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Q8CIV3

- LIPH_MOUSE

UniProt

Q8CIV3 - LIPH_MOUSE

Protein

Lipase member H

Gene

Liph

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei154 – 1541NucleophileBy similarity
    Active sitei178 – 1781Charge relay systemBy similarity
    Active sitei248 – 2481Charge relay systemBy similarity

    GO - Molecular functioni

    1. heparin binding Source: Ensembl
    2. phospholipase activity Source: Ensembl

    GO - Biological processi

    1. lipid catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Lipid degradation, Lipid metabolism

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lipase member H (EC:3.1.1.-)
    Gene namesi
    Name:Liph
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 16

    Organism-specific databases

    MGIiMGI:2388029. Liph.

    Subcellular locationi

    Secreted. Membrane By similarity; Peripheral membrane protein By similarity

    GO - Cellular componenti

    1. extracellular region Source: MGI
    2. extracellular space Source: Ensembl
    3. plasma membrane Source: Ensembl

    Keywords - Cellular componenti

    Membrane, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1616Sequence AnalysisAdd
    BLAST
    Chaini17 – 451435Lipase member HPRO_0000273322Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi66 – 661N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi233 ↔ 246By similarity
    Disulfide bondi270 ↔ 281By similarity
    Disulfide bondi284 ↔ 292By similarity
    Disulfide bondi427 ↔ 446By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PRIDEiQ8CIV3.

    PTM databases

    PhosphoSiteiQ8CIV3.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    BgeeiQ8CIV3.
    CleanExiMM_LIPH.
    GenevestigatoriQ8CIV3.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8CIV3.
    SMRiQ8CIV3. Positions 39-443.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the AB hydrolase superfamily. Lipase family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG39787.
    GeneTreeiENSGT00750000117553.
    HOGENOMiHOG000234386.
    HOVERGENiHBG080640.
    InParanoidiQ8CIV3.
    OMAiITAYPCD.
    OrthoDBiEOG79PJP2.
    PhylomeDBiQ8CIV3.
    TreeFamiTF324997.

    Family and domain databases

    Gene3Di3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR000734. Lipase.
    IPR013818. Lipase_N.
    IPR016272. Lipoprotein_lipase_LIPH.
    [Graphical view]
    PANTHERiPTHR11610. PTHR11610. 1 hit.
    PfamiPF00151. Lipase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
    PRINTSiPR00821. TAGLIPASE.
    SUPFAMiSSF53474. SSF53474. 1 hit.

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8CIV3-1) [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

    MLRLCFFISF MCLVKSDTDE TCPSFTRLSF HSAVVGTGLS VRLMLYTQRD    50
    QTCAQIINST ALGSLNVTKK TTFIIHGFRP TGSPPVWIEE LVQSLISVQE 100
    MNVVVVDWNR GATTVIYPHA SSKTRQVASI LKEFIDQMLV KGASLDNIYM 150
    IGVSLGAHIA GFVGESYEGK LGRVTGLDPA GPLFNGRPPE ERLDPSDALF 200
    VDVIHSDTDA LGYKEALGHI DFYPNGGLDQ PGCPKTIFGG IKYFKCDHQM 250
    SVYLYLASLQ NNCSITAYPC DSYRDYRNGK CVSCGAGQIV PCPRVGYYAD 300
    SWKEYLWDRD PPMTKAFFDT AETKPYCMYH YFVDIVSWNK SVRRGFITIK 350
    LRGEDGNITE SKIDHEPSAF EKYHQVSLLA RFNRDLDKVA EISLLFSTGS 400
    VVGPKYKLRV LQMKLRSLAH PDRPHLCRYD LVLMENVETS FQPILCSQQQ 450
    M 451
    Length:451
    Mass (Da):50,675
    Last modified:January 23, 2007 - v2
    Checksum:iDBB7F5311A08D70A
    GO
    Isoform 2 (identifier: Q8CIV3-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         210-211: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:449
    Mass (Da):50,491
    Checksum:iB3312ECF3950A2B7
    GO
    Isoform 3 (identifier: Q8CIV3-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         210-239: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:421
    Mass (Da):47,514
    Checksum:i127552E1012959DC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti29 – 291S → N in BAE36182. (PubMed:16141072)Curated
    Sequence conflicti146 – 1461D → N in BAE23014. (PubMed:16141072)Curated
    Sequence conflicti251 – 2511S → Y in BAE36182. (PubMed:16141072)Curated
    Sequence conflicti395 – 3951L → M in AAM18804. (PubMed:12213196)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei210 – 23930Missing in isoform 3. 1 PublicationVSP_022505Add
    BLAST
    Alternative sequencei210 – 2112Missing in isoform 2. 1 PublicationVSP_022506

