NGLY1_MOUSE
ID NGLY1_MOUSE Reviewed; 651 AA.
AC Q9JI78; Q8K113; Q9CTK3;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase;
DE Short=PNGase;
DE Short=mPNGase;
DE EC=3.5.1.52;
DE AltName: Full=N-glycanase 1;
DE AltName: Full=Peptide:N-glycanase;
GN Name=Ngly1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10831608; DOI=10.1083/jcb.149.5.1039;
RA Suzuki T., Park H., Hollingsworth N.M., Sternglanz R., Lennarz W.J.;
RT "PNG1, a yeast gene encoding a highly conserved peptide:N-glycanase.";
RL J. Cell Biol. 149:1039-1052(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=129/SvJ;
RX PubMed=12711318; DOI=10.1016/s0006-291x(03)00600-4;
RA Suzuki T., Kwofie M.A., Lennarz W.J.;
RT "Ngly1, a mouse gene encoding a deglycosylating enzyme implicated in
RT proteasomal degradation: expression, genomic organization, and chromosomal
RT mapping.";
RL Biochem. Biophys. Res. Commun. 304:326-332(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=8021270; DOI=10.1016/s0021-9258(17)32485-7;
RA Suzuki T., Seko A., Kitajima K., Inoue Y., Inoue S.;
RT "Purification and enzymatic properties of peptide:N-glycanase from C3H
RT mouse-derived L-929 fibroblast cells. Possible widespread occurrence of
RT post-translational remodification of proteins by N-deglycosylation.";
RL J. Biol. Chem. 269:17611-17618(1994).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH
RP RAD23B; PSMC1 AND SAKS1.
RX PubMed=11562482; DOI=10.1073/pnas.201393498;
RA Park H., Suzuki T., Lennarz W.J.;
RT "Identification of proteins that interact with mammalian peptide:N-
RT glycanase and implicate this hydrolase in the proteasome-dependent pathway
RT for protein degradation.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:11163-11168(2001).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-306.
RX PubMed=12606569; DOI=10.1093/emboj/cdg107;
RA Hirsch C., Blom D., Ploegh H.L.;
RT "A role for N-glycanase in the cytosolic turnover of glycoproteins.";
RL EMBO J. 22:1036-1046(2003).
RN [8]
RP ACTIVITY REGULATION.
RX PubMed=15610852; DOI=10.1016/j.chembiol.2004.11.010;
RA Misaghi S., Pacold M.E., Blom D., Ploegh H.L., Korbel G.A.;
RT "Using a small molecule inhibitor of peptide: N-glycanase to probe its role
RT in glycoprotein turnover.";
RL Chem. Biol. 11:1677-1687(2004).
RN [9]
RP FUNCTION, AND INTERACTION WITH RAD23B AND PSMC1.
RX PubMed=15358861; DOI=10.1073/pnas.0405663101;
RA Katiyar S., Li G., Lennarz W.J.;
RT "A complex between peptide:N-glycanase and two proteasome-linked proteins
RT suggests a mechanism for the degradation of misfolded glycoproteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13774-13779(2004).
RN [10]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH DERL1.
RX PubMed=16055502; DOI=10.1091/mbc.e05-04-0345;
RA Katiyar S., Joshi S., Lennarz W.J.;
RT "The retrotranslocation protein derlin-1 binds peptide:N-glycanase to the
RT endoplasmic reticulum.";
RL Mol. Biol. Cell 16:4584-4594(2005).
RN [11]
RP INTERACTION WITH PSMC1; RAD23B AND VCP.
RX PubMed=16249333; DOI=10.1073/pnas.0507155102;
RA Li G., Zhou X., Zhao G., Schindelin H., Lennarz W.J.;
RT "Multiple modes of interaction of the deglycosylation enzyme, mouse peptide
RT N-glycanase, with the proteasome.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:15809-15814(2005).
RN [12]
RP ERRATUM OF PUBMED:16249333.
RA Li G., Zhou X., Zhao G., Schindelin H., Lennarz W.J.;
RL Proc. Natl. Acad. Sci. U.S.A. 103:1153-1153(2006).
RN [13]
RP INTERACTION WITH AMFR; PSMC1; SAKS1; RAD23B AND VCP, DOMAIN, AND
RP MUTAGENESIS OF ASN-41; ASN-58 AND 79-GLY-PHE-80.
