NGLY1_HUMAN
ID NGLY1_HUMAN Reviewed; 654 AA.
AC Q96IV0; B4DJE9; Q59FB1; Q6PJD8; Q9BVR8; Q9NR70;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase;
DE Short=PNGase;
DE Short=hPNGase;
DE EC=3.5.1.52;
DE AltName: Full=N-glycanase 1;
DE AltName: Full=Peptide:N-glycanase;
GN Name=NGLY1; Synonyms=PNG1;
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).
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 [LARGE SCALE MRNA] (ISOFORM 5).
RC TISSUE=Subthalamic nucleus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 4-654 (ISOFORM 2).
RC TISSUE=Lymph, Placenta, and Uterus;
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 INTERACTION WITH VCP.
RX PubMed=15362974; DOI=10.1042/bj20041498;
RA McNeill H., Knebel A., Arthur J.S., Cuenda A., Cohen P.;
RT "A novel UBA and UBX domain protein that binds polyubiquitin and VCP and is
RT a substrate for SAPKs.";
RL Biochem. J. 384:391-400(2004).
RN [7]
RP FUNCTION.
RX PubMed=14749736; DOI=10.1038/sj.emboj.7600090;
RA Blom D., Hirsch C., Stern P., Tortorella D., Ploegh H.L.;
RT "A glycosylated type I membrane protein becomes cytosolic when peptide: N-
RT glycanase is compromised.";
RL EMBO J. 23:650-658(2004).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, 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 [9]
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 [10]
RP 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 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [12]
RP INVOLVEMENT IN CDDG1.
RX PubMed=22581936; DOI=10.1136/jmedgenet-2012-100819;
RA Need A.C., Shashi V., Hitomi Y., Schoch K., Shianna K.V., McDonald M.T.,
RA Meisler M.H., Goldstein D.B.;
RT "Clinical application of exome sequencing in undiagnosed genetic
RT conditions.";
RL J. Med. Genet. 49:353-361(2012).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-137, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP INVOLVEMENT IN CDDG1.
RX PubMed=24651605; DOI=10.1038/gim.2014.22;
RA Enns G.M., Shashi V., Bainbridge M., Gambello M.J., Zahir F.R., Bast T.,
RA Crimian R., Schoch K., Platt J., Cox R., Bernstein J.A., Scavina M.,
RA Walter R.S., Bibb A., Jones M., Hegde M., Graham B.H., Need A.C.,
RA Oviedo A., Schaaf C.P., Boyle S., Butte A.J., Chen R., Clark M.J.,
RA Haraksingh R., Cowan T.M., He P., Langlois S., Zoghbi H.Y., Snyder M.,
RA Gibbs R.A., Freeze H.H., Goldstein D.B.;
RT "Mutations in NGLY1 cause an inherited disorder of the endoplasmic
RT reticulum-associated degradation pathway.";
RL Genet. Med. 16:751-758(2014).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 11-109 IN COMPLEX WITH VCP, AND
RP DOMAIN.
RX PubMed=16807242; DOI=10.1074/jbc.m601173200;
RA Allen M.D., Buchberger A., Bycroft M.;
RT "The PUB domain functions as a p97 binding module in human peptide N-
RT glycanase.";
RL J. Biol. Chem. 281:25502-25508(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:14749736, 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; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
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 -!- 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:15358861, ECO:0000269|PubMed:15362974,
CC ECO:0000269|PubMed:16055502, ECO:0000269|PubMed:16807242}.
