EST2C_RAT
ID EST2C_RAT Reviewed; 561 AA.
AC O70631; G3V9D8;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 17-JUN-2020, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Acylcarnitine hydrolase;
DE Short=ACH M1;
DE EC=3.1.1.28;
DE AltName: Full=Carboxylic ester hydrolase {ECO:0000255|RuleBase:RU361235};
DE EC=3.1.1.- {ECO:0000255|RuleBase:RU361235};
DE Flags: Precursor;
GN Name=Ces2c {ECO:0000312|RGD:621510};
GN Synonyms=Ces2 {ECO:0000312|RGD:621510}, Ces2l {ECO:0000312|RGD:621510};
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 {ECO:0000312|EMBL:BAA25692.1};
RN [1] {ECO:0000312|EMBL:BAA25690.1, ECO:0000312|EMBL:BAA25692.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Wistar {ECO:0000312|EMBL:BAA25692.1};
RC TISSUE=Liver {ECO:0000312|EMBL:BAA25692.1};
RA Sone T., Sawada T., Kunitomo T., Takabatake E., Wang C.Y., Isobe M.;
RT "Molecular cloning and characterization of a phenobarbital-inducible
RT carboxylesterase in rat liver.";
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:BAD77829.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley {ECO:0000312|EMBL:BAD77829.1};
RC TISSUE=Liver {ECO:0000312|EMBL:BAD77829.1};
RX PubMed=15794950; DOI=10.1016/j.bcp.2005.01.017;
RA Furihata T., Hosokawa M., Fujii A., Derbel M., Satoh T., Chiba K.;
RT "Dexamethasone-induced methylprednisolone hemisuccinate hydrolase: its
RT identification as a member of the rat carboxylesterase 2 family and its
RT unique existence in plasma.";
RL Biochem. Pharmacol. 69:1287-1297(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12230550; DOI=10.1046/j.1432-1033.2002.03121.x;
RA Sanghani S.P., Davis W.I., Dumaual N.G., Mahrenholz A., Bosron W.F.;
RT "Identification of microsomal rat liver carboxylesterases and their
RT activity with retinyl palmitate.";
RL Eur. J. Biochem. 269:4387-4398(2002).
CC -!- FUNCTION: Hydrolase with high activity towards palmitoylcarnitine. Is
CC also active with p-nitrophenylacetate and alpha-naphthylacetate (By
CC similarity). May also hydrolyze retinyl esters (PubMed:12230550).
CC {ECO:0000250|UniProtKB:Q91WG0, ECO:0000269|PubMed:12230550}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinyl hexadecanoate + H2O = all-trans-retinol +
CC H(+) + hexadecanoate; Xref=Rhea:RHEA:13933, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336,
CC ChEBI:CHEBI:17616; Evidence={ECO:0000305|PubMed:12230550};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13934;
CC Evidence={ECO:0000305|PubMed:12230550};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-acyl-(R)-carnitine = (R)-carnitine + a fatty acid +
CC H(+); Xref=Rhea:RHEA:17101, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16347, ChEBI:CHEBI:28868, ChEBI:CHEBI:75659; EC=3.1.1.28;
CC Evidence={ECO:0000250|UniProtKB:Q91WG0};
CC -!- SUBCELLULAR LOCATION: Microsome {ECO:0000269|PubMed:12230550}.
CC Endoplasmic reticulum {ECO:0000250|UniProtKB:Q91WG0}.
CC -!- TISSUE SPECIFICITY: Expressed in liver, stomach and kidney.
CC {ECO:0000269|PubMed:12230550}.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000255, ECO:0000255|RuleBase:RU361235}.
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DR EMBL; AB010570; BAA25690.1; -; Genomic_DNA.
DR EMBL; AB010635; BAA25692.1; -; mRNA.
DR EMBL; AB191005; BAD77829.1; -; mRNA.
DR EMBL; AABR07007139; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07007140; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07007141; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07007143; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07007142; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07007144; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473986; EDL94590.1; -; Genomic_DNA.
