AL1L2_HUMAN
ID AL1L2_HUMAN Reviewed; 923 AA.
AC Q3SY69; Q3SY68; Q68D62; Q6AI55; Q8N922;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Mitochondrial 10-formyltetrahydrofolate dehydrogenase {ECO:0000305|PubMed:21238436};
DE Short=Mitochondrial 10-FTHFDH {ECO:0000303|PubMed:21238436};
DE Short=mtFDH {ECO:0000303|PubMed:21238436};
DE EC=1.5.1.6 {ECO:0000269|PubMed:21238436};
DE AltName: Full=Aldehyde dehydrogenase family 1 member L2 {ECO:0000303|PubMed:21238436};
GN Name=ALDH1L2 {ECO:0000303|PubMed:21238436, ECO:0000312|HGNC:HGNC:26777};
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] (ISOFORMS 1 AND 2).
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-752 (ISOFORM 1).
RC TISSUE=Chondrocyte;
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 MRNA] OF 221-511 (ISOFORM 3), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 762-923 (ISOFORM 1).
RC TISSUE=Cervix, and Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-903, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [5]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=20498374; DOI=10.1074/jbc.m110.128843;
RA Krupenko N.I., Dubard M.E., Strickland K.C., Moxley K.M., Oleinik N.V.,
RA Krupenko S.A.;
RT "ALDH1L2 is the mitochondrial homolog of 10-formyltetrahydrofolate
RT dehydrogenase.";
RL J. Biol. Chem. 285:23056-23063(2010).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, PHOSPHOPANTETHEINYLATION AT SER-375, DOMAIN,
RP AND MUTAGENESIS OF SER-374 AND SER-375.
RX PubMed=21238436; DOI=10.1016/j.cbi.2011.01.008;
RA Strickland K.C., Krupenko N.I., Dubard M.E., Hu C.J., Tsybovsky Y.,
RA Krupenko S.A.;
RT "Enzymatic properties of ALDH1L2, a mitochondrial 10-formyltetrahydrofolate
RT dehydrogenase.";
RL Chem. Biol. Interact. 191:129-136(2011).
RN [7]
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).
CC -!- FUNCTION: Mitochondrial 10-formyltetrahydrofolate dehydrogenase that
CC catalyzes the NADP(+)-dependent conversion of 10-formyltetrahydrofolate
CC to tetrahydrofolate and carbon dioxide. {ECO:0000269|PubMed:21238436}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-10-formyltetrahydrofolate + H2O + NADP(+) = (6S)-5,6,7,8-
CC tetrahydrofolate + CO2 + H(+) + NADPH; Xref=Rhea:RHEA:10180,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57453, ChEBI:CHEBI:57454, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.5.1.6;
CC Evidence={ECO:0000269|PubMed:21238436};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10181;
CC Evidence={ECO:0000305|PubMed:21238436};
CC -!- INTERACTION:
CC Q3SY69; P42858: HTT; NbExp=3; IntAct=EBI-6916128, EBI-466029;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:20498374}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q3SY69-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3SY69-2; Sequence=VSP_030752, VSP_030753;
CC Name=3;
CC IsoId=Q3SY69-3; Sequence=VSP_030754, VSP_030755;
CC -!- TISSUE SPECIFICITY: Highly expressed in pancreas, heart, brain and
CC skeletal muscle. {ECO:0000269|PubMed:20498374}.
CC -!- DOMAIN: The N-terminal hydrolase domain has an NADP-independent
CC formyltetrahydrofolate hydrolase activity, releasing formate and
CC tetrahydrofolate. {ECO:0000250|UniProtKB:P28037}.
CC -!- DOMAIN: The C-terminal aldehyde dehydrogenase domain has an NADP-
CC dependent dehydrogenase activity. It catalyzes the oxidation of
CC formate, released by the hydrolysis of formyltetrahydrofolate, into
CC CO2. {ECO:0000250|UniProtKB:P28037}.
CC -!- DOMAIN: The carrier domain is phosphopantetheinylated and uses the 4'-
CC phosphopantetheine/4'-PP swinging arm to transfer the formyl group
CC released by the N-terminal formyltetrahydrofolate hydrolase activity to
CC the C-terminal aldehyde dehydrogenase domain that catalyzes its NADP-
CC dependent oxidation into CO2 (PubMed:21238436). The overall NADP-
CC dependent physiological reaction requires the 3 domains (N-terminal
CC hydrolase, C-terminal aldehyde dehydrogenase and carrier domains) to
CC convert formyltetrahydrofolate into tetrahydrofolate and CO2 (By
CC similarity). {ECO:0000250|UniProtKB:P28037,
CC ECO:0000269|PubMed:21238436}.
CC -!- PTM: Phosphopantetheinylation at Ser-375 by AASDHPPT is required for
CC the formyltetrahydrofolate dehydrogenase activity.
CC {ECO:0000269|PubMed:21238436}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the GART family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the aldehyde
CC dehydrogenase family. ALDH1L subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI03936.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
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DR EMBL; BC103934; AAI03935.1; -; mRNA.
DR EMBL; BC103935; AAI03936.1; ALT_SEQ; mRNA.
DR EMBL; AK095827; BAC04634.1; -; mRNA.
DR EMBL; CR627287; CAH10368.1; ALT_TERM; mRNA.
DR EMBL; CR749561; CAH18358.1; -; mRNA.
DR CCDS; CCDS31891.1; -. [Q3SY69-1]
DR RefSeq; NP_001029345.2; NM_001034173.3. [Q3SY69-1]
DR RefSeq; XP_011536291.1; XM_011537989.2. [Q3SY69-3]
DR AlphaFoldDB; Q3SY69; -.
DR SMR; Q3SY69; -.
DR BioGRID; 127759; 32.
DR IntAct; Q3SY69; 14.
DR MINT; Q3SY69; -.
DR STRING; 9606.ENSP00000258494; -.
DR iPTMnet; Q3SY69; -.
DR PhosphoSitePlus; Q3SY69; -.
DR BioMuta; ALDH1L2; -.
DR DMDM; 166198355; -.
DR EPD; Q3SY69; -.
DR jPOST; Q3SY69; -.
DR MassIVE; Q3SY69; -.
DR MaxQB; Q3SY69; -.
DR PaxDb; Q3SY69; -.
DR PeptideAtlas; Q3SY69; -.
DR PRIDE; Q3SY69; -.
DR ProteomicsDB; 61843; -. [Q3SY69-1]
DR ProteomicsDB; 61844; -. [Q3SY69-2]
DR ProteomicsDB; 61845; -. [Q3SY69-3]
DR Antibodypedia; 30615; 101 antibodies from 22 providers.
DR DNASU; 160428; -.
DR Ensembl; ENST00000258494.14; ENSP00000258494.9; ENSG00000136010.14. [Q3SY69-1]
DR Ensembl; ENST00000552270.1; ENSP00000447538.1; ENSG00000136010.14. [Q3SY69-2]
DR GeneID; 160428; -.
DR KEGG; hsa:160428; -.
DR MANE-Select; ENST00000258494.14; ENSP00000258494.9; NM_001034173.4; NP_001029345.2.
DR UCSC; uc001tlc.4; human. [Q3SY69-1]
DR CTD; 160428; -.
DR DisGeNET; 160428; -.
DR GeneCards; ALDH1L2; -.
DR HGNC; HGNC:26777; ALDH1L2.
DR HPA; ENSG00000136010; Group enriched (pancreas, salivary gland).
DR MIM; 613584; gene.
DR neXtProt; NX_Q3SY69; -.
DR OpenTargets; ENSG00000136010; -.
DR PharmGKB; PA134928545; -.
DR VEuPathDB; HostDB:ENSG00000136010; -.
DR eggNOG; KOG2452; Eukaryota.
DR GeneTree; ENSGT00940000158018; -.
DR HOGENOM; CLU_014974_0_0_1; -.
DR InParanoid; Q3SY69; -.
DR OMA; NEQVFMA; -.
DR PhylomeDB; Q3SY69; -.
DR TreeFam; TF354242; -.
DR BioCyc; MetaCyc:HS06100-MON; -.
DR BRENDA; 1.5.1.6; 2681.
DR PathwayCommons; Q3SY69; -.
DR Reactome; R-HSA-196757; Metabolism of folate and pterines.
DR SignaLink; Q3SY69; -.
DR BioGRID-ORCS; 160428; 6 hits in 1074 CRISPR screens.
DR ChiTaRS; ALDH1L2; human.
DR GeneWiki; ALDH1L2; -.
DR GenomeRNAi; 160428; -.
DR Pharos; Q3SY69; Tbio.
DR PRO; PR:Q3SY69; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q3SY69; protein.
DR Bgee; ENSG00000136010; Expressed in tibia and 159 other tissues.
DR ExpressionAtlas; Q3SY69; baseline and differential.
DR Genevisible; Q3SY69; HS.
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:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IBA:GO_Central.
DR GO; GO:0016155; F:formyltetrahydrofolate dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0016742; F:hydroxymethyl-, formyl- and related transferase activity; IEA:InterPro.
DR GO; GO:0009258; P:10-formyltetrahydrofolate catabolic process; IDA:UniProtKB.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:Ensembl.
DR GO; GO:0046655; P:folic acid metabolic process; IEA:Ensembl.
DR GO; GO:0006740; P:NADPH regeneration; IDA:UniProtKB.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.10.25.10; -; 1.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR InterPro; IPR011407; 10_FTHF_DH.
DR InterPro; IPR036736; ACP-like_sf.
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; IPR005793; Formyl_trans_C.
DR InterPro; IPR037022; Formyl_trans_C_sf.
DR InterPro; IPR002376; Formyl_transf_N.
DR InterPro; IPR036477; Formyl_transf_N_sf.
DR InterPro; IPR011034; Formyl_transferase-like_C_sf.
DR InterPro; IPR001555; GART_AS.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR Pfam; PF00171; Aldedh; 1.
DR Pfam; PF02911; Formyl_trans_C; 1.
DR Pfam; PF00551; Formyl_trans_N; 1.
