AL7A1_HUMAN
ID AL7A1_HUMAN Reviewed; 539 AA.
AC P49419; B2R669; B4DIC7; B4DMA0; E7EPT3; O14619; Q6IPU8; Q9BUL4;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 5.
DT 03-AUG-2022, entry version 212.
DE RecName: Full=Alpha-aminoadipic semialdehyde dehydrogenase {ECO:0000305|PubMed:20207735};
DE Short=Alpha-AASA dehydrogenase {ECO:0000305|PubMed:16491085};
DE EC=1.2.1.31 {ECO:0000269|PubMed:16491085, ECO:0000269|PubMed:20207735};
DE AltName: Full=Aldehyde dehydrogenase family 7 member A1;
DE EC=1.2.1.3 {ECO:0000269|PubMed:20207735, ECO:0000269|PubMed:21338592};
DE AltName: Full=Antiquitin-1;
DE AltName: Full=Betaine aldehyde dehydrogenase;
DE EC=1.2.1.8 {ECO:0000269|PubMed:20207735};
DE AltName: Full=Delta1-piperideine-6-carboxylate dehydrogenase;
DE Short=P6c dehydrogenase;
DE Flags: Precursor;
GN Name=ALDH7A1 {ECO:0000312|HGNC:HGNC:877}; Synonyms=ATQ1;
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] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC TISSUE=Kidney, Liver, and Placenta;
RX PubMed=8088832; DOI=10.1006/geno.1994.1279;
RA Lee P., Kuhl W., Gelbart T., Kamimura T., West C., Beutler E.;
RT "Homology between a human protein and a protein of the green garden pea.";
RL Genomics 21:371-378(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Brain, Caudate nucleus, and Hippocampus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLN-439.
RC TISSUE=Placenta, 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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 233-268, AND TISSUE SPECIFICITY.
RX PubMed=9417906; DOI=10.1006/geno.1997.5026;
RA Skvorak A.B., Robertson N.G., Yin Y., Weremowicz S., Her H., Bieber F.R.,
RA Beisel K.W., Lynch E.D., Beier D.R., Morton C.C.;
RT "An ancient conserved gene expressed in the human inner ear:
RT identification, expression analysis, and chromosomal mapping of human and
RT mouse antiquitin (ATQ1).";
RL Genomics 46:191-199(1997).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 (ISOFORM 2), CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 2), AND IDENTIFICATION
RP BY MASS 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 [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 FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=21338592; DOI=10.1016/j.cbi.2011.02.016;
RA Brocker C., Cantore M., Failli P., Vasiliou V.;
RT "Aldehyde dehydrogenase 7A1 (ALDH7A1) attenuates reactive aldehyde and
RT oxidative stress induced cytotoxicity.";
RL Chem. Biol. Interact. 191:269-277(2011).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 (ISOFORM 2), CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 2), AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [10]
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 [11]
RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 30-526, FUNCTION,
RP BIOPHYSICOCHEMICAL PROPERTIES, ALTERNATIVE SPLICING, SUBCELLULAR LOCATION,
RP CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=20207735; DOI=10.1074/jbc.m109.077925;
RA Brocker C., Lassen N., Estey T., Pappa A., Cantore M., Orlova V.V.,
RA Chavakis T., Kavanagh K.L., Oppermann U., Vasiliou V.;
RT "Aldehyde dehydrogenase 7A1 (ALDH7A1) is a novel enzyme involved in
RT cellular defense against hyperosmotic stress.";
RL J. Biol. Chem. 285:18452-18463(2010).
RN [12] {ECO:0007744|PDB:4ZUK, ECO:0007744|PDB:4ZUL, ECO:0007744|PDB:4ZVW, ECO:0007744|PDB:4ZVX, ECO:0007744|PDB:4ZVY}
RP X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) OF 29-539 IN COMPLEX WITH NAD AND
RP (S)-2-AMINO-6-OXOHEXANOATE, SUBUNIT, AND ACTIVE SITE.
