ASGL1_HUMAN
ID ASGL1_HUMAN Reviewed; 308 AA.
AC Q7L266; B2R7Q0; Q567Q4; Q6P1P0; Q8NI34; Q9H6F7;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Isoaspartyl peptidase/L-asparaginase;
DE EC=3.4.19.5 {ECO:0000269|PubMed:19839645};
DE EC=3.5.1.1 {ECO:0000269|PubMed:19839645, ECO:0000269|PubMed:22891768, ECO:0000269|PubMed:27106100};
DE AltName: Full=Asparaginase-like protein 1 {ECO:0000303|PubMed:19839645};
DE AltName: Full=Beta-aspartyl-peptidase {ECO:0000303|PubMed:19839645};
DE AltName: Full=Isoaspartyl dipeptidase;
DE AltName: Full=L-asparagine amidohydrolase;
DE Contains:
DE RecName: Full=Isoaspartyl peptidase/L-asparaginase alpha chain;
DE Contains:
DE RecName: Full=Isoaspartyl peptidase/L-asparaginase beta chain;
DE Flags: Precursor;
GN Name=ASRGL1; Synonyms=ALP, CRASH;
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), TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Testis;
RX PubMed=11984834; DOI=10.1002/mrd.10092;
RA Bush L.A., Herr J.C., Wolkowicz M., Sherman N.E., Shore A.,
RA Flickinger C.J.;
RT "A novel asparaginase-like protein is a sperm autoantigen in rats.";
RL Mol. Reprod. Dev. 62:233-247(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=14654938;
RA Evtimova V., Zeillinger R., Kaul S., Weidle U.H.;
RT "Identification of CRASH, a gene deregulated in gynecological tumors.";
RL Int. J. Oncol. 24:33-41(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Corpus callosum;
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].
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Eye, Lung, and Skin;
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 ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE,
RP MUTAGENESIS OF THR-168, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP AUTOCATALYTIC CLEAVAGE.
RX PubMed=19839645; DOI=10.1021/bi901397h;
RA Cantor J.R., Stone E.M., Chantranupong L., Georgiou G.;
RT "The human asparaginase-like protein 1 hASRGL1 is an Ntn hydrolase with
RT beta-aspartyl peptidase activity.";
RL Biochemistry 48:11026-11031(2009).
RN [8]
RP SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, VARIANT ARG-178,
RP CHARACTERIZATION OF VARIANT ARG-178, CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=27106100; DOI=10.1093/hmg/ddw113;
RA Biswas P., Chavali V.R., Agnello G., Stone E., Chakarova C., Duncan J.L.,
RA Kannabiran C., Homsher M., Bhattacharya S.S., Naeem M.A., Kimchi A.,
RA Sharon D., Iwata T., Riazuddin S., Reddy G.B., Hejtmancik J.F.,
RA Georgiou G., Riazuddin S.A., Ayyagari R.;
RT "A missense mutation in ASRGL1 is involved in causing autosomal recessive
RT retinal degeneration.";
RL Hum. Mol. Genet. 25:2483-2497(2016).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEXES WITH ASPARTATE, ACTIVE
RP SITE, SUBUNIT, ACTIVITY REGULATION, AND AUTOCATALYTIC CLEAVAGE.
RX PubMed=22861376; DOI=10.1021/bi300870g;
RA Nomme J., Su Y., Konrad M., Lavie A.;
RT "Structures of apo and product-bound human L-asparaginase: insights into
RT the mechanism of autoproteolysis and substrate hydrolysis.";
RL Biochemistry 51:6816-6826(2012).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), CATALYTIC ACTIVITY, MUTAGENESIS OF
RP THR-168, AND SUBUNIT.
RX PubMed=22891768; DOI=10.1021/cb300232n;
RA Li W., Cantor J.R., Yogesha S.D., Yang S., Chantranupong L., Liu J.Q.,
RA Agnello G., Georgiou G., Stone E.M., Zhang Y.;
RT "Uncoupling intramolecular processing and substrate hydrolysis in the N-
RT terminal nucleophile hydrolase hASRGL1 by circular permutation.";
RL ACS Chem. Biol. 7:1840-1847(2012).
CC -!- FUNCTION: Has both L-asparaginase and beta-aspartyl peptidase activity.
CC May be involved in the production of L-aspartate, which can act as an
CC excitatory neurotransmitter in some brain regions. Is highly active
CC with L-Asp beta-methyl ester. Besides, has catalytic activity toward
CC beta-aspartyl dipeptides and their methyl esters, including beta-L-Asp-
CC L-Phe, beta-L-Asp-L-Phe methyl ester (aspartame), beta-L-Asp-L-Ala,
CC beta-L-Asp-L-Leu and beta-L-Asp-L-Lys. Does not have
CC aspartylglucosaminidase activity and is inactive toward GlcNAc-L-Asn.
CC Likewise, has no activity toward glutamine.
CC {ECO:0000269|PubMed:19839645, ECO:0000269|PubMed:27106100}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-asparagine = L-aspartate + NH4(+);
CC Xref=Rhea:RHEA:21016, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29991, ChEBI:CHEBI:58048; EC=3.5.1.1;
CC Evidence={ECO:0000269|PubMed:19839645, ECO:0000269|PubMed:22891768,
CC ECO:0000269|PubMed:27106100};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of a beta-linked Asp residue from the N-terminus of a
CC polypeptide.; EC=3.4.19.5; Evidence={ECO:0000269|PubMed:19839645};
CC -!- ACTIVITY REGULATION: Glycine accelerates autocleavage into an alpha and
CC beta chain. {ECO:0000269|PubMed:22861376}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.4 mM for L-asparagine (L-Asn) {ECO:0000269|PubMed:19839645};
CC KM=0.4 mM for L-aspartic acid beta-methyl ester
CC {ECO:0000269|PubMed:19839645};
CC KM=0.4 mM for L-Asp-L-Phe {ECO:0000269|PubMed:19839645};
CC KM=1.0 mM for L-Asp-L-Ala {ECO:0000269|PubMed:19839645};
CC KM=0.1 mM for L-aspartic acid beta-hydroxamate
CC {ECO:0000269|PubMed:27106100};
CC -!- SUBUNIT: Heterodimer of an alpha and beta chain produced by
CC autocleavage. This heterodimer may then dimerize in turn, giving rise
CC to a heterotetramer. {ECO:0000269|PubMed:22861376,
CC ECO:0000269|PubMed:22891768}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11984834,
CC ECO:0000269|PubMed:27106100}. Note=Midpiece of sperm tail.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7L266-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7L266-2; Sequence=VSP_028287;
CC -!- TISSUE SPECIFICITY: Expressed in brain, kidney, testis and tissues of
CC the gastrointestinal tract. Present in sperm (at protein level). Over-
CC expressed in uterine, mammary, prostatic and ovarian carcinoma.
CC {ECO:0000269|PubMed:11984834, ECO:0000269|PubMed:14654938}.
CC -!- INDUCTION: By 5-alpha-di-hydrotestosterone and progesterone.
CC {ECO:0000269|PubMed:14654938}.
CC -!- PTM: Cleaved into an alpha and beta chain by autocatalysis; this
CC activates the enzyme. The N-terminal residue of the beta subunit is
CC responsible for the nucleophile hydrolase activity.
CC {ECO:0000269|PubMed:19839645, ECO:0000269|PubMed:22861376}.
CC -!- SIMILARITY: Belongs to the Ntn-hydrolase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15302.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB15302.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence.; Evidence={ECO:0000305};
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DR EMBL; AF411076; AAM28434.1; -; mRNA.
DR EMBL; AK025969; BAB15302.1; ALT_INIT; mRNA.
DR EMBL; AK091894; BAG52437.1; -; mRNA.
DR EMBL; AK313069; BAG35897.1; -; mRNA.
DR EMBL; CH471076; EAW74012.1; -; Genomic_DNA.
DR EMBL; BC021295; AAH21295.3; -; mRNA.
DR EMBL; BC064963; AAH64963.1; -; mRNA.
DR EMBL; BC093070; AAH93070.1; -; mRNA.
DR CCDS; CCDS8019.1; -. [Q7L266-1]
DR RefSeq; NP_001077395.1; NM_001083926.1. [Q7L266-1]
DR RefSeq; NP_079356.3; NM_025080.3. [Q7L266-1]
DR RefSeq; XP_005274362.1; XM_005274305.3. [Q7L266-2]
DR RefSeq; XP_005274363.1; XM_005274306.2. [Q7L266-2]
DR PDB; 3TKJ; X-ray; 2.30 A; A/B=2-308.
DR PDB; 4ET0; X-ray; 3.30 A; A/B=2-308.
DR PDB; 4O0C; X-ray; 1.50 A; A/B=1-308.
DR PDB; 4O0D; X-ray; 1.95 A; A/B=1-308.
DR PDB; 4O0E; X-ray; 1.71 A; A/B=1-308.
DR PDB; 4O0F; X-ray; 1.92 A; A/B=1-308.
DR PDB; 4O0G; X-ray; 2.10 A; A/B=1-308.
DR PDB; 4O0H; X-ray; 1.97 A; A/B=1-308.
DR PDB; 4OSX; X-ray; 1.95 A; A/B=1-308.
DR PDB; 4OSY; X-ray; 1.91 A; A/B=1-308.
DR PDB; 4PVP; X-ray; 1.85 A; A/B=1-308.
DR PDB; 4PVQ; X-ray; 2.13 A; A/B=1-308.
DR PDB; 4PVR; X-ray; 1.75 A; A/B=1-308.
DR PDB; 4PVS; X-ray; 1.84 A; A/B=1-308.
DR PDB; 4ZM9; X-ray; 2.51 A; A/B/C/D=2-308.
DR PDBsum; 3TKJ; -.
DR PDBsum; 4ET0; -.
DR PDBsum; 4O0C; -.
DR PDBsum; 4O0D; -.
DR PDBsum; 4O0E; -.
DR PDBsum; 4O0F; -.
DR PDBsum; 4O0G; -.
DR PDBsum; 4O0H; -.
DR PDBsum; 4OSX; -.
DR PDBsum; 4OSY; -.
DR PDBsum; 4PVP; -.
DR PDBsum; 4PVQ; -.
DR PDBsum; 4PVR; -.
DR PDBsum; 4PVS; -.
DR PDBsum; 4ZM9; -.
DR AlphaFoldDB; Q7L266; -.
DR SMR; Q7L266; -.
DR BioGRID; 123142; 18.
DR IntAct; Q7L266; 7.
DR MINT; Q7L266; -.
DR STRING; 9606.ENSP00000400057; -.
DR DrugBank; DB00174; Asparagine.
DR DrugBank; DB00128; Aspartic acid.
DR MEROPS; T02.002; -.
DR iPTMnet; Q7L266; -.
DR PhosphoSitePlus; Q7L266; -.
DR BioMuta; ASRGL1; -.
DR DMDM; 158706477; -.
DR UCD-2DPAGE; Q7L266; -.
DR EPD; Q7L266; -.
DR jPOST; Q7L266; -.
DR MassIVE; Q7L266; -.
DR MaxQB; Q7L266; -.
DR PaxDb; Q7L266; -.
DR PeptideAtlas; Q7L266; -.
DR PRIDE; Q7L266; -.
DR ProteomicsDB; 68755; -. [Q7L266-1]
DR ProteomicsDB; 68756; -. [Q7L266-2]
DR Antibodypedia; 14797; 273 antibodies from 33 providers.
DR DNASU; 80150; -.
DR Ensembl; ENST00000301776.9; ENSP00000301776.5; ENSG00000162174.12. [Q7L266-1]
DR Ensembl; ENST00000415229.6; ENSP00000400057.2; ENSG00000162174.12. [Q7L266-1]
DR GeneID; 80150; -.
DR KEGG; hsa:80150; -.
DR MANE-Select; ENST00000415229.6; ENSP00000400057.2; NM_001083926.2; NP_001077395.1.
DR UCSC; uc001nte.5; human. [Q7L266-1]
DR CTD; 80150; -.
DR DisGeNET; 80150; -.
DR GeneCards; ASRGL1; -.
DR HGNC; HGNC:16448; ASRGL1.
DR HPA; ENSG00000162174; Tissue enhanced (brain, cervix, testis).
DR MIM; 609212; gene.
DR neXtProt; NX_Q7L266; -.
DR OpenTargets; ENSG00000162174; -.
DR PharmGKB; PA25059; -.
DR VEuPathDB; HostDB:ENSG00000162174; -.
DR eggNOG; KOG1592; Eukaryota.
DR GeneTree; ENSGT00950000183045; -.
DR HOGENOM; CLU_021603_1_2_1; -.
DR InParanoid; Q7L266; -.
DR OMA; YSRMRWK; -.
DR PhylomeDB; Q7L266; -.
DR TreeFam; TF323960; -.
DR BioCyc; MetaCyc:HS08648-MON; -.
DR BRENDA; 3.4.19.5; 2681.
DR BRENDA; 3.5.1.1; 2681.
DR PathwayCommons; Q7L266; -.
DR Reactome; R-HSA-8964208; Phenylalanine metabolism.
DR SignaLink; Q7L266; -.
DR BioGRID-ORCS; 80150; 18 hits in 1088 CRISPR screens.
DR ChiTaRS; ASRGL1; human.
DR GeneWiki; ASRGL1; -.
DR GenomeRNAi; 80150; -.
DR Pharos; Q7L266; Tbio.
DR PRO; PR:Q7L266; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q7L266; protein.
DR Bgee; ENSG00000162174; Expressed in sperm and 166 other tissues.
DR ExpressionAtlas; Q7L266; baseline and differential.
DR Genevisible; Q7L266; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0001917; C:photoreceptor inner segment; ISS:UniProtKB.
DR GO; GO:0004067; F:asparaginase activity; IDA:UniProtKB.
DR GO; GO:0008798; F:beta-aspartyl-peptidase activity; IDA:UniProtKB.
DR GO; GO:0033345; P:asparagine catabolic process via L-aspartate; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04702; ASRGL1_like; 1.
DR InterPro; IPR033844; ASRGL1_meta.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR000246; Peptidase_T2.
DR PANTHER; PTHR10188; PTHR10188; 1.
DR Pfam; PF01112; Asparaginase_2; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Autocatalytic cleavage;
KW Cytoplasm; Hydrolase; Protease; Reference proteome.
FT CHAIN 1..167
FT /note="Isoaspartyl peptidase/L-asparaginase alpha chain"
FT /id="PRO_0000305204"
FT CHAIN 168..308
FT /note="Isoaspartyl peptidase/L-asparaginase beta chain"
FT /id="PRO_0000420556"
FT ACT_SITE 168
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:19839645,
FT ECO:0000269|PubMed:22861376"
FT BINDING 196..199
FT /ligand="substrate"
FT BINDING 219..222
FT /ligand="substrate"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT VAR_SEQ 1..128
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028287"
FT VARIANT 178
FT /note="G -> R (found in a large family with early-onset
FT recessive retinal degeneration; abolishes autocleavage
FT resulting in loss of enzymatic activity; increased protein
FT aggregation; changes protein localization that becomes
FT perinuclear, does not change ligand affinity for L-aspartic
FT acid beta-hydroxamate)"
FT /evidence="ECO:0000269|PubMed:27106100"
FT /id="VAR_081118"
FT MUTAGEN 168
FT /note="T->A,C: Abolishes activation by autocleavage.
FT Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:19839645,
FT ECO:0000269|PubMed:22891768"
FT MUTAGEN 168
FT /note="T->S: Strongly reduced enzyme activity."
FT /evidence="ECO:0000269|PubMed:19839645,
FT ECO:0000269|PubMed:22891768"
FT CONFLICT 181
FT /note="A -> T (in Ref. 1; AAM28434)"
FT /evidence="ECO:0000305"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:4O0C"
FT HELIX 17..38
FT /evidence="ECO:0007829|PDB:4O0C"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:4O0C"
FT HELIX 44..57
FT /evidence="ECO:0007829|PDB:4O0C"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:4O0C"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:4O0H"
FT STRAND 77..83
FT /evidence="ECO:0007829|PDB:4O0C"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:4O0C"
FT STRAND 89..95
FT /evidence="ECO:0007829|PDB:4O0C"
FT HELIX 101..111
FT /evidence="ECO:0007829|PDB:4O0C"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:4O0C"
FT HELIX 119..128
FT /evidence="ECO:0007829|PDB:4O0C"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:4O0C"
FT HELIX 142..152
FT /evidence="ECO:0007829|PDB:4O0C"
FT STRAND 169..174
FT /evidence="ECO:0007829|PDB:4O0C"
FT STRAND 180..186
FT /evidence="ECO:0007829|PDB:4O0C"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:4O0C"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:4O0C"
FT TURN 211..213
FT /evidence="ECO:0007829|PDB:4O0C"
FT STRAND 214..220
FT /evidence="ECO:0007829|PDB:4O0C"
FT HELIX 222..228
FT /evidence="ECO:0007829|PDB:4O0C"
FT HELIX 230..239
FT /evidence="ECO:0007829|PDB:4O0C"
FT HELIX 244..259
FT /evidence="ECO:0007829|PDB:4O0C"
FT STRAND 263..269
FT /evidence="ECO:0007829|PDB:4O0C"
FT STRAND 274..282
FT /evidence="ECO:0007829|PDB:4O0C"
FT STRAND 285..289
FT /evidence="ECO:0007829|PDB:4O0C"
FT STRAND 292..298
FT /evidence="ECO:0007829|PDB:4O0C"
FT STRAND 303..306
FT /evidence="ECO:0007829|PDB:4O0C"
SQ SEQUENCE 308 AA; 32055 MW; 84E3D6C2D1555B32 CRC64;
MNPIVVVHGG GAGPISKDRK ERVHQGMVRA ATVGYGILRE GGSAVDAVEG AVVALEDDPE
FNAGCGSVLN TNGEVEMDAS IMDGKDLSAG AVSAVQCIAN PIKLARLVME KTPHCFLTDQ
GAAQFAAAMG VPEIPGEKLV TERNKKRLEK EKHEKGAQKT DCQKNLGTVG AVALDCKGNV
AYATSTGGIV NKMVGRVGDS PCLGAGGYAD NDIGAVSTTG HGESILKVNL ARLTLFHIEQ
GKTVEEAADL SLGYMKSRVK GLGGLIVVSK TGDWVAKWTS TSMPWAAAKD GKLHFGIDPD
DTTITDLP
