AL4A1_MOUSE
ID AL4A1_MOUSE Reviewed; 562 AA.
AC Q8CHT0; B1AXW8; Q7TND0; Q8BXM3; Q8R0N1; Q8R1S2;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial;
DE Short=P5C dehydrogenase;
DE EC=1.2.1.88;
DE AltName: Full=Aldehyde dehydrogenase family 4 member A1;
DE AltName: Full=L-glutamate gamma-semialdehyde dehydrogenase;
DE Flags: Precursor;
GN Name=Aldh4a1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Retina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney, and Liver;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-30; LYS-92; LYS-98; LYS-113;
RP LYS-129; LYS-174; LYS-346; LYS-357; LYS-394 AND LYS-508, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-51; LYS-92; LYS-98; LYS-113;
RP LYS-129; LYS-174; LYS-317; LYS-357; LYS-364; LYS-375; LYS-461; LYS-508;
RP LYS-530 AND LYS-551, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.24 ANGSTROMS) OF 21-562.
RX PubMed=22868767; DOI=10.1107/s0907444912019580;
RA Pemberton T.A., Still B.R., Christensen E.M., Singh H., Srivastava D.,
RA Tanner J.J.;
RT "Proline: Mother Nature's cryoprotectant applied to protein
RT crystallography.";
RL Acta Crystallogr. D 68:1010-1018(2012).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 21-562 IN COMPLEXES WITH
RP GLUTAMATE AND NAD, SUBUNIT, AND ACTIVE SITE.
RX PubMed=22516612; DOI=10.1016/j.jmb.2012.04.010;
RA Srivastava D., Singh R.K., Moxley M.A., Henzl M.T., Becker D.F.,
RA Tanner J.J.;
RT "The three-dimensional structural basis of type II hyperprolinemia.";
RL J. Mol. Biol. 420:176-189(2012).
CC -!- FUNCTION: Irreversible conversion of delta-1-pyrroline-5-carboxylate
CC (P5C), derived either from proline or ornithine, to glutamate. This is
CC a necessary step in the pathway interconnecting the urea and
CC tricarboxylic acid cycles. The preferred substrate is glutamic gamma-
CC semialdehyde, other substrates include succinic, glutaric and adipic
CC semialdehydes (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamate 5-semialdehyde + NAD(+) = 2 H(+) + L-
CC glutamate + NADH; Xref=Rhea:RHEA:30235, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:58066; EC=1.2.1.88;
CC -!- PATHWAY: Amino-acid degradation; L-proline degradation into L-
CC glutamate; L-glutamate from L-proline: step 2/2.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:22516612}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC -!- PTM: Acetylation of Lys-98, Lys-113 and Lys-401 is observed in liver
CC mitochondria from fasted mice but not from fed mice.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AK044712; BAC32045.1; -; mRNA.
DR EMBL; AL831790; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466615; EDL13315.1; -; Genomic_DNA.
DR EMBL; BC024133; AAH24133.1; -; mRNA.
DR EMBL; BC026589; AAH26589.1; -; mRNA.
DR EMBL; BC039281; AAH39281.2; -; mRNA.
DR EMBL; BC056226; AAH56226.1; -; mRNA.
DR CCDS; CCDS18848.1; -.
DR RefSeq; NP_780647.3; NM_175438.4.
DR PDB; 3V9J; X-ray; 1.30 A; A/B=21-562.
DR PDB; 3V9K; X-ray; 1.50 A; A/B=21-562.
DR PDB; 3V9L; X-ray; 1.50 A; A/B=21-562.
DR PDB; 4E3X; X-ray; 1.24 A; A/B=21-562.
DR PDB; 4LGZ; X-ray; 1.68 A; A/B=21-562.
DR PDB; 4LH0; X-ray; 1.67 A; A/B=21-562.
DR PDB; 4LH1; X-ray; 1.67 A; A/B=21-562.
DR PDB; 4LH2; X-ray; 1.67 A; A/B=21-562.
DR PDB; 4LH3; X-ray; 1.81 A; A/B=21-562.
DR PDB; 7MER; X-ray; 1.74 A; A/B=21-562.
DR PDB; 7MES; X-ray; 1.37 A; A/B=21-562.
DR PDBsum; 3V9J; -.
DR PDBsum; 3V9K; -.
DR PDBsum; 3V9L; -.
DR PDBsum; 4E3X; -.
DR PDBsum; 4LGZ; -.
DR PDBsum; 4LH0; -.
DR PDBsum; 4LH1; -.
DR PDBsum; 4LH2; -.
DR PDBsum; 4LH3; -.
DR PDBsum; 7MER; -.
DR PDBsum; 7MES; -.
DR AlphaFoldDB; Q8CHT0; -.
DR SMR; Q8CHT0; -.
DR BioGRID; 229346; 4.
DR IntAct; Q8CHT0; 3.
DR STRING; 10090.ENSMUSP00000043821; -.
DR iPTMnet; Q8CHT0; -.
DR PhosphoSitePlus; Q8CHT0; -.
DR SwissPalm; Q8CHT0; -.
DR EPD; Q8CHT0; -.
DR jPOST; Q8CHT0; -.
DR MaxQB; Q8CHT0; -.
DR PaxDb; Q8CHT0; -.
DR PeptideAtlas; Q8CHT0; -.
DR PRIDE; Q8CHT0; -.
DR ProteomicsDB; 281963; -.
DR Antibodypedia; 1590; 318 antibodies from 31 providers.
DR DNASU; 212647; -.
DR Ensembl; ENSMUST00000039818; ENSMUSP00000043821; ENSMUSG00000028737.
DR GeneID; 212647; -.
DR KEGG; mmu:212647; -.
DR UCSC; uc012dnu.1; mouse.
DR CTD; 8659; -.
DR MGI; MGI:2443883; Aldh4a1.
DR VEuPathDB; HostDB:ENSMUSG00000028737; -.
DR eggNOG; KOG2455; Eukaryota.
DR GeneTree; ENSGT00560000077335; -.
DR HOGENOM; CLU_005391_4_1_1; -.
DR InParanoid; Q8CHT0; -.
DR OMA; FAGIHFT; -.
DR OrthoDB; 454791at2759; -.
DR PhylomeDB; Q8CHT0; -.
DR TreeFam; TF300481; -.
DR BRENDA; 1.2.1.88; 3474.
DR Reactome; R-MMU-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-MMU-70688; Proline catabolism.
DR UniPathway; UPA00261; UER00374.
DR BioGRID-ORCS; 212647; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Aldh4a1; mouse.
DR PRO; PR:Q8CHT0; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8CHT0; protein.
DR Bgee; ENSMUSG00000028737; Expressed in right kidney and 171 other tissues.
DR Genevisible; Q8CHT0; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0003842; F:1-pyrroline-5-carboxylate dehydrogenase activity; IDA:MGI.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0010133; P:proline catabolic process to glutamate; IEA:UniProtKB-UniPathway.
DR CDD; cd07123; ALDH_F4-17_P5CDH; 1.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR005931; P5CDH/ALDH4A1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR TIGRFAMs; TIGR01236; D1pyr5carbox1; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Mitochondrion; NAD; Oxidoreductase;
KW Phosphoprotein; Proline metabolism; Reference proteome; Transit peptide.
FT TRANSIT 1..23
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 24..562
FT /note="Delta-1-pyrroline-5-carboxylate dehydrogenase,
FT mitochondrial"
FT /id="PRO_0000007174"
FT ACT_SITE 313
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008,
FT ECO:0000269|PubMed:22516612"
FT ACT_SITE 347
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008,
FT ECO:0000269|PubMed:22516612"
FT BINDING 207
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT BINDING 232
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT BINDING 285..289
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT BINDING 446
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT BINDING 512
FT /ligand="substrate"
FT SITE 210
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MOD_RES 30
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30038"
FT MOD_RES 51
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 92
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 92
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 98
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 98
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 113
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 113
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 129
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 129
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 174
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 174
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 317
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 346
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 357
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 357
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 364
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 375
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 394
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 461
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 508
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 508
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 530
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 551
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT CONFLICT 18
FT /note="G -> S (in Ref. 1; BAC32045 and 4; AAH56226/
FT AAH39281/AAH24133)"
FT /evidence="ECO:0000305"
FT CONFLICT 32
FT /note="T -> A (in Ref. 1; BAC32045 and 4; AAH56226/
FT AAH39281/AAH24133)"
FT /evidence="ECO:0000305"
FT CONFLICT 47
FT /note="D -> G (in Ref. 1; BAC32045)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="M -> T (in Ref. 1; BAC32045 and 4; AAH56226/
FT AAH39281/AAH24133)"
FT /evidence="ECO:0000305"
FT CONFLICT 467
FT /note="Q -> K (in Ref. 1; BAC32045 and 4; AAH56226/
FT AAH39281/AAH24133/AAH26589)"
FT /evidence="ECO:0000305"
FT HELIX 44..54
FT /evidence="ECO:0007829|PDB:4E3X"
FT TURN 55..58
FT /evidence="ECO:0007829|PDB:4E3X"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:4E3X"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:4E3X"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:4E3X"
FT STRAND 85..94
FT /evidence="ECO:0007829|PDB:4E3X"
FT HELIX 98..117
FT /evidence="ECO:0007829|PDB:4E3X"
FT HELIX 120..135
FT /evidence="ECO:0007829|PDB:4E3X"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:4E3X"
FT HELIX 139..150
FT /evidence="ECO:0007829|PDB:4E3X"
FT HELIX 154..160
FT /evidence="ECO:0007829|PDB:4E3X"
FT HELIX 163..179
FT /evidence="ECO:0007829|PDB:4E3X"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:4E3X"
FT STRAND 200..206
FT /evidence="ECO:0007829|PDB:4E3X"
FT HELIX 212..224
FT /evidence="ECO:0007829|PDB:4E3X"
FT STRAND 229..232
FT /evidence="ECO:0007829|PDB:4E3X"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:4E3X"
FT HELIX 238..250
FT /evidence="ECO:0007829|PDB:4E3X"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:4E3X"
FT HELIX 265..272
FT /evidence="ECO:0007829|PDB:4E3X"
FT STRAND 278..285
FT /evidence="ECO:0007829|PDB:4E3X"
FT HELIX 287..299
FT /evidence="ECO:0007829|PDB:4E3X"
FT TURN 300..303
FT /evidence="ECO:0007829|PDB:4E3X"
FT STRAND 309..313
FT /evidence="ECO:0007829|PDB:4E3X"
FT STRAND 318..322
FT /evidence="ECO:0007829|PDB:4E3X"
FT HELIX 328..340
FT /evidence="ECO:0007829|PDB:4E3X"
FT HELIX 341..344
FT /evidence="ECO:0007829|PDB:4E3X"
FT STRAND 350..356
FT /evidence="ECO:0007829|PDB:4E3X"
FT HELIX 357..359
FT /evidence="ECO:0007829|PDB:4E3X"
FT HELIX 360..372
FT /evidence="ECO:0007829|PDB:4E3X"
FT TURN 379..381
FT /evidence="ECO:0007829|PDB:4E3X"
FT HELIX 393..408
FT /evidence="ECO:0007829|PDB:4E3X"
FT STRAND 412..416
FT /evidence="ECO:0007829|PDB:4E3X"
FT STRAND 423..425
FT /evidence="ECO:0007829|PDB:4E3X"
FT STRAND 431..436
FT /evidence="ECO:0007829|PDB:4E3X"
FT HELIX 441..443
FT /evidence="ECO:0007829|PDB:4E3X"
FT STRAND 449..457
FT /evidence="ECO:0007829|PDB:4E3X"
FT HELIX 459..461
FT /evidence="ECO:0007829|PDB:4E3X"
FT HELIX 462..471
FT /evidence="ECO:0007829|PDB:4E3X"
FT STRAND 472..482
FT /evidence="ECO:0007829|PDB:4E3X"
FT HELIX 486..495
FT /evidence="ECO:0007829|PDB:4E3X"
FT TURN 496..499
FT /evidence="ECO:0007829|PDB:4E3X"
FT STRAND 501..507
FT /evidence="ECO:0007829|PDB:4E3X"
FT TURN 514..516
FT /evidence="ECO:0007829|PDB:4E3X"
FT HELIX 536..540
FT /evidence="ECO:0007829|PDB:4E3X"
FT STRAND 544..549
FT /evidence="ECO:0007829|PDB:4E3X"
FT HELIX 559..561
FT /evidence="ECO:0007829|PDB:3V9J"
SQ SEQUENCE 562 AA; 61841 MW; 4D8A0C9C68A99478 CRC64;
MLPLPSLRRS LLSHAWRGAG LRWKHTSSLK VTNEPILAFS QGSPERDALQ KALKDLKGQM
EAIPCVVGDE EVWTSDIQYQ LSPFNHAHKV AKFCYADKAL LNRAIDAALA ARKEWDLKPM
ADRAQVFLKA ADMLSGPRRA EVLAKTMVGQ GKTVIQAEID AAAELIDFFR FNAKFAVELE
GEQPISVPPS TNHTVYRGLE GFVAAISPFN FTAIGGNLAG APALMGNVVL WKPSDTAMLA
SYAVYRILRE AGLPPNIIQF VPADGPTFGD TVTSSEHLCG INFTGSVPTF KHLWRQVAQN
LDRFRTFPRL AGECGGKNFH FVHSSADVDS VVSGTLRSAF EYGGQKCSAC SRLYVPKSLW
PQIKGRLLEE HSRIKVGDPA EDFGTFFSAV IDAKAFARIK KWLEHARSSP SLSILAGGQC
NESVGYYVEP CIIESKDPQE PIMKEEIFGP VLTVYVYPDD KYRETLQLVD STTSYGLTGA
VFAQDKAIVQ EATRMLRNAA GNFYINDKST GSVVGQQPFG GARASGTNDK PGGPHYILRW
TSPQVIKETH KPLGDWRYSY MQ
