CK054_RAT
ID CK054_RAT Reviewed; 315 AA.
AC Q5U2Q3;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Ester hydrolase C11orf54 homolog;
DE EC=3.1.-.-;
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 [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 [2]
RP PROTEIN SEQUENCE OF 26-43; 149-169 AND 245-263, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
CC -!- FUNCTION: Exhibits ester hydrolase activity on the substrate p-
CC nitrophenyl acetate. {ECO:0000250}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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DR EMBL; BC085915; AAH85915.1; -; mRNA.
DR RefSeq; NP_001014228.1; NM_001014206.1.
DR AlphaFoldDB; Q5U2Q3; -.
DR SMR; Q5U2Q3; -.
DR STRING; 10116.ENSRNOP00000014496; -.
DR iPTMnet; Q5U2Q3; -.
DR PhosphoSitePlus; Q5U2Q3; -.
DR SwissPalm; Q5U2Q3; -.
DR PaxDb; Q5U2Q3; -.
DR PRIDE; Q5U2Q3; -.
DR GeneID; 363016; -.
DR KEGG; rno:363016; -.
DR UCSC; RGD:1309534; rat.
DR CTD; 363016; -.
DR RGD; 1309534; RGD1309534.
DR VEuPathDB; HostDB:ENSRNOG00000010887; -.
DR eggNOG; KOG4048; Eukaryota.
DR HOGENOM; CLU_055541_0_0_1; -.
DR InParanoid; Q5U2Q3; -.
DR OMA; HIMPDFS; -.
DR OrthoDB; 877242at2759; -.
DR PhylomeDB; Q5U2Q3; -.
DR TreeFam; TF313169; -.
DR PRO; PR:Q5U2Q3; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000010887; Expressed in adult mammalian kidney and 19 other tissues.
DR Genevisible; Q5U2Q3; RN.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; ISO:RGD.
DR GO; GO:0008270; F:zinc ion binding; ISO:RGD.
DR InterPro; IPR015021; DUF1907.
DR PANTHER; PTHR13204; PTHR13204; 1.
DR Pfam; PF08925; DUF1907; 1.
DR SMART; SM01168; DUF1907; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase; Metal-binding; Nucleus;
KW Reference proteome; Zinc.
FT CHAIN 1..315
FT /note="Ester hydrolase C11orf54 homolog"
FT /id="PRO_0000246031"
FT BINDING 266
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 268
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 278
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 315 AA; 34993 MW; 61121CBB8E960CB2 CRC64;
MACTEFSFHV PSLEELAEVL QKGLKDNFAH VQVSVVDCPD LTKEPFTFPV KGICGQTRIA
EVGGVPYLLP LVNKKKVYDL NEIAKEIKLP GAFILGAGAG PFQTLGFNSE FMPIVQTASE
HHQPVNGSYF ARANPADGKC LLEKYSQKYP DFGCALLANL FASEGQPGKV IEVQAKKRTG
EHNFVSCMRQ TLEKHYGDKP VGMGGTFLVQ KGKVKAHIMP AEFSSCSLNS DEAVNQWLNF
YEMKAPLVCL PVFVSKDPGL DLRLEHTHFF SHHGEGGHYH YDTTPDTVEY LGYFSPAQFL
YRIDQPKETH AFGRD