ASM3A_HUMAN
ID ASM3A_HUMAN Reviewed; 453 AA.
AC Q92484; B7Z729; Q8WV13;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Acid sphingomyelinase-like phosphodiesterase 3a;
DE Short=ASM-like phosphodiesterase 3a;
DE EC=3.1.4.- {ECO:0000269|PubMed:25288789, ECO:0000269|PubMed:26783088};
DE Flags: Precursor;
GN Name=SMPDL3A; Synonyms=ASML3A;
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] (ISOFORM 2).
RC TISSUE=Synovium;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 [MRNA] OF 277-453 (ISOFORM 1/2).
RA Hofmann K.;
RT "Acid sphingomyelinase is a member of a multi-gene family and shares motifs
RT with a large family of metallo-phosphoesterases.";
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-222; ASN-263 AND ASN-356.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [7]
RP CATALYTIC ACTIVITY, FUNCTION, LACK OF SPHINGOMYELIN PHOSPHODIESTERASE
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBCELLULAR
RP LOCATION, GLYCOSYLATION, INDUCTION BY CHOLESTEROL, AND TISSUE SPECIFICITY.
RX PubMed=25288789; DOI=10.1074/jbc.m114.612341;
RA Traini M., Quinn C.M., Sandoval C., Johansson E., Schroder K., Kockx M.,
RA Meikle P.J., Jessup W., Kritharides L.;
RT "Sphingomyelin phosphodiesterase acid-like 3A (SMPDL3A) is a novel
RT nucleotide phosphodiesterase regulated by cholesterol in human
RT macrophages.";
RL J. Biol. Chem. 289:32895-32913(2014).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 34-443 IN COMPLEX WITH CMP;
RP PHOSPHORIBOSE AND ZINC IONS, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, DISULFIDE BONDS,
RP GLYCOSYLATION AT ASN-69; ASN-131 AND ASN-356, AND ACTIVITY REGULATION.
RX PubMed=26783088; DOI=10.1111/febs.13655;
RA Lim S.M., Yeung K., Tresaugues L., Ling T.H., Nordlund P.;
RT "The structure and catalytic mechanism of human sphingomyelin
RT phosphodiesterase like 3a - an acid sphingomyelinase homolog with a novel
RT nucleotide hydrolase activity.";
RL FEBS J. 283:1107-1123(2016).
CC -!- FUNCTION: Has in vitro nucleotide phosphodiesterase activity with
CC nucleoside triphosphates, such as ATP (PubMed:25288789,
CC PubMed:26783088). Has in vitro activity with p-nitrophenyl-TMP
CC (PubMed:25288789). Has lower activity with nucleoside diphosphates, and
CC no activity with nucleoside monophosphates (PubMed:25288789,
CC PubMed:26783088). Has in vitro activity with CDP-choline, giving rise
CC to CMP and phosphocholine. Has in vitro activity with CDP-ethanolamine
CC (PubMed:26783088). Does not have sphingomyelin phosphodiesterase
CC activity (PubMed:25288789, PubMed:26783088).
CC {ECO:0000269|PubMed:25288789, ECO:0000269|PubMed:26783088}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:26783088};
CC Note=Binds 2 Zn(2+) per subunit. {ECO:0000269|PubMed:26783088};
CC -!- ACTIVITY REGULATION: Requires micromolar levels of Zn(2+) for activity
CC (PubMed:26783088). Inhibited by millimolar levels of Zn(2+)
CC (PubMed:25288789, PubMed:26783088). {ECO:0000269|PubMed:25288789,
CC ECO:0000269|PubMed:26783088}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=326 uM for ATP {ECO:0000269|PubMed:26783088};
CC KM=306 uM for ADP {ECO:0000269|PubMed:26783088};
CC KM=348 uM for ADP-ribose {ECO:0000269|PubMed:26783088};
CC KM=390 uM for CDP-ethanolamine {ECO:0000269|PubMed:26783088};
CC KM=262 uM for CDP-choline {ECO:0000269|PubMed:26783088};
CC pH dependence:
CC Optimum pH is 4-6. {ECO:0000269|PubMed:25288789};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:26783088}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25288789}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q92484-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q92484-2; Sequence=VSP_054640;
CC -!- TISSUE SPECIFICITY: Detected in blood serum. Detected in macrophages
CC (at protein level). {ECO:0000269|PubMed:25288789}.
CC -!- INDUCTION: Up-regulated in macrophages in response to cholesterol
CC accumulation. Up-regulated by cAMP. {ECO:0000269|PubMed:25288789}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:25288789}.
CC -!- SIMILARITY: Belongs to the acid sphingomyelinase family. {ECO:0000305}.
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DR EMBL; AK301365; BAH13465.1; -; mRNA.
DR EMBL; AL732431; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48164.1; -; Genomic_DNA.
DR EMBL; BC018999; AAH18999.1; -; mRNA.
DR EMBL; Y08136; CAA69330.1; -; mRNA.
DR CCDS; CCDS5128.1; -. [Q92484-1]
DR CCDS; CCDS69190.1; -. [Q92484-2]
DR RefSeq; NP_001273067.1; NM_001286138.1. [Q92484-2]
DR RefSeq; NP_006705.1; NM_006714.4. [Q92484-1]
DR PDB; 5EBB; X-ray; 2.60 A; A/B/C=34-443.
DR PDB; 5EBE; X-ray; 3.00 A; A=33-450, B/C=33-447.
DR PDBsum; 5EBB; -.
DR PDBsum; 5EBE; -.
DR AlphaFoldDB; Q92484; -.
DR SMR; Q92484; -.
DR BioGRID; 116128; 2.
DR IntAct; Q92484; 2.
DR STRING; 9606.ENSP00000357425; -.
DR GlyConnect; 987; 3 N-Linked glycans (2 sites).
DR GlyGen; Q92484; 7 sites, 4 N-linked glycans (2 sites).
DR iPTMnet; Q92484; -.
DR PhosphoSitePlus; Q92484; -.
DR BioMuta; SMPDL3A; -.
DR DMDM; 39932730; -.
DR EPD; Q92484; -.
DR jPOST; Q92484; -.
DR MassIVE; Q92484; -.
DR MaxQB; Q92484; -.
DR PaxDb; Q92484; -.
DR PeptideAtlas; Q92484; -.
DR PRIDE; Q92484; -.
DR ProteomicsDB; 6826; -.
DR ProteomicsDB; 75265; -. [Q92484-1]
DR Antibodypedia; 32649; 135 antibodies from 22 providers.
DR DNASU; 10924; -.
DR Ensembl; ENST00000368440.5; ENSP00000357425.4; ENSG00000172594.13. [Q92484-1]
DR Ensembl; ENST00000539041.5; ENSP00000442152.1; ENSG00000172594.13. [Q92484-2]
DR GeneID; 10924; -.
DR KEGG; hsa:10924; -.
DR MANE-Select; ENST00000368440.5; ENSP00000357425.4; NM_006714.5; NP_006705.1.
DR UCSC; uc003pzg.5; human. [Q92484-1]
DR CTD; 10924; -.
DR DisGeNET; 10924; -.
DR GeneCards; SMPDL3A; -.
DR HGNC; HGNC:17389; SMPDL3A.
DR HPA; ENSG00000172594; Low tissue specificity.
DR MIM; 610728; gene.
DR neXtProt; NX_Q92484; -.
DR OpenTargets; ENSG00000172594; -.
DR PharmGKB; PA134932128; -.
DR VEuPathDB; HostDB:ENSG00000172594; -.
DR eggNOG; KOG3770; Eukaryota.
DR GeneTree; ENSGT00950000183182; -.
DR HOGENOM; CLU_014743_0_0_1; -.
DR InParanoid; Q92484; -.
DR OMA; VICDKTC; -.
DR OrthoDB; 1142100at2759; -.
DR PhylomeDB; Q92484; -.
DR TreeFam; TF313674; -.
DR BRENDA; 3.1.4.1; 2681.
DR BRENDA; 3.1.4.12; 2681.
DR PathwayCommons; Q92484; -.
DR SABIO-RK; Q92484; -.
DR SignaLink; Q92484; -.
DR BioGRID-ORCS; 10924; 14 hits in 1069 CRISPR screens.
DR ChiTaRS; SMPDL3A; human.
DR GenomeRNAi; 10924; -.
DR Pharos; Q92484; Tbio.
DR PRO; PR:Q92484; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q92484; protein.
DR Bgee; ENSG00000172594; Expressed in upper leg skin and 198 other tissues.
DR Genevisible; Q92484; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0009143; P:nucleoside triphosphate catabolic process; IDA:UniProtKB.
DR CDD; cd00842; MPP_ASMase; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR017064; ASM-like_Pdiesterase_prd.
DR InterPro; IPR045473; ASM_C.
