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P54310

- LIPS_MOUSE

UniProt

P54310 - LIPS_MOUSE

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Protein

Hormone-sensitive lipase

Gene

Lipe

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

In adipose tissue and heart, it primarily hydrolyzes stored triglycerides to free fatty acids, while in steroidogenic tissues, it principally converts cholesteryl esters to free cholesterol for steroid hormone production.1 Publication

Catalytic activityi

Diacylglycerol + H2O = monoacylglycerol + a carboxylate.
Triacylglycerol + H2O = diacylglycerol + a carboxylate.
Monoacylglycerol + H2O = glycerol + a carboxylate.

Enzyme regulationi

Rapidly activated by cAMP-dependent phosphorylation under the influence of catecholamines. Dephosphorylation and inactivation are controlled by insulin (By similarity). Interacts with PLIN5.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei349 – 3491PROSITE-ProRule annotation
Active sitei423 – 4231PROSITE-ProRule annotation

GO - Molecular functioni

  1. hormone-sensitive lipase activity Source: UniProtKB-EC
  2. protein kinase binding Source: UniProtKB
  3. rRNA primary transcript binding Source: UniProtKB
  4. triglyceride lipase activity Source: MGI

GO - Biological processi

  1. cholesterol metabolic process Source: UniProtKB-KW
  2. diacylglycerol catabolic process Source: MGI
  3. lipid catabolic process Source: UniProtKB
  4. long-chain fatty acid catabolic process Source: MGI
  5. termination of RNA polymerase I transcription Source: UniProtKB
  6. transcription initiation from RNA polymerase I promoter Source: UniProtKB
  7. triglyceride catabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Cholesterol metabolism, Lipid degradation, Lipid metabolism, Steroid metabolism, Sterol metabolism

Enzyme and pathway databases

BRENDAi3.1.1.79. 3474.
UniPathwayiUPA00256.

Protein family/group databases

MEROPSiS09.993.

Names & Taxonomyi

Protein namesi
Recommended name:
Hormone-sensitive lipase (EC:3.1.1.79)
Short name:
HSL
Gene namesi
Name:Lipe
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:96790. Lipe.

Subcellular locationi

Cell membrane By similarity. Membranecaveola By similarity. Cytoplasmcytosol By similarity
Note: Found in the high-density caveolae. Translocates to the cytoplasm from the caveolae upon insulin stimulation.By similarity

GO - Cellular componenti

  1. caveola Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. cytosol Source: MGI
  4. lipid particle Source: UniProtKB
  5. mitochondrion Source: UniProtKB
  6. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 759759Hormone-sensitive lipasePRO_0000071548Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei557 – 5571PhosphoserineBy similarity
Modified residuei559 – 5591Phosphoserine; by AMPK1 Publication
Modified residuei650 – 6501PhosphoserineBy similarity
Modified residuei651 – 6511PhosphoserineBy similarity

Post-translational modificationi

Phosphorylation by AMPK may block translocation to lipid droplets.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP54310.
PaxDbiP54310.
PRIDEiP54310.

PTM databases

PhosphoSiteiP54310.

Expressioni

Gene expression databases

BgeeiP54310.
CleanExiMM_LIPE.
ExpressionAtlasiP54310. baseline and differential.
GenevestigatoriP54310.

Interactioni

Subunit structurei

Interacts with PTRF in the adipocyte cytoplasm.By similarity

Structurei

3D structure databases

ProteinModelPortaliP54310.
SMRiP54310. Positions 334-524.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi349 – 3513Involved in the stabilization of the negatively charged intermediate by the formation of the oxyanion holeBy similarity

