YDJC_MOUSE
ID YDJC_MOUSE Reviewed; 310 AA.
AC Q14BV6; Q8C5Z5; Q9D8Z7;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Carbohydrate deacetylase {ECO:0000250|UniProtKB:Q53WD3};
DE EC=3.5.1.- {ECO:0000250|UniProtKB:Q53WD3};
GN Name=Ydjc;
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=Pancreas, 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).
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).
CC -!- FUNCTION: Probably catalyzes the deacetylation of acetylated
CC carbohydrates an important step in the degradation of oligosaccharides.
CC {ECO:0000250|UniProtKB:Q53WD3}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q53WD3};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q14BV6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14BV6-2; Sequence=VSP_032788;
CC -!- SIMILARITY: Belongs to the YdjC deacetylase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC36514.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK007503; BAB25075.1; -; mRNA.
DR EMBL; AK076869; BAC36514.1; ALT_FRAME; mRNA.
DR EMBL; BC115584; AAI15585.1; -; mRNA.
DR EMBL; BC115585; AAI15586.1; -; mRNA.
DR CCDS; CCDS27996.1; -. [Q14BV6-1]
DR RefSeq; NP_081216.1; NM_026940.4. [Q14BV6-1]
DR AlphaFoldDB; Q14BV6; -.
DR SMR; Q14BV6; -.
DR STRING; 10090.ENSMUSP00000069864; -.
DR iPTMnet; Q14BV6; -.
DR PhosphoSitePlus; Q14BV6; -.
DR EPD; Q14BV6; -.
DR MaxQB; Q14BV6; -.
DR PaxDb; Q14BV6; -.
DR PRIDE; Q14BV6; -.
DR ProteomicsDB; 275116; -. [Q14BV6-1]
DR ProteomicsDB; 275117; -. [Q14BV6-2]
DR Antibodypedia; 54203; 65 antibodies from 11 providers.
DR DNASU; 69101; -.
DR Ensembl; ENSMUST00000069064; ENSMUSP00000069864; ENSMUSG00000041774. [Q14BV6-1]
DR Ensembl; ENSMUST00000231726; ENSMUSP00000156244; ENSMUSG00000041774. [Q14BV6-2]
DR GeneID; 69101; -.
DR KEGG; mmu:69101; -.
DR UCSC; uc007ykg.1; mouse. [Q14BV6-2]
DR UCSC; uc007ykj.2; mouse. [Q14BV6-1]
DR CTD; 150223; -.
DR MGI; MGI:1916351; Ydjc.
DR VEuPathDB; HostDB:ENSMUSG00000041774; -.
DR eggNOG; ENOG502RYFJ; Eukaryota.
DR GeneTree; ENSGT00390000002575; -.
DR HOGENOM; CLU_064244_1_0_1; -.
DR InParanoid; Q14BV6; -.
DR OMA; HPQEGGC; -.
DR OrthoDB; 845079at2759; -.
DR PhylomeDB; Q14BV6; -.
DR TreeFam; TF329340; -.
DR BioGRID-ORCS; 69101; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Ydjc; mouse.
DR PRO; PR:Q14BV6; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q14BV6; protein.
DR Bgee; ENSMUSG00000041774; Expressed in spermatid and 156 other tissues.
DR ExpressionAtlas; Q14BV6; baseline and differential.
DR Genevisible; Q14BV6; MM.
DR GO; GO:0019213; F:deacetylase activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR006879; YdjC-like.
DR PANTHER; PTHR31609; PTHR31609; 1.
DR Pfam; PF04794; YdjC; 1.
DR SUPFAM; SSF88713; SSF88713; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Carbohydrate metabolism; Hydrolase; Magnesium;
KW Metal-binding; Reference proteome.
FT CHAIN 1..310
FT /note="Carbohydrate deacetylase"
FT /id="PRO_0000328775"
FT ACT_SITE 13
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q53WD3"
FT BINDING 14
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q53WD3"
FT BINDING 134
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q53WD3"
FT VAR_SEQ 202..310
FT /note="WTDAFVGLSTCGRHMSAHRVLGSLARALEDIPAGHALTAELMAHPGYPSVPP
FT AGGCGEGPDAFSCSWERLHELHVLTAPTLRAWLAQNGVQLCAIDDLDSKRPGEGVPL
FT -> DSSWSVTTAECSEGFAEFCSAGILPSLQTENQCDLGHTGGKGRSPESFLPCTLGIA
FT LGMWSVLCFPRIAV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032788"
FT CONFLICT 108
FT /note="Q -> P (in Ref. 1; BAC36514)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="P -> L (in Ref. 2; AAI15586)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="V -> E (in Ref. 1; BAC36514)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 310 AA; 33094 MW; 9D3302745CC24048 CRC64;
MAFPRVRLVV TADDFGYCPR RDEGIVEAFL AGTVTSVSLL VNGTAAESAA ELARRHSIPT
GLHANLSEGR PVGPARHNAS SLLSPEGFFL GKMGFREALA AGDVALPQVR EELEAQLSRF
RELLGRSPTH VDGHQHVHVL PGVCQVFAEA LQAYGVRFTR LPAERGVGSC AWLEAPARAF
ACTVERDARA AIGPFSRHGL RWTDAFVGLS TCGRHMSAHR VLGSLARALE DIPAGHALTA
ELMAHPGYPS VPPAGGCGEG PDAFSCSWER LHELHVLTAP TLRAWLAQNG VQLCAIDDLD
SKRPGEGVPL