RX PubMed=26260980; DOI=10.1021/acs.biochem.5b00754;
RA Luo M., Tanner J.J.;
RT "Structural Basis of Substrate Recognition by Aldehyde Dehydrogenase 7A1.";
RL Biochemistry 54:5513-5522(2015).
RN [13]
RP VARIANTS PDE 110-ARG--GLN-539 DEL; VAL-199 AND GLN-427, FUNCTION, CATALYTIC
RP ACTIVITY, AND CHARACTERIZATION OF VARIANTS PDE 110-ARG--GLN-539 DEL;
RP VAL-199 AND GLN-427.
RX PubMed=16491085; DOI=10.1038/nm1366;
RA Mills P.B., Struys E., Jakobs C., Plecko B., Baxter P., Baumgartner M.,
RA Willemsen M.A.A.P., Omran H., Tacke U., Uhlenberg B., Weschke B.,
RA Clayton P.T.;
RT "Mutations in antiquitin in individuals with pyridoxine-dependent
RT seizures.";
RL Nat. Med. 12:307-309(2006).
RN [14]
RP VARIANTS PDE VAL-202; GLU-291; ILE-301; GLN-335; GLY-395; GLN-427 AND
RP ASN-458.
RX PubMed=17068770; DOI=10.1002/humu.20433;
RA Plecko B., Paul K., Paschke E., Stoeckler-Ipsiroglu S., Struys E.,
RA Jakobs C., Hartmann H., Luecke T., di Capua M., Korenke C., Hikel C.,
RA Reutershahn E., Freilinger M., Baumeister F., Bosch F., Erwa W.;
RT "Biochemical and molecular characterization of 18 patients with pyridoxine-
RT dependent epilepsy and mutations of the antiquitin (ALDH7A1) gene.";
RL Hum. Mutat. 28:19-26(2007).
CC -!- FUNCTION: Multifunctional enzyme mediating important protective
CC effects. Metabolizes betaine aldehyde to betaine, an important cellular
CC osmolyte and methyl donor. Protects cells from oxidative stress by
CC metabolizing a number of lipid peroxidation-derived aldehydes. Involved
CC in lysine catabolism. {ECO:0000269|PubMed:16491085,
CC ECO:0000269|PubMed:20207735, ECO:0000269|PubMed:21338592}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) + nonanal = 2 H(+) + NADH + nonanoate;
CC Xref=Rhea:RHEA:69759, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32361, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:84268; Evidence={ECO:0000269|PubMed:20207735};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69760;
CC Evidence={ECO:0000305|PubMed:20207735};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-2-amino-6-oxohexanoate + H2O + NAD(+) = 2 H(+) + L-2-
CC aminoadipate + NADH; Xref=Rhea:RHEA:12308, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:58321, ChEBI:CHEBI:58672; EC=1.2.1.31;
CC Evidence={ECO:0000269|PubMed:16491085, ECO:0000269|PubMed:20207735};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12309;
CC Evidence={ECO:0000305|PubMed:16491085, ECO:0000305|PubMed:20207735};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:15305, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15710, ChEBI:CHEBI:17750, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.8;
CC Evidence={ECO:0000269|PubMed:20207735};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15306;
CC Evidence={ECO:0000305|PubMed:20207735};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.3;
CC Evidence={ECO:0000305|PubMed:20207735};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16186;
CC Evidence={ECO:0000305|PubMed:20207735};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexanal + NAD(+) = 2 H(+) + hexanoate + NADH;
CC Xref=Rhea:RHEA:67276, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17120, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:88528; Evidence={ECO:0000269|PubMed:20207735,
