LYPL1_MOUSE
ID LYPL1_MOUSE Reviewed; 239 AA.
AC Q3UFF7; Q8R065;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Lysophospholipase-like protein 1 {ECO:0000305};
DE EC=3.1.2.22 {ECO:0000250|UniProtKB:Q5VWZ2};
GN Name=Lyplal1 {ECO:0000312|MGI:MGI:2385115};
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=Pancreas;
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 TISSUE=Mammary tumor;
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=Brain, Brown adipose tissue, Kidney, Liver, Pancreas, and Testis;
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).
CC -!- FUNCTION: Has depalmitoylating activity toward KCNMA1. Does not exhibit
CC phospholipase nor triacylglycerol lipase activity, able to hydrolyze
CC only short chain substrates due to its shallow active site (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + S-hexadecanoyl-L-cysteinyl-[protein] = H(+) +
CC hexadecanoate + L-cysteinyl-[protein]; Xref=Rhea:RHEA:19233,
CC Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:74151; EC=3.1.2.22;
CC Evidence={ECO:0000250|UniProtKB:Q5VWZ2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19234;
CC Evidence={ECO:0000250|UniProtKB:Q5VWZ2};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. AB hydrolase 2
CC family. {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; AK148533; BAE28604.1; -; mRNA.
DR EMBL; BC027340; AAH27340.1; -; mRNA.
DR CCDS; CCDS15600.1; -.
DR RefSeq; NP_666218.2; NM_146106.2.
DR AlphaFoldDB; Q3UFF7; -.
DR SMR; Q3UFF7; -.
DR BioGRID; 230556; 14.
DR STRING; 10090.ENSMUSP00000048229; -.
DR ChEMBL; CHEMBL3259491; -.
DR ESTHER; mouse-lypl1; LYsophospholipase_carboxylesterase.
DR iPTMnet; Q3UFF7; -.
DR PhosphoSitePlus; Q3UFF7; -.
DR SwissPalm; Q3UFF7; -.
DR jPOST; Q3UFF7; -.
DR MaxQB; Q3UFF7; -.
DR PaxDb; Q3UFF7; -.
DR PRIDE; Q3UFF7; -.
DR ProteomicsDB; 291979; -.
DR DNASU; 226791; -.
DR GeneID; 226791; -.
DR KEGG; mmu:226791; -.
DR CTD; 127018; -.
DR MGI; MGI:2385115; Lyplal1.
DR eggNOG; KOG2112; Eukaryota.
DR InParanoid; Q3UFF7; -.
DR OrthoDB; 1373549at2759; -.
DR PhylomeDB; Q3UFF7; -.
DR BioGRID-ORCS; 226791; 1 hit in 74 CRISPR screens.
DR PRO; PR:Q3UFF7; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q3UFF7; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IBA:GO_Central.
DR GO; GO:0008474; F:palmitoyl-(protein) hydrolase activity; IBA:GO_Central.
DR GO; GO:0042997; P:negative regulation of Golgi to plasma membrane protein transport; IMP:MGI.
DR GO; GO:0002084; P:protein depalmitoylation; IMP:MGI.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR003140; PLipase/COase/thioEstase.
DR Pfam; PF02230; Abhydrolase_2; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Hydrolase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q5VWZ2"
FT CHAIN 2..239
FT /note="Lysophospholipase-like protein 1"
FT /id="PRO_0000227558"
FT ACT_SITE 125
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 180
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 212
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q5VWZ2"
FT CONFLICT 58
FT /note="I -> T (in Ref. 2; AAH27340)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="I -> V (in Ref. 1; BAE28604)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="L -> Q (in Ref. 1; BAE28604)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 239 AA; 26354 MW; FFAEB2541158E73F CRC64;
MAAVPSAVHL PRCVVSPTGR HSASLIFLHG SGHSGQGQRE WIKHVLNQDL TFQHIKIIYP
TAPSRPYTPL KGGLSNVWFD RFKISMDCPE HLESIDSMCQ VLSGLIDEEV KTGIQKSRIL
IGGFSMGGCM AMHLAYRSHP DVAGVFVLSG FLNKASVVYQ DLQQGGRMLP ELFQCHGSAD
NLVLHAWGKE TNSKLKSLGV STTFHSLPNL NHELNKTELE KLKSWILTRL PGETDGQSE
