ALG13_MOUSE
ID ALG13_MOUSE Reviewed; 1166 AA.
AC Q9D8C3; A3KGC8; A3KGD0; A3KGD1; Q8BUA4; Q9D5Z6;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Putative bifunctional UDP-N-acetylglucosamine transferase and deubiquitinase ALG13;
DE EC=2.4.1.141;
DE EC=3.4.19.12;
DE AltName: Full=Asparagine-linked glycosylation 13 homolog;
DE AltName: Full=Glycosyltransferase 28 domain-containing protein 1;
DE AltName: Full=UDP-N-acetylglucosamine transferase subunit ALG13 homolog;
GN Name=Alg13; Synonyms=Glt28d1;
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 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Head, Small intestine, and Thymus;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Fetal brain;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Spleen, 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: [Isoform 1]: Possible multifunctional enzyme with both
CC glycosyltransferase and deubiquitinase activities.
CC -!- FUNCTION: [Isoform 2]: May be involved in protein N-glycosylation,
CC second step of the dolichol-linked oligosaccharide pathway (By.
CC similarity).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-acetyl-alpha-D-glucosaminyl-diphosphodolichol + UDP-N-
CC acetyl-alpha-D-glucosamine = H(+) + N,N'-diacetylchitobiosyl
CC diphosphodolichol + UDP; Xref=Rhea:RHEA:23380, Rhea:RHEA-COMP:9519,
CC Rhea:RHEA-COMP:9520, ChEBI:CHEBI:15378, ChEBI:CHEBI:57269,
CC ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:58427;
CC EC=2.4.1.141;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12;
CC -!- SUBUNIT: Isoform 2 may interact with ALG14. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250}. Note=Could
CC be recruited to the cytosolic face of the endoplasmic reticulum
CC membrane through its interaction with ALG14. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9D8C3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D8C3-2; Sequence=VSP_039304, VSP_039305;
CC -!- SIMILARITY: Belongs to the glycosyltransferase 28 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAM45938.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAM45939.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AK008162; BAB25504.1; -; mRNA.
DR EMBL; AK014790; BAB29554.1; -; mRNA.
DR EMBL; AK086546; BAC39689.1; -; mRNA.
DR EMBL; AK089102; BAC40750.1; -; mRNA.
DR EMBL; AL713978; CAM45936.1; -; Genomic_DNA.
DR EMBL; AL713978; CAM45938.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL713978; CAM45939.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH466610; EDL14725.1; -; Genomic_DNA.
DR EMBL; BC053004; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC137692; AAI37693.1; -; mRNA.
DR CCDS; CCDS30456.1; -. [Q9D8C3-2]
DR RefSeq; NP_080523.2; NM_026247.3. [Q9D8C3-2]
DR AlphaFoldDB; Q9D8C3; -.
DR SMR; Q9D8C3; -.
DR BioGRID; 212284; 3.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR PhosphoSitePlus; Q9D8C3; -.
DR jPOST; Q9D8C3; -.
DR MaxQB; Q9D8C3; -.
DR PeptideAtlas; Q9D8C3; -.
DR PRIDE; Q9D8C3; -.
DR ProteomicsDB; 296093; -. [Q9D8C3-1]
DR ProteomicsDB; 296094; -. [Q9D8C3-2]
DR ABCD; Q9D8C3; 1 sequenced antibody.
DR Antibodypedia; 490; 170 antibodies from 20 providers.
DR DNASU; 67574; -.
DR Ensembl; ENSMUST00000070801; ENSMUSP00000068403; ENSMUSG00000041718. [Q9D8C3-2]
DR GeneID; 67574; -.
DR KEGG; mmu:67574; -.
DR UCSC; uc009ums.2; mouse. [Q9D8C3-2]
DR UCSC; uc009umu.2; mouse. [Q9D8C3-1]
DR CTD; 79868; -.
DR MGI; MGI:1914824; Alg13.
DR VEuPathDB; HostDB:ENSMUSG00000041718; -.
DR GeneTree; ENSGT00940000159922; -.
DR HOGENOM; CLU_085408_2_2_1; -.
DR InParanoid; Q9D8C3; -.
DR OMA; FNDKLMD; -.
DR OrthoDB; 222767at2759; -.
DR PhylomeDB; Q9D8C3; -.
DR TreeFam; TF313788; -.
DR Reactome; R-MMU-446193; Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.
DR BioGRID-ORCS; 67574; 7 hits in 75 CRISPR screens.
DR ChiTaRS; Alg13; mouse.
DR PRO; PR:Q9D8C3; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9D8C3; protein.
DR Bgee; ENSMUSG00000041718; Expressed in animal zygote and 235 other tissues.
DR ExpressionAtlas; Q9D8C3; baseline and differential.
DR Genevisible; Q9D8C3; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004577; F:N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:1901215; P:negative regulation of neuron death; IMP:MGI.
