ID   NPL_HUMAN               Reviewed;         320 AA.
AC   Q9BXD5; B2R839; Q4G0Q8; Q4G0Z2; Q64L88; Q6PEL0;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 166.
DE   RecName: Full=N-acetylneuraminate lyase {ECO:0000305};
DE            Short=NALase;
DE            EC=4.1.3.3 {ECO:0000269|PubMed:33895133};
DE   AltName: Full=N-acetylneuraminate pyruvate-lyase;
DE   AltName: Full=N-acetylneuraminic acid aldolase;
DE   AltName: Full=Sialate lyase;
DE   AltName: Full=Sialate-pyruvate lyase;
DE   AltName: Full=Sialic acid aldolase;
DE   AltName: Full=Sialic acid lyase;
GN   Name=NPL {ECO:0000312|HGNC:HGNC:16781}; Synonyms=C1orf13;
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 1).
RX   PubMed=11318611; DOI=10.1006/geno.2001.6500;
RA   Sood R., Bonner T.I., Malakowska I., Stephan D.A., Robbins C.M.,
RA   Connors T.D., Morgenbesser S.D., Su K., Faruque M.U., Pinkett H.,
RA   Graham C., Baxevanis A.D., Klinger K.W., Landes G.M., Trent J.M.,
RA   Carpten J.D.;
RT   "Cloning and characterization of 13 novel transcripts and the human RGS8
RT   gene from the 1q25 region encompassing the hereditary prostate cancer
RT   (HPC1) locus.";
RL   Genomics 73:211-222(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RX   PubMed=16147865; DOI=10.1080/10425170400020373;
RA   Wu M., Gu S., Xu J., Zou X., Zheng H., Jin Z., Xie Y., Ji C., Mao Y.;
RT   "A novel splice variant of human gene NPL, mainly expressed in human liver,
RT   kidney and peripheral blood leukocyte.";
RL   DNA Seq. 16:137-142(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Teratocarcinoma;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3; 4 AND 5).
RC   TISSUE=Hypothalamus, Kidney, and Testis;
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   [6]
RP   PATHWAY.
RX   PubMed=22692205; DOI=10.1074/jbc.m112.363549;
RA   Bergfeld A.K., Pearce O.M., Diaz S.L., Pham T., Varki A.;
RT   "Metabolism of vertebrate amino sugars with N-glycolyl groups: elucidating
RT   the intracellular fate of the non-human sialic acid N-glycolylneuraminic
RT   acid.";
RL   J. Biol. Chem. 287:28865-28881(2012).
RN   [7]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=33895133; DOI=10.1016/j.jbc.2021.100699;
RA   Kentache T., Thabault L., Deumer G., Haufroid V., Frederick R.,
RA   Linster C.L., Peracchi A., Veiga-da-Cunha M., Bommer G.T.,
RA   Van Schaftingen E.;
RT   "The metalloprotein YhcH is an anomerase providing N-acetylneuraminate
RT   aldolase with the open form of its substrate.";
RL   J. Biol. Chem. 296:100699-100699(2021).
RN   [8] {ECO:0007744|PDB:6ARH}
RP   X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS), AND SUBUNIT.
RA   Pearce F.G., Bundela R., Keown J.R.;
RT   "Crystal structure of Human NAL at a resolution of 1.6 Angstrom.";
RL   Submitted (AUG-2017) to the PDB data bank.
CC   -!- FUNCTION: Catalyzes the cleavage of N-acetylneuraminic acid (sialic
CC       acid) to form pyruvate and N-acetylmannosamine via a Schiff base
CC       intermediate (PubMed:33895133). It prevents sialic acids from being
CC       recycled and returning to the cell surface (PubMed:33895133). Involved
CC       in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway
CC       (PubMed:22692205, PubMed:33895133). Although human is not able to
CC       catalyze formation of Neu5Gc due to the inactive CMAHP enzyme, Neu5Gc
CC       is present in food and must be degraded (Probable).
CC       {ECO:0000269|PubMed:22692205, ECO:0000269|PubMed:33895133,
CC       ECO:0000305|PubMed:22692205}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=aceneuramate = N-acetyl-D-mannosamine + pyruvate;
CC         Xref=Rhea:RHEA:23296, ChEBI:CHEBI:15361, ChEBI:CHEBI:17122,
CC         ChEBI:CHEBI:173083; EC=4.1.3.3;
CC         Evidence={ECO:0000269|PubMed:33895133};
CC   -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation.