RX PubMed=16709668; DOI=10.1073/pnas.0602747103;
RA Li G., Zhao G., Zhou X., Schindelin H., Lennarz W.J.;
RT "The AAA ATPase p97 links peptide N-glycanase to the endoplasmic reticulum-
RT associated E3 ligase autocrine motility factor receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:8348-8353(2006).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 164-450 IN COMPLEX WITH RAD23 AND
RP Z-VAD-FMK, COFACTOR, AND ZINC-BINDING.
RX PubMed=16500903; DOI=10.1074/jbc.m600137200;
RA Zhao G., Zhou X., Wang L., Li G., Kisker C., Lennarz W.J., Schindelin H.;
RT "Structure of the mouse peptide N-glycanase-HR23 complex suggests co-
RT evolution of the endoplasmic reticulum-associated degradation and DNA
RT repair pathways.";
RL J. Biol. Chem. 281:13751-13761(2006).
CC -!- FUNCTION: Specifically deglycosylates the denatured form of N-linked
CC glycoproteins in the cytoplasm and assists their proteasome-mediated
CC degradation. Cleaves the beta-aspartyl-glucosamine (GlcNAc) of the
CC glycan and the amide side chain of Asn, converting Asn to Asp. Prefers
CC proteins containing high-mannose over those bearing complex type
CC oligosaccharides. Can recognize misfolded proteins in the endoplasmic
CC reticulum that are exported to the cytosol to be destroyed and
CC deglycosylate them, while it has no activity toward native proteins.
CC Deglycosylation is a prerequisite for subsequent proteasome-mediated
CC degradation of some, but not all, misfolded glycoproteins.
CC {ECO:0000269|PubMed:11562482, ECO:0000269|PubMed:12606569,
CC ECO:0000269|PubMed:15358861}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of an N(4)-(acetyl-beta-D-glucosaminyl)asparagine
CC residue in which the glucosamine residue may be further glycosylated,
CC to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a
CC peptide containing an aspartate residue.; EC=3.5.1.52;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:16500903};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:16500903};
CC -!- ACTIVITY REGULATION: Inhibited by Z-VAD-fmk, a well-known caspase
CC inhibitor, which inhibits enzyme activity through covalent binding of
CC the carbohydrate to the single Cys-306 residue.
CC {ECO:0000269|PubMed:15610852}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=114 uM for fetuin glycopeptide I {ECO:0000269|PubMed:8021270};
CC Vmax=0.0964 nmol/min/mg enzyme with fetuin glycopeptide I as
CC substrate {ECO:0000269|PubMed:8021270};
CC -!- SUBUNIT: Component of a complex required to couple retrotranslocation,
CC ubiquitination and deglycosylation composed of NGLY1, SAKS1, AMFR, VCP
CC and RAD23B. Interacts with the proteasome components RAD23B and PSMC1.
CC Interacts with directly with VCP. Interacts with DERL1, bringing it
CC close to the endoplasmic reticulum membrane. Interacts with SAKS1.
CC {ECO:0000269|PubMed:11562482, ECO:0000269|PubMed:15358861,
CC ECO:0000269|PubMed:16055502, ECO:0000269|PubMed:16249333,
CC ECO:0000269|PubMed:16500903, ECO:0000269|PubMed:16709668}.
CC -!- INTERACTION:
CC Q9JI78; Q9R049: Amfr; NbExp=5; IntAct=EBI-3648128, EBI-3648125;
CC Q9JI78; Q01853: Vcp; NbExp=9; IntAct=EBI-3648128, EBI-80597;
CC Q9JI78; P54725: RAD23A; Xeno; NbExp=2; IntAct=EBI-3648128, EBI-746453;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11562482,
CC ECO:0000269|PubMed:12606569, ECO:0000269|PubMed:16055502}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with highest level in
CC testis. {ECO:0000269|PubMed:11562482, ECO:0000269|PubMed:12711318}.
CC -!- DOMAIN: The PUB domain mediates the interaction with VCP.
CC {ECO:0000269|PubMed:16709668}.