DR GO; GO:1904262; P:negative regulation of TORC1 signaling; IMP:MGI.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IMP:MGI.
DR CDD; cd04508; TUDOR; 1.
DR InterPro; IPR007235; Glyco_trans_28_C.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR002999; Tudor.
DR Pfam; PF04101; Glyco_tran_28_C; 1.
DR Pfam; PF02338; OTU; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50802; OTU; 1.
DR PROSITE; PS50304; TUDOR; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Glycosyltransferase;
KW Hydrolase; Multifunctional enzyme; Protease; Reference proteome;
KW Thiol protease; Transferase; Ubl conjugation pathway.
FT CHAIN 1..1166
FT /note="Putative bifunctional UDP-N-acetylglucosamine
FT transferase and deubiquitinase ALG13"
FT /id="PRO_0000254574"
FT DOMAIN 225..346
FT /note="OTU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00139"
FT DOMAIN 486..546
FT /note="Tudor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT REGION 1..125
FT /note="Glycosyltransferase activity"
FT /evidence="ECO:0000250"
FT REGION 126..394
FT /note="Deubiquitinase activity"
FT /evidence="ECO:0000250"
FT REGION 393..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 921..966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 998..1056
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..437
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..960
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1002..1030
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1031..1056
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 233
FT /note="For deubiquitinase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 236
FT /note="Nucleophile; for deubiquitinase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 339
FT /note="For deubiquitinase activity"
FT /evidence="ECO:0000250"
FT VAR_SEQ 128..165
FT /note="RVLSCPAPVSLLLVLLGSAKILQQLPSATLSCFGYLPT -> STLPGLLQSM
FT DLSTLKCYPPGQPEKFSAFLDKVVGLQK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_039304"
FT VAR_SEQ 166..1166
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_039305"
FT CONFLICT Q9D8C3-2:149
FT /note="Q -> H (in Ref. 1; BAB29554)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1166 AA; 128664 MW; 5F045ACF188BBE8A CRC64;
MKRAFVTVGT TSFDELVARV VANDCVQILE SLGYNHLVLQ VGRGTVVPKP FRTESFTLDV
YRYKDSLKED LQQADLVISH AGAGSCLESL EKGKPLVVVV NEKLMNNHQF ELAKQLHKEG
HLFYCTCRVL SCPAPVSLLL VLLGSAKILQ QLPSATLSCF GYLPTQAPVL VATAYSYLHS
VFSSFPPLST FLIIPCTMQK GWKKYCGQKS LNEASMDEYL GSLGLFRKVV AKDASCLFRA
ISEQLFHSQI HHLQIRRACV SYMKENQQAF ESYVEGSFEK YLERLGDPKE SAGQLELKAL
SLIYNRDFII YRYPGKPPTQ VTDNGFEDKI ILCYSNNGHY DSVYSKEFQS TAGICQAILY
ELLYKDVFVV DEETLKTAVD LFRSGSRRNK HHALTASVEG SSDQKSSTED RTEEAAACSS
AASTPEGNKQ GTERQKVPES PSKMLFPYKV LKALDPEIYR NVEFDAWLDS RKELQKSECV
EYGGRYYFLG DKCQVCMESG GKYYNAHIQE IDNDKSSVVV FIEEFAERHS IPLAHVRPVN
QVALLPSWNA IPIRNGRGYP TITGGYFPEI VMTDMNMKQR KKMFKKFRGK EIYMTMAYSR
GDPLVPSRIQ HSMHYGHDPL LYYSQTAGHI LSSQHFYPQH SSQRQGRGYG MPRDSSHLIS
KQNLPNPKVG FCSGSGRKCC QSYDNVSYRS RSFRRSHRQM HCMNKGCQYG FAPENGVEET
VTFYALEEGN ETAYSTLPNN GGPTTMVPAT SGYCVARQGY NSCKPPLNSG DSNDHCDNGG
YHGDYLYSSE QGYETSSVYT TTVSTANLSL QDSGPSSVPQ DTVTSYNYPQ KVLENSAAIA
VSWASHVPVP VIPNCAGDNE ALRTSDISSQ NAIQPGFVPP PAQGSPAYLE PSAAGAAGAA
AAAAAAAAPV ATPVAAPLPL PPPLPPPPPA TLEAGDASGF PLPPPPPPPP PPPPPYSYDP
SGSDLPQDTK VLQYYFNLGL QCYHHNYWHP MVYMPHVQQQ LQPQPQPQPQ PQPQPQPQPQ
PQPQQPQQQQ PPPQQQQQQQ EQVHGESYPD CTEQPLVDQS APQVYSDVVR EDGTQADVST
NDTFPIADAV PLPHGAVYYP VMTDPYGSPL LGFDSYVPVA SDYSSIAMWH PVNAACGASA
QIHGAMNPGP IGYMLLPNSP HYTPQN
