PGGHG_MOUSE
ID PGGHG_MOUSE Reviewed; 690 AA.
AC Q8BP56; Q571E9; Q8R585;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Protein-glucosylgalactosylhydroxylysine glucosidase {ECO:0000250|UniProtKB:Q32M88};
DE EC=3.2.1.107 {ECO:0000250|UniProtKB:Q32M88};
DE AltName: Full=Acid trehalase-like protein 1 {ECO:0000250|UniProtKB:Q32M88};
GN Name=Pgghg {ECO:0000312|MGI:MGI:2444047};
GN Synonyms=Athl1 {ECO:0000312|MGI:MGI:2444047};
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Pancreatic islet;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 77-690 (ISOFORM 3).
RC STRAIN=C57BL/6J, and Czech II; TISSUE=Brain, and Mammary tumor;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Lung, and Spleen;
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).
CC -!- FUNCTION: Catalyzes the hydrolysis of glucose from the disaccharide
CC unit linked to hydroxylysine residues of collagen and collagen-like
CC proteins. {ECO:0000250|UniProtKB:Q32M88}.
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:0000250|UniProtKB:Q32M88};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BP56-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BP56-2; Sequence=VSP_032897, VSP_032898, VSP_032899;
CC Name=3;
CC IsoId=Q8BP56-3; Sequence=VSP_032900;
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 65 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD90165.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK077662; BAC36936.1; -; mRNA.
DR EMBL; AK220240; BAD90165.1; ALT_INIT; Transcribed_RNA.
DR EMBL; BC023151; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC056953; AAH56953.1; -; mRNA.
DR CCDS; CCDS21992.1; -. [Q8BP56-1]
DR RefSeq; NP_663362.2; NM_145387.4. [Q8BP56-1]
DR AlphaFoldDB; Q8BP56; -.
DR SMR; Q8BP56; -.
DR STRING; 10090.ENSMUSP00000078372; -.
DR CAZy; GH65; Glycoside Hydrolase Family 65.
DR iPTMnet; Q8BP56; -.
DR PhosphoSitePlus; Q8BP56; -.
DR EPD; Q8BP56; -.
DR MaxQB; Q8BP56; -.
DR PaxDb; Q8BP56; -.
DR PeptideAtlas; Q8BP56; -.
DR PRIDE; Q8BP56; -.
DR ProteomicsDB; 301802; -. [Q8BP56-1]
DR ProteomicsDB; 301803; -. [Q8BP56-2]
DR ProteomicsDB; 301804; -. [Q8BP56-3]
DR Antibodypedia; 48910; 23 antibodies from 14 providers.
DR DNASU; 212974; -.
DR Ensembl; ENSMUST00000079403; ENSMUSP00000078372; ENSMUSG00000062031. [Q8BP56-1]
DR Ensembl; ENSMUST00000164580; ENSMUSP00000128214; ENSMUSG00000062031. [Q8BP56-3]
DR GeneID; 212974; -.
DR KEGG; mmu:212974; -.
DR UCSC; uc009kiw.1; mouse. [Q8BP56-1]
DR CTD; 80162; -.
DR MGI; MGI:2444047; Pgghg.
DR VEuPathDB; HostDB:ENSMUSG00000062031; -.
DR eggNOG; KOG4125; Eukaryota.
DR GeneTree; ENSGT00390000006297; -.
DR HOGENOM; CLU_006285_4_2_1; -.
DR InParanoid; Q8BP56; -.
DR OMA; ATHRIYA; -.
DR OrthoDB; 125022at2759; -.
DR PhylomeDB; Q8BP56; -.
DR TreeFam; TF300109; -.
DR BioGRID-ORCS; 212974; 2 hits in 74 CRISPR screens.
DR PRO; PR:Q8BP56; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8BP56; protein.
DR Bgee; ENSMUSG00000062031; Expressed in external carotid artery and 200 other tissues.
DR ExpressionAtlas; Q8BP56; baseline and differential.
DR Genevisible; Q8BP56; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IBA:GO_Central.
DR GO; GO:0047402; F:protein-glucosylgalactosylhydroxylysine glucosidase activity; ISO:MGI.
DR GO; GO:0005975; P:carbohydrate metabolic process; ISO:MGI.
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..690
FT /note="Protein-glucosylgalactosylhydroxylysine glucosidase"
FT /id="PRO_0000329005"
FT ACT_SITE 429
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q32M88"
FT BINDING 299..300
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D6XZ22"
FT BINDING 497..498
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D6XZ22"
FT VAR_SEQ 302..448
FT /note="DIWMFPNILMFHPEAARAILEYRVRTLGGALKNGQNLGYQGAKFAWESASTG
FT LEVCPEDIYGTQEIHINGAVALAFQLYYYYTQDSKLFQEDGGWDVVSSVAEFWCSRVEW
FT SSQDKMYHLKGVMPPDEYHSGVNNSVYTNVLVQNSL -> VHPTLHWLHRGSCMQRFRA
FT LP (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_032897"
FT VAR_SEQ 538..608
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_032898"
FT VAR_SEQ 673..690
FT /note="GQKVSFPHSAGRIQRSSP -> EGLLSPLSWPDTKVIPIAAQKFFRGS (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032900"
FT VAR_SEQ 674..690
FT /note="QKVSFPHSAGRIQRSSP -> RE (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_032899"
FT CONFLICT 277
FT /note="H -> Y (in Ref. 2; BAD90165)"
FT /evidence="ECO:0000305"
FT CONFLICT 529
FT /note="S -> P (in Ref. 3; BC023151)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 690 AA; 76488 MW; 91F426E955C273BD CRC64;
MDGSEDDPTI FSARCLPSDP RLWATVTNSY LGTRVYHDTI HINGVYNGAV GDTHRASLPS
PLNVQLEAPA GTEQLTETFT LDTNTGSFLH TLEGPSFRAS QRIYAHRVLP HVLVFSVSIA
RLTTGNKPIT VPLRADFSPE SPDLDLRVGP DFQGLRYLHG HVLNPEQPGE PQQEVHMLWM
PVPPALTLGE EEKDRTWEFL TVVGSSQAEA QDCFAEALQL QTRGVLYTIH ADSWGRLWAG
CGLDVAGPLA LRQALRGSLY YLFSELPQPG TQGFISHGLS PGGLSNGSKE ECYWGHIFWD
QDIWMFPNIL MFHPEAARAI LEYRVRTLGG ALKNGQNLGY QGAKFAWESA STGLEVCPED
IYGTQEIHIN GAVALAFQLY YYYTQDSKLF QEDGGWDVVS SVAEFWCSRV EWSSQDKMYH
LKGVMPPDEY HSGVNNSVYT NVLVQNSLHF AAALAKDLGL PIRKQWLEVA DRIKIPFDSE
QNFHPEFDGY ERGEEVKQAD VVLLGYPVPF PLTPDIRRKN LETYEAVTSP QGPAMTWSMF
AVGWMELRDP SRAQVHLSRS FANVTEPFKV WTENADGSGA VNFLTGMGGF LQAALFGCTG
FRITEAGVTF DPLCPDLVSR VSVSGISYLG NKINFAFSKD SVTLEVTARA EPWAPLLEAE
LWPSLAHLPL TPGQKVSFPH SAGRIQRSSP
