LIPM_HUMAN
ID LIPM_HUMAN Reviewed; 423 AA.
AC Q5VYY2; A6PVS3; B2RXK7; B5MCR3;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 139.
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 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), FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Keratinocyte;
RX PubMed=17562024; DOI=10.1186/gb-2007-8-6-r107;
RA Toulza E., Mattiuzzo N.R., Galliano M.F., Jonca N., Dossat C., Jacob D.,
RA de Daruvar A., Wincker P., Serre G., Guerrin M.;
RT "Large-scale identification of human genes implicated in epidermal barrier
RT function.";
RL Genome Biol. 8:R107.1-R107.23(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(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: 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.
CC {ECO:0000269|PubMed:17562024}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5VYY2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5VYY2-2; Sequence=VSP_056261;
CC -!- TISSUE SPECIFICITY: Exclusively expressed in the epidermis within the
CC granular keratinocytes. {ECO:0000269|PubMed:17562024}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; EF426484; ABR08389.1; -; mRNA.
DR EMBL; AL353113; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL358532; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC157888; AAI57889.1; -; mRNA.
DR EMBL; BC171908; AAI71908.1; -; mRNA.
DR CCDS; CCDS44457.1; -. [Q5VYY2-1]
DR RefSeq; NP_001121687.1; NM_001128215.1. [Q5VYY2-1]
DR AlphaFoldDB; Q5VYY2; -.
DR SMR; Q5VYY2; -.
DR STRING; 9606.ENSP00000383901; -.
DR ESTHER; human-LIPM; Acidic_Lipase.
DR GlyGen; Q5VYY2; 1 site.
DR iPTMnet; Q5VYY2; -.
DR PhosphoSitePlus; Q5VYY2; -.
DR BioMuta; LIPM; -.
DR DMDM; 147647745; -.
DR MassIVE; Q5VYY2; -.
DR PaxDb; Q5VYY2; -.
DR PeptideAtlas; Q5VYY2; -.
DR PRIDE; Q5VYY2; -.
DR ProteomicsDB; 3465; -.
DR ProteomicsDB; 65658; -. [Q5VYY2-1]
DR Antibodypedia; 56561; 71 antibodies from 12 providers.
DR DNASU; 340654; -.
DR Ensembl; ENST00000404743.9; ENSP00000383901.3; ENSG00000173239.14. [Q5VYY2-1]
DR Ensembl; ENST00000539337.2; ENSP00000440375.1; ENSG00000173239.14. [Q5VYY2-2]
DR GeneID; 340654; -.
DR KEGG; hsa:340654; -.
DR MANE-Select; ENST00000404743.9; ENSP00000383901.3; NM_001128215.1; NP_001121687.1.
DR UCSC; uc009xtm.2; human. [Q5VYY2-1]
DR CTD; 340654; -.
DR DisGeNET; 340654; -.
DR GeneCards; LIPM; -.
DR HGNC; HGNC:23455; LIPM.
DR HPA; ENSG00000173239; Tissue enriched (skin).
DR MIM; 613923; gene.
DR neXtProt; NX_Q5VYY2; -.
DR OpenTargets; ENSG00000173239; -.
DR PharmGKB; PA162394101; -.
DR VEuPathDB; HostDB:ENSG00000173239; -.
DR eggNOG; KOG2624; Eukaryota.
DR GeneTree; ENSGT00940000156860; -.
DR HOGENOM; CLU_010974_0_0_1; -.
DR InParanoid; Q5VYY2; -.
DR OMA; GHMPTKA; -.
DR OrthoDB; 651396at2759; -.
DR PhylomeDB; Q5VYY2; -.
DR TreeFam; TF315485; -.
DR PathwayCommons; Q5VYY2; -.
DR Reactome; R-HSA-6809371; Formation of the cornified envelope.
DR BioGRID-ORCS; 340654; 19 hits in 1065 CRISPR screens.
DR GenomeRNAi; 340654; -.
DR Pharos; Q5VYY2; Tbio.
DR PRO; PR:Q5VYY2; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q5VYY2; protein.
DR Bgee; ENSG00000173239; Expressed in skin of leg and 28 other tissues.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0004465; F:lipoprotein lipase activity; TAS:Reactome.
DR GO; GO:0070268; P:cornification; TAS:Reactome.
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..33
FT /evidence="ECO:0000255"
FT CHAIN 34..423
FT /note="Lipase member M"
FT /id="PRO_0000286829"
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 VAR_SEQ 1..49
FT /note="MLETLSRQWIVSHRMEMWLLILVAYMFQRNVNSVHMPTKAVDPEAFMNI ->
FT MTRPLDRKQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056261"
FT VARIANT 274
FT /note="L -> S (in dbSNP:rs3910680)"
FT /id="VAR_059382"
FT VARIANT 418
FT /note="R -> W (in dbSNP:rs11202862)"
FT /id="VAR_032191"
SQ SEQUENCE 423 AA; 48233 MW; 9B622EEB88F05478 CRC64;
MLETLSRQWI VSHRMEMWLL ILVAYMFQRN VNSVHMPTKA VDPEAFMNIS EIIQHQGYPC
EEYEVATEDG YILSVNRIPR GLVQPKKTGS RPVVLLQHGL VGGASNWISN LPNNSLGFIL
ADAGFDVWMG NSRGNAWSRK HKTLSIDQDE FWAFSYDEMA RFDLPAVINF ILQKTGQEKI
YYVGYSQGTT MGFIAFSTMP ELAQKIKMYF ALAPIATVKH AKSPGTKFLL LPDMMIKGLF
GKKEFLYQTR FLRQLVIYLC GQVILDQICS NIMLLLGGFN TNNMNMSRAS VYAAHTLAGT
SVQNILHWSQ AVNSGELRAF DWGSETKNLE KCNQPTPVRY RVRDMTVPTA MWTGGQDWLS
NPEDVKMLLS EVTNLIYHKN IPEWAHVDFI WGLDAPHRMY NEIIHLMQQE ETNLSQGRCE
AVL
