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GLB1L_MOUSE
ID   GLB1L_MOUSE             Reviewed;         646 AA.
AC   Q8VC60; Q8CDK6; Q9D631;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Beta-galactosidase-1-like protein;
DE            EC=3.2.1.-;
DE   Flags: Precursor;
GN   Name=Glb1l;
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] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Head, and Testis;
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 1).
RC   STRAIN=FVB/N; TISSUE=Kidney;
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, and Testis;
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: Probable glycosyl hydrolase. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8VC60-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8VC60-2; Sequence=VSP_030060, VSP_030061, VSP_030062;
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family. {ECO:0000305}.
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DR   EMBL; AK014667; BAB29494.1; -; mRNA.
DR   EMBL; AK029925; BAC26681.1; -; mRNA.
DR   EMBL; BC021773; AAH21773.1; -; mRNA.
DR   CCDS; CCDS48291.1; -. [Q8VC60-1]
DR   RefSeq; NP_083286.1; NM_029010.1. [Q8VC60-1]
DR   RefSeq; XP_006496616.1; XM_006496553.3. [Q8VC60-1]
DR   RefSeq; XP_006496617.1; XM_006496554.3. [Q8VC60-1]
DR   RefSeq; XP_017168026.1; XM_017312537.1. [Q8VC60-1]
DR   AlphaFoldDB; Q8VC60; -.
DR   SMR; Q8VC60; -.
DR   STRING; 10090.ENSMUSP00000109253; -.
DR   CAZy; GH35; Glycoside Hydrolase Family 35.
DR   GlyGen; Q8VC60; 2 sites.
DR   PhosphoSitePlus; Q8VC60; -.
DR   EPD; Q8VC60; -.
DR   MaxQB; Q8VC60; -.
DR   PaxDb; Q8VC60; -.
DR   PeptideAtlas; Q8VC60; -.
DR   PRIDE; Q8VC60; -.
DR   ProteomicsDB; 271225; -. [Q8VC60-1]
DR   ProteomicsDB; 271226; -. [Q8VC60-2]
DR   Antibodypedia; 34313; 65 antibodies from 14 providers.
DR   Ensembl; ENSMUST00000113623; ENSMUSP00000109253; ENSMUSG00000026200. [Q8VC60-1]
DR   Ensembl; ENSMUST00000155716; ENSMUSP00000136285; ENSMUSG00000026200. [Q8VC60-1]
DR   GeneID; 74577; -.
DR   KEGG; mmu:74577; -.
DR   UCSC; uc007bog.1; mouse. [Q8VC60-2]
DR   UCSC; uc011wnk.1; mouse. [Q8VC60-1]
DR   CTD; 79411; -.
DR   MGI; MGI:1921827; Glb1l.
DR   VEuPathDB; HostDB:ENSMUSG00000026200; -.
DR   eggNOG; KOG0496; Eukaryota.
DR   GeneTree; ENSGT00950000182942; -.
DR   HOGENOM; CLU_007853_7_2_1; -.
DR   InParanoid; Q8VC60; -.
DR   OMA; GSYGACD; -.
DR   OrthoDB; 179316at2759; -.
DR   PhylomeDB; Q8VC60; -.
DR   TreeFam; TF314816; -.
DR   Reactome; R-MMU-1660662; Glycosphingolipid metabolism.
DR   Reactome; R-MMU-2022857; Keratan sulfate degradation.
DR   Reactome; R-MMU-2024096; HS-GAG degradation.
DR   BioGRID-ORCS; 74577; 3 hits in 72 CRISPR screens.
DR   ChiTaRS; Glb1l; mouse.
DR   PRO; PR:Q8VC60; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q8VC60; protein.
DR   Bgee; ENSMUSG00000026200; Expressed in spermatocyte and 142 other tissues.
DR   ExpressionAtlas; Q8VC60; baseline and differential.
DR   Genevisible; Q8VC60; MM.
DR   GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
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   InterPro; IPR026283; B-gal_1-like.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR   InterPro; IPR001944; Glycoside_Hdrlase_35.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR23421; PTHR23421; 1.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PIRSF; PIRSF006336; B-gal; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Glycoprotein; Glycosidase; Hydrolase;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..646
FT                   /note="Beta-galactosidase-1-like protein"
FT                   /id="PRO_0000313606"
FT   ACT_SITE        182
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        260
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        93
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        239
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1..76
FT                   /note="MPPDLPSLLLRLVVLLLLSQAEARSFVVDREHDRFLLDGVPFRYVSGSLHYF
FT                   RVPPVLWADRLLKMQLSGLNAVQF -> MAQNLFLAASLQVLSLLGNLWVLLTSSFLS
FT                   (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_030060"
FT   VAR_SEQ         560..573
FT                   /note="GQVWINGFNLGRYW -> VLLTVVEGIVGGTL (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_030061"
FT   VAR_SEQ         574..646
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_030062"
FT   CONFLICT        466
FT                   /note="R -> S (in Ref. 1; BAC26681)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   646 AA;  73279 MW;  FB46941BDE62C832 CRC64;
     MPPDLPSLLL RLVVLLLLSQ AEARSFVVDR EHDRFLLDGV PFRYVSGSLH YFRVPPVLWA
     DRLLKMQLSG LNAVQFYVPW NYHEPEPGIY NFNGSRDLIA FLNEAAKVNL LVILRPGPYI
     CAEWEMGGLP SWLLRNPNIH LRTSDPAFLE AVDSWFKVLL PKIYPFLYHN GGNIISIQVE
     NEYGSYKACD FKYMRHLAGL FRALLGDKIL LFTTDGPHGL RCGSLQGLYT TIDFGPADNV
     TRIFSLLREY EPHGPLVNSE YYTGWLDYWG QNHSTRSSPA VAQGLEKMLK LGASVNMYMF
     HGGTNFGYWN GADEKGRFLP ITTSYDYDAP ISEAGDPTPK LFAIRNVISK FQEIPLGPLP
     PPSPKMKFGP LTMSLDGNLL SFLDFLCPQG PIHSVLPLTF EAVKLDHGFM LYRTYLTSPV
     LEPTPFWVPN NGIHDRAYVM VDGVLKGVLE RSLKQELYLT GTVGTRLDIL LENMGRLSFG
     SNHSDFKGLL EAPLLGQTIL TEWMMFPLKV DKLVKWWFPL QLMKRALPQA SSVPAFYSAK
     FPVFGLLGDT FLYLPGWTKG QVWINGFNLG RYWTMRGPQQ TLYVPRLLLF GRSINKITLL
     ELENVPHNPQ VQFLDKPILN STLHWGYNFL LSETQGSFEP MELSGH
 
 
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