KEG1_RAT
ID KEG1_RAT Reviewed; 295 AA.
AC Q9Z2Y0; Q68G42;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 106.
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=Hepatocellular carcinoma-enriched protein of 33 kDa;
DE Short=HP33;
DE AltName: Full=Kidney-expressed gene 1 protein;
GN Name=Keg1; Synonyms=Hp33;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=10194414; DOI=10.1242/jcs.112.9.1353;
RA Nakadai T., Kishimoto T., Miyazawa Y., Okada N., Makino Y., Obinata T.,
RA Tamura T.;
RT "HP33: hepatocellular carcinoma-enriched 33-kDa protein with similarity to
RT mitochondrial N-acyltransferase but localized in a microtubule-dependent
RT manner at the centrosome.";
RL J. Cell Sci. 112:1353-1364(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC 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 INTERACTION WITH GAMMA-TUBULIN.
RX PubMed=10470852; DOI=10.1093/dnares/6.3.207;
RA Nakadai T., Okada N., Makino Y., Tamura T.;
RT "Structure of rat gamma-tubulin and its binding to HP33.";
RL DNA Res. 6:207-209(1999).
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.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:10194414}. Note=Also localizes
CC in regions surrounding the centrosome. The centrosomal localization is
CC dependent on microtubules.
CC -!- TISSUE SPECIFICITY: Specifically expressed in kidney and liver. Up-
CC regulated in the regenerating liver as well as in hepatocellular
CC carcinoma. {ECO:0000269|PubMed:10194414}.
CC -!- SIMILARITY: Belongs to the glycine N-acyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AB019693; BAA34427.1; -; mRNA.
DR EMBL; BC078701; AAH78701.1; -; mRNA.
DR RefSeq; NP_599157.2; NM_134330.2.
DR AlphaFoldDB; Q9Z2Y0; -.
DR SMR; Q9Z2Y0; -.
DR STRING; 10116.ENSRNOP00000016593; -.
DR iPTMnet; Q9Z2Y0; -.
DR PhosphoSitePlus; Q9Z2Y0; -.
DR PaxDb; Q9Z2Y0; -.
DR PRIDE; Q9Z2Y0; -.
DR Ensembl; ENSRNOT00000016593; ENSRNOP00000016593; ENSRNOG00000012387.
DR GeneID; 171179; -.
DR KEGG; rno:171179; -.
DR UCSC; RGD:621231; rat.
DR CTD; 219970; -.
DR RGD; 621231; Keg1.
DR eggNOG; ENOG502SDQB; Eukaryota.
DR GeneTree; ENSGT00950000183133; -.
DR HOGENOM; CLU_060336_0_0_1; -.
DR InParanoid; Q9Z2Y0; -.
DR OMA; EAPCEWH; -.
DR OrthoDB; 1221333at2759; -.
DR PhylomeDB; Q9Z2Y0; -.
DR TreeFam; TF353258; -.
DR PRO; PR:Q9Z2Y0; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000012387; Expressed in adult mammalian kidney and 2 other tissues.
DR Genevisible; Q9Z2Y0; RN.
DR GO; GO:0005813; C:centrosome; NAS:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0043015; F:gamma-tubulin binding; NAS:UniProtKB.
DR GO; GO:0047961; F:glycine N-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016410; F:N-acyltransferase activity; IBA:GO_Central.
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_0000281877"
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:0000250|UniProtKB:Q9DCY0"
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:0000250|UniProtKB:Q9DCY0"
FT MOD_RES 124
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DCY0"
FT MOD_RES 124
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DCY0"
FT MOD_RES 128
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DCY0"
FT MOD_RES 128
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DCY0"
FT MOD_RES 140
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DCY0"
FT MOD_RES 140
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DCY0"
FT MOD_RES 150
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DCY0"
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"
FT CONFLICT 108
FT /note="A -> S (in Ref. 1; BAA34427)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 295 AA; 34016 MW; 8CDB7248EDAF2B2F CRC64;
MFYIQSSEAL QILKNSLRKH LPESLKVYGT VFHMNQGNPF KLKAVVDKWP DFNTVVIRPQ
EQDMTDDLDH YNNTYLIYSK DPKHCQEFLG SSDVINWKQH LQIQSSQADL GKVIENLGAT
NLGKVKHKQC FLYMVSHTAK KLTPSLVDAK HLVVSSEKPT PFDHQLFKFA RLDVKHAALV
NSIWYFGGNE KSQKFIERCI FTFPSVCIMG PEGTPVSWAL MDHTGELRMA GTLPKYRHQN
LIYHVAFHQV HTLEKLGFPM YLHVDKVNLT IQRMSAVLGH VPMPCTWNQW NWVPL
