ID GLBL2_MOUSE Reviewed; 636 AA.
AC Q3UPY5; Q8CFT1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 24-JAN-2024, entry version 114.
DE RecName: Full=Beta-galactosidase-1-like protein 2;
DE EC=3.2.1.-;
DE Flags: Precursor;
GN Name=Glb1l2;
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; TISSUE=Eye;
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=Eye;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3UPY5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UPY5-2; Sequence=VSP_031000;
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK143057; BAE25259.1; -; mRNA.
DR EMBL; BC038479; AAH38479.1; -; mRNA.
DR CCDS; CCDS40566.1; -. [Q3UPY5-2]
DR CCDS; CCDS80971.1; -. [Q3UPY5-1]
DR RefSeq; NP_001297697.1; NM_001310768.1.
DR RefSeq; NP_722498.1; NM_153803.1.
DR AlphaFoldDB; Q3UPY5; -.
DR SMR; Q3UPY5; -.
DR BioGRID; 232689; 2.
DR STRING; 10090.ENSMUSP00000047128; -.
DR CAZy; GH35; Glycoside Hydrolase Family 35.
DR iPTMnet; Q3UPY5; -.
DR PhosphoSitePlus; Q3UPY5; -.
DR MaxQB; Q3UPY5; -.
DR PaxDb; 10090-ENSMUSP00000047128; -.
DR ProteomicsDB; 263362; -. [Q3UPY5-1]
DR ProteomicsDB; 263363; -. [Q3UPY5-2]
DR DNASU; 244757; -.
DR GeneID; 244757; -.
DR KEGG; mmu:244757; -.
DR UCSC; uc009opt.1; mouse. [Q3UPY5-2]
DR AGR; MGI:2388283; -.
DR CTD; 89944; -.
DR MGI; MGI:2388283; Glb1l2.
DR eggNOG; KOG0496; Eukaryota.
DR InParanoid; Q3UPY5; -.
DR OrthoDB; 5489808at2759; -.
DR PhylomeDB; Q3UPY5; -.
DR TreeFam; TF354299; -.
DR Reactome; R-MMU-2022857; Keratan sulfate degradation.
DR Reactome; R-MMU-2024096; HS-GAG degradation.
DR Reactome; R-MMU-9840310; Glycosphingolipid catabolism.
DR BioGRID-ORCS; 244757; 2 hits in 61 CRISPR screens.
DR ChiTaRS; Glb1l2; mouse.
DR PRO; PR:Q3UPY5; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q3UPY5; Protein.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005773; C:vacuole; IBA:GO_Central.
DR GO; GO:0004565; F:beta-galactosidase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR026283; B-gal_1-like.
DR InterPro; IPR048912; BetaGal1-like_ABD1.
DR InterPro; IPR048913; BetaGal_gal-bd.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR InterPro; IPR019801; Glyco_hydro_35_CS.
DR InterPro; IPR001944; Glycoside_Hdrlase_35.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR PANTHER; PTHR23421:SF53; BETA-GALACTOSIDASE-1-LIKE PROTEIN 2; 1.
DR Pfam; PF21317; BetaGal_ABD_1; 1.
DR Pfam; PF21467; BetaGal_gal-bd; 1.
DR Pfam; PF01301; Glyco_hydro_35; 1.
DR PIRSF; PIRSF006336; B-gal; 1.
DR PRINTS; PR00742; GLHYDRLASE35.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Glycosidase; Hydrolase; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..636
FT /note="Beta-galactosidase-1-like protein 2"
FT /id="PRO_0000317514"
FT ACT_SITE 201
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 277
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT VAR_SEQ 29
FT /note="R -> RYLNPKVGSCDHEGALR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031000"
FT CONFLICT 172
FT /note="E -> D (in Ref. 2; AAH38479)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 636 AA; 72236 MW; 934B12CF5CAF15AE CRC64;
MPKWSLRRRP GRTLGLLLLL VLSFLVLRRL NWSTLVPLWL QHQRLGLRTK GPDFILEDSI
FQILGGSIHY FRVPREYWRD RLLKLKACGL NTLTTYVPWN LHEPERGKFD FSGNLDLEAF
IQLAAKIGLW VILRPGPYIC SEIDLGGLPS WLLQDPDMKL RTTYHGFTKA VELYFDHLMS
RVVPLQYKHG GPIIAVQVEN EYGSYNKDRA YMPYIKKALE DRGIIEMLLT SDNKDGLEKG
VVDGVLATIN LQSQQELMAL NTVLLSIQGI QPKMVMEYWT GWFDSWGGSH NILDSSEVLQ
TVSAIIKDGS SINLYMFHGG TNFGFINGAM HFNDYKADVT SYDYDAILTE AGDYTAKYTK
LRELFGTVSG IPPPPPPELT AKMVYEPMSP ALYLSLWDAI QYMDKPVTSE TPINMENLPV
NNGNGQAFGY VLYETTIFSS GVLSGLVRDR GQVFLNRVSI GFLDYKTTKI TIPLTQGYTI
LRILVENRGR VNYGNNIDSQ RKGLIGNLYL NNKALKNFKI YSLDMTKQFL QRFDMDNWSV
IPKELTFPAF FLGALSVGIY PSDTFLKLEG WVKGVVFVNG HNLGRYWNVG PQETLYLPGV
WLDKGINKVI IFEETMSGSM VQSTDIPHLG RNQYIN
//
