Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q8CIV3 (LIPH_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lipase member H

EC=3.1.1.-
Gene names
Name:Liph
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length451 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Hydrolyzes specifically phosphatidic acid (PA) to produce lysophosphatidic acid (LPA) By similarity.

Subcellular location

Secreted. Membrane; Peripheral membrane protein By similarity.

Tissue specificity

Expressed in placenta and colon. Weakly expressed in small intestine. Ref.1

Sequence similarities

Belongs to the AB hydrolase superfamily. Lipase family.

Ontologies

Keywords
   Biological processLipid degradation
Lipid metabolism
   Cellular componentMembrane
Secreted
   Coding sequence diversityAlternative splicing
   DomainSignal
   Molecular functionHydrolase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processlipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from sequence orthology Ref.1. Source: MGI

extracellular space

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionheparin binding

Inferred from electronic annotation. Source: Ensembl

phospholipase activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8CIV3-1)

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.
Isoform 2 (identifier: Q8CIV3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     210-211: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q8CIV3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     210-239: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Potential
Chain17 – 451435Lipase member H
PRO_0000273322

Sites

Active site1541Nucleophile By similarity
Active site1781Charge relay system By similarity
Active site2481Charge relay system By similarity

Amino acid modifications

Glycosylation661N-linked (GlcNAc...) Potential
Disulfide bond233 ↔ 246 By similarity
Disulfide bond270 ↔ 281 By similarity
Disulfide bond284 ↔ 292 By similarity
Disulfide bond427 ↔ 446 By similarity

Natural variations

Alternative sequence210 – 23930Missing in isoform 3.
VSP_022505
Alternative sequence210 – 2112Missing in isoform 2.
VSP_022506

Experimental info

Sequence conflict291S → N in BAE36182. Ref.2
Sequence conflict1461D → N in BAE23014. Ref.2
Sequence conflict2511S → Y in BAE36182. Ref.2
Sequence conflict3951L → M in AAM18804. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: DBB7F5311A08D70A

FASTA45150,675
        10         20         30         40         50         60 
MLRLCFFISF MCLVKSDTDE TCPSFTRLSF HSAVVGTGLS VRLMLYTQRD QTCAQIINST 

        70         80         90        100        110        120 
ALGSLNVTKK TTFIIHGFRP TGSPPVWIEE LVQSLISVQE MNVVVVDWNR GATTVIYPHA 

       130        140        150        160        170        180 
SSKTRQVASI LKEFIDQMLV KGASLDNIYM IGVSLGAHIA GFVGESYEGK LGRVTGLDPA 

       190        200        210        220        230        240 
GPLFNGRPPE ERLDPSDALF VDVIHSDTDA LGYKEALGHI DFYPNGGLDQ PGCPKTIFGG 

       250        260        270        280        290        300 
IKYFKCDHQM SVYLYLASLQ NNCSITAYPC DSYRDYRNGK CVSCGAGQIV PCPRVGYYAD 

       310        320        330        340        350        360 
SWKEYLWDRD PPMTKAFFDT AETKPYCMYH YFVDIVSWNK SVRRGFITIK LRGEDGNITE 

       370        380        390        400        410        420 
SKIDHEPSAF EKYHQVSLLA RFNRDLDKVA EISLLFSTGS VVGPKYKLRV LQMKLRSLAH 

       430        440        450 
PDRPHLCRYD LVLMENVETS FQPILCSQQQ M 

« Hide

Isoform 2 [UniParc].

Checksum: B3312ECF3950A2B7
Show »

FASTA44950,491
Isoform 3 [UniParc].

Checksum: 127552E1012959DC
Show »

FASTA42147,514

References

« Hide 'large scale' references
[1]"Lipase h, a new member of the triglyceride lipase family synthesized by the intestine."
Jin W., Broedl U., Monajemi H., Glick J., Rader D.
Genomics 80:268-273(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
Strain: CD-1.
[2]"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. expand/collapse author list , 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: Cecum, Head, Testis and Urinary bladder.
[3]"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] (ISOFORM 3).
Strain: FVB/N.
Tissue: Mammary tumor.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY093499 mRNA. Translation: AAM18804.1.
AK048150 mRNA. Translation: BAC33259.1.
AK134352 mRNA. Translation: BAE22108.1.
AK136503 mRNA. Translation: BAE23014.1.
AK161067 mRNA. Translation: BAE36182.1.
AK162492 mRNA. Translation: BAE36944.1.
BC037489 mRNA. Translation: AAH37489.1.
RefSeqNP_001077363.1. NM_001083894.1.
NP_700453.1. NM_153404.3.
UniGeneMm.33192.

3D structure databases

ProteinModelPortalQ8CIV3.
SMRQ8CIV3. Positions 39-443.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ8CIV3.

Proteomic databases

PRIDEQ8CIV3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000060673; ENSMUSP00000062310; ENSMUSG00000044626. [Q8CIV3-1]
ENSMUST00000074230; ENSMUSP00000073853; ENSMUSG00000044626. [Q8CIV3-3]
GeneID239759.
KEGGmmu:239759.
UCSCuc007yru.1. mouse. [Q8CIV3-1]
uc007yrv.1. mouse. [Q8CIV3-3]
uc012adk.1. mouse. [Q8CIV3-2]

Organism-specific databases

CTD200879.
MGIMGI:2388029. Liph.

Phylogenomic databases

eggNOGNOG39787.
GeneTreeENSGT00750000117553.
HOGENOMHOG000234386.
HOVERGENHBG080640.
InParanoidQ8CIV3.
OMAITAYPCD.
OrthoDBEOG79PJP2.
PhylomeDBQ8CIV3.
TreeFamTF324997.

Gene expression databases

BgeeQ8CIV3.
CleanExMM_LIPH.
GenevestigatorQ8CIV3.

Family and domain databases

InterProIPR000734. Lipase.
IPR013818. Lipase_N.
IPR016272. Lipoprotein_lipase_LIPH.
[Graphical view]
PANTHERPTHR11610. PTHR11610. 1 hit.
PfamPF00151. Lipase. 1 hit.
[Graphical view]
PIRSFPIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
PRINTSPR00821. TAGLIPASE.
ProtoNetSearch...

Other

NextBio384267.
PROQ8CIV3.
SOURCESearch...

Entry information

Entry nameLIPH_MOUSE
AccessionPrimary (citable) accession number: Q8CIV3
Secondary accession number(s): Q3TRT3 expand/collapse secondary AC list , Q3TTZ0, Q3UWA2, Q8BXB5, Q8CI45
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 81 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot