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 27-MAR-2024, entry version 171. 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, RC Pancreas, 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 GlyGen; Q8CHT0; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q8CHT0; -. DR PhosphoSitePlus; Q8CHT0; -. DR SwissPalm; Q8CHT0; -. DR EPD; Q8CHT0; -. DR jPOST; Q8CHT0; -. DR MaxQB; Q8CHT0; -. DR PaxDb; 10090-ENSMUSP00000043821; -. DR PeptideAtlas; Q8CHT0; -. DR ProteomicsDB; 281963; -. DR Pumba; Q8CHT0; -. DR Antibodypedia; 1590; 345 antibodies from 31 providers. DR DNASU; 212647; -. DR Ensembl; ENSMUST00000039818.10; ENSMUSP00000043821.10; ENSMUSG00000028737.16. DR GeneID; 212647; -. DR KEGG; mmu:212647; -. DR UCSC; uc012dnu.1; mouse. DR AGR; MGI:2443883; -. 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; 4536at2759; -. 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 77 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 174 other cell types or tissues. 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 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 NCBIfam; TIGR01236; D1pyr5carbox1; 1. DR PANTHER; PTHR14516; 1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE FAMILY MEMBER; 1. DR PANTHER; PTHR14516:SF3; DELTA-1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE, MITOCHONDRIAL; 1. DR Pfam; PF00171; Aldedh; 1. DR SUPFAM; SSF53720; ALDH-like; 1. DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1. DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1. DR Genevisible; Q8CHT0; MM. 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; FT AAH56226/AAH39281/AAH24133)" FT /evidence="ECO:0000305" FT CONFLICT 32 FT /note="T -> A (in Ref. 1; BAC32045 and 4; FT AAH56226/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; FT AAH56226/AAH39281/AAH24133)" FT /evidence="ECO:0000305" FT CONFLICT 467 FT /note="Q -> K (in Ref. 1; BAC32045 and 4; FT AAH56226/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 //