NALD2_HUMAN
ID NALD2_HUMAN Reviewed; 740 AA.
AC Q9Y3Q0; B3KQR4; Q4KKV4; Q4VAM9;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=N-acetylated-alpha-linked acidic dipeptidase 2;
DE EC=3.4.17.21;
DE AltName: Full=Glutamate carboxypeptidase III;
DE Short=GCPIII;
DE AltName: Full=N-acetylated-alpha-linked acidic dipeptidase II;
DE Short=NAALADase II;
GN Name=NAALAD2;
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), AND FUNCTION.
RC TISSUE=Lung carcinoma;
RX PubMed=10085079; DOI=10.1074/jbc.274.13.8470;
RA Pangalos M.N., Neefs J.-M., Somers M., Verhasselt P., Bekkers M.,
RA van der Helm L., Fraiponts E., Ashton D., Gordon R.D.;
RT "Isolation and expression of novel human glutamate carboxypeptidases with
RT N-acetylated alpha-linked acidic dipeptidase and dipeptidyl peptidase IV
RT activity.";
RL J. Biol. Chem. 274:8470-8483(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP ILE-101.
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 X-RAY CRYSTALLOGRAPHY (1.29 ANGSTROMS) OF 36-740 ALONE AND IN COMPLEX WITH
RP GLUTAMATE AND INHIBITORS, SUBUNIT, ZINC-BINDING SITES, COFACTOR, AND
RP GLYCOSYLATION AT ASN-111; ASN-185; ASN-449 AND ASN-628.
RX PubMed=19678840; DOI=10.1111/j.1742-4658.2009.07152.x;
RA Hlouchova K., Barinka C., Konvalinka J., Lubkowski J.;
RT "Structural insight into the evolutionary and pharmacologic homology of
RT glutamate carboxypeptidases II and III.";
RL FEBS J. 276:4448-4462(2009).
CC -!- FUNCTION: Has N-acetylated-alpha-linked-acidic dipeptidase (NAALADase)
CC activity. Also exhibits a dipeptidyl-peptidase IV type activity.
CC Inactivates the peptide neurotransmitter N-acetylaspartylglutamate.
CC {ECO:0000269|PubMed:10085079}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an unsubstituted, C-terminal glutamyl residue,
CC typically from Ac-Asp-Glu or folylpoly-gamma-glutamates.;
CC EC=3.4.17.21;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:19678840};
CC Note=Binds 2 Zn(2+) ions per subunit. Required for NAALADase activity.
CC {ECO:0000269|PubMed:19678840};
CC -!- ACTIVITY REGULATION: Inhibited by quisqualate.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19678840}.
CC -!- INTERACTION:
CC Q9Y3Q0; Q9UHD4: CIDEB; NbExp=3; IntAct=EBI-2863682, EBI-7062247;
CC Q9Y3Q0; Q6NTF9-3: RHBDD2; NbExp=3; IntAct=EBI-2863682, EBI-17589229;
CC Q9Y3Q0; B2RUZ4: SMIM1; NbExp=3; IntAct=EBI-2863682, EBI-12188413;
CC Q9Y3Q0; O76024: WFS1; NbExp=3; IntAct=EBI-2863682, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q04609};
CC Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q04609}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y3Q0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y3Q0-2; Sequence=VSP_054147, VSP_054148;
CC -!- TISSUE SPECIFICITY: Highest expression in the testis. Also found in
CC ovary and spleen. Weak expression in prostate, heart and placenta. In
CC brain, expressed in striatum, parietal cortex and ventral striatum with
CC lower levels in hippocampus, brain stem, putamen and superior
CC colliculus.
CC -!- DOMAIN: The NAALADase activity is found in the central region, the
CC dipeptidyl peptidase IV type activity in the C-terminal.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC {ECO:0000305}.
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DR EMBL; AJ012370; CAB39967.1; -; mRNA.
DR EMBL; AK075390; BAG52126.1; -; mRNA.
DR EMBL; AP000648; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471065; EAW66865.1; -; Genomic_DNA.
DR EMBL; BC096316; AAH96316.1; -; mRNA.
DR EMBL; BC096317; AAH96317.1; -; mRNA.
DR EMBL; BC096318; AAH96318.1; -; mRNA.
DR EMBL; BC099646; AAH99646.1; -; mRNA.
DR CCDS; CCDS8288.1; -. [Q9Y3Q0-1]
DR RefSeq; NP_001287859.1; NM_001300930.1.
DR RefSeq; NP_005458.1; NM_005467.3. [Q9Y3Q0-1]
DR PDB; 3FEC; X-ray; 1.49 A; A=36-740.
DR PDB; 3FED; X-ray; 1.29 A; A=36-740.
DR PDB; 3FEE; X-ray; 1.56 A; A=36-740.
DR PDB; 3FF3; X-ray; 1.37 A; A=36-740.
DR PDBsum; 3FEC; -.
DR PDBsum; 3FED; -.
DR PDBsum; 3FEE; -.
DR PDBsum; 3FF3; -.
DR AlphaFoldDB; Q9Y3Q0; -.
DR SMR; Q9Y3Q0; -.
DR BioGRID; 115321; 12.
DR IntAct; Q9Y3Q0; 9.
DR STRING; 9606.ENSP00000432481; -.
DR BindingDB; Q9Y3Q0; -.
DR ChEMBL; CHEMBL2609; -.
DR MEROPS; M28.012; -.
DR GlyGen; Q9Y3Q0; 7 sites.
DR iPTMnet; Q9Y3Q0; -.
DR PhosphoSitePlus; Q9Y3Q0; -.
DR BioMuta; NAALAD2; -.
DR DMDM; 20139300; -.
DR EPD; Q9Y3Q0; -.
DR jPOST; Q9Y3Q0; -.
DR MassIVE; Q9Y3Q0; -.
DR MaxQB; Q9Y3Q0; -.
DR PaxDb; Q9Y3Q0; -.
DR PeptideAtlas; Q9Y3Q0; -.
DR PRIDE; Q9Y3Q0; -.
DR ProteomicsDB; 62191; -.
DR ProteomicsDB; 86058; -. [Q9Y3Q0-1]
DR Antibodypedia; 67811; 51 antibodies from 16 providers.
DR DNASU; 10003; -.
DR Ensembl; ENST00000375944.7; ENSP00000365111.3; ENSG00000077616.11. [Q9Y3Q0-2]
DR Ensembl; ENST00000534061.6; ENSP00000432481.1; ENSG00000077616.11. [Q9Y3Q0-1]
DR Ensembl; ENST00000644696.1; ENSP00000494081.1; ENSG00000285516.2. [Q9Y3Q0-2]
DR Ensembl; ENST00000647397.2; ENSP00000494766.1; ENSG00000285516.2. [Q9Y3Q0-1]
DR GeneID; 10003; -.
DR KEGG; hsa:10003; -.
DR MANE-Select; ENST00000534061.6; ENSP00000432481.1; NM_005467.4; NP_005458.1.
DR UCSC; uc001pdf.5; human. [Q9Y3Q0-1]
DR CTD; 10003; -.
DR DisGeNET; 10003; -.
DR GeneCards; NAALAD2; -.
DR HGNC; HGNC:14526; NAALAD2.
DR HPA; ENSG00000077616; Tissue enhanced (pituitary gland, testis).
DR MIM; 611636; gene.
DR neXtProt; NX_Q9Y3Q0; -.
DR OpenTargets; ENSG00000077616; -.
DR PharmGKB; PA31430; -.
DR VEuPathDB; HostDB:ENSG00000077616; -.
DR eggNOG; KOG2195; Eukaryota.
DR GeneTree; ENSGT01030000234598; -.
DR InParanoid; Q9Y3Q0; -.
DR OMA; PGDDGNM; -.
DR OrthoDB; 804230at2759; -.
DR PhylomeDB; Q9Y3Q0; -.
DR TreeFam; TF312981; -.
DR PathwayCommons; Q9Y3Q0; -.
DR Reactome; R-HSA-8963693; Aspartate and asparagine metabolism.
DR SignaLink; Q9Y3Q0; -.
DR SIGNOR; Q9Y3Q0; -.
DR BioGRID-ORCS; 10003; 13 hits in 1067 CRISPR screens.
DR ChiTaRS; NAALAD2; human.
DR EvolutionaryTrace; Q9Y3Q0; -.
DR GenomeRNAi; 10003; -.
DR Pharos; Q9Y3Q0; Tchem.