CC ECO:0000269|PubMed:21338592};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67277;
CC Evidence={ECO:0000305|PubMed:20207735, ECO:0000305|PubMed:21338592};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) + octanal = 2 H(+) + NADH + octanoate;
CC Xref=Rhea:RHEA:44100, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17935, ChEBI:CHEBI:25646, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; Evidence={ECO:0000269|PubMed:20207735,
CC ECO:0000269|PubMed:21338592};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44101;
CC Evidence={ECO:0000305|PubMed:20207735, ECO:0000305|PubMed:21338592};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-non-2-enal + H2O + NAD(+) = (E)-non-2-enoate + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:69767, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:142592,
CC ChEBI:CHEBI:143908; Evidence={ECO:0000269|PubMed:20207735};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69768;
CC Evidence={ECO:0000305|PubMed:20207735};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-4-hydroxynon-2-enal + H2O + NAD(+) = (E)-4-hydroxynon-2-
CC enoate + 2 H(+) + NADH; Xref=Rhea:RHEA:67248, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:58968, ChEBI:CHEBI:142920;
CC Evidence={ECO:0000269|PubMed:21338592};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67249;
CC Evidence={ECO:0000305|PubMed:21338592};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=28.5 uM for nonanal {ECO:0000269|PubMed:20207735};
CC KM=5.3 uM for trans-2-nonenal {ECO:0000269|PubMed:20207735};
CC KM=39.1 uM for hexanal {ECO:0000269|PubMed:20207735};
CC KM=17.5 uM for octanal {ECO:0000269|PubMed:20207735};
CC KM=41.1 uM for betaine aldehyde {ECO:0000269|PubMed:20207735};
CC KM=169 uM for L-2-aminoadipate 6-semialdehyde
CC {ECO:0000269|PubMed:20207735};
CC KM=530.2 uM for benzaldehyde {ECO:0000269|PubMed:20207735};
CC KM=647.4 uM for propanal {ECO:0000269|PubMed:20207735};
CC KM=7374.3 uM for glyceraldehyde {ECO:0000269|PubMed:20207735};
CC KM=119.5 uM for (E)-4-hydroxynon-2-enal
CC {ECO:0000269|PubMed:21338592};
CC Vmax=364.9 nmol/min/mg enzyme toward nonanal
CC {ECO:0000269|PubMed:20207735};
CC Vmax=323.5 nM/min/mg enzyme toward (E)-4-hydroxynon-2-enal
CC {ECO:0000269|PubMed:21338592};
CC Vmax=34.9 nmol/min/mg enzyme toward trans-2-nonenal
CC {ECO:0000269|PubMed:20207735};
CC Vmax=243.3 nmol/min/mg enzyme toward hexanal
CC {ECO:0000269|PubMed:20207735};
CC Vmax=72.3 nmol/min/mg enzyme toward octanal
CC {ECO:0000269|PubMed:20207735};
CC Vmax=101.4 nmol/min/mg enzyme toward betaine aldehyde
CC {ECO:0000269|PubMed:20207735};
CC Vmax=276.2 nmol/min/mg enzyme toward L-2-aminoadipate 6-semialdehyde
CC {ECO:0000269|PubMed:20207735};
CC Vmax=125.2 nmol/min/mg enzyme toward benzaldehyde
CC {ECO:0000269|PubMed:20207735};
CC Vmax=69.9 nmol/min/mg enzyme toward propanal
CC {ECO:0000269|PubMed:20207735};
CC Vmax=174 nmol/min/mg enzyme toward glyceraldehyde
CC {ECO:0000269|PubMed:20207735};
CC -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via
CC choline pathway; betaine from betaine aldehyde: step 1/1.
CC {ECO:0000305|PubMed:20207735}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:20207735,
CC ECO:0000269|PubMed:26260980}.
CC -!- INTERACTION:
CC P49419; Q12929: EPS8; NbExp=2; IntAct=EBI-726842, EBI-375576;
CC P49419-2; P49419-2: ALDH7A1; NbExp=3; IntAct=EBI-11107920, EBI-11107920;
CC P49419-2; P80188: LCN2; NbExp=3; IntAct=EBI-11107920, EBI-11911016;
CC P49419-2; Q9HB07: MYG1; NbExp=3; IntAct=EBI-11107920, EBI-709754;
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytosol
CC {ECO:0000269|PubMed:20207735}. Nucleus {ECO:0000269|PubMed:20207735}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion
CC {ECO:0000269|PubMed:20207735}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=hALDH7A1_v1 {ECO:0000303|PubMed:20207735,
CC ECO:0000303|PubMed:21338592};
CC IsoId=P49419-1; Sequence=Displayed;
CC Name=2; Synonyms=hALDH7A1_v2 {ECO:0000303|PubMed:20207735,
CC ECO:0000303|PubMed:21338592};
CC IsoId=P49419-2; Sequence=VSP_038987;
CC Name=4;
CC IsoId=P49419-4; Sequence=VSP_045905;
CC -!- TISSUE SPECIFICITY: Abundant in hepatoma cells and fetal cochlea,
CC ovary, eye, heart, adrenal gland, liver and kidney. Low levels present
CC in adult peripheral blood leukocytes and fetal brain, thymus, spleen,
CC skeletal muscle, lung and tongue. {ECO:0000269|PubMed:8088832,
CC ECO:0000269|PubMed:9417906}.
CC -!- DISEASE: Pyridoxine-dependent epilepsy (PDE) [MIM:266100]:
CC Characterized by a combination of various seizure types. It usually
CC occurs in the first hours of life and is unresponsive to standard
CC anticonvulsants, responding only to immediate administration of
CC pyridoxine hydrochloride. {ECO:0000269|PubMed:16491085,
CC ECO:0000269|PubMed:17068770}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC51935.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH02515.3; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH71712.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH73174.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG35366.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG58439.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
CC Sequence=BAG59812.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; S74728; AAB31966.1; -; mRNA.
DR EMBL; AK312459; BAG35366.1; ALT_INIT; mRNA.
DR EMBL; AK295526; BAG58439.1; ALT_SEQ; mRNA.
DR EMBL; AK297365; BAG59812.1; ALT_INIT; mRNA.
DR EMBL; AC093535; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC099513; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002515; AAH02515.3; ALT_INIT; mRNA.
DR EMBL; BC071712; AAH71712.1; ALT_INIT; mRNA.
DR EMBL; BC073174; AAH73174.1; ALT_INIT; mRNA.
DR EMBL; AF002696; AAC51935.1; ALT_SEQ; Genomic_DNA.
DR CCDS; CCDS4137.2; -. [P49419-1]
DR CCDS; CCDS56380.2; -. [P49419-4]
DR PIR; A54676; A54676.
DR RefSeq; NP_001173.2; NM_001182.4. [P49419-1]
DR RefSeq; NP_001188306.1; NM_001201377.1. [P49419-2]
DR RefSeq; NP_001189333.2; NM_001202404.1. [P49419-4]
DR PDB; 2J6L; X-ray; 1.30 A; A/B/C/D/E/F/G/H=30-527.
DR PDB; 4X0T; X-ray; 2.40 A; A/B/C/D=29-539.
DR PDB; 4X0U; X-ray; 1.95 A; A/B/C/D=29-539.
DR PDB; 4ZUK; X-ray; 2.00 A; A/B/C/D/E/F/G/H=29-539.
DR PDB; 4ZUL; X-ray; 1.76 A; A/B/C/D/E/F/G/H=29-539.
DR PDB; 4ZVW; X-ray; 2.40 A; A/B/C/D/E/F/G/H=29-539.
DR PDB; 4ZVX; X-ray; 1.90 A; A/B=29-539.
DR PDB; 4ZVY; X-ray; 1.90 A; A/B=29-539.
DR PDB; 6O4B; X-ray; 1.85 A; A/B/C/D/E/F/G/H=29-539.
DR PDB; 6O4C; X-ray; 1.70 A; A/B/C/D/E/F/G/H=29-539.
DR PDB; 6O4D; X-ray; 1.88 A; A/B/C/D/E/F/G/H=29-539.
DR PDB; 6O4E; X-ray; 1.75 A; A/B/C/D/E/F/G/H=29-539.
DR PDB; 6O4F; X-ray; 1.90 A; A/B/C/D/E/F/G/H=29-539.
DR PDB; 6O4G; X-ray; 2.05 A; A/B/C/D/E/F/G/H=29-539.
DR PDB; 6O4H; X-ray; 2.05 A; A/B/C/D/E/F/G/H=29-539.