CC       {ECO:0000269|PubMed:22692205, ECO:0000269|PubMed:33895133}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|Ref.8}.
CC   -!- INTERACTION:
CC       Q9BXD5; Q9BXD5: NPL; NbExp=4; IntAct=EBI-10287915, EBI-10287915;
CC       Q9BXD5; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-10287915, EBI-741158;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q9BXD5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9BXD5-2; Sequence=VSP_022518;
CC       Name=3;
CC         IsoId=Q9BXD5-3; Sequence=VSP_022522;
CC       Name=4;
CC         IsoId=Q9BXD5-4; Sequence=VSP_022521, VSP_022522;
CC       Name=5;
CC         IsoId=Q9BXD5-5; Sequence=VSP_022519, VSP_022520;
CC   -!- TISSUE SPECIFICITY: Isoform 2 is expressed in placenta, liver, kidney,
CC       pancreas, spleen, thymus, ovary, small intestine and peripheral blood
CC       leukocyte. {ECO:0000269|PubMed:16147865}.
CC   -!- MISCELLANEOUS: [Isoform 5]: May be produced at very low levels due to a
CC       premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC       decay. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the DapA family. NanA subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BC042003; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF338436; AAK25795.1; -; mRNA.
DR   EMBL; AY336748; AAQ82432.1; -; mRNA.
DR   EMBL; AK313225; BAG36036.1; -; mRNA.
DR   EMBL; AL355999; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL513344; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC034966; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC042003; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC058003; AAH58003.1; -; mRNA.
DR   EMBL; BC125051; AAI25052.1; -; mRNA.
DR   CCDS; CCDS1350.1; -. [Q9BXD5-1]
DR   CCDS; CCDS55666.1; -. [Q9BXD5-4]
DR   CCDS; CCDS55667.1; -. [Q9BXD5-2]
DR   RefSeq; NP_001186979.1; NM_001200050.1. [Q9BXD5-2]
DR   RefSeq; NP_001186980.1; NM_001200051.1. [Q9BXD5-4]
DR   RefSeq; NP_001186985.1; NM_001200056.1. [Q9BXD5-3]
DR   RefSeq; NP_110396.1; NM_030769.2. [Q9BXD5-1]
DR   PDB; 6ARH; X-ray; 1.60 A; A/B/C/D=1-320.
DR   PDBsum; 6ARH; -.
DR   AlphaFoldDB; Q9BXD5; -.
DR   SMR; Q9BXD5; -.
DR   BioGRID; 123344; 8.
DR   IntAct; Q9BXD5; 3.
DR   STRING; 9606.ENSP00000258317; -.
DR   iPTMnet; Q9BXD5; -.
DR   PhosphoSitePlus; Q9BXD5; -.
DR   BioMuta; NPL; -.
DR   DMDM; 74752428; -.
DR   jPOST; Q9BXD5; -.
DR   MassIVE; Q9BXD5; -.
DR   MaxQB; Q9BXD5; -.
DR   PaxDb; 9606-ENSP00000258317; -.
DR   PeptideAtlas; Q9BXD5; -.
DR   ProteomicsDB; 79405; -. [Q9BXD5-1]
DR   ProteomicsDB; 79406; -. [Q9BXD5-2]
DR   ProteomicsDB; 79407; -. [Q9BXD5-3]
DR   ProteomicsDB; 79408; -. [Q9BXD5-4]
DR   ProteomicsDB; 79409; -. [Q9BXD5-5]
DR   Pumba; Q9BXD5; -.
DR   Antibodypedia; 34441; 153 antibodies from 20 providers.
DR   DNASU; 80896; -.
DR   Ensembl; ENST00000258317.6; ENSP00000258317.2; ENSG00000135838.14. [Q9BXD5-1]
DR   Ensembl; ENST00000367552.6; ENSP00000356523.2; ENSG00000135838.14. [Q9BXD5-4]
DR   Ensembl; ENST00000367553.6; ENSP00000356524.1; ENSG00000135838.14. [Q9BXD5-1]
DR   Ensembl; ENST00000367554.7; ENSP00000356525.3; ENSG00000135838.14. [Q9BXD5-2]
DR   Ensembl; ENST00000367555.5; ENSP00000356526.1; ENSG00000135838.14. [Q9BXD5-4]
DR   GeneID; 80896; -.
DR   KEGG; hsa:80896; -.
DR   MANE-Select; ENST00000367553.6; ENSP00000356524.1; NM_030769.3; NP_110396.1.
DR   UCSC; uc001gpo.2; human. [Q9BXD5-1]
DR   AGR; HGNC:16781; -.
DR   CTD; 80896; -.
DR   DisGeNET; 80896; -.
DR   GeneCards; NPL; -.
DR   HGNC; HGNC:16781; NPL.
DR   HPA; ENSG00000135838; Tissue enhanced (kidney, placenta).
DR   MIM; 611412; gene.
DR   neXtProt; NX_Q9BXD5; -.
DR   OpenTargets; ENSG00000135838; -.
DR   PharmGKB; PA25602; -.
DR   VEuPathDB; HostDB:ENSG00000135838; -.
DR   eggNOG; ENOG502QQA3; Eukaryota.
DR   GeneTree; ENSGT00530000063604; -.
DR   HOGENOM; CLU_924263_0_0_1; -.
DR   InParanoid; Q9BXD5; -.
DR   OMA; TGEFTTM; -.
DR   OrthoDB; 101328at2759; -.
DR   PhylomeDB; Q9BXD5; -.
DR   TreeFam; TF353639; -.
DR   BRENDA; 4.1.3.3; 2681.
DR   PathwayCommons; Q9BXD5; -.
DR   Reactome; R-HSA-4085001; Sialic acid metabolism.
DR   SignaLink; Q9BXD5; -.
DR   UniPathway; UPA00629; -.
DR   BioGRID-ORCS; 80896; 37 hits in 1153 CRISPR screens.
DR   ChiTaRS; NPL; human.
DR   GenomeRNAi; 80896; -.
DR   Pharos; Q9BXD5; Tbio.
DR   PRO; PR:Q9BXD5; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q9BXD5; Protein.
DR   Bgee; ENSG00000135838; Expressed in monocyte and 159 other cell types or tissues.
DR   ExpressionAtlas; Q9BXD5; baseline and differential.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0008747; F:N-acetylneuraminate lyase activity; IDA:UniProtKB.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0019262; P:N-acetylneuraminate catabolic process; IDA:UniProtKB.
DR   CDD; cd00954; NAL; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR002220; DapA-like.
DR   InterPro; IPR005264; NanA.
DR   PANTHER; PTHR12128; DIHYDRODIPICOLINATE SYNTHASE; 1.
DR   PANTHER; PTHR12128:SF21; N-ACETYLNEURAMINATE LYASE; 1.
DR   Pfam; PF00701; DHDPS; 1.
DR   PIRSF; PIRSF001365; DHDPS; 1.
DR   PRINTS; PR00146; DHPICSNTHASE.
DR   SMART; SM01130; DHDPS; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   Genevisible; Q9BXD5; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Carbohydrate metabolism; Cytoplasm;
KW   Lyase; Reference proteome; Schiff base.
FT   CHAIN           1..320
FT                   /note="N-acetylneuraminate lyase"
FT                   /id="PRO_0000273352"
FT   ACT_SITE        143
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6L4"
FT   ACT_SITE        173
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6L4"
FT   BINDING         51
FT                   /ligand="aceneuramate"
FT                   /ligand_id="ChEBI:CHEBI:173083"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6L4"
FT   BINDING         52
FT                   /ligand="aceneuramate"
FT                   /ligand_id="ChEBI:CHEBI:173083"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6L4"
FT   BINDING         175
FT                   /ligand="aceneuramate"
FT                   /ligand_id="ChEBI:CHEBI:173083"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6L4"
FT   BINDING         199
FT                   /ligand="aceneuramate"
FT                   /ligand_id="ChEBI:CHEBI:173083"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6L4"
FT   BINDING         201
FT                   /ligand="aceneuramate"
FT                   /ligand_id="ChEBI:CHEBI:173083"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6L4"
FT   BINDING         202
FT                   /ligand="aceneuramate"
FT                   /ligand_id="ChEBI:CHEBI:173083"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6L4"
FT   BINDING         218
FT                   /ligand="aceneuramate"
FT                   /ligand_id="ChEBI:CHEBI:173083"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6L4"
FT   VAR_SEQ         1..77
FT                   /note="MAFPKKKLQGLVAATITPMTENGEINFSVIGQYVDYLVKEQGVKNIFVNGTT
FT                   GEGLSLSVSERRQVAEEWVTKGKDK -> MSRAPGILASWRRAPSLSVQKGSQTARHTC
FT                   HPEVPLGNCFLPVYKASPLTVTRLWAER (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16147865"
FT                   /id="VSP_022518"
FT   VAR_SEQ         78..109