DR PRO; PR:Q9Y3Q0; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9Y3Q0; protein.
DR Bgee; ENSG00000077616; Expressed in adrenal tissue and 98 other tissues.
DR ExpressionAtlas; Q9Y3Q0; baseline and differential.
DR Genevisible; Q9Y3Q0; HS.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0004180; F:carboxypeptidase activity; IBA:GO_Central.
DR GO; GO:0016805; F:dipeptidase activity; NAS:UniProtKB.
DR GO; GO:0008239; F:dipeptidyl-peptidase activity; NAS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0008236; F:serine-type peptidase activity; NAS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; NAS:UniProtKB.
DR Gene3D; 1.20.930.40; -; 1.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR007484; Peptidase_M28.
DR InterPro; IPR039373; Peptidase_M28B.
DR InterPro; IPR007365; TFR-like_dimer_dom.
DR InterPro; IPR036757; TFR-like_dimer_dom_sf.
DR PANTHER; PTHR10404; PTHR10404; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR Pfam; PF04253; TFR_dimer; 1.
DR SUPFAM; SSF47672; SSF47672; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Carboxypeptidase;
KW Cell membrane; Dipeptidase; Glycoprotein; Hydrolase; Membrane;
KW Metal-binding; Metalloprotease; Multifunctional enzyme; Protease;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix;
KW Zinc.
FT CHAIN 1..740
FT /note="N-acetylated-alpha-linked acidic dipeptidase 2"
FT /id="PRO_0000174121"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..31
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..740
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 264..577
FT /note="NAALADase"
FT ACT_SITE 414
FT /note="Nucleophile; for NAALADase activity"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT ACT_SITE 618
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 656
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 679
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19678840,
FT ECO:0007744|PDB:3FEC, ECO:0007744|PDB:3FED,
FT ECO:0007744|PDB:3FEE, ECO:0007744|PDB:3FF3"
FT BINDING 247
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19678840,
FT ECO:0007744|PDB:3FEC, ECO:0007744|PDB:3FED,
FT ECO:0007744|PDB:3FEE, ECO:0007744|PDB:3FF3"
FT BINDING 259
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:19678840,
FT ECO:0007744|PDB:3FEC, ECO:0007744|PDB:3FED,
FT ECO:0007744|PDB:3FEE, ECO:0007744|PDB:3FF3"
FT BINDING 262
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:19678840,
FT ECO:0007744|PDB:3FEC, ECO:0007744|PDB:3FED,
FT ECO:0007744|PDB:3FEE, ECO:0007744|PDB:3FF3"
FT BINDING 367
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:19678840,
FT ECO:0007744|PDB:3FEC, ECO:0007744|PDB:3FED,
FT ECO:0007744|PDB:3FEE, ECO:0007744|PDB:3FF3"
FT BINDING 377
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:19678840,
FT ECO:0007744|PDB:3FEC, ECO:0007744|PDB:3FED,
FT ECO:0007744|PDB:3FEE, ECO:0007744|PDB:3FF3"
FT BINDING 377
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:19678840,
FT ECO:0007744|PDB:3FEC, ECO:0007744|PDB:3FED,
FT ECO:0007744|PDB:3FEE, ECO:0007744|PDB:3FF3"
FT BINDING 414
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19678840,
FT ECO:0007744|PDB:3FEC, ECO:0007744|PDB:3FED,
FT ECO:0007744|PDB:3FEE, ECO:0007744|PDB:3FF3"
FT BINDING 415
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:19678840,
FT ECO:0007744|PDB:3FEC, ECO:0007744|PDB:3FED,
FT ECO:0007744|PDB:3FEE, ECO:0007744|PDB:3FF3"
FT BINDING 423
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:19678840,
FT ECO:0007744|PDB:3FEC, ECO:0007744|PDB:3FED,
FT ECO:0007744|PDB:3FEE, ECO:0007744|PDB:3FF3"
FT BINDING 426
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:19678840,
FT ECO:0007744|PDB:3FEC, ECO:0007744|PDB:3FED,
FT ECO:0007744|PDB:3FEE, ECO:0007744|PDB:3FF3"
FT BINDING 443
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:19678840,
FT ECO:0007744|PDB:3FEC, ECO:0007744|PDB:3FED,
FT ECO:0007744|PDB:3FEE, ECO:0007744|PDB:3FF3"
FT BINDING 507..508
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19678840,
FT ECO:0007744|PDB:3FEC, ECO:0007744|PDB:3FEE,
FT ECO:0007744|PDB:3FF3"
FT BINDING 524..526
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT BINDING 542..543
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19678840,
FT ECO:0007744|PDB:3FEC, ECO:0007744|PDB:3FED,
FT ECO:0007744|PDB:3FEE, ECO:0007744|PDB:3FF3"
FT BINDING 542
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT BINDING 543
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:19678840,
FT ECO:0007744|PDB:3FEC, ECO:0007744|PDB:3FED,
FT ECO:0007744|PDB:3FEE, ECO:0007744|PDB:3FF3"
FT BINDING 689..690
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19678840,
FT ECO:0007744|PDB:3FEC, ECO:0007744|PDB:3FED,
FT ECO:0007744|PDB:3FEE, ECO:0007744|PDB:3FF3"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19678840,
FT ECO:0007744|PDB:3FEC, ECO:0007744|PDB:3FED,
FT ECO:0007744|PDB:3FEE, ECO:0007744|PDB:3FF3"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19678840,
FT ECO:0007744|PDB:3FEC, ECO:0007744|PDB:3FED,
FT ECO:0007744|PDB:3FEE, ECO:0007744|PDB:3FF3"
FT CARBOHYD 314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19678840,
FT ECO:0007744|PDB:3FEC, ECO:0007744|PDB:3FED,
FT ECO:0007744|PDB:3FEE, ECO:0007744|PDB:3FF3"
FT CARBOHYD 603
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 628
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19678840,
FT ECO:0007744|PDB:3FEC, ECO:0007744|PDB:3FED,
FT ECO:0007744|PDB:3FEE, ECO:0007744|PDB:3FF3"
FT VAR_SEQ 266..305
FT /note="EYTFRLDVEEGVGIPRIPVHPIGYNDAEILLRYLGGIAPP -> GTSYLLQV
FT ATTNMLENHFLESMMLSLILKIKPTLVWPGKK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054147"
FT VAR_SEQ 306..740
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054148"
FT VARIANT 101
FT /note="V -> I (in dbSNP:rs11018879)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_034120"
FT VARIANT 446
FT /note="I -> V (in dbSNP:rs10830430)"
FT /id="VAR_034121"
FT HELIX 47..54
FT /evidence="ECO:0007829|PDB:3FED"
FT HELIX 57..67
FT /evidence="ECO:0007829|PDB:3FED"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:3FED"
FT HELIX 77..93
FT /evidence="ECO:0007829|PDB:3FED"
FT STRAND 96..109
FT /evidence="ECO:0007829|PDB:3FED"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:3FED"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:3FED"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:3FED"
FT HELIX 172..180
FT /evidence="ECO:0007829|PDB:3FED"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:3FED"
FT HELIX 200..209
FT /evidence="ECO:0007829|PDB:3FED"
FT STRAND 213..218
FT /evidence="ECO:0007829|PDB:3FED"
FT HELIX 221..224
FT /evidence="ECO:0007829|PDB:3FED"
FT TURN 232..234
FT /evidence="ECO:0007829|PDB:3FED"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:3FED"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:3FED"
FT STRAND 284..287
FT /evidence="ECO:0007829|PDB:3FED"
FT HELIX 289..297
FT /evidence="ECO:0007829|PDB:3FED"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:3FED"
FT STRAND 312..315
FT /evidence="ECO:0007829|PDB:3FED"
FT STRAND 320..323
FT /evidence="ECO:0007829|PDB:3FED"
FT STRAND 331..336
FT /evidence="ECO:0007829|PDB:3FED"
FT STRAND 339..352
FT /evidence="ECO:0007829|PDB:3FED"
FT STRAND 355..367
FT /evidence="ECO:0007829|PDB:3FED"
FT STRAND 371..373
FT /evidence="ECO:0007829|PDB:3FED"
FT TURN 375..378
FT /evidence="ECO:0007829|PDB:3FED"
FT HELIX 379..397
FT /evidence="ECO:0007829|PDB:3FED"
FT STRAND 403..412
FT /evidence="ECO:0007829|PDB:3FED"
FT HELIX 414..416
FT /evidence="ECO:0007829|PDB:3FED"
FT HELIX 419..435
FT /evidence="ECO:0007829|PDB:3FED"
FT STRAND 436..441
FT /evidence="ECO:0007829|PDB:3FED"
FT STRAND 445..447
FT /evidence="ECO:0007829|PDB:3FED"
FT STRAND 449..456
FT /evidence="ECO:0007829|PDB:3FED"
FT HELIX 458..460
FT /evidence="ECO:0007829|PDB:3FED"
FT HELIX 461..468
FT /evidence="ECO:0007829|PDB:3FED"
FT HELIX 483..490
FT /evidence="ECO:0007829|PDB:3FED"
FT STRAND 491..493
FT /evidence="ECO:0007829|PDB:3FED"
FT STRAND 496..500
FT /evidence="ECO:0007829|PDB:3FED"
FT STRAND 507..509
FT /evidence="ECO:0007829|PDB:3FED"
FT HELIX 512..516
FT /evidence="ECO:0007829|PDB:3FED"
FT STRAND 522..528
FT /evidence="ECO:0007829|PDB:3FED"
FT TURN 531..533
FT /evidence="ECO:0007829|PDB:3FED"
FT STRAND 536..538
FT /evidence="ECO:0007829|PDB:3FED"
FT TURN 540..543
FT /evidence="ECO:0007829|PDB:3FED"
FT HELIX 549..555
FT /evidence="ECO:0007829|PDB:3FED"
FT HELIX 561..579
FT /evidence="ECO:0007829|PDB:3FED"
FT HELIX 587..605
FT /evidence="ECO:0007829|PDB:3FED"
FT HELIX 606..608
FT /evidence="ECO:0007829|PDB:3FED"
FT HELIX 609..615
FT /evidence="ECO:0007829|PDB:3FED"
FT HELIX 620..640
FT /evidence="ECO:0007829|PDB:3FED"
FT HELIX 648..664
FT /evidence="ECO:0007829|PDB:3FED"
FT STRAND 679..685
FT /evidence="ECO:0007829|PDB:3FED"
FT STRAND 688..695
FT /evidence="ECO:0007829|PDB:3FED"
FT HELIX 696..702
FT /evidence="ECO:0007829|PDB:3FED"
FT HELIX 705..707
FT /evidence="ECO:0007829|PDB:3FED"
FT HELIX 711..736
FT /evidence="ECO:0007829|PDB:3FED"
SQ SEQUENCE 740 AA; 83592 MW; 040624D691ECF879 CRC64;
MAESRGRLYL WMCLAAALAS FLMGFMVGWF IKPLKETTTS VRYHQSIRWK LVSEMKAENI
KSFLRSFTKL PHLAGTEQNF LLAKKIQTQW KKFGLDSAKL VHYDVLLSYP NETNANYISI
VDEHETEIFK TSYLEPPPDG YENVTNIVPP YNAFSAQGMP EGDLVYVNYA RTEDFFKLER
EMGINCTGKI VIARYGKIFR GNKVKNAMLA GAIGIILYSD PADYFAPEVQ PYPKGWNLPG
TAAQRGNVLN LNGAGDPLTP GYPAKEYTFR LDVEEGVGIP RIPVHPIGYN DAEILLRYLG
GIAPPDKSWK GALNVSYSIG PGFTGSDSFR KVRMHVYNIN KITRIYNVVG TIRGSVEPDR
YVILGGHRDS WVFGAIDPTS GVAVLQEIAR SFGKLMSKGW RPRRTIIFAS WDAEEFGLLG
STEWAEENVK ILQERSIAYI NSDSSIEGNY TLRVDCTPLL YQLVYKLTKE IPSPDDGFES
KSLYESWLEK DPSPENKNLP RINKLGSGSD FEAYFQRLGI ASGRARYTKN KKTDKYSSYP
VYHTIYETFE LVEKFYDPTF KKQLSVAQLR GALVYELVDS KIIPFNIQDY AEALKNYAAS
IYNLSKKHDQ QLTDHGVSFD SLFSAVKNFS EAASDFHKRL IQVDLNNPIA VRMMNDQLML
LERAFIDPLG LPGKLFYRHI IFAPSSHNKY AGESFPGIYD AIFDIENKAN SRLAWKEVKK
HISIAAFTIQ AAAGTLKEVL
