LIPK_HUMAN
ID LIPK_HUMAN Reviewed; 399 AA.
AC Q5VXJ0; A7KIH8;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 132.
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 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], 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).
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 -!- 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; EF426482; ABR08387.1; -; mRNA.
DR EMBL; AL358532; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS44455.1; -.
DR RefSeq; NP_001073987.1; NM_001080518.1.
DR RefSeq; XP_011538379.1; XM_011540077.1.
DR AlphaFoldDB; Q5VXJ0; -.
DR SMR; Q5VXJ0; -.
DR BioGRID; 568761; 12.
DR STRING; 9606.ENSP00000383900; -.
DR ESTHER; human-LIPK; Acidic_Lipase.
DR GlyConnect; 1459; 3 N-Linked glycans (1 site).
DR GlyGen; Q5VXJ0; 2 sites, 3 N-linked glycans (1 site).
DR iPTMnet; Q5VXJ0; -.
DR PhosphoSitePlus; Q5VXJ0; -.
DR BioMuta; LIPK; -.
DR DMDM; 147647699; -.
DR MassIVE; Q5VXJ0; -.
DR PaxDb; Q5VXJ0; -.
DR PeptideAtlas; Q5VXJ0; -.
DR PRIDE; Q5VXJ0; -.
DR ProteomicsDB; 65597; -.
DR Antibodypedia; 56554; 105 antibodies from 15 providers.
DR DNASU; 643414; -.
DR Ensembl; ENST00000404190.3; ENSP00000383900.1; ENSG00000204021.5.
DR GeneID; 643414; -.
DR KEGG; hsa:643414; -.
DR MANE-Select; ENST00000404190.3; ENSP00000383900.1; NM_001080518.2; NP_001073987.1.
DR UCSC; uc010qmv.3; human.
DR CTD; 643414; -.
DR DisGeNET; 643414; -.
DR GeneCards; LIPK; -.
DR HGNC; HGNC:23444; LIPK.
DR HPA; ENSG00000204021; Tissue enriched (skin).
DR MIM; 613922; gene.
DR neXtProt; NX_Q5VXJ0; -.
DR OpenTargets; ENSG00000204021; -.
DR PharmGKB; PA162394100; -.
DR VEuPathDB; HostDB:ENSG00000204021; -.
DR eggNOG; KOG2624; Eukaryota.
DR GeneTree; ENSGT00940000160031; -.
DR HOGENOM; CLU_010974_0_0_1; -.
DR InParanoid; Q5VXJ0; -.
DR OMA; WGLNIKE; -.
DR OrthoDB; 651396at2759; -.
DR PhylomeDB; Q5VXJ0; -.
DR TreeFam; TF315485; -.
DR PathwayCommons; Q5VXJ0; -.
DR Reactome; R-HSA-6809371; Formation of the cornified envelope.
DR BioGRID-ORCS; 643414; 9 hits in 1066 CRISPR screens.
DR GenomeRNAi; 643414; -.
DR Pharos; Q5VXJ0; Tbio.
DR PRO; PR:Q5VXJ0; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q5VXJ0; protein.
DR Bgee; ENSG00000204021; Expressed in skin of abdomen and 21 other tissues.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
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 Disulfide bond; Glycoprotein; Hydrolase; Lipid degradation;
KW Lipid metabolism; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..399
FT /note="Lipase member K"
FT /id="PRO_0000286699"
FT DOMAIN 78..378
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 172
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 343
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT ACT_SITE 372
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 246..255
FT /evidence="ECO:0000250"
FT VARIANT 331
FT /note="M -> I (in dbSNP:rs1214464)"
FT /id="VAR_032160"
FT VARIANT 391
FT /note="I -> T (in dbSNP:rs17112457)"
FT /id="VAR_032161"
SQ SEQUENCE 399 AA; 45563 MW; C12D8DFC294B176E CRC64;
MWQLLAAACW MLLLGSMYGY DKKGNNANPE ANMNISQIIS YWGYPYEEYD VTTKDGYILG
IYRIPHGRGC PGRTAPKPAV YLQHGLIASA SNWICNLPNN SLAFLLADSG YDVWLGNSRG
NTWSRKHLKL SPKSPEYWAF SLDEMAKYDL PATINFIIEK TGQKRLYYVG HSQGTTIAFI
AFSTNPELAK KIKIFFALAP VVTVKYTQSP MKKLTTLSRR VVKVLFGDKM FHPHTLFDQF
IATKVCNRKL FRRICSNFLF TLSGFDPQNL NMSRLDVYLS HNPAGTSVQN MLHWAQAVNS
GQLQAFDWGN SDQNMMHFHQ LTPPLYNITK MEVPTAIWNG GQDIVADPKD VENLLPQIAN
LIYYKLIPHY NHVDFYLGED APQEIYQDLI ILMEEYLQN