CC -!- INTERACTION:
CC Q96IV0; Q6AI39: BICRAL; NbExp=3; IntAct=EBI-6165879, EBI-1012434;
CC Q96IV0; Q96NT3: GUCD1; NbExp=4; IntAct=EBI-6165879, EBI-8293751;
CC Q96IV0; Q96NT3-2: GUCD1; NbExp=3; IntAct=EBI-6165879, EBI-11978177;
CC Q96IV0; Q99743: NPAS2; NbExp=3; IntAct=EBI-6165879, EBI-3932727;
CC Q96IV0; Q02548: PAX5; NbExp=3; IntAct=EBI-6165879, EBI-296331;
CC Q96IV0; P26367: PAX6; NbExp=3; IntAct=EBI-6165879, EBI-747278;
CC Q96IV0; P54725: RAD23A; NbExp=13; IntAct=EBI-6165879, EBI-746453;
CC Q96IV0; P54727: RAD23B; NbExp=12; IntAct=EBI-6165879, EBI-954531;
CC Q96IV0; Q99081-3: TCF12; NbExp=3; IntAct=EBI-6165879, EBI-11952764;
CC Q96IV0; O14545: TRAFD1; NbExp=7; IntAct=EBI-6165879, EBI-1396921;
CC Q96IV0; Q9BYV2: TRIM54; NbExp=7; IntAct=EBI-6165879, EBI-2130429;
CC Q96IV0; Q9UMX0: UBQLN1; NbExp=7; IntAct=EBI-6165879, EBI-741480;
CC Q96IV0; Q9UMX0-2: UBQLN1; NbExp=3; IntAct=EBI-6165879, EBI-10173939;
CC Q96IV0; Q14CS0: UBXN2B; NbExp=7; IntAct=EBI-6165879, EBI-1993619;
CC Q96IV0; Q2NL98: VMAC; NbExp=3; IntAct=EBI-6165879, EBI-2803134;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15358861}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q96IV0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96IV0-2; Sequence=VSP_020344;
CC Name=3;
CC IsoId=Q96IV0-3; Sequence=VSP_020345, VSP_020346;
CC Name=4;
CC IsoId=Q96IV0-4; Sequence=VSP_020343;
CC Name=5;
CC IsoId=Q96IV0-5; Sequence=VSP_043501;
CC -!- DOMAIN: The PUB domain mediates the interaction with VCP.
CC {ECO:0000269|PubMed:16807242}.
CC -!- DISEASE: Congenital disorder of deglycosylation 1 (CDDG1) [MIM:615273]:
CC An autosomal recessive multisystem disorder characterized by
CC developmental delay, hypotonia, abnormal involuntary movements and
CC alacrima or poor tear production. Other features include microcephaly,
CC intractable seizures, abnormal eye movements and evidence of liver
CC dysfunction, probably due to cytoplasmic accumulation of storage
CC material in vacuoles. {ECO:0000269|PubMed:22581936,
CC ECO:0000269|PubMed:24651605}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: In case of infection by cytomegaloviruses, it is not
CC essential for degradation of MHC class I heavy chains.
CC -!- SIMILARITY: Belongs to the transglutaminase-like superfamily. PNGase
CC family. {ECO:0000255|PROSITE-ProRule:PRU00731}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH17220.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD92786.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF250924; AAF74720.2; -; mRNA.
DR EMBL; AK296047; BAG58811.1; -; mRNA.
DR EMBL; AB209549; BAD92786.1; ALT_INIT; mRNA.
DR EMBL; AC092798; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000963; AAH00963.1; -; mRNA.
DR EMBL; BC007226; AAH07226.1; -; mRNA.
DR EMBL; BC017220; AAH17220.1; ALT_SEQ; mRNA.
DR CCDS; CCDS33719.1; -. [Q96IV0-1]
DR CCDS; CCDS46777.1; -. [Q96IV0-5]
DR CCDS; CCDS46778.1; -. [Q96IV0-2]
DR CCDS; CCDS46779.1; -. [Q96IV0-3]
DR RefSeq; NP_001138765.1; NM_001145293.1. [Q96IV0-2]
DR RefSeq; NP_001138766.1; NM_001145294.1. [Q96IV0-5]
DR RefSeq; NP_001138767.1; NM_001145295.1. [Q96IV0-3]
DR RefSeq; NP_060767.2; NM_018297.3. [Q96IV0-1]
DR PDB; 2CCQ; X-ray; 1.60 A; A=11-109.
DR PDB; 2CM0; X-ray; 1.90 A; A=11-109.
DR PDBsum; 2CCQ; -.
DR PDBsum; 2CM0; -.
DR AlphaFoldDB; Q96IV0; -.
DR SMR; Q96IV0; -.
DR BioGRID; 120885; 84.
DR IntAct; Q96IV0; 24.
DR MINT; Q96IV0; -.
DR STRING; 9606.ENSP00000280700; -.
DR BindingDB; Q96IV0; -.
DR ChEMBL; CHEMBL4523429; -.
DR iPTMnet; Q96IV0; -.
DR PhosphoSitePlus; Q96IV0; -.
DR BioMuta; NGLY1; -.
DR DMDM; 74732105; -.
DR EPD; Q96IV0; -.
DR jPOST; Q96IV0; -.
DR MassIVE; Q96IV0; -.
DR MaxQB; Q96IV0; -.
DR PaxDb; Q96IV0; -.
DR PeptideAtlas; Q96IV0; -.
DR PRIDE; Q96IV0; -.
DR ProteomicsDB; 76857; -. [Q96IV0-1]
DR ProteomicsDB; 76858; -. [Q96IV0-2]
DR ProteomicsDB; 76859; -. [Q96IV0-3]
DR ProteomicsDB; 76860; -. [Q96IV0-4]
DR ProteomicsDB; 76861; -. [Q96IV0-5]
DR Antibodypedia; 27393; 52 antibodies from 16 providers.
DR DNASU; 55768; -.
DR Ensembl; ENST00000280700.10; ENSP00000280700.5; ENSG00000151092.18. [Q96IV0-1]
DR Ensembl; ENST00000396649.7; ENSP00000379886.3; ENSG00000151092.18. [Q96IV0-3]
DR Ensembl; ENST00000417874.6; ENSP00000389888.2; ENSG00000151092.18. [Q96IV0-5]
DR Ensembl; ENST00000428257.5; ENSP00000387430.1; ENSG00000151092.18. [Q96IV0-2]
DR GeneID; 55768; -.
DR KEGG; hsa:55768; -.
DR MANE-Select; ENST00000280700.10; ENSP00000280700.5; NM_018297.4; NP_060767.2.
DR UCSC; uc003cdl.4; human. [Q96IV0-1]
DR CTD; 55768; -.
DR DisGeNET; 55768; -.
DR GeneCards; NGLY1; -.
DR GeneReviews; NGLY1; -.
DR HGNC; HGNC:17646; NGLY1.
DR HPA; ENSG00000151092; Low tissue specificity.
DR MalaCards; NGLY1; -.
DR MIM; 610661; gene.
DR MIM; 615273; phenotype.
DR neXtProt; NX_Q96IV0; -.
DR OpenTargets; ENSG00000151092; -.
DR Orphanet; 404454; Alacrimia-choreoathetosis-liver dysfunction syndrome.
DR PharmGKB; PA38462; -.
DR VEuPathDB; HostDB:ENSG00000151092; -.
DR eggNOG; KOG0909; Eukaryota.
DR GeneTree; ENSGT00390000006540; -.
DR HOGENOM; CLU_030187_0_0_1; -.
DR InParanoid; Q96IV0; -.
DR OMA; IKPSVEY; -.
DR OrthoDB; 917526at2759; -.
DR PhylomeDB; Q96IV0; -.
DR TreeFam; TF315254; -.
DR BRENDA; 3.5.1.52; 2681.
DR PathwayCommons; Q96IV0; -.
DR Reactome; R-HSA-532668; N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
DR SignaLink; Q96IV0; -.
DR SIGNOR; Q96IV0; -.
DR BioGRID-ORCS; 55768; 83 hits in 1080 CRISPR screens.
DR ChiTaRS; NGLY1; human.
DR EvolutionaryTrace; Q96IV0; -.
DR GeneWiki; NGLY1; -.
DR GenomeRNAi; 55768; -.
DR Pharos; Q96IV0; Tbio.
DR PRO; PR:Q96IV0; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q96IV0; protein.
DR Bgee; ENSG00000151092; Expressed in sperm and 203 other tissues.
DR ExpressionAtlas; Q96IV0; baseline and differential.
DR Genevisible; Q96IV0; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IGI:FlyBase.