DR RefSeq; NP_598270.1; NM_133586.2.
DR RefSeq; XP_017445895.1; XM_017590406.1.
DR RefSeq; XP_017445925.1; XM_017590436.1.
DR AlphaFoldDB; O70631; -.
DR SMR; O70631; -.
DR STRING; 10116.ENSRNOP00000043426; -.
DR ESTHER; ratno-pbcxe; Carb_B_Chordata.
DR MEROPS; S09.999; -.
DR GeneID; 171118; -.
DR KEGG; rno:171118; -.
DR CTD; 234671; -.
DR RGD; 621510; Ces2c.
DR RGD; 11416512; LOC108348093.
DR VEuPathDB; HostDB:ENSRNOG00000048823; -.
DR VEuPathDB; HostDB:ENSRNOG00000069933; -.
DR eggNOG; KOG1516; Eukaryota.
DR OrthoDB; 754103at2759; -.
DR PhylomeDB; O70631; -.
DR TreeFam; TF315470; -.
DR BRENDA; 3.1.1.1; 5301.
DR PRO; PR:O70631; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Proteomes; UP000234681; Chromosome 1.
DR Bgee; ENSRNOG00000036571; Expressed in duodenum and 16 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:UniProtKB.
DR GO; GO:0047619; F:acylcarnitine hydrolase activity; ISO:RGD.
DR GO; GO:0047376; F:all-trans-retinyl-palmitate hydrolase, all-trans-retinol forming activity; IEA:RHEA.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IDA:UniProtKB.
DR GO; GO:0001523; P:retinoid metabolic process; TAS:UniProtKB.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002018; CarbesteraseB.
DR InterPro; IPR019826; Carboxylesterase_B_AS.
DR InterPro; IPR019819; Carboxylesterase_B_CS.
DR Pfam; PF00135; COesterase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
DR PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Endoplasmic reticulum; Hydrolase; Lipid metabolism;
KW Microsome; Reference proteome; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255|RuleBase:RU361235"
FT CHAIN 27..561
FT /note="Acylcarnitine hydrolase"
FT /evidence="ECO:0000255|RuleBase:RU361235"
FT /id="PRO_5010896427"
FT ACT_SITE 230
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT ACT_SITE 347
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P23141"
FT ACT_SITE 459
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P23141"
FT DISULFID 97..125
FT /evidence="ECO:0000250|UniProtKB:P23141"
FT DISULFID 282..293
FT /evidence="ECO:0000250|UniProtKB:P23141"
FT CONFLICT 335
FT /note="H -> R (in Ref. 4; EDL94590)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 561 AA; 62170 MW; BB1B740129E15E2F CRC64;
MARKQPHSWL NAVLFGLLLI LIHVWGQDSP ESSSIRTTHT GQVRGKLDHV RDTKAGVHTF
LGIPFAKAPV GPLRFAPPED PEPWSGVRDG TSHPAMCLQN IDMLDEVGLT DMKMILSSIP
MSEDCLYLNI YTPAHAHEGS NLPVMVCIHG GALVIGMASM CDGSLLAVNE DLVVVAIQYR
LGVLGFFSTG DEHARGNWGY LDQVAALRWV QQNIAHFGGN PNRVTIFGVS AGGTSVSSHV
ISPMSQGLFH GAIMESGVAL LPDLISETSE TVSTTVAKLS GCEATDSETL VRCLRAKSGA
EILVINKVFK MIPAVVDGEF LPRHPKELLA SEDFHPVPSI IGVNTDEYCC TIPMVMGTAQ
IIKELSRENL QAVLKDTAAQ MMLPPECGDL LMEEYMGNTD DPQTLQIQYA EMMGDFLFVI
PALQVAHFQR SHAPVYFYEF QHAPSYFKNV RPPHVKADHA DEVPFVFGSF FWGIKVDFTE
EEKLLSRRMM KYWANFARHG NPNSEGLPYW PVLDHDEQYL QLDTQPAVDR ALKARRLQFW
TKTLPQKIQE LNGAQKNHAE L
