PGGHG_HUMAN
ID PGGHG_HUMAN Reviewed; 737 AA.
AC Q32M88; Q658X8; Q8TEG9; Q9H635;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Protein-glucosylgalactosylhydroxylysine glucosidase {ECO:0000303|PubMed:26682924};
DE EC=3.2.1.107 {ECO:0000269|PubMed:26682924};
DE AltName: Full=Acid trehalase-like protein 1 {ECO:0000312|HGNC:HGNC:26210};
GN Name=PGGHG {ECO:0000303|PubMed:26682924, ECO:0000312|HGNC:HGNC:26210};
GN Synonyms=ATHL1 {ECO:0000312|HGNC:HGNC:26210};
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Spleen;
RX PubMed=12693554; DOI=10.1093/dnares/10.1.49;
RA Jikuya H., Takano J., Kikuno R., Hirosawa M., Nagase T., Nomura N.,
RA Ohara O.;
RT "Characterization of long cDNA clones from human adult spleen. II. The
RT complete sequences of 81 cDNA clones.";
RL DNA Res. 10:49-57(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 160-500.
RC TISSUE=Small intestine;
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 MRNA] OF 163-737.
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 424-737 (ISOFORM 1).
RC TISSUE=Stomach;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, AND MUTAGENESIS OF ASP-301;
RP ASP-429; GLU-430 AND GLU-574.
RX PubMed=26682924; DOI=10.1016/j.bbrc.2015.12.005;
RA Hamazaki H., Hamazaki M.H.;
RT "Catalytic site of human protein-glucosylgalactosylhydroxylysine
RT glucosidase: Three crucial carboxyl residues were determined by cloning and
RT site-directed mutagenesis.";
RL Biochem. Biophys. Res. Commun. 469:357-362(2016).
CC -!- FUNCTION: Catalyzes the hydrolysis of glucose from the disaccharide
CC unit linked to hydroxylysine residues of collagen and collagen-like
CC proteins. {ECO:0000269|PubMed:26682924}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5R)-5-O-[alpha-D-glucosyl-(1->2)-beta-D-galactosyl]-5-
CC hydroxy-L-lysyl-[collagen] + H2O = (5R)-5-O-(beta-D-galactosyl)-5-
CC hydroxy-L-lysyl-[collagen] + D-glucose; Xref=Rhea:RHEA:11068,
CC Rhea:RHEA-COMP:12753, Rhea:RHEA-COMP:12754, ChEBI:CHEBI:4167,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:133443, ChEBI:CHEBI:133452;
CC EC=3.2.1.107; Evidence={ECO:0000269|PubMed:26682924};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q32M88-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q32M88-2; Sequence=VSP_032895, VSP_032896;
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 65 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI09258.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI09259.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB15431.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB84981.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC136475; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK074155; BAB84981.1; ALT_INIT; mRNA.
DR EMBL; AK026288; BAB15431.1; ALT_INIT; mRNA.
DR EMBL; BC109257; AAI09258.1; ALT_INIT; mRNA.
DR EMBL; BC109258; AAI09259.1; ALT_INIT; mRNA.
DR EMBL; AL832932; CAH56316.1; -; mRNA.
DR CCDS; CCDS31322.2; -. [Q32M88-1]
DR RefSeq; NP_079368.3; NM_025092.4. [Q32M88-1]
DR RefSeq; XP_011518685.1; XM_011520383.2. [Q32M88-1]
DR RefSeq; XP_016873844.1; XM_017018355.1. [Q32M88-1]
DR AlphaFoldDB; Q32M88; -.
DR SMR; Q32M88; -.
DR BioGRID; 123150; 3.
DR STRING; 9606.ENSP00000387185; -.
DR CAZy; GH65; Glycoside Hydrolase Family 65.
DR iPTMnet; Q32M88; -.
DR PhosphoSitePlus; Q32M88; -.
DR BioMuta; PGGHG; -.
DR DMDM; 182627595; -.
DR EPD; Q32M88; -.
DR jPOST; Q32M88; -.
DR MassIVE; Q32M88; -.
DR MaxQB; Q32M88; -.
DR PaxDb; Q32M88; -.
DR PeptideAtlas; Q32M88; -.
DR PRIDE; Q32M88; -.
DR ProteomicsDB; 61596; -. [Q32M88-1]
DR ProteomicsDB; 61597; -. [Q32M88-2]
DR Antibodypedia; 48910; 23 antibodies from 14 providers.
DR DNASU; 80162; -.
DR Ensembl; ENST00000409548.7; ENSP00000387185.2; ENSG00000142102.16. [Q32M88-1]
DR GeneID; 80162; -.
DR KEGG; hsa:80162; -.
DR MANE-Select; ENST00000409548.7; ENSP00000387185.2; NM_025092.5; NP_079368.3.
DR UCSC; uc010qvu.3; human. [Q32M88-1]
DR CTD; 80162; -.
DR DisGeNET; 80162; -.
DR GeneCards; PGGHG; -.
