPTAC; CPTAC-1375; -.
DR CPTAC; CPTAC-1376; -.
DR EPD; P09972; -.
DR jPOST; P09972; -.
DR MassIVE; P09972; -.
DR MaxQB; P09972; -.
DR PaxDb; P09972; -.
DR PeptideAtlas; P09972; -.
DR PRIDE; P09972; -.
DR ProteomicsDB; 52287; -.
DR Antibodypedia; 1111; 463 antibodies from 34 providers.
DR DNASU; 230; -.
DR Ensembl; ENST00000226253.9; ENSP00000226253.4; ENSG00000109107.14.
DR Ensembl; ENST00000395321.6; ENSP00000378731.2; ENSG00000109107.14.
DR GeneID; 230; -.
DR KEGG; hsa:230; -.
DR MANE-Select; ENST00000226253.9; ENSP00000226253.4; NM_005165.3; NP_005156.1.
DR UCSC; uc002hbp.4; human.
DR CTD; 230; -.
DR DisGeNET; 230; -.
DR GeneCards; ALDOC; -.
DR HGNC; HGNC:418; ALDOC.
DR HPA; ENSG00000109107; Group enriched (brain, choroid plexus, retina).
DR MIM; 103870; gene.
DR neXtProt; NX_P09972; -.
DR OpenTargets; ENSG00000109107; -.
DR PharmGKB; PA24711; -.
DR VEuPathDB; HostDB:ENSG00000109107; -.
DR eggNOG; KOG1557; Eukaryota.
DR GeneTree; ENSGT00950000182987; -.
DR HOGENOM; CLU_031243_0_0_1; -.
DR InParanoid; P09972; -.
DR OMA; WRELLYS; -.
DR OrthoDB; 799973at2759; -.
DR PhylomeDB; P09972; -.
DR TreeFam; TF314203; -.
DR BioCyc; MetaCyc:HS03200-MON; -.
DR PathwayCommons; P09972; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-70171; Glycolysis.
DR Reactome; R-HSA-70263; Gluconeogenesis.
DR SABIO-RK; P09972; -.
DR SignaLink; P09972; -.
DR SIGNOR; P09972; -.
DR UniPathway; UPA00109; UER00183.
DR BioGRID-ORCS; 230; 34 hits in 1078 CRISPR screens.
DR ChiTaRS; ALDOC; human.
DR EvolutionaryTrace; P09972; -.
DR GeneWiki; Aldolase_C; -.
DR GenomeRNAi; 230; -.
DR Pharos; P09972; Tbio.
DR PRO; PR:P09972; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P09972; protein.
DR Bgee; ENSG00000109107; Expressed in right hemisphere of cerebellum and 187 other tissues.
DR ExpressionAtlas; P09972; baseline and differential.
DR Genevisible; P09972; HS.
DR GO; GO:0005856; C:cytoskeleton; IC:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR GO; GO:1904724; C:tertiary granule lumen; TAS:Reactome.
DR GO; GO:0008092; F:cytoskeletal protein binding; IDA:BHF-UCL.
DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IDA:UniProtKB.
DR GO; GO:0030855; P:epithelial cell differentiation; IEP:UniProtKB.
DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IDA:UniProtKB.
DR GO; GO:0006000; P:fructose metabolic process; TAS:ProtInc.
DR GO; GO:0006094; P:gluconeogenesis; IEA:Ensembl.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR029768; Aldolase_I_AS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000741; FBA_I.
DR PANTHER; PTHR11627; PTHR11627; 1.
DR Pfam; PF00274; Glycolytic; 1.
DR PROSITE; PS00158; ALDOLASE_CLASS_I; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Glycolysis; Lyase; Phosphoprotein;
KW Reference proteome; Schiff base.
FT CHAIN 1..364
FT /note="Fructose-bisphosphate aldolase C"
FT /id="PRO_0000216947"
FT ACT_SITE 188
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 230
FT /note="Schiff-base intermediate with dihydroxyacetone-P"
FT BINDING 56
FT /ligand="substrate"
FT BINDING 147
FT /ligand="substrate"
FT SITE 364
FT /note="Necessary for preference for fructose 1,6-
FT bisphosphate over fructose 1-phosphate"
FT MOD_RES 5
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P05065"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 111
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05065"
FT CONFLICT 311
FT /note="L -> V (in Ref. 2; CAA30270)"
FT /evidence="ECO:0000305"
FT HELIX 10..23
FT /evidence="ECO:0007829|PDB:1XFB"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:1XFB"
FT HELIX 37..45
FT /evidence="ECO:0007829|PDB:1XFB"
FT HELIX 53..64
FT /evidence="ECO:0007829|PDB:1XFB"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:1XFB"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:1XFB"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:1XFB"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:1XFB"
FT HELIX 94..100
FT /evidence="ECO:0007829|PDB:1XFB"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:1XFB"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:1XFB"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:1XFB"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:1XFB"
FT HELIX 131..140
FT /evidence="ECO:0007829|PDB:1XFB"
FT STRAND 145..152
FT /evidence="ECO:0007829|PDB:1XFB"
FT HELIX 161..179
FT /evidence="ECO:0007829|PDB:1XFB"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:1XFB"
FT STRAND 184..191
FT /evidence="ECO:0007829|PDB:1XFB"
FT HELIX 199..219
FT /evidence="ECO:0007829|PDB:1XFB"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:1XFB"
FT HELIX 246..257
FT /evidence="ECO:0007829|PDB:1XFB"
FT TURN 258..260
FT /evidence="ECO:0007829|PDB:1XFB"
FT STRAND 267..271
FT /evidence="ECO:0007829|PDB:1XFB"
FT HELIX 277..288
FT /evidence="ECO:0007829|PDB:1XFB"
FT STRAND 295..303
FT /evidence="ECO:0007829|PDB:1XFB"
FT HELIX 304..314
FT /evidence="ECO:0007829|PDB:1XFB"
FT HELIX 321..338
FT /evidence="ECO:0007829|PDB:1XFB"
FT TURN 339..341
FT /evidence="ECO:0007829|PDB:1XFB"
SQ SEQUENCE 364 AA; 39456 MW; 506A570B3E507971 CRC64;
MPHSYPALSA EQKKELSDIA LRIVAPGKGI LAADESVGSM AKRLSQIGVE NTEENRRLYR
QVLFSADDRV KKCIGGVIFF HETLYQKDDN GVPFVRTIQD KGIVVGIKVD KGVVPLAGTD
GETTTQGLDG LSERCAQYKK DGADFAKWRC VLKISERTPS ALAILENANV LARYASICQQ
NGIVPIVEPE ILPDGDHDLK RCQYVTEKVL AAVYKALSDH HVYLEGTLLK PNMVTPGHAC
PIKYTPEEIA MATVTALRRT VPPAVPGVTF LSGGQSEEEA SFNLNAINRC PLPRPWALTF
SYGRALQASA LNAWRGQRDN AGAATEEFIK RAEVNGLAAQ GKYEGSGEDG GAAAQSLYIA
NHAY