CC -!- SIMILARITY: Belongs to the transglutaminase-like superfamily. PNGase
CC family. {ECO:0000255|PROSITE-ProRule:PRU00731}.
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DR EMBL; AF250927; AAF74723.1; -; mRNA.
DR EMBL; AY225417; AAP03060.1; -; Genomic_DNA.
DR EMBL; AK003279; BAB22686.1; -; mRNA.
DR EMBL; AK028248; BAC25839.1; -; mRNA.
DR EMBL; BC028961; AAH28961.1; -; mRNA.
DR CCDS; CCDS26832.1; -.
DR RefSeq; NP_067479.2; NM_021504.3.
DR PDB; 2D5U; NMR; -; A=1-119.
DR PDB; 2F4M; X-ray; 1.85 A; A=164-450.
DR PDB; 2F4O; X-ray; 2.26 A; A=164-450.
DR PDB; 2G9F; X-ray; 1.90 A; A=451-651.
DR PDB; 2G9G; X-ray; 2.00 A; A=451-651.
DR PDB; 2HPJ; X-ray; 1.70 A; A=12-110.
DR PDB; 2HPL; X-ray; 1.80 A; A=12-111.
DR PDB; 2I74; X-ray; 1.75 A; A/B=471-651.
DR PDBsum; 2D5U; -.
DR PDBsum; 2F4M; -.
DR PDBsum; 2F4O; -.
DR PDBsum; 2G9F; -.
DR PDBsum; 2G9G; -.
DR PDBsum; 2HPJ; -.
DR PDBsum; 2HPL; -.
DR PDBsum; 2I74; -.
DR AlphaFoldDB; Q9JI78; -.
DR SMR; Q9JI78; -.
DR BioGRID; 208478; 13.
DR CORUM; Q9JI78; -.
DR DIP; DIP-41155N; -.
DR IntAct; Q9JI78; 9.
DR MINT; Q9JI78; -.
DR STRING; 10090.ENSMUSP00000022310; -.
DR iPTMnet; Q9JI78; -.
DR PhosphoSitePlus; Q9JI78; -.
DR EPD; Q9JI78; -.
DR MaxQB; Q9JI78; -.
DR PaxDb; Q9JI78; -.
DR PeptideAtlas; Q9JI78; -.
DR PRIDE; Q9JI78; -.
DR ProteomicsDB; 252834; -.
DR Antibodypedia; 27393; 52 antibodies from 16 providers.
DR DNASU; 59007; -.
DR Ensembl; ENSMUST00000022310; ENSMUSP00000022310; ENSMUSG00000021785.
DR GeneID; 59007; -.
DR KEGG; mmu:59007; -.
DR UCSC; uc007sgz.1; mouse.
DR CTD; 55768; -.
DR MGI; MGI:1913276; Ngly1.
DR VEuPathDB; HostDB:ENSMUSG00000021785; -.
DR eggNOG; KOG0909; Eukaryota.
DR GeneTree; ENSGT00390000006540; -.
DR HOGENOM; CLU_030187_1_0_1; -.
DR InParanoid; Q9JI78; -.
DR OMA; IKPSVEY; -.
DR OrthoDB; 917526at2759; -.
DR PhylomeDB; Q9JI78; -.
DR TreeFam; TF315254; -.
DR BRENDA; 3.5.1.52; 3474.
DR Reactome; R-MMU-532668; N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
DR SABIO-RK; Q9JI78; -.
DR BioGRID-ORCS; 59007; 6 hits in 72 CRISPR screens.
DR ChiTaRS; Ngly1; mouse.
DR EvolutionaryTrace; Q9JI78; -.
DR PRO; PR:Q9JI78; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9JI78; protein.
DR Bgee; ENSMUSG00000021785; Expressed in interventricular septum and 256 other tissues.
DR ExpressionAtlas; Q9JI78; baseline and differential.
DR Genevisible; Q9JI78; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000224; F:peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase activity; ISS:MGI.
DR GO; GO:0071712; P:ER-associated misfolded protein catabolic process; ISO:MGI.
DR GO; GO:0006516; P:glycoprotein catabolic process; IDA:UniProtKB.
DR GO; GO:0006517; P:protein deglycosylation; ISO:MGI.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IBA:GO_Central.
DR Gene3D; 2.60.120.1020; -; 1.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR038680; PAW_sf.
