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Q05816

- FABP5_MOUSE

UniProt

Q05816 - FABP5_MOUSE

Protein

Fatty acid-binding protein, epidermal

Gene

Fabp5

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

    High specificity for fatty acids. Highest affinity for C18 chain length By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei109 – 1091Fatty acidBy similarity

    GO - Molecular functioni

    1. fatty acid binding Source: Ensembl
    2. transporter activity Source: InterPro

    GO - Biological processi

    1. glucose metabolic process Source: MGI
    2. glucose transport Source: MGI
    3. lipid metabolic process Source: MGI
    4. phosphatidylcholine biosynthetic process Source: MGI
    5. response to wounding Source: Ensembl

    Keywords - Biological processi

    Transport

    Keywords - Ligandi

    Lipid-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fatty acid-binding protein, epidermal
    Alternative name(s):
    Epidermal-type fatty acid-binding protein
    Short name:
    E-FABP
    Fatty acid-binding protein 5
    Keratinocyte lipid-binding protein
    Psoriasis-associated fatty acid-binding protein homolog
    Short name:
    PA-FABP
    Gene namesi
    Name:Fabp5
    Synonyms:Fabpe, Klbp, Mal1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 3

    Organism-specific databases

    MGIiMGI:101790. Fabp5.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 135134Fatty acid-binding protein, epidermalPRO_0000067378Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Disulfide bondi120 ↔ 127By similarity
    Modified residuei131 – 1311PhosphotyrosineBy similarity

    Keywords - PTMi

    Acetylation, Disulfide bond, Phosphoprotein

    Proteomic databases

    MaxQBiQ05816.
    PaxDbiQ05816.
    PRIDEiQ05816.

    2D gel databases

    REPRODUCTION-2DPAGEQ05816.
    UCD-2DPAGEQ05816.

    PTM databases

    PhosphoSiteiQ05816.

    Expressioni

    Tissue specificityi

    Most abundant in keratinocytes and also in stratified epithelia of epidermis and tongue. Relatively high levels found in adipose and mammary tissues and small amounts found in heart, brain, liver, spleen, muscle and lung.

    Gene expression databases

    BgeeiQ05816.
    CleanExiMM_FABP5.
    GenevestigatoriQ05816.

    Interactioni

    Protein-protein interaction databases

    BioGridi200959. 1 interaction.
    IntActiQ05816. 4 interactions.
    MINTiMINT-1869678.

    Structurei

    Secondary structure

    1
    135
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 74
    Beta strandi9 – 1810
    Helixi19 – 268
    Helixi30 – 378
    Beta strandi42 – 487
    Beta strandi51 – 577
    Beta strandi62 – 687
    Beta strandi73 – 764
    Beta strandi82 – 909
    Beta strandi93 – 1008
    Beta strandi103 – 11210
    Beta strandi115 – 1228
    Beta strandi125 – 1339

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4AZNX-ray2.51A/B1-135[»]
    4AZOX-ray2.33A1-135[»]
    4AZPX-ray2.10A1-135[»]
    4AZQX-ray2.00A1-135[»]
    ProteinModelPortaliQ05816.
    SMRiQ05816. Positions 2-135.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni129 – 1313Fatty acid bindingBy similarity

    Domaini

    Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior.By similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG309791.
    HOGENOMiHOG000004829.
    HOVERGENiHBG005633.
    InParanoidiQ05816.
    KOiK08754.
    OMAiVECDMNG.
    OrthoDBiEOG7NW6BZ.
    PhylomeDBiQ05816.
    TreeFamiTF316894.