DR PDB; 6O4I; X-ray; 1.75 A; A/B/C/D/E/F/G/H=29-539.
DR PDB; 6O4K; X-ray; 2.06 A; A/B/C/D/E/F/G/H=29-539.
DR PDB; 6O4L; X-ray; 1.85 A; A/B/C/D=29-539.
DR PDB; 6U2X; X-ray; 2.15 A; A/B/C/D/E/F/G/H=29-539.
DR PDB; 6V0Z; X-ray; 2.02 A; A/B/C/D/E/F/G/H=29-539.
DR PDBsum; 2J6L; -.
DR PDBsum; 4X0T; -.
DR PDBsum; 4X0U; -.
DR PDBsum; 4ZUK; -.
DR PDBsum; 4ZUL; -.
DR PDBsum; 4ZVW; -.
DR PDBsum; 4ZVX; -.
DR PDBsum; 4ZVY; -.
DR PDBsum; 6O4B; -.
DR PDBsum; 6O4C; -.
DR PDBsum; 6O4D; -.
DR PDBsum; 6O4E; -.
DR PDBsum; 6O4F; -.
DR PDBsum; 6O4G; -.
DR PDBsum; 6O4H; -.
DR PDBsum; 6O4I; -.
DR PDBsum; 6O4K; -.
DR PDBsum; 6O4L; -.
DR PDBsum; 6U2X; -.
DR PDBsum; 6V0Z; -.
DR AlphaFoldDB; P49419; -.
DR SASBDB; P49419; -.
DR SMR; P49419; -.
DR BioGRID; 106990; 87.
DR IntAct; P49419; 24.
DR MINT; P49419; -.
DR STRING; 9606.ENSP00000387123; -.
DR DrugBank; DB11638; Artenimol.
DR DrugBank; DB00157; NADH.
DR iPTMnet; P49419; -.
DR MetOSite; P49419; -.
DR PhosphoSitePlus; P49419; -.
DR SwissPalm; P49419; -.
DR BioMuta; ALDH7A1; -.
DR DMDM; 294862544; -.
DR UCD-2DPAGE; P49419; -.
DR CPTAC; CPTAC-15; -.
DR CPTAC; CPTAC-16; -.
DR EPD; P49419; -.
DR jPOST; P49419; -.
DR MassIVE; P49419; -.
DR MaxQB; P49419; -.
DR PaxDb; P49419; -.
DR PeptideAtlas; P49419; -.
DR PRIDE; P49419; -.
DR ProteomicsDB; 17435; -.
DR ProteomicsDB; 56006; -. [P49419-1]
DR ProteomicsDB; 56007; -. [P49419-2]
DR Antibodypedia; 13922; 272 antibodies from 28 providers.
DR DNASU; 501; -.
DR Ensembl; ENST00000409134.8; ENSP00000387123.3; ENSG00000164904.18. [P49419-1]
DR Ensembl; ENST00000553117.5; ENSP00000448593.1; ENSG00000164904.18. [P49419-4]
DR GeneID; 501; -.
DR KEGG; hsa:501; -.
DR MANE-Select; ENST00000409134.8; ENSP00000387123.3; NM_001182.5; NP_001173.2.
DR UCSC; uc003ktx.5; human. [P49419-1]
DR CTD; 501; -.
DR DisGeNET; 501; -.
DR GeneCards; ALDH7A1; -.
DR GeneReviews; ALDH7A1; -.
DR HGNC; HGNC:877; ALDH7A1.
DR HPA; ENSG00000164904; Tissue enhanced (liver).
DR MalaCards; ALDH7A1; -.
DR MIM; 107323; gene.
DR MIM; 266100; phenotype.
DR neXtProt; NX_P49419; -.
DR OpenTargets; ENSG00000164904; -.
DR Orphanet; 3006; Pyridoxine-dependent epilepsy.
DR PharmGKB; PA24704; -.
DR VEuPathDB; HostDB:ENSG00000164904; -.
DR eggNOG; KOG2453; Eukaryota.
DR GeneTree; ENSGT00940000154938; -.
DR InParanoid; P49419; -.
DR OMA; DAWKVYM; -.
DR OrthoDB; 692580at2759; -.
DR PhylomeDB; P49419; -.
DR TreeFam; TF300388; -.
DR BioCyc; MetaCyc:HS09157-MON; -.
DR BRENDA; 1.2.1.3; 2681.
DR BRENDA; 1.2.1.31; 2681.
DR PathwayCommons; P49419; -.
DR Reactome; R-HSA-6798163; Choline catabolism.
DR Reactome; R-HSA-71064; Lysine catabolism.
DR SABIO-RK; P49419; -.
DR SignaLink; P49419; -.
DR UniPathway; UPA00529; UER00386.
DR BioGRID-ORCS; 501; 15 hits in 1075 CRISPR screens.
DR ChiTaRS; ALDH7A1; human.
DR EvolutionaryTrace; P49419; -.
DR GeneWiki; ALDH7A1; -.
DR GenomeRNAi; 501; -.
DR Pharos; P49419; Tbio.
DR PRO; PR:P49419; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P49419; protein.
DR Bgee; ENSG00000164904; Expressed in right lobe of liver and 171 other tissues.
DR ExpressionAtlas; P49419; baseline and differential.
DR Genevisible; P49419; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IDA:UniProtKB.
DR GO; GO:0008802; F:betaine-aldehyde dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0004043; F:L-aminoadipate-semialdehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0006081; P:cellular aldehyde metabolic process; ISS:UniProtKB.
DR GO; GO:0042426; P:choline catabolic process; TAS:Reactome.
DR GO; GO:0019285; P:glycine betaine biosynthetic process from choline; IEA:UniProtKB-UniPathway.
DR GO; GO:0007605; P:sensory perception of sound; TAS:ProtInc.
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; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR044638; ALDH7A1-like.
DR PANTHER; PTHR43521; PTHR43521; 1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Disease variant; Epilepsy; Mitochondrion; NAD; Nucleus; Oxidoreductase;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..26
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 27..539
FT /note="Alpha-aminoadipic semialdehyde dehydrogenase"
FT /id="PRO_0000056490"
FT ACT_SITE 296
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT ACT_SITE 330
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:26260980"
FT BINDING 192..194
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:20207735,
FT ECO:0000269|PubMed:26260980, ECO:0007744|PDB:2J6L,
FT ECO:0007744|PDB:4X0T, ECO:0007744|PDB:4ZUK,
FT ECO:0007744|PDB:4ZVY"
FT BINDING 218
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:20207735,
FT ECO:0000269|PubMed:26260980, ECO:0007744|PDB:2J6L,
FT ECO:0007744|PDB:4X0T, ECO:0007744|PDB:4ZUK,
FT ECO:0007744|PDB:4ZVY"
FT BINDING 258..259
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:20207735,
FT ECO:0000269|PubMed:26260980, ECO:0007744|PDB:2J6L,
FT ECO:0007744|PDB:4X0T, ECO:0007744|PDB:4ZUK,
FT ECO:0007744|PDB:4ZVY"
FT BINDING 274..275
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:20207735,
FT ECO:0000269|PubMed:26260980, ECO:0007744|PDB:2J6L,
FT ECO:0007744|PDB:4X0T, ECO:0007744|PDB:4ZUK,
FT ECO:0007744|PDB:4ZVY"
FT BINDING 296..297
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:20207735,
FT ECO:0000269|PubMed:26260980, ECO:0007744|PDB:2J6L,
FT ECO:0007744|PDB:4X0T"
FT BINDING 331
FT /ligand="(S)-2-amino-6-oxohexanoate"
FT /ligand_id="ChEBI:CHEBI:58321"
FT /evidence="ECO:0007744|PDB:4ZUL"
FT BINDING 427
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:20207735,
FT ECO:0000269|PubMed:26260980, ECO:0007744|PDB:2J6L,
FT ECO:0007744|PDB:4X0T"
FT BINDING 489
FT /ligand="(S)-2-amino-6-oxohexanoate"
FT /ligand_id="ChEBI:CHEBI:58321"
FT /evidence="ECO:0007744|PDB:4ZUL"
FT BINDING 490
FT /ligand="(S)-2-amino-6-oxohexanoate"
FT /ligand_id="ChEBI:CHEBI:58321"
FT /evidence="ECO:0007744|PDB:4ZUL"
FT SITE 195
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MOD_RES 94
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DBF1"
FT MOD_RES 94
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DBF1"
FT MOD_RES 462
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBF1"
FT MOD_RES 500
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBF1"
FT MOD_RES 537
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBF1"
FT VAR_SEQ 1..28
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8088832"
FT /id="VSP_038987"
FT VAR_SEQ 337..400
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045905"
FT VARIANT 110..539
FT /note="Missing (in PDE; loss of alpha-AASA dehydrogenase
FT activity)"
FT /evidence="ECO:0000269|PubMed:16491085"
FT /id="VAR_085776"
FT VARIANT 199
FT /note="A -> V (in PDE; loss of alpha-AASA dehydrogenase
FT activity; dbSNP:rs121912709)"
FT /evidence="ECO:0000269|PubMed:16491085"
FT /id="VAR_031718"
FT VARIANT 202
FT /note="G -> V (in PDE)"
FT /evidence="ECO:0000269|PubMed:17068770"
FT /id="VAR_069184"
FT VARIANT 291
FT /note="G -> E (in PDE)"
FT /evidence="ECO:0000269|PubMed:17068770"
FT /id="VAR_069185"
FT VARIANT 301
FT /note="N -> I (in PDE; dbSNP:rs121912711)"
FT /evidence="ECO:0000269|PubMed:17068770"
FT /id="VAR_069186"
FT VARIANT 335
FT /note="R -> Q (in PDE; dbSNP:rs754449549)"
FT /evidence="ECO:0000269|PubMed:17068770"
FT /id="VAR_069187"
FT VARIANT 395
FT /note="V -> G (in PDE)"
FT /evidence="ECO:0000269|PubMed:17068770"
FT /id="VAR_069188"
FT VARIANT 412
FT /note="T -> A (in dbSNP:rs2306618)"
FT /id="VAR_028202"
FT VARIANT 427
FT /note="E -> Q (in PDE; loss of alpha-AASA dehydrogenase
FT activity; dbSNP:rs121912707)"
FT /evidence="ECO:0000269|PubMed:16491085,
FT ECO:0000269|PubMed:17068770"
FT /id="VAR_031719"
FT VARIANT 439
FT /note="K -> Q (in dbSNP:rs12514417)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_028203"
FT VARIANT 458
FT /note="S -> N (in PDE)"
FT /evidence="ECO:0000269|PubMed:17068770"
FT /id="VAR_069189"
FT CONFLICT 236
FT /note="K -> R (in Ref. 2; BAG59812)"
FT /evidence="ECO:0000305"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:2J6L"
FT HELIX 37..45
FT /evidence="ECO:0007829|PDB:2J6L"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:2J6L"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:2J6L"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:2J6L"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:2J6L"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:2J6L"
FT HELIX 85..102
FT /evidence="ECO:0007829|PDB:2J6L"
FT HELIX 107..123
FT /evidence="ECO:0007829|PDB:2J6L"
FT HELIX 125..135
FT /evidence="ECO:0007829|PDB:2J6L"
FT HELIX 140..160
FT /evidence="ECO:0007829|PDB:2J6L"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:2J6L"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:2J6L"
FT STRAND 176..184
FT /evidence="ECO:0007829|PDB:2J6L"
FT STRAND 186..191
FT /evidence="ECO:0007829|PDB:2J6L"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:2J6L"
FT HELIX 199..210
FT /evidence="ECO:0007829|PDB:2J6L"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:2J6L"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:2J6L"
FT HELIX 224..240
FT /evidence="ECO:0007829|PDB:2J6L"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:2J6L"
FT STRAND 248..251
FT /evidence="ECO:0007829|PDB:2J6L"
FT HELIX 255..263
FT /evidence="ECO:0007829|PDB:2J6L"
FT STRAND 268..274
FT /evidence="ECO:0007829|PDB:2J6L"
FT HELIX 276..288
FT /evidence="ECO:0007829|PDB:2J6L"
FT STRAND 292..296
FT /evidence="ECO:0007829|PDB:2J6L"
FT STRAND 301..305
FT /evidence="ECO:0007829|PDB:2J6L"
FT HELIX 311..323
FT /evidence="ECO:0007829|PDB:2J6L"
FT HELIX 324..327
FT /evidence="ECO:0007829|PDB:2J6L"
FT STRAND 333..339
FT /evidence="ECO:0007829|PDB:2J6L"
FT TURN 340..342
FT /evidence="ECO:0007829|PDB:2J6L"
FT HELIX 343..355
FT /evidence="ECO:0007829|PDB:2J6L"
FT HELIX 375..390
FT /evidence="ECO:0007829|PDB:2J6L"
FT STRAND 394..397
FT /evidence="ECO:0007829|PDB:2J6L"
FT STRAND 403..407
FT /evidence="ECO:0007829|PDB:2J6L"
FT STRAND 412..416
FT /evidence="ECO:0007829|PDB:2J6L"
FT HELIX 422..425
FT /evidence="ECO:0007829|PDB:2J6L"
FT STRAND 429..438
FT /evidence="ECO:0007829|PDB:2J6L"
FT HELIX 441..449
FT /evidence="ECO:0007829|PDB:2J6L"
FT STRAND 451..453
FT /evidence="ECO:0007829|PDB:4X0U"
FT STRAND 455..460
FT /evidence="ECO:0007829|PDB:2J6L"
FT HELIX 464..471
FT /evidence="ECO:0007829|PDB:2J6L"
FT STRAND 478..485
FT /evidence="ECO:0007829|PDB:2J6L"
FT STRAND 494..496
FT /evidence="ECO:0007829|PDB:2J6L"
FT HELIX 500..502
FT /evidence="ECO:0007829|PDB:2J6L"
FT TURN 504..506
FT /evidence="ECO:0007829|PDB:4X0U"
FT STRAND 507..509
FT /evidence="ECO:0007829|PDB:2J6L"
FT HELIX 512..516
FT /evidence="ECO:0007829|PDB:2J6L"
FT STRAND 517..525
FT /evidence="ECO:0007829|PDB:2J6L"
FT HELIX 533..535
FT /evidence="ECO:0007829|PDB:6O4E"
FT INIT_MET P49419-2:1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES P49419-2:2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
SQ SEQUENCE 539 AA; 58487 MW; 05385562F71312B6 CRC64;
MWRLPRALCV HAAKTSKLSG PWSRPAAFMS TLLINQPQYA WLKELGLREE NEGVYNGSWG
GRGEVITTYC PANNEPIARV RQASVADYEE TVKKAREAWK IWADIPAPKR GEIVRQIGDA
LREKIQVLGS LVSLEMGKIL VEGVGEVQEY VDICDYAVGL SRMIGGPILP SERSGHALIE
QWNPVGLVGI ITAFNFPVAV YGWNNAIAMI CGNVCLWKGA PTTSLISVAV TKIIAKVLED
NKLPGAICSL TCGGADIGTA MAKDERVNLL SFTGSTQVGK QVGLMVQERF GRSLLELGGN
NAIIAFEDAD LSLVVPSALF AAVGTAGQRC TTARRLFIHE SIHDEVVNRL KKAYAQIRVG
NPWDPNVLYG PLHTKQAVSM FLGAVEEAKK EGGTVVYGGK VMDRPGNYVE PTIVTGLGHD
ASIAHTETFA PILYVFKFKN EEEVFAWNNE VKQGLSSSIF TKDLGRIFRW LGPKGSDCGI
VNVNIPTSGA EIGGAFGGEK HTGGGRESGS DAWKQYMRRS TCTINYSKDL PLAQGIKFQ
