PGGHG_CHICK
ID PGGHG_CHICK Reviewed; 702 AA.
AC F1NZI4; A0A0H5AGM0; A0A0H5B0F3; A0A1D5PBV8;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2016, sequence version 3.
DT 03-AUG-2022, entry version 57.
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:0000305};
GN Name=PGGHG {ECO:0000303|PubMed:26682924};
GN Synonyms=ATHL1 {ECO:0000303|PubMed:26682924};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031 {ECO:0000312|Proteomes:UP000000539};
RN [1] {ECO:0000312|EMBL:BAR88294.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, CATALYTIC
RP ACTIVITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo {ECO:0000312|EMBL:BAR88294.1};
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).
RN [2] {ECO:0000312|Proteomes:UP000000539}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl {ECO:0000312|Proteomes:UP000000539};
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
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=F1NZI4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F1NZI4-2; Sequence=VSP_058888;
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 65 family. {ECO:0000305}.
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DR EMBL; LC011569; BAR88294.1; -; mRNA.
DR EMBL; LC011570; BAR88295.1; -; mRNA.
DR EMBL; AADN04000190; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001305330.1; NM_001318401.1.
DR RefSeq; XP_015141747.1; XM_015286261.1. [F1NZI4-1]
DR AlphaFoldDB; F1NZI4; -.
DR SMR; F1NZI4; -.
DR STRING; 9031.ENSGALP00000006728; -.
DR PaxDb; F1NZI4; -.
DR Ensembl; ENSGALT00000006739; ENSGALP00000006728; ENSGALG00000004234. [F1NZI4-1]
DR Ensembl; ENSGALT00000055588; ENSGALP00000050240; ENSGALG00000004234. [F1NZI4-2]
DR GeneID; 422991; -.
DR KEGG; gga:422991; -.
DR CTD; 80162; -.
DR VEuPathDB; HostDB:geneid_422991; -.
DR eggNOG; KOG4125; Eukaryota.
DR GeneTree; ENSGT00390000006297; -.
DR HOGENOM; CLU_006285_4_2_1; -.
DR InParanoid; F1NZI4; -.
DR OMA; ATHRIYA; -.
DR OrthoDB; 125022at2759; -.
DR TreeFam; TF300109; -.
DR BRENDA; 3.2.1.107; 1306.
DR PRO; PR:F1NZI4; -.
DR Proteomes; UP000000539; Chromosome 5.
DR Bgee; ENSGALG00000004234; Expressed in liver and 8 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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..702
FT /note="Protein-glucosylgalactosylhydroxylysine glucosidase"
FT /id="PRO_0000439598"
FT ACT_SITE 440
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q32M88"
FT BINDING 310..311
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D6XZ22"
FT BINDING 508..509
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D6XZ22"
FT VAR_SEQ 1..8
FT /note="MSMRGSGK -> MLGGRWPCDGMRWEKL (in isoform 2)"
FT /id="VSP_058888"
FT CONFLICT 131
FT /note="W -> R (in Ref. 1; BAR88294/BAR88295)"
FT /evidence="ECO:0000305"
FT CONFLICT 352
FT /note="K -> E (in Ref. 1; BAR88294/BAR88295)"
FT /evidence="ECO:0000305"
FT CONFLICT 428
FT /note="Q -> R (in Ref. 1; BAR88294/BAR88295)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 702 AA; 78358 MW; 2FFBF56748C47187 CRC64;
MSMRGSGKLW LVMADGQEDP AVFTSTCLPS DSRLLATVTN AYLGTRVYRN ILHVSGVYNG
AAGDTHRADI PSPVNVRMTV PDGDVPVETF TLNTRTGTFS HKLESSSYTA THQIYAHHSL
VHLMAFSITI WRSAGTSQPI TVQLQAPFVP KSQDLDLQQG PDFQGAHYIY GQTLVPEVEG
GPQPTVHMLW TPVPQAVTLH EEEQERRWEF LTAVAESEEE AKRSYSEGLA RMAAGSLHSS
HTRAWAALWR GCCVDLEGPL PLRQALYGCL YYLLSAIPPQ GTPGFHFHGI SPGGLSNGTR
GEDYWGHVFW DQDTWIFPNI LLFYPEAARA ILEYRIRTLE GALLNAQEQG YKGAKFPWES
AATGREVCPE DIYGAQEIHI TGDVLMAFEQ YYHTTQDQKL FRTDGGWELV SAVAQYWCSR
MVWSEEEQCY HIRGVMPPDE YHYQVDNSAY TNAVAQRSLN FAASVARDFF IPVPEEWVEC
AKKVKVPFDA VRKYHPEYDG YSPGEPVKQA DVVLLGFPLM HPMHPEVRRN DLVMYEPVTE
LSGPAMTWSM FAVGWLELKE TQRAQGLLNK CFSNITEPFK IWVENSDGSG AVNFLTGMGG
FLQAVLFGYT GFRITKTNLR FDPAFPSDVS KLEVTGVSYL GSKLKFSITK EKMRIAVTKC
PLHPPLEAVL EESGQRFPLH EGQSISFPTA AGCIQKAPSE GL
