LIPK_MOUSE
ID LIPK_MOUSE Reviewed; 398 AA.
AC Q8BM14; Q7TML7;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Lipase member K;
DE EC=3.1.1.-;
DE AltName: Full=Lipase-like abhydrolase domain-containing protein 2;
DE Flags: Precursor;
GN Name=Lipk; Synonyms=Lipl2;
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] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=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] (ISOFORM 2).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BM14-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BM14-2; Sequence=VSP_025143;
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; AK037106; BAC29705.1; -; mRNA.
DR EMBL; AK162706; BAE37029.1; -; mRNA.
DR EMBL; BC055815; AAH55815.1; -; mRNA.
DR CCDS; CCDS57143.1; -. [Q8BM14-2]
DR CCDS; CCDS89381.1; -. [Q8BM14-1]
DR RefSeq; NP_001192278.1; NM_001205349.1. [Q8BM14-2]
DR RefSeq; NP_766425.1; NM_172837.4. [Q8BM14-1]
DR AlphaFoldDB; Q8BM14; -.
DR SMR; Q8BM14; -.
DR BioGRID; 232215; 1.
DR STRING; 10090.ENSMUSP00000053913; -.
DR ESTHER; mouse-LIPK; Acidic_Lipase.
DR GlyGen; Q8BM14; 2 sites.
DR PhosphoSitePlus; Q8BM14; -.
DR PaxDb; Q8BM14; -.
DR PRIDE; Q8BM14; -.
DR ProteomicsDB; 290034; -. [Q8BM14-1]
DR ProteomicsDB; 290035; -. [Q8BM14-2]
DR Antibodypedia; 56554; 105 antibodies from 15 providers.
DR DNASU; 240633; -.
DR Ensembl; ENSMUST00000054260; ENSMUSP00000053913; ENSMUSG00000024771. [Q8BM14-2]
DR Ensembl; ENSMUST00000225505; ENSMUSP00000152955; ENSMUSG00000024771. [Q8BM14-1]
DR GeneID; 240633; -.
DR KEGG; mmu:240633; -.
DR UCSC; uc008hfx.2; mouse. [Q8BM14-1]
DR UCSC; uc012bkr.2; mouse. [Q8BM14-2]
DR CTD; 643414; -.
DR MGI; MGI:2679259; Lipk.
DR VEuPathDB; HostDB:ENSMUSG00000024771; -.
DR eggNOG; KOG2624; Eukaryota.
DR GeneTree; ENSGT00940000160031; -.
DR HOGENOM; CLU_010974_0_0_1; -.
DR InParanoid; Q8BM14; -.
DR OMA; WGLNIKE; -.
DR OrthoDB; 651396at2759; -.
DR PhylomeDB; Q8BM14; -.
DR TreeFam; TF315485; -.
DR Reactome; R-MMU-6809371; Formation of the cornified envelope.
DR BioGRID-ORCS; 240633; 4 hits in 77 CRISPR screens.
DR ChiTaRS; Lipk; mouse.
DR PRO; PR:Q8BM14; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q8BM14; protein.
DR Bgee; ENSMUSG00000024771; Expressed in esophagus and 27 other tissues.
DR ExpressionAtlas; Q8BM14; baseline and differential.
DR Genevisible; Q8BM14; MM.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
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 Alternative splicing; Disulfide bond; Glycoprotein; Hydrolase;
KW Lipid degradation; Lipid metabolism; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..398
FT /note="Lipase member K"
FT /id="PRO_0000286700"
FT DOMAIN 78..377
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 171
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 342
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT ACT_SITE 371
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 245..254
FT /evidence="ECO:0000250"
FT VAR_SEQ 34
FT /note="I -> IVCVFQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025143"
FT CONFLICT 4
FT /note="L -> F (in Ref. 2; AAH55815)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 398 AA; 45243 MW; 0D318436D38103CD CRC64;
MWWLLATTCC VLLSGPIDGY KQESITNPEA NMNISELISY WGYPYEKHDV ITEDGYILGT
YRIPHGKGCS RKTAPKAVVY LQHGLIASAN NWICNLPNNS LAFLLADSGY DVWLGNSRGN
TWSRNHLRLS PKSPQYWAFS WDEMAKYDLP ATVNLILEKS GQKQLFYVGH SQGTTIAFIA
FSTNPELAKK IRLFFALAPV ATVKYTRSPM KKLTTLSRKA VKVLFGDKMF STHTWFEQFI
ATKVCNRKLF HQLCSNFLFS LSGFDPQNLN MSRLDVYLSQ SPAGTSVQNM LHWAQAVNSG
QLQAFDWGNP DQNMMHFNQL TPPVYNISKM RVPTAMWSGG QDVVADAKDT KNLLPKIANL
IYYKEIPHYN HMDFYLGQDA PQEVYGDLIR MIEESLQN
