CES1P_HUMAN
ID CES1P_HUMAN Reviewed; 287 AA.
AC Q9UKY3; A2RRL8; B9ZVS2;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Putative inactive carboxylesterase 4;
DE AltName: Full=Inactive carboxylesterase 1 pseudogene 1;
DE AltName: Full=Placental carboxylesterase 3;
DE Short=PCE-3;
DE Flags: Precursor;
GN Name=CES1P1; Synonyms=CES4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Placenta;
RX PubMed=10452915; DOI=10.1053/plac.1999.0407;
RA Yan B., Matoney L., Yang D.;
RT "Human carboxylesterases in term placentae: enzymatic characterization,
RT molecular cloning and evidence for the existence of multiple forms.";
RL Placenta 20:599-607(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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: Has no esterase activity. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UKY3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UKY3-2; Sequence=VSP_029004;
CC -!- TISSUE SPECIFICITY: Expressed in placenta.
CC {ECO:0000269|PubMed:10452915}.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
CC -!- CAUTION: In contrast to other members of the family, it is shorter and
CC lacks the C-terminal part that contains the conserved Glu and His
CC active sites. {ECO:0000305}.
CC -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF14185.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF106005; AAF14185.1; ALT_FRAME; mRNA.
DR EMBL; AC136621; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC131699; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; Q9UKY3; -.
DR SMR; Q9UKY3; -.
DR DrugBank; DB08612; 1,1,1-TRIFLUORO-3-(OCTYLTHIO)ACETONE.
DR MEROPS; S09.986; -.
DR GlyGen; Q9UKY3; 1 site.
DR BioMuta; HGNC:18546; -.
DR DMDM; 215273984; -.
DR jPOST; Q9UKY3; -.
DR MassIVE; Q9UKY3; -.
DR MaxQB; Q9UKY3; -.
DR PeptideAtlas; Q9UKY3; -.
DR PRIDE; Q9UKY3; -.
DR ProteomicsDB; 84910; -. [Q9UKY3-1]
DR ProteomicsDB; 84911; -. [Q9UKY3-2]
DR GeneCards; CES1P1; -.
DR HGNC; HGNC:18546; CES1P1.
DR neXtProt; NX_Q9UKY3; -.
DR InParanoid; Q9UKY3; -.
DR PhylomeDB; Q9UKY3; -.
DR PathwayCommons; Q9UKY3; -.
DR Pharos; Q9UKY3; Tdark.
DR PRO; PR:Q9UKY3; -.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; Q9UKY3; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005811; C:lipid droplet; IBA:GO_Central.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IBA:GO_Central.
DR GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
DR GO; GO:0016042; P:lipid catabolic process; IBA:GO_Central.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002018; CarbesteraseB.
DR InterPro; IPR019819; Carboxylesterase_B_CS.
DR Pfam; PF00135; COesterase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
PE 5: Uncertain;
KW Alternative splicing; Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..287
FT /note="Putative inactive carboxylesterase 4"
FT /id="PRO_0000308588"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..136
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029004"
FT CONFLICT 19
FT /note="G -> V (in Ref. 1; AAF14185)"
FT /evidence="ECO:0000305"
FT CONFLICT 21
FT /note="L -> P (in Ref. 1; AAF14185)"
FT /evidence="ECO:0000305"
FT CONFLICT 26
FT /note="L -> V (in Ref. 1; AAF14185)"
FT /evidence="ECO:0000305"
FT CONFLICT 30
FT /note="L -> V (in Ref. 1; AAF14185)"
FT /evidence="ECO:0000305"
FT CONFLICT 39
FT /note="V -> I (in Ref. 1; AAF14185)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="L -> P (in Ref. 1; AAF14185)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="N -> S (in Ref. 1; AAF14185)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="S -> L (in Ref. 1; AAF14185)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="W -> C (in Ref. 3; BC131699)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="V -> A (in Ref. 1; AAF14185 and 3; BC131699)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="R -> W (in Ref. 1; AAF14185 and 3; BC131699)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="P -> H (in Ref. 1; AAF14185 and 3; BC131699)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 287 AA; 30679 MW; 2CB2AAECEE2C81BD CRC64;
MWLPALVLAT LAASAAWAGH LSSPPLVDTL HGKVLGKFVS LEGFAQPVAV FLGIPFAKPP
LGPLRFTLPQ PAEPWNFVKN ATSYPPMFTQ DPKAGQLISE LFTNRKENIP LKLSEDCLYL
NIYTPADLTK KNRLPVMVWI HGGGLMVGAA STYDGLALAA HENVVVVTIQ YRLGIWGFFS
TGDEHSPGNW GHLDQLAALH WVQDNIASFG GNPGSVTIFG GSVGGESVSV LVLSPLAKNL
FHRAISESGV ALTSVLVKKG DVKPLAEVGL RLVRLRLDTP TSLALCS