Sequence similaritiesi

Belongs to the 'GDXG' lipolytic enzyme family.Curated

Phylogenomic databases

eggNOGiCOG0657.
GeneTreeiENSGT00730000111056.
HOGENOMiHOG000047722.
HOVERGENiHBG000187.
InParanoidiP54310.
KOiK07188.
OrthoDBiEOG7KSX7S.
TreeFamiTF314423.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR013094. AB_hydrolase_3.
IPR010468. HSL_N.
IPR002168. Lipase_GDXG_AS.
[Graphical view]
PfamiPF07859. Abhydrolase_3. 2 hits.
PF06350. HSL_N. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 2 hits.
PROSITEiPS01173. LIPASE_GDXG_HIS. 1 hit.
PS01174. LIPASE_GDXG_SER. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P54310-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDLRTMTQSL VTLAEDNMAF FSSQGPGETA RRLSNVFAGV REQALGLEPT
60 70 80 90 100
LGQLLGVAHH FDLDTETPAN GYRSLVHTAR CCLAHLLHKS RYVASNRKSI
110 120 130 140 150
FFRASHNLAE LEAYLAALTQ LRAMAYYAQR LLTINRPGVL FFEGDEGLTA
160 170 180 190 200
DFLQEYVTLH KGCFYGRCLG FQFTPAIRPF LQTLSIGLVS FGEHYKRNET
210 220 230 240 250
GLSVTASSLF TGGRFAIDPE LRGAEFERII QNLDVHFWKA FWNITEIEVL
260 270 280 290 300
SSLANMASTT VRVSRLLSLP PEAFEMPLTS DPRLTVTISP PLAHTGPAPV
310 320 330 340 350
LARLISYDLR EGQDSKVLNS LAKSEGPRLE LRPRPHQAPR SRALVVHIHG
360 370 380 390 400
GGFVAQTSKS HEPYLKNWAQ ELGVPIFSID YSLAPEAPFP RALEECFFAY
410 420 430 440 450
CWAVKHCDLL GSTGERICLA GDSAGGNLCI TVSLRAAAYG VRVPDGIMAA
460 470 480 490 500
YPVTTLQSSA SPSRLLSLMD PLLPLSVLSK CVSAYSGTEA EDHFDSDQKA
510 520 530 540 550
LGVMGLVQRD TSLFLRDLRL GASSWLNSFL ELSGRKPQKT TSPTAESVRP
560 570 580 590 600
TESMRRSVSE AALAQPEGLL GTDTLKKLTI KDLSNSEPSD SPEMSQSMET
610 620 630 640 650
LGPSTPSDVN FFLRPGNSQE EAEAKDEVRP MDGVPRVRAA FPEGFHPRRS
660 670 680 690 700
SQGVLHMPLY TSPIVKNPFM SPLLAPDSML KTLPPVHLVA CALDPMLDDS
710 720 730 740 750
VMFARRLRDL GQPVTLKVVE DLPHGFLSLA ALCRETRQAT EFCVQRIRLI

LTPPAAPLN
Length:759
Mass (Da):83,348
Last modified:January 24, 2006 - v2
Checksum:i3419AF52F6C85FF4
GO
Isoform 2 (identifier: P54310-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MEPAVESAPVGAQASKQGKEGSKNRSRRRWRKGKIKASAFSHSM

Show »
Length:802
Mass (Da):88,027
Checksum:i3D0D4870E898AE5B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti113 – 1131A → T in BAE41414. (PubMed:16141072)Curated
Sequence conflicti311 – 3111E → D in BAE41414. (PubMed:16141072)Curated
Sequence conflicti330 – 3312EL → DV in AAC52163. (PubMed:7698747)Curated
Sequence conflicti530 – 5301L → P in AAC52163. (PubMed:7698747)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MEPAVESAPVGAQASKQGKE GSKNRSRRRWRKGKIKASAF SHSM in isoform 2. 1 PublicationVSP_053335

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U08188 mRNA. Translation: AAC52163.1.
AF179427 Genomic DNA. Translation: AAC53069.1.
AC162443 Genomic DNA. No translation available.
AC169209 Genomic DNA. No translation available.
AK029984 mRNA. Translation: BAC26716.1.
AK169858 mRNA. Translation: BAE41414.1.
BC021642 mRNA. Translation: AAH21642.1.
CCDSiCCDS20981.1. [P54310-2]
CCDS20982.1. [P54310-1]
PIRiI49007.
RefSeqiNP_001034596.1. NM_001039507.2. [P54310-1]
NP_034849.2. NM_010719.5. [P54310-2]
XP_006539634.1. XM_006539571.1. [P54310-1]
XP_006539635.1. XM_006539572.1. [P54310-1]
UniGeneiMm.158548.
Mm.333679.

Genome annotation databases

EnsembliENSMUST00000003207; ENSMUSP00000003207; ENSMUSG00000003123. [P54310-2]
ENSMUST00000054301; ENSMUSP00000050935; ENSMUSG00000003123. [P54310-1]
GeneIDi16890.
KEGGimmu:16890.
UCSCiuc009fsp.1. mouse. [P54310-1]
uc009fsr.1. mouse.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U08188 mRNA. Translation: AAC52163.1 .
AF179427 Genomic DNA. Translation: AAC53069.1 .
AC162443 Genomic DNA. No translation available.
AC169209 Genomic DNA. No translation available.
AK029984 mRNA. Translation: BAC26716.1 .
AK169858 mRNA. Translation: BAE41414.1 .
BC021642 mRNA. Translation: AAH21642.1 .
CCDSi CCDS20981.1. [P54310-2 ]
CCDS20982.1. [P54310-1 ]
PIRi I49007.
RefSeqi NP_001034596.1. NM_001039507.2. [P54310-1 ]
NP_034849.2. NM_010719.5. [P54310-2 ]
XP_006539634.1. XM_006539571.1. [P54310-1 ]
XP_006539635.1. XM_006539572.1. [P54310-1 ]
UniGenei Mm.158548.
Mm.333679.

3D structure databases

ProteinModelPortali P54310.
SMRi P54310. Positions 334-524.
ModBasei Search...
MobiDBi Search...

Chemistry

ChEMBLi CHEMBL5935.

Protein family/group databases

MEROPSi S09.993.

PTM databases

PhosphoSitei P54310.

Proteomic databases

MaxQBi P54310.
PaxDbi P54310.
PRIDEi P54310.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000003207 ; ENSMUSP00000003207 ; ENSMUSG00000003123 . [P54310-2 ]
ENSMUST00000054301 ; ENSMUSP00000050935 ; ENSMUSG00000003123 . [P54310-1 ]
GeneIDi 16890.
KEGGi mmu:16890.
UCSCi uc009fsp.1. mouse. [P54310-1 ]
uc009fsr.1. mouse.

Organism-specific databases

CTDi 3991.
MGIi MGI:96790. Lipe.

Phylogenomic databases

eggNOGi COG0657.
GeneTreei ENSGT00730000111056.
HOGENOMi HOG000047722.
HOVERGENi HBG000187.
InParanoidi P54310.
KOi K07188.
OrthoDBi EOG7KSX7S.
TreeFami TF314423.

Enzyme and pathway databases

UniPathwayi UPA00256 .
BRENDAi 3.1.1.79. 3474.

Miscellaneous databases

NextBioi 290908.
PROi P54310.
SOURCEi Search...

Gene expression databases

Bgeei P54310.
CleanExi MM_LIPE.
ExpressionAtlasi P54310. baseline and differential.
Genevestigatori P54310.

Family and domain databases

Gene3Di 3.40.50.1820. 2 hits.
InterProi IPR029058. AB_hydrolase.
IPR013094. AB_hydrolase_3.
IPR010468. HSL_N.
IPR002168. Lipase_GDXG_AS.
[Graphical view ]
Pfami PF07859. Abhydrolase_3. 2 hits.
PF06350. HSL_N. 1 hit.
[Graphical view ]
SUPFAMi SSF53474. SSF53474. 2 hits.
PROSITEi PS01173. LIPASE_GDXG_HIS. 1 hit.
PS01174. LIPASE_GDXG_SER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of the gene for mouse hormone-sensitive lipase."
    Li Z., Sumida M., Birchbauer A., Schotz M.C., Reue K.
    Genomics 24:259-265(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Hormone-sensitive lipase (Lipe): sequence analysis of the 129Sv mouse Lipe gene."
    Sztrolovics R., Wang S.P., Lapierre P., Chen H.S., Robert M.-F., Mitchell G.A.
    Mamm. Genome 8:86-89(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/Sv.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Testis.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFOM 1).
    Strain: FVB/N.
    Tissue: Salivary gland.
  6. "Anti-lipolytic action of AMP-activated protein kinase in rodent adipocytes."
    Daval M., Diot-Dupuy F., Bazin R., Hainault I., Viollet B., Vaulont S., Hajduch E., Ferre P., Foufelle F.
    J. Biol. Chem. 280:25250-25257(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY AMPK.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "Activation of hormone-sensitive lipase requires two steps, protein phosphorylation and binding to the PAT-1 domain of lipid droplet coat proteins."
    Wang H., Hu L., Dalen K., Dorward H., Marcinkiewicz A., Russell D., Gong D., Londos C., Yamaguchi T., Holm C., Rizzo M.A., Brasaemle D., Sztalryd C.
    J. Biol. Chem. 284:32116-32125(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PLIN5.
  9. "The stoichiometry of protein phosphorylation in adipocyte lipid droplets: analysis by N-terminal isotope tagging and enzymatic dephosphorylation."
    Kanshin E., Wang S., Ashmarina L., Fedjaev M., Nifant'ev I., Mitchell G.A., Pshezhetsky A.V.
    Proteomics 9:5067-5077(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-559.
  10. "Ablation of TRIP-Br2, a regulator of fat lipolysis, thermogenesis and oxidative metabolism, prevents diet-induced obesity and insulin resistance."
    Liew C.W., Boucher J., Cheong J.K., Vernochet C., Koh H.J., Mallol C., Townsend K., Langin D., Kawamori D., Hu J., Tseng Y.H., Hellerstein M.K., Farmer S.R., Goodyear L., Doria A., Blueher M., Hsu S.I., Kulkarni R.N.
    Nat. Med. 19:217-226(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS LIPOLYTIC ENZYME.

Entry informationi

Entry nameiLIPS_MOUSE
AccessioniPrimary (citable) accession number: P54310
Secondary accession number(s): P97866
, Q3TE34, Q6GU16, Q8CDI9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 24, 2006
Last modified: October 29, 2014
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3