DR Pfam; PF00550; PP-binding; 1.
DR PIRSF; PIRSF036489; 10-FTHFDH; 1.
DR SUPFAM; SSF50486; SSF50486; 1.
DR SUPFAM; SSF53328; SSF53328; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00373; GART; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Mitochondrion; NADP;
KW One-carbon metabolism; Oxidoreductase; Phosphopantetheine; Phosphoprotein;
KW Reference proteome; Transit peptide.
FT CHAIN 1..923
FT /note="Mitochondrial 10-formyltetrahydrofolate
FT dehydrogenase"
FT /id="PRO_0000316001"
FT TRANSIT 1..19
FT /note="Mitochondrion; not cleaved"
FT /evidence="ECO:0000305|PubMed:20498374"
FT DOMAIN 339..416
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 23..331
FT /note="Hydrolase domain"
FT /evidence="ECO:0000250|UniProtKB:P28037"
FT REGION 438..923
FT /note="Aldehyde dehydrogenase domain"
FT /evidence="ECO:0000250|UniProtKB:P28037"
FT ACT_SITE 128
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P28037"
FT ACT_SITE 694
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28037"
FT ACT_SITE 728
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P28037"
FT BINDING 110..112
FT /ligand="(6S)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57454"
FT /evidence="ECO:0000250|UniProtKB:O75891"
FT BINDING 164
FT /ligand="(6S)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57454"
FT /evidence="ECO:0000250|UniProtKB:O75891"
FT BINDING 592..594
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P28037"
FT BINDING 618..621
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P28037"
FT BINDING 651..656
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P28037"
FT BINDING 671..672
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P28037"
FT BINDING 694..695
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P28037"
FT BINDING 778
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P28037"
FT BINDING 825..827
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P28037"
FT SITE 164
FT /note="Essential for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P28037"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75891"
FT MOD_RES 60
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8R0Y6"
FT MOD_RES 375
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000269|PubMed:21238436"
FT MOD_RES 650
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75891"
FT MOD_RES 681
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8K009"
FT MOD_RES 788
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8R0Y6"
FT MOD_RES 903
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 199..203
FT /note="VEAVQ -> KLSNS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030752"
FT VAR_SEQ 204..923
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030753"
FT VAR_SEQ 512..516
FT /note="RLADL -> SMRMN (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_030754"
FT VAR_SEQ 517..923
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_030755"
FT MUTAGEN 374
FT /note="S->A: No effect on phosphopantetheinylation."
FT /evidence="ECO:0000269|PubMed:21238436"
FT MUTAGEN 375
FT /note="S->A: Loss of phosphopantetheinylation."
FT /evidence="ECO:0000269|PubMed:21238436"
FT CONFLICT 712
FT /note="A -> T (in Ref. 1; AAI03935)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 923 AA; 101746 MW; C5DD74506F08AAFE CRC64;
MLRRGSQALR RFSTGRVYFK NKLKLALIGQ SLFGQEVYSH LRKEGHRVVG VFTVPDKDGK
ADPLALAAEK DGTPVFKLPK WRVKGKTIKE VAEAYRSVGA ELNVLPFCTQ FIPMDIIDSP
KHGSIIYHPS ILPRHRGASA INWTLIMGDK KAGFSVFWAD DGLDTGPILL QRSCDVEPND
TVDALYNRFL FPEGIKAMVE AVQLIADGKA PRIPQPEEGA TYEGIQKKEN AEISWDQSAE
VLHNWIRGHD KVPGAWTEIN GQMVTFYGST LLNSSVPPGE PLEIKGAKKP GLVTKNGLVL
FGNDGKALTV RNLQFEDGKM IPASQYFSTG ETSVVELTAE EVKVAETIKV IWAGILSNVP
IIEDSTDFFK SGASSMDVAR LVEEIRQKCG GLQLQNEDVY MATKFEGFIQ KVVRKLRGED
QEVELVVDYI SKEVNEIMVK MPYQCFINGQ FTDADDGKTY DTINPTDGST ICKVSYASLA
DVDKAVAAAK DAFENGEWGR MNARERGRLM YRLADLLEEN QEELATIEAL DSGAVYTLAL
KTHIGMSVQT FRYFAGWCDK IQGSTIPINQ ARPNRNLTFT KKEPLGVCAI IIPWNYPLMM
LAWKSAACLA AGNTLVLKPA QVTPLTALKF AELSVKAGFP KGVINIIPGS GGIAGQRLSE
HPDIRKLGFT GSTPIGKQIM KSCAVSNLKK VSLELGGKSP LIIFNDCELD KAVRMGMGAV
FFNKGENCIA AGRLFVEESI HDEFVTRVVE EIKKMKIGDP LDRSTDHGPQ NHKAHLEKLL
QYCETGVKEG ATLVYGGRQV QRPGFFMEPT VFTDVEDYMY LAKEESFGPI MVISKFQNGD
IDGVLQRANS TEYGLASGVF TRDINKAMYV SEKLEAGTVF INTYNKTDVA APFGGVKQSG
FGKDLGEEAL NEYLKTKTVT LEY