DR InterPro; IPR041805; ASMase/PPN1_MPP.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR Pfam; PF19272; ASMase_C; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PIRSF; PIRSF036767; ASM-like_PDE; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Disulfide bond; Glycoprotein;
KW Hydrolase; Metal-binding; Reference proteome; Secreted; Signal; Zinc.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..453
FT /note="Acid sphingomyelinase-like phosphodiesterase 3a"
FT /id="PRO_0000002328"
FT BINDING 45
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:26783088"
FT BINDING 47
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:26783088"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:26783088"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:26783088"
FT BINDING 114
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26783088"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26783088"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:26783088"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:26783088"
FT BINDING 252
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:26783088"
FT BINDING 293
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:26783088"
FT BINDING 295
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:26783088"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:26783088"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:26783088"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:26783088"
FT CARBOHYD 437
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 62..81
FT /evidence="ECO:0007744|PDB:5EBB, ECO:0007744|PDB:5EBE"
FT DISULFID 420..424
FT /evidence="ECO:0000255"
FT DISULFID 430..443
FT /evidence="ECO:0007744|PDB:5EBB, ECO:0007744|PDB:5EBE"
FT VAR_SEQ 1..131
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054640"
FT VARIANT 16
FT /note="H -> Y (in dbSNP:rs12523814)"
FT /id="VAR_048338"
FT VARIANT 161
FT /note="P -> S (in dbSNP:rs28385609)"
FT /id="VAR_048339"
FT CONFLICT 452
FT /note="N -> K (in Ref. 5; CAA69330)"
FT /evidence="ECO:0000305"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:5EBB"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:5EBB"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:5EBB"
FT HELIX 85..97
FT /evidence="ECO:0007829|PDB:5EBB"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:5EBB"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:5EBB"
FT HELIX 122..139
FT /evidence="ECO:0007829|PDB:5EBB"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:5EBE"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:5EBB"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:5EBB"
FT HELIX 166..175
FT /evidence="ECO:0007829|PDB:5EBB"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:5EBB"
FT HELIX 181..190
FT /evidence="ECO:0007829|PDB:5EBB"
FT STRAND 193..197
FT /evidence="ECO:0007829|PDB:5EBB"
FT STRAND 200..207
FT /evidence="ECO:0007829|PDB:5EBB"
FT HELIX 210..213
FT /evidence="ECO:0007829|PDB:5EBB"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:5EBB"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:5EBB"
FT HELIX 229..242
FT /evidence="ECO:0007829|PDB:5EBB"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:5EBB"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:5EBB"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:5EBB"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:5EBB"
FT HELIX 269..281
FT /evidence="ECO:0007829|PDB:5EBB"
FT TURN 282..285
FT /evidence="ECO:0007829|PDB:5EBB"
FT STRAND 286..291
FT /evidence="ECO:0007829|PDB:5EBB"
FT STRAND 298..303
FT /evidence="ECO:0007829|PDB:5EBB"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:5EBE"
FT STRAND 309..315
FT /evidence="ECO:0007829|PDB:5EBB"
FT STRAND 334..340
FT /evidence="ECO:0007829|PDB:5EBB"
FT TURN 342..344
FT /evidence="ECO:0007829|PDB:5EBB"
FT STRAND 347..355
FT /evidence="ECO:0007829|PDB:5EBB"
FT HELIX 357..363
FT /evidence="ECO:0007829|PDB:5EBB"
FT STRAND 368..373
FT /evidence="ECO:0007829|PDB:5EBB"
FT HELIX 374..378
FT /evidence="ECO:0007829|PDB:5EBB"
FT STRAND 381..383
FT /evidence="ECO:0007829|PDB:5EBE"
FT HELIX 385..395
FT /evidence="ECO:0007829|PDB:5EBB"
FT HELIX 401..410
FT /evidence="ECO:0007829|PDB:5EBB"
FT TURN 411..413
FT /evidence="ECO:0007829|PDB:5EBB"
FT HELIX 422..433
FT /evidence="ECO:0007829|PDB:5EBB"
FT HELIX 437..442
FT /evidence="ECO:0007829|PDB:5EBB"
SQ SEQUENCE 453 AA; 51260 MW; 2EFE762BF663984B CRC64;
MALVRALVCC LLTAWHCRSG LGLPVAPAGG RNPPPAIGQF WHVTDLHLDP TYHITDDHTK
VCASSKGANA SNPGPFGDVL CDSPYQLILS AFDFIKNSGQ EASFMIWTGD SPPHVPVPEL
STDTVINVIT NMTTTIQSLF PNLQVFPALG NHDYWPQDQL PVVTSKVYNA VANLWKPWLD
EEAISTLRKG GFYSQKVTTN PNLRIISLNT NLYYGPNIMT LNKTDPANQF EWLESTLNNS
QQNKEKVYII AHVPVGYLPS SQNITAMREY YNEKLIDIFQ KYSDVIAGQF YGHTHRDSIM
VLSDKKGSPV NSLFVAPAVT PVKSVLEKQT NNPGIRLFQY DPRDYKLLDM LQYYLNLTEA
NLKGESIWKL EYILTQTYDI EDLQPESLYG LAKQFTILDS KQFIKYYNYF FVSYDSSVTC
DKTCKAFQIC AIMNLDNISY ADCLKQLYIK HNY