DR InterPro; IPR006588; Peptide_N_glycanase_PAW_dom.
DR InterPro; IPR036339; PUB-like_dom_sf.
DR InterPro; IPR018997; PUB_domain.
DR InterPro; IPR002931; Transglutaminase-like.
DR Pfam; PF04721; PAW; 1.
DR Pfam; PF09409; PUB; 1.
DR Pfam; PF01841; Transglut_core; 1.
DR SMART; SM00613; PAW; 1.
DR SMART; SM00460; TGc; 1.
DR SUPFAM; SSF143503; SSF143503; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS51398; PAW; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Hydrolase; Metal-binding;
KW Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q96IV0"
FT CHAIN 2..651
FT /note="Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine
FT amidase"
FT /id="PRO_0000248973"
FT DOMAIN 30..91
FT /note="PUB"
FT DOMAIN 451..651
FT /note="PAW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00731"
FT ACT_SITE 306
FT /note="Nucleophile"
FT ACT_SITE 333
FT ACT_SITE 350
FT BINDING 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 250
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 280
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 283
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q96IV0"
FT MUTAGEN 41
FT /note="N->P: Abolishes interaction with VCP."
FT /evidence="ECO:0000269|PubMed:16709668"
FT MUTAGEN 58
FT /note="N->A: Does not affect the interaction with VCP."
FT /evidence="ECO:0000269|PubMed:16709668"
FT MUTAGEN 79..80
FT /note="GF->AA: Abolishes interaction with VCP."
FT /evidence="ECO:0000269|PubMed:16709668"
FT MUTAGEN 306
FT /note="C->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:12606569"
FT CONFLICT 509
FT /note="I -> T (in Ref. 1; AAF74723 and 2; AAP03060)"
FT /evidence="ECO:0000305"
FT HELIX 15..20
FT /evidence="ECO:0007829|PDB:2HPJ"
FT HELIX 25..43
FT /evidence="ECO:0007829|PDB:2HPJ"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:2D5U"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:2HPJ"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:2HPJ"
FT HELIX 59..64
FT /evidence="ECO:0007829|PDB:2HPJ"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:2HPJ"
FT HELIX 71..78
FT /evidence="ECO:0007829|PDB:2HPJ"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:2HPJ"
FT HELIX 95..109
FT /evidence="ECO:0007829|PDB:2HPJ"
FT HELIX 167..180
FT /evidence="ECO:0007829|PDB:2F4M"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:2F4M"
FT HELIX 185..194
FT /evidence="ECO:0007829|PDB:2F4M"
FT HELIX 197..211
FT /evidence="ECO:0007829|PDB:2F4M"
FT HELIX 223..236
FT /evidence="ECO:0007829|PDB:2F4M"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:2F4M"
FT STRAND 255..261
FT /evidence="ECO:0007829|PDB:2F4O"
FT HELIX 266..269
FT /evidence="ECO:0007829|PDB:2F4M"
FT STRAND 275..280
FT /evidence="ECO:0007829|PDB:2F4M"
FT TURN 281..284
FT /evidence="ECO:0007829|PDB:2F4M"
FT STRAND 285..290
FT /evidence="ECO:0007829|PDB:2F4M"
FT HELIX 295..301
FT /evidence="ECO:0007829|PDB:2F4M"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:2F4M"
FT HELIX 306..319
FT /evidence="ECO:0007829|PDB:2F4M"
FT STRAND 324..329
FT /evidence="ECO:0007829|PDB:2F4M"
FT TURN 330..332
FT /evidence="ECO:0007829|PDB:2F4M"
FT STRAND 333..340
FT /evidence="ECO:0007829|PDB:2F4M"
FT TURN 341..344
FT /evidence="ECO:0007829|PDB:2F4M"
FT STRAND 345..350
FT /evidence="ECO:0007829|PDB:2F4M"
FT TURN 351..354
FT /evidence="ECO:0007829|PDB:2F4M"
FT STRAND 355..357
FT /evidence="ECO:0007829|PDB:2F4M"
FT HELIX 359..361
FT /evidence="ECO:0007829|PDB:2F4M"
FT TURN 362..365
FT /evidence="ECO:0007829|PDB:2F4M"
FT STRAND 373..376
FT /evidence="ECO:0007829|PDB:2F4M"
FT STRAND 381..383
FT /evidence="ECO:0007829|PDB:2F4M"
FT HELIX 385..388
FT /evidence="ECO:0007829|PDB:2F4M"
FT HELIX 392..398
FT /evidence="ECO:0007829|PDB:2F4M"
FT HELIX 404..419
FT /evidence="ECO:0007829|PDB:2F4M"
FT HELIX 424..441
FT /evidence="ECO:0007829|PDB:2F4M"
FT STRAND 458..462
FT /evidence="ECO:0007829|PDB:2G9G"
FT HELIX 482..487
FT /evidence="ECO:0007829|PDB:2I74"
FT STRAND 489..495
FT /evidence="ECO:0007829|PDB:2I74"
FT TURN 496..499
FT /evidence="ECO:0007829|PDB:2I74"
FT STRAND 500..503
FT /evidence="ECO:0007829|PDB:2I74"
FT HELIX 504..506
FT /evidence="ECO:0007829|PDB:2G9F"
FT STRAND 509..513
FT /evidence="ECO:0007829|PDB:2I74"
FT HELIX 514..517
FT /evidence="ECO:0007829|PDB:2I74"
FT STRAND 519..529
FT /evidence="ECO:0007829|PDB:2I74"
FT TURN 530..533
FT /evidence="ECO:0007829|PDB:2I74"
FT STRAND 534..539
FT /evidence="ECO:0007829|PDB:2I74"
FT STRAND 544..553
FT /evidence="ECO:0007829|PDB:2I74"
FT HELIX 555..557
FT /evidence="ECO:0007829|PDB:2I74"
FT STRAND 559..567
FT /evidence="ECO:0007829|PDB:2I74"
FT STRAND 569..572
FT /evidence="ECO:0007829|PDB:2I74"
FT STRAND 577..583
FT /evidence="ECO:0007829|PDB:2I74"
FT STRAND 588..591
FT /evidence="ECO:0007829|PDB:2I74"
FT STRAND 598..600
FT /evidence="ECO:0007829|PDB:2I74"
FT TURN 602..605
FT /evidence="ECO:0007829|PDB:2I74"
FT STRAND 607..616
FT /evidence="ECO:0007829|PDB:2I74"
FT HELIX 620..625
FT /evidence="ECO:0007829|PDB:2I74"
FT STRAND 626..633
FT /evidence="ECO:0007829|PDB:2I74"
FT STRAND 641..650
FT /evidence="ECO:0007829|PDB:2I74"
SQ SEQUENCE 651 AA; 74275 MW; F9D7A35726482F81 CRC64;
MASATLGSSS SSASPAVAEL CQNTPETFLE ASKLLLTYAD NILRNPSDEK YRSIRIGNTA
FSTRLLPVRG AVECLFEMGF EEGETHLIFP KKASVEQLQK IRDLIAIERS SRLDGSSKKV
QFSQHPAAAK LPLEQSEDPA GLIRHSGNQT GQLPSLPSAP MVVGDSTILK VLQSNIQHVQ
LYENPVLQEK ALTCIPVSEL KRKAQEKLFR ARKLDKGTNV SDEDFLLLEL LHWFKEEFFR
WVNNIVCSKC GGETRSRDEA LLPNDDELKW GAKNVENHYC DACQLSNRFP RYNNPEKLLE
TRCGRCGEWA NCFTLCCRAL GFEARYVWDY TDHVWTEVYS PSQQRWLHCD ACEDVCDKPL
LYEIGWGKKL SYIIAFSKDE VVDVTWRYSC KHDEVMSRRT KVKEELLRET INGLNKQRQL
SLSESRRKEL LQRIIVELVE FISPKTPRPG ELGGRVSGSL AWRVARGETG LERKEILFIP
SENEKISKQF HLRYDIVRDR YIRVSDNNIN ISGWENGVWK MESIFRKVEK DWNMVYLARK
EGSSFAYISW KFECGSAGLK VDTVSIRTSS QSFESGSVRW KLRSETAQVN LLGDKNLRSY
NDFSGATEVT LEAELSRGDG DVAWQHTQLF RQSLNDSGEN GLEIIITFND L