    Family and domain databases

    Gene3Di2.40.128.20. 1 hit.
    InterProiIPR012674. Calycin.
    IPR011038. Calycin-like.
    IPR000463. Fatty_acid-bd.
    IPR000566. Lipocln_cytosolic_FA-bd_dom.
    [Graphical view]
    PfamiPF00061. Lipocalin. 1 hit.
    [Graphical view]
    PRINTSiPR00178. FATTYACIDBP.
    SUPFAMiSSF50814. SSF50814. 1 hit.
    PROSITEiPS00214. FABP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q05816-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASLKDLEGK WRLMESHGFE EYMKELGVGL ALRKMAAMAK PDCIITCDGN    50
    NITVKTESTV KTTVFSCNLG EKFDETTADG RKTETVCTFQ DGALVQHQQW 100
    DGKESTITRK LKDGKMIVEC VMNNATCTRV YEKVQ 135
    Length:135
    Mass (Da):15,137
    Last modified:January 23, 2007 - v3
    Checksum:i6A6C8DBEBB046185
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X70100 mRNA. Translation: CAA49703.1.
    AJ223066 Genomic DNA. Translation: CAA11069.1.
    AF061015, AF061014 Genomic DNA. Translation: AAC82368.1.
    AK008782 mRNA. Translation: BAB25890.1.
    AK011551 mRNA. Translation: BAB27692.1.
    BC002008 mRNA. Translation: AAH02008.1.
    CCDSiCCDS38388.1.
    PIRiA47497.
    RefSeqiNP_034764.1. NM_010634.3.
    UniGeneiMm.741.

    Genome annotation databases

    EnsembliENSMUST00000029046; ENSMUSP00000029046; ENSMUSG00000027533.
    GeneIDi16592.
    KEGGimmu:16592.
    UCSCiuc008opg.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X70100 mRNA. Translation: CAA49703.1 .
    AJ223066 Genomic DNA. Translation: CAA11069.1 .
    AF061015 , AF061014 Genomic DNA. Translation: AAC82368.1 .
    AK008782 mRNA. Translation: BAB25890.1 .
    AK011551 mRNA. Translation: BAB27692.1 .
    BC002008 mRNA. Translation: AAH02008.1 .
    CCDSi CCDS38388.1.
    PIRi A47497.
    RefSeqi NP_034764.1. NM_010634.3.
    UniGenei Mm.741.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4AZN X-ray 2.51 A/B 1-135 [» ]
    4AZO X-ray 2.33 A 1-135 [» ]
    4AZP X-ray 2.10 A 1-135 [» ]
    4AZQ X-ray 2.00 A 1-135 [» ]
    ProteinModelPortali Q05816.
    SMRi Q05816. Positions 2-135.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 200959. 1 interaction.
    IntActi Q05816. 4 interactions.
    MINTi MINT-1869678.

    PTM databases

    PhosphoSitei Q05816.

    2D gel databases

    REPRODUCTION-2DPAGE Q05816.
    UCD-2DPAGE Q05816.

    Proteomic databases

    MaxQBi Q05816.
    PaxDbi Q05816.
    PRIDEi Q05816.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000029046 ; ENSMUSP00000029046 ; ENSMUSG00000027533 .
    GeneIDi 16592.
    KEGGi mmu:16592.
    UCSCi uc008opg.1. mouse.

    Organism-specific databases

    CTDi 2171.
    MGIi MGI:101790. Fabp5.

    Phylogenomic databases

    eggNOGi NOG309791.
    HOGENOMi HOG000004829.
    HOVERGENi HBG005633.
    InParanoidi Q05816.
    KOi K08754.
    OMAi VECDMNG.
    OrthoDBi EOG7NW6BZ.
    PhylomeDBi Q05816.
    TreeFami TF316894.

    Miscellaneous databases

    NextBioi 290145.
    PROi Q05816.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q05816.
    CleanExi MM_FABP5.
    Genevestigatori Q05816.

    Family and domain databases

    Gene3Di 2.40.128.20. 1 hit.
    InterProi IPR012674. Calycin.
    IPR011038. Calycin-like.
    IPR000463. Fatty_acid-bd.
    IPR000566. Lipocln_cytosolic_FA-bd_dom.
    [Graphical view ]
    Pfami PF00061. Lipocalin. 1 hit.
    [Graphical view ]
    PRINTSi PR00178. FATTYACIDBP.
    SUPFAMi SSF50814. SSF50814. 1 hit.
    PROSITEi PS00214. FABP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Tumor-specific overexpression of a novel keratinocyte lipid-binding protein. Identification and characterization of a cloned sequence activated during multistage carcinogenesis in mouse skin."
      Krieg P., Feil S., Fuerstenberger G., Bowden T.G.
      J. Biol. Chem. 268:17362-17369(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Keratinocyte.
    2. "Cloning and chromosomal localisation of the murine epidermal-type fatty acid binding protein gene (Fabpe)."
      Bleck B., Hohoff C., Binas B., Rustow B., Dixkens