DR GO; GO:0071712; P:ER-associated misfolded protein catabolic process; IEA:Ensembl.
DR GO; GO:0006516; P:glycoprotein catabolic process; IDA:UniProtKB.
DR GO; GO:0006517; P:protein deglycosylation; IDA:FlyBase.
DR GO; GO:0006457; P:protein folding; TAS:Reactome.
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; Alternative splicing; Cytoplasm; Hydrolase;
KW Metal-binding; Phosphoprotein; Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..654
FT /note="Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine
FT amidase"
FT /id="PRO_0000248971"
FT DOMAIN 30..91
FT /note="PUB"
FT DOMAIN 454..654
FT /note="PAW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00731"
FT REGION 112..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 309
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 336
FT /evidence="ECO:0000250"
FT ACT_SITE 353
FT /evidence="ECO:0000250"
FT BINDING 250
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 253
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 283
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 286
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 137
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..523
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_020343"
FT VAR_SEQ 1..43
FT /note="MAAAALGSSSGSASPAVAELCQNTPETFLEASKLLLTYADNIL -> M (in
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043501"
FT VAR_SEQ 335..383
FT /note="DHVWTEVYSPSQQRWLHCDACEDVCDKPLLYEIGWGKKLSYVIAFSKDE ->
FT ELQRTLSLKLTTLKEIGKTFLRISKRQKLIQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020344"
FT VAR_SEQ 538..558
FT /note="VYLARKEGSSFAYISWKFECG -> ITVFTPMLIFLVPLKLFWKQN (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020345"
FT VAR_SEQ 559..654
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020346"
FT VARIANT 581
FT /note="V -> I (in dbSNP:rs7621398)"
FT /id="VAR_027385"
FT VARIANT 591
FT /note="Q -> R (in dbSNP:rs7635089)"
FT /id="VAR_027386"
FT HELIX 15..20
FT /evidence="ECO:0007829|PDB:2CCQ"
FT HELIX 25..44
FT /evidence="ECO:0007829|PDB:2CCQ"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:2CCQ"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:2CCQ"
FT HELIX 59..64
FT /evidence="ECO:0007829|PDB:2CCQ"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:2CCQ"
FT HELIX 71..78
FT /evidence="ECO:0007829|PDB:2CCQ"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:2CCQ"
FT HELIX 95..106
FT /evidence="ECO:0007829|PDB:2CCQ"
SQ SEQUENCE 654 AA; 74390 MW; 94BD44316EA66AF6 CRC64;
MAAAALGSSS GSASPAVAEL CQNTPETFLE ASKLLLTYAD NILRNPNDEK YRSIRIGNTA
FSTRLLPVRG AVECLFEMGF EEGETHLIFP KKASVEQLQK IRDLIAIERS SRLDGSNKSH
KVKSSQQPAA STQLPTTPSS NPSGLNQHTR NRQGQSSDPP SASTVAADSA ILEVLQSNIQ
HVLVYENPAL QEKALACIPV QELKRKSQEK LSRARKLDKG INISDEDFLL LELLHWFKEE
FFHWVNNVLC SKCGGQTRSR DRSLLPSDDE LKWGAKEVED HYCDACQFSN RFPRYNNPEK
LLETRCGRCG EWANCFTLCC RAVGFEARYV WDYTDHVWTE VYSPSQQRWL HCDACEDVCD
KPLLYEIGWG KKLSYVIAFS KDEVVDVTWR YSCKHEEVIA RRTKVKEALL RDTINGLNKQ
RQLFLSENRR KELLQRIIVE LVEFISPKTP KPGELGGRIS GSVAWRVARG EMGLQRKETL
FIPCENEKIS KQLHLCYNIV KDRYVRVSNN NQTISGWENG VWKMESIFRK VETDWHMVYL
ARKEGSSFAY ISWKFECGSV GLKVDSISIR TSSQTFQTGT VEWKLRSDTA QVELTGDNSL
HSYADFSGAT EVILEAELSR GDGDVAWQHT QLFRQSLNDH EENCLEIIIK FSDL
