KEG1_MOUSE
ID KEG1_MOUSE Reviewed; 295 AA.
AC Q9DCY0;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Glycine N-acyltransferase-like protein Keg1;
DE EC=2.3.1.13;
DE AltName: Full=Acyl-CoA:glycine N-acyltransferase protein Keg1;
DE AltName: Full=Kidney-expressed gene 1 protein;
GN Name=Keg1;
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].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
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].
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 Liver;
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).
RN [4]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-124; LYS-128 AND LYS-140, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-43; LYS-83; LYS-124; LYS-128;
RP LYS-140 AND LYS-150, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- FUNCTION: Acyltransferase which transfers the acyl group to the N-
CC terminus of glycine. Can conjugate a multitude of substrates to form a
CC variety of N-acylglycines (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl-CoA + glycine = an N-acylglycine + CoA + H(+);
CC Xref=Rhea:RHEA:19869, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57670, ChEBI:CHEBI:58342; EC=2.3.1.13;
CC -!- SUBUNIT: Binds to microtubules. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250}. Note=Also localizes in regions
CC surrounding the centrosome. The centrosomal localization is dependent
CC on microtubules (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycine N-acyltransferase family.
CC {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; AK002360; BAB22039.1; -; mRNA.
DR EMBL; AK165515; BAE38231.1; -; mRNA.
DR EMBL; BC010803; AAH10803.1; -; mRNA.
DR CCDS; CCDS29636.1; -.
DR RefSeq; NP_083826.1; NM_029550.4.
DR AlphaFoldDB; Q9DCY0; -.
DR SMR; Q9DCY0; -.
DR STRING; 10090.ENSMUSP00000025598; -.
DR iPTMnet; Q9DCY0; -.
DR PhosphoSitePlus; Q9DCY0; -.
DR jPOST; Q9DCY0; -.
DR MaxQB; Q9DCY0; -.
DR PaxDb; Q9DCY0; -.
DR PeptideAtlas; Q9DCY0; -.
DR PRIDE; Q9DCY0; -.
DR ProteomicsDB; 264741; -.
DR DNASU; 64697; -.
DR Ensembl; ENSMUST00000025598; ENSMUSP00000025598; ENSMUSG00000024694.
DR GeneID; 64697; -.
DR KEGG; mmu:64697; -.
DR UCSC; uc008gul.2; mouse.
DR CTD; 64697; -.
DR MGI; MGI:1928492; Keg1.
DR VEuPathDB; HostDB:ENSMUSG00000024694; -.
DR eggNOG; ENOG502SDQB; Eukaryota.
DR GeneTree; ENSGT00950000183133; -.
DR InParanoid; Q9DCY0; -.
DR OMA; EAPCEWH; -.
DR OrthoDB; 1221333at2759; -.
DR PhylomeDB; Q9DCY0; -.
DR TreeFam; TF353258; -.
DR BioGRID-ORCS; 64697; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Keg1; mouse.
DR PRO; PR:Q9DCY0; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q9DCY0; protein.
DR Bgee; ENSMUSG00000024694; Expressed in right kidney and 53 other tissues.
DR ExpressionAtlas; Q9DCY0; baseline and differential.
DR Genevisible; Q9DCY0; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0047961; F:glycine N-acyltransferase activity; ISO:MGI.
DR GO; GO:0047962; F:glycine N-benzoyltransferase activity; ISO:MGI.
DR GO; GO:0016410; F:N-acyltransferase activity; IBA:GO_Central.
DR GO; GO:1901787; P:benzoyl-CoA metabolic process; ISO:MGI.
DR GO; GO:0006544; P:glycine metabolic process; ISO:MGI.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR010313; Glycine_N-acyltransferase.
DR InterPro; IPR013652; Glycine_N-acyltransferase_C.
DR InterPro; IPR015938; Glycine_N-acyltransferase_N.
DR PANTHER; PTHR15298; PTHR15298; 1.
DR Pfam; PF08444; Gly_acyl_tr_C; 1.
DR Pfam; PF06021; Gly_acyl_tr_N; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
PE 1: Evidence at protein level;
KW Acetylation; Acyltransferase; Cytoplasm; Cytoskeleton; Microtubule;
KW Reference proteome; Transferase.
FT CHAIN 1..295
FT /note="Glycine N-acyltransferase-like protein Keg1"
FT /id="PRO_0000281876"
FT MOD_RES 41
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q5FW57"
FT MOD_RES 41
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q5FW57"
FT MOD_RES 43
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 48
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q5FW57"
FT MOD_RES 48
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q5FW57"
FT MOD_RES 80
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q5FW57"
FT MOD_RES 83
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 124
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 124
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 128
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 128
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 140
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 140
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 150
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 255
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q5FW57"
FT MOD_RES 255
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q5FW57"
SQ SEQUENCE 295 AA; 33723 MW; 29D5D1D7B98534DC CRC64;
MFCLQSSQAL QVLENSLRKH LPESLKVYGT VFHINQGNPF KLKTLVDKWP DFNTVVIRPQ
EEDMTDDLDH YNNTYLVYSK DPKHCQEFLG SSEVINWKQH LQIQSSQSDL GKVIESLGAT
NLGKVKHKQC FLYMVCQTAK KLAPSLMDAK NLVVSRNKLT PLDQQLFKFA SLDVTHAALV
NSLWHFGGNE KSQKFIERCI FTFPSFCIMG PEGTPVSWTL MDHTGELRMG GTLPKYRRQS
LIYHVASQQI QTLEKLGFPM YAHVDKANFT VQRMVGLLGQ ILLPCTWNQW NCVPL