DR HGNC; HGNC:26210; PGGHG.
DR HPA; ENSG00000142102; Tissue enriched (pancreas).
DR neXtProt; NX_Q32M88; -.
DR OpenTargets; ENSG00000142102; -.
DR PharmGKB; PA142672576; -.
DR VEuPathDB; HostDB:ENSG00000142102; -.
DR eggNOG; KOG4125; Eukaryota.
DR GeneTree; ENSGT00390000006297; -.
DR HOGENOM; CLU_006285_4_2_1; -.
DR InParanoid; Q32M88; -.
DR PhylomeDB; Q32M88; -.
DR TreeFam; TF300109; -.
DR BioCyc; MetaCyc:ENSG00000142102-MON; -.
DR PathwayCommons; Q32M88; -.
DR BioGRID-ORCS; 80162; 6 hits in 1077 CRISPR screens.
DR ChiTaRS; PGGHG; human.
DR GenomeRNAi; 80162; -.
DR Pharos; Q32M88; Tbio.
DR PRO; PR:Q32M88; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q32M88; protein.
DR Bgee; ENSG00000142102; Expressed in body of pancreas and 160 other tissues.
DR ExpressionAtlas; Q32M88; baseline and differential.
DR Genevisible; Q32M88; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IBA:GO_Central.
DR GO; GO:0047402; F:protein-glucosylgalactosylhydroxylysine glucosidase activity; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IDA:UniProtKB.
DR Gene3D; 1.50.10.10; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR005195; Glyco_hydro_65_M.
DR Pfam; PF03632; Glyco_hydro_65m; 1.
DR SUPFAM; SSF48208; SSF48208; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Glycosidase; Hydrolase; Reference proteome.
FT CHAIN 1..737
FT /note="Protein-glucosylgalactosylhydroxylysine glucosidase"
FT /id="PRO_0000329004"
FT REGION 681..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..737
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 430
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:26682924"
FT BINDING 300..301
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:26682924"
FT BINDING 498..499
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D6XZ22"
FT VAR_SEQ 303..354
FT /note="DLWMFPSILMFHPEAARAILEYRIRTLDGALENAQNLGYQGAKFAWESADSG
FT -> VSTVHPAPATQQATHGGPRSLPSLGPGLWLGKHRDCGKREEAWKVCRSLVEE (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:12693554"
FT /id="VSP_032895"
FT VAR_SEQ 355..737
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12693554"
FT /id="VSP_032896"
FT MUTAGEN 301
FT /note="D->E,N: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:26682924"
FT MUTAGEN 429
FT /note="D->E: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:26682924"
FT MUTAGEN 429
FT /note="D->N: Significantly impairs catalytic activity."
FT /evidence="ECO:0000269|PubMed:26682924"
FT MUTAGEN 430
FT /note="E->D,Q: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:26682924"
FT MUTAGEN 574
FT /note="E->D,Q: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:26682924"
FT CONFLICT 487..500
FT /note="EFDGYEPGEVVKQA -> KFQLRVPWEDFFRC (in Ref. 3;
FT BAB15431)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 737 AA; 80655 MW; 6EAEEE2FF90F3CD2 CRC64;
MEDAGEDPTT FAAHSLPSDP RLLATVTNAY LGTRVFHDTL HVSGVYNGAG GDTHRAMLPS
PLNVRLEAPA GMGEQLTETF ALDTNTGSFL HTLEGPRFRA SQCIYAHRTL PHVLAFRVSI
ARLAPGSGPI TLLLRSAFSP ESPDLDLHQG PDFQGARYLY GHTLTPEQPG GPQQEVHMLW
TPAPPDLTLG EGEEARTWDF LTAVGGSQAE AQACLTEALQ LQARGALYTA HAQAWAQLWV
ECGLDVVGPL QLRQALRGSL YYLLSALPQP KAPGYICHGL SPGGLSNGSR EECYWGHVFW
DQDLWMFPSI LMFHPEAARA ILEYRIRTLD GALENAQNLG YQGAKFAWES ADSGLEVCPE
DIYGVQEVHV NGAVVLAFEL YYHTTQDLQL FREAGGWDVV RAVAEFWCSR VEWSPREEKY
HLRGVMSPDE YHSGVNNSVY TNVLVQNSLR FAAALAQDLG LPIPSQWLAV ADKIKVPFDV
EQNFHPEFDG YEPGEVVKQA DVVLLGYPVP FSLSPDVRRK NLEIYEAVTS PQGPAMTWSM
FAVGWMELKD AVRARGLLDR SFANMAEPFK VWTENADGSG AVNFLTGMGG FLQAVVFGCT
GFRVTRAGVT FDPVCLSGIS RVSVSGIFYQ GNKLNFSFSE DSVTVEVTAR AGPWAPHLEA
ELWPSQSRLS LLPGHKVSFP RSAGRIQMSP PKLPGSSSSE FPGRTFSDVR DPLQSPLWVT
LGSSSPTESL TVDPASE