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS37295.1. [Q8CIV3-3]
    CCDS37296.1. [Q8CIV3-1]
    RefSeqiNP_001077363.1. NM_001083894.1. [Q8CIV3-1]
    NP_001276511.1. NM_001289582.1. [Q8CIV3-2]
    NP_700453.1. NM_153404.3. [Q8CIV3-3]
    UniGeneiMm.33192.

    Genome annotation databases

    EnsembliENSMUST00000060673; ENSMUSP00000062310; ENSMUSG00000044626. [Q8CIV3-1]
    ENSMUST00000074230; ENSMUSP00000073853; ENSMUSG00000044626. [Q8CIV3-3]
    GeneIDi239759.
    KEGGimmu:239759.
    UCSCiuc007yru.1. mouse. [Q8CIV3-1]
    uc007yrv.1. mouse. [Q8CIV3-3]
    uc012adk.1. mouse. [Q8CIV3-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS37295.1. [Q8CIV3-3 ]
    CCDS37296.1. [Q8CIV3-1 ]
    RefSeqi NP_001077363.1. NM_001083894.1. [Q8CIV3-1 ]
    NP_001276511.1. NM_001289582.1. [Q8CIV3-2 ]
    NP_700453.1. NM_153404.3. [Q8CIV3-3 ]
    UniGenei Mm.33192.

    3D structure databases

    ProteinModelPortali Q8CIV3.
    SMRi Q8CIV3. Positions 39-443.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q8CIV3.

    Proteomic databases

    PRIDEi Q8CIV3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000060673 ; ENSMUSP00000062310 ; ENSMUSG00000044626 . [Q8CIV3-1 ]
    ENSMUST00000074230 ; ENSMUSP00000073853 ; ENSMUSG00000044626 . [Q8CIV3-3 ]
    GeneIDi 239759.
    KEGGi mmu:239759.
    UCSCi uc007yru.1. mouse. [Q8CIV3-1 ]
    uc007yrv.1. mouse. [Q8CIV3-3 ]
    uc012adk.1. mouse. [Q8CIV3-2 ]

    Organism-specific databases

    CTDi 200879.
    MGIi MGI:2388029. Liph.

    Phylogenomic databases

    eggNOGi NOG39787.
    GeneTreei ENSGT00750000117553.
    HOGENOMi HOG000234386.
    HOVERGENi HBG080640.
    InParanoidi Q8CIV3.
    OMAi ITAYPCD.
    OrthoDBi EOG79PJP2.
    PhylomeDBi Q8CIV3.
    TreeFami TF324997.

    Miscellaneous databases

    NextBioi 384267.
    PROi Q8CIV3.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8CIV3.
    CleanExi MM_LIPH.
    Genevestigatori Q8CIV3.

    Family and domain databases

    Gene3Di 3.40.50.1820. 1 hit.
    InterProi IPR029058. AB_hydrolase.
    IPR000734. Lipase.
    IPR013818. Lipase_N.
    IPR016272. Lipoprotein_lipase_LIPH.
    [Graphical view ]
    PANTHERi PTHR11610. PTHR11610. 1 hit.
    Pfami PF00151. Lipase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000865. Lipoprotein_lipase_LIPH. 1 hit.
    PRINTSi PR00821. TAGLIPASE.
    SUPFAMi SSF53474. SSF53474. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.

    Entry informationi

    Entry nameiLIPH_MOUSE
    AccessioniPrimary (citable) accession number: Q8CIV3
    Secondary accession number(s): Q3TRT3
    , Q3TTZ0, Q3UWA2, Q8BXB5, Q8CI45
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2007
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 85 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3