FT                   /note="LDQVIIHVGALSLKESQELAQHAAEIGADGIA -> SNHHKLGTIRTTQSRQ
FT                   SSFRRQLKAWHSGSHL (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_022519"
FT   VAR_SEQ         110..320
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_022520"
FT   VAR_SEQ         203..246
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_022521"
FT   VAR_SEQ         260..320
FT                   /note="GFGVSQTKAIMTLVSGIPMGPPRLPLQKASREFTDSAEAKLKSLDFLSFTDL
FT                   KDGNLEAGS -> ENSKLKVSKNQRTLPLGTTNFPFLH (in isoform 3 and
FT                   isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_022522"
FT   CONFLICT        4
FT                   /note="P -> S (in Ref. 5; BC034966)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        98
FT                   /note="Q -> E (in Ref. 5; BC042003)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        212
FT                   /note="A -> E (in Ref. 5; BC042003)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        260
FT                   /note="G -> V (in Ref. 3; BAG36036)"
FT                   /evidence="ECO:0000305"
FT   STRAND          10..14
FT                   /evidence="ECO:0007829|PDB:6ARH"
FT   STRAND          23..25
FT                   /evidence="ECO:0007829|PDB:6ARH"
FT   HELIX           27..29
FT                   /evidence="ECO:0007829|PDB:6ARH"
FT   HELIX           30..40
FT                   /evidence="ECO:0007829|PDB:6ARH"
FT   STRAND          45..50
FT                   /evidence="ECO:0007829|PDB:6ARH"
FT   TURN            51..54
FT                   /evidence="ECO:0007829|PDB:6ARH"
FT   HELIX           55..57
FT                   /evidence="ECO:0007829|PDB:6ARH"
FT   HELIX           60..74
FT                   /evidence="ECO:0007829|PDB:6ARH"
FT   TURN            75..77
FT                   /evidence="ECO:0007829|PDB:6ARH"
FT   STRAND          79..84
FT                   /evidence="ECO:0007829|PDB:6ARH"
FT   HELIX           90..103
FT                   /evidence="ECO:0007829|PDB:6ARH"
FT   STRAND          106..111
FT                   /evidence="ECO:0007829|PDB:6ARH"
FT   HELIX           121..132
FT                   /evidence="ECO:0007829|PDB:6ARH"
FT   STRAND          140..144
FT                   /evidence="ECO:0007829|PDB:6ARH"
FT   HELIX           146..149
FT                   /evidence="ECO:0007829|PDB:6ARH"
FT   HELIX           155..159
FT                   /evidence="ECO:0007829|PDB:6ARH"
FT   HELIX           162..165
FT                   /evidence="ECO:0007829|PDB:6ARH"
FT   STRAND          169..174
FT                   /evidence="ECO:0007829|PDB:6ARH"
FT   HELIX           179..187
FT                   /evidence="ECO:0007829|PDB:6ARH"
FT   STRAND          195..198
FT                   /evidence="ECO:0007829|PDB:6ARH"
FT   HELIX           201..203
FT                   /evidence="ECO:0007829|PDB:6ARH"
FT   HELIX           204..209
FT                   /evidence="ECO:0007829|PDB:6ARH"
FT   STRAND          214..218
FT                   /evidence="ECO:0007829|PDB:6ARH"
FT   HELIX           220..235
FT                   /evidence="ECO:0007829|PDB:6ARH"
FT   HELIX           239..259
FT                   /evidence="ECO:0007829|PDB:6ARH"
FT   HELIX           263..274
FT                   /evidence="ECO:0007829|PDB:6ARH"
FT   HELIX           290..302
FT                   /evidence="ECO:0007829|PDB:6ARH"
SQ   SEQUENCE   320 AA;  35163 MW;  FC0EBA9B05FE9E62 CRC64;
     MAFPKKKLQG LVAATITPMT ENGEINFSVI GQYVDYLVKE QGVKNIFVNG TTGEGLSLSV
     SERRQVAEEW VTKGKDKLDQ VIIHVGALSL KESQELAQHA AEIGADGIAV IAPFFLKPWT
     KDILINFLKE VAAAAPALPF YYYHIPALTG VKIRAEELLD GILDKIPTFQ GLKFSDTDLL
     DFGQCVDQNR QQQFAFLFGV DEQLLSALVM GATGAVGSTY NYLGKKTNQM LEAFEQKDFS
     LALNYQFCIQ RFINFVVKLG FGVSQTKAIM TLVSGIPMGP PRLPLQKASR EFTDSAEAKL
     KSLDFLSFTD LKDGNLEAGS
//