NPL_HUMAN
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 03-AUG-2022, entry version 158.
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; 2.
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; Q9BXD5; -.
DR PeptideAtlas; Q9BXD5; -.
DR PRIDE; 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 Antibodypedia; 34441; 131 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 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; LPPMRYK; -.
DR OrthoDB; 1238597at2759; -.
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; 24 hits in 1073 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 157 other tissues.
DR ExpressionAtlas; Q9BXD5; baseline and differential.
DR Genevisible; Q9BXD5; HS.
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; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002220; DapA-like.
DR InterPro; IPR005264; NanA.
DR PANTHER; PTHR12128; PTHR12128; 1.
DR Pfam; PF00701; DHDPS; 1.
DR PIRSF; PIRSF001365; DHDPS; 1.
DR PRINTS; PR00146; DHPICSNTHASE.
DR SMART; SM01130; DHDPS; 1.
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 173
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000250"
FT BINDING 51..52
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 143
FT /note="Involved in proton transfer during cleavage"
FT /evidence="ECO:0000250"
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
