ID LIPN_MOUSE Reviewed; 400 AA.
AC Q3U4B4;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE RecName: Full=Lipase member N;
DE EC=3.1.1.-;
DE AltName: Full=Lipase-like abhydrolase domain-containing protein 4;
DE Flags: Precursor;
GN Name=Lipn; Synonyms=Lipl4;
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=NOD; TISSUE=Dendritic cell;
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).
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; AK154333; BAE32519.1; -; mRNA.
DR CCDS; CCDS37962.1; -.
DR RefSeq; NP_081616.1; NM_027340.2.
DR RefSeq; XP_006527396.1; XM_006527333.2.
DR AlphaFoldDB; Q3U4B4; -.
DR SMR; Q3U4B4; -.
DR BioGRID; 213899; 1.
DR STRING; 10090.ENSMUSP00000025682; -.
DR ESTHER; mouse-LIPN; Acidic_Lipase.
DR GlyCosmos; Q3U4B4; 1 site, No reported glycans.
DR GlyGen; Q3U4B4; 1 site.
DR PaxDb; 10090-ENSMUSP00000025682; -.
DR ProteomicsDB; 290036; -.
DR Antibodypedia; 48305; 85 antibodies from 12 providers.
DR Ensembl; ENSMUST00000025682.12; ENSMUSP00000025682.6; ENSMUSG00000024770.15.
DR GeneID; 70166; -.
DR KEGG; mmu:70166; -.
DR UCSC; uc008hfz.1; mouse.
DR AGR; MGI:1917416; -.
DR CTD; 643418; -.
DR MGI; MGI:1917416; Lipn.
DR VEuPathDB; HostDB:ENSMUSG00000024770; -.
DR eggNOG; KOG2624; Eukaryota.
DR GeneTree; ENSGT00940000161695; -.
DR HOGENOM; CLU_010974_0_0_1; -.
DR InParanoid; Q3U4B4; -.
DR OMA; MFGTKGF; -.
DR OrthoDB; 5474043at2759; -.
DR PhylomeDB; Q3U4B4; -.
DR TreeFam; TF315485; -.
DR Reactome; R-MMU-6809371; Formation of the cornified envelope.
DR BioGRID-ORCS; 70166; 1 hit in 77 CRISPR screens.
DR ChiTaRS; Lipn; mouse.
DR PRO; PR:Q3U4B4; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q3U4B4; Protein.
DR Bgee; ENSMUSG00000024770; Expressed in lumbar subsegment of spinal cord and 14 other cell types or tissues.
DR ExpressionAtlas; Q3U4B4; baseline and differential.
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; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR025483; Lipase_euk.
DR PANTHER; PTHR11005:SF16; LIPASE MEMBER N; 1.
DR PANTHER; PTHR11005; LYSOSOMAL ACID LIPASE-RELATED; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PIRSF; PIRSF000862; Steryl_ester_lip; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..400
FT /note="Lipase member N"
FT /id="PRO_0000286832"
FT DOMAIN 81..381
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 175
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 346
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT ACT_SITE 375
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT CARBOHYD 274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 249..258
FT /evidence="ECO:0000250"
SQ SEQUENCE 400 AA; 45744 MW; 6C5A5B201EA5905A CRC64;
MPMMWLFLTT ACLIPGTLSA GGFLDFENKV NPEVWMNASE IIMYNGYPSE EYDVTTADGY
ILAINRIPHG RAQTGQTGPR PVVYMQHALF ADNAYWLENF ANGSLGFILA DAGYDVWMGN
SRGNTWSRRH KTLSANEEKF WAFSFNEMAK YDLPGIIDFI VNKTGQEKLY FIGHSLGTTI
GFVAFSTMPE LAQRIKMNFA LGPVISFKYP TSVFTNLFLL PKSIIKLVFG TKGVLLEDKN
ARMSFITFCN QKLLQPLCSE FMSLWAGFNK KNMNMSRLDV YMAHAPTGSS IQNMLHIKQL
YRSDEFRAYD WGSEAENMNH YNQSYPPLYD LTAMKVPTAI WAGGHDVLVT PQDVARILPQ
ITNLRYFKQF PDWNHFDFVW GLDAPQRLYS KIISLMKEYF
//
