LIPM_MOUSE
ID LIPM_MOUSE Reviewed; 422 AA.
AC Q8K2A6; Q8BJ28;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Lipase member M;
DE EC=3.1.1.-;
DE AltName: Full=Lipase-like abhydrolase domain-containing protein 3;
DE Flags: Precursor;
GN Name=Lipm; Synonyms=Lipl3;
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=Mammary gland, Neonatal skin, and Vagina;
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 STRAIN=Czech II; 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).
CC -!- FUNCTION: Plays a highly specific role in the last step of keratinocyte
CC differentiation. May have an essential function in lipid metabolism of
CC the most differentiated epidermal layers (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; AK037091; BAC29699.1; -; mRNA.
DR EMBL; AK037214; BAC29757.1; -; mRNA.
DR EMBL; AK085719; BAC39517.1; -; mRNA.
DR EMBL; BC031933; AAH31933.1; -; mRNA.
DR CCDS; CCDS50419.1; -.
DR RefSeq; NP_076392.1; NM_023903.1.
DR RefSeq; XP_006527529.1; XM_006527466.3.
DR AlphaFoldDB; Q8K2A6; -.
DR SMR; Q8K2A6; -.
DR STRING; 10090.ENSMUSP00000025685; -.
DR ESTHER; mouse-LIPM; Acidic_Lipase.
DR MEROPS; S33.A58; -.
DR GlyGen; Q8K2A6; 1 site.
DR iPTMnet; Q8K2A6; -.
DR PhosphoSitePlus; Q8K2A6; -.
DR PaxDb; Q8K2A6; -.
DR PRIDE; Q8K2A6; -.
DR ProteomicsDB; 292333; -.
DR Antibodypedia; 56561; 71 antibodies from 12 providers.
DR Ensembl; ENSMUST00000025685; ENSMUSP00000025685; ENSMUSG00000056078.
DR GeneID; 78753; -.
DR KEGG; mmu:78753; -.
DR UCSC; uc008hga.2; mouse.
DR CTD; 340654; -.
DR MGI; MGI:1926003; Lipm.
DR VEuPathDB; HostDB:ENSMUSG00000056078; -.
DR eggNOG; KOG2624; Eukaryota.
DR GeneTree; ENSGT00940000156860; -.
DR HOGENOM; CLU_010974_0_0_1; -.
DR InParanoid; Q8K2A6; -.
DR OMA; GHMPTKA; -.
DR OrthoDB; 651396at2759; -.
DR PhylomeDB; Q8K2A6; -.
DR TreeFam; TF315485; -.
DR Reactome; R-MMU-6809371; Formation of the cornified envelope.
DR BioGRID-ORCS; 78753; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Lipm; mouse.
DR PRO; PR:Q8K2A6; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q8K2A6; protein.
DR Bgee; ENSMUSG00000056078; Expressed in esophagus and 40 other tissues.
DR Genevisible; Q8K2A6; MM.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR025483; Lipase_euk.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PIRSF; PIRSF000862; Steryl_ester_lip; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hydrolase; Lipid degradation;
KW Lipid metabolism; Reference proteome; Secreted; Signal.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..422
FT /note="Lipase member M"
FT /id="PRO_0000286830"
FT DOMAIN 92..392
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 186
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 357
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT ACT_SITE 386
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 260..269
FT /evidence="ECO:0000250"
FT CONFLICT 72
FT /note="I -> F (in Ref. 1; BAC29757)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 422 AA; 48254 MW; C6EFBC140963E051 CRC64;
MSEILSRVWT VSHRVEIWLL ILVAYLLQRN VNSGHLPTKA ADPEAFMNVS EIIKHKGYPS
EEYEVATEDG YILSVNRIPR GQTRLKKEGS RPVVLLQHGL LGDASNWISN LPNNSLGFIL
ADAGFDVWMG NSRGNTWSRK HKTLSIDQDE FWAFSYDEMA RFDLPAVINF ILQKTGQKKV
YYVGYSQGTT MGFIAFSTMP ELAHKIKMYF ALAPIATVKY ARSPGTKFLL LPDMMIKVLF
GRQEFLYQTR FFRQLFIYLC GQMILDQICS NIILLLGGFN TNNMNMSRAN VYVAHTPAGT
SVQNILHWSQ AVNSGELRAF DWGSETKNQE KCNQPTPIRY KVRDMMVPTA MWTGGQDWLS
NPDDVKTLLS EVTNLIYHKN IPEWAHVDFI WGLDAPQRVY NEIIHLMKQE PNLPQGTCRV
KL
