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Database: UniProt
Entry: M7ASG2_CHEMY
LinkDB: M7ASG2_CHEMY
Original site: M7ASG2_CHEMY 
ID   M7ASG2_CHEMY            Unreviewed;       641 AA.
AC   M7ASG2;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase {ECO:0000256|ARBA:ARBA00018546};
DE            EC=3.5.1.52 {ECO:0000256|ARBA:ARBA00012158};
DE   AltName: Full=N-glycanase 1 {ECO:0000256|ARBA:ARBA00029604};
DE   AltName: Full=Peptide:N-glycanase {ECO:0000256|ARBA:ARBA00032901};
DE   Flags: Fragment;
GN   ORFNames=UY3_15302 {ECO:0000313|EMBL:EMP27614.1};
OS   Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX   NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP27614.1, ECO:0000313|Proteomes:UP000031443};
RN   [1] {ECO:0000313|Proteomes:UP000031443}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23624526; DOI=10.1038/ng.2615;
RA   Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA   White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA   Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA   Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA   Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT   "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT   into the development and evolution of the turtle-specific body plan.";
RL   Nat. Genet. 45:701-706(2013).
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:0000256|ARBA:ARBA00024870}.
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         Evidence={ECO:0000256|ARBA:ARBA00001650};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the transglutaminase-like superfamily. PNGase
CC       family. {ECO:0000256|ARBA:ARBA00009390, ECO:0000256|PROSITE-
CC       ProRule:PRU00731}.
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DR   EMBL; KB568670; EMP27614.1; -; Genomic_DNA.
DR   AlphaFoldDB; M7ASG2; -.
DR   STRING; 8469.M7ASG2; -.
DR   eggNOG; KOG0909; Eukaryota.
DR   Proteomes; UP000031443; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000224; F:peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006516; P:glycoprotein catabolic process; IEA:InterPro.
DR   CDD; cd10459; PUB_PNGase; 1.
DR   Gene3D; 1.20.58.2190; -; 1.
DR   Gene3D; 2.20.25.10; -; 1.
DR   Gene3D; 3.10.620.30; -; 1.
DR   Gene3D; 2.60.120.1020; Peptide N glycanase, PAW domain; 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   PANTHER; PTHR12143; PEPTIDE N-GLYCANASE PNGASE -RELATED; 1.
DR   PANTHER; PTHR12143:SF19; PEPTIDE-N(4)-(N-ACETYL-BETA-GLUCOSAMINYL)ASPARAGINE AMIDASE; 1.
DR   Pfam; PF04721; PAW; 1.
DR   Pfam; PF09409; PUB; 1.
DR   Pfam; PF01841; Transglut_core; 1.
DR   SMART; SM00613; PAW; 1.
DR   SMART; SM00580; PUG; 1.
DR   SMART; SM00460; TGc; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF143503; PUG domain-like; 1.
DR   PROSITE; PS51398; PAW; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          445..641
FT                   /note="PAW"
FT                   /evidence="ECO:0000259|PROSITE:PS51398"
FT   REGION          103..124
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..124
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EMP27614.1"
FT   NON_TER         641
FT                   /evidence="ECO:0000313|EMBL:EMP27614.1"
SQ   SEQUENCE   641 AA;  73551 MW;  4C322083C3299BE6 CRC64;
     GPSPPPRSRA VSELCQNARD TFLEASRLLL TYADNILRHP NEEKYRSIRI GNPAFSTRLL
     PVRGAVECLF EMGFEEGETH LVFPKEASIE QLHKIRDLIA GERNSRLSES SQTQRSGSSQ
     TVTNMQHIVP QSSRAADSTL IPVNRQLQTS AAQSAEMESE TIFFKTLQSN FQHVQVYENQ
     SLQKKALASI PVQALKEKAQ EKLAQAKKVD EGTHVNEDDF LLLELLQWFK GEFFQWVNNL
     ACSKCGGQTE PKGLLSPNDE DLRWNANRVE NHHCNQCQFS NRFPRYNNPE KLLETRRGRC
     GEWANCFTLC CRAIGFEARY VWDSTDHVWT EVYSSSQQRW LHCDPCETVC DKPLLYEIGW
     GKKLSYVIAF SKDEVVDVTW RYSCKHEELL SRRTQVKEAA LRETIERLNK LRQQSLSESR
     KRVLLERIIV ELVEFISPKT PKPGELGGRI SGSKAWRVAR GEIGSERRKE VIFIPSGKEK
     TSKLFHLTYN IVEDCYTRLS NNNEKITGWE EGVWKTESLW RKVETDWKMV YLARKEGSSS
     SYICWKFECG SVGLKIDNIS IRTNSQTFHS GRIRWRLRSN IAQVDLTGDK ILRSYSDFSD
     ATEVILEAEL SGGDGDIAWQ HTQLFRESLS NSGENCLEII I
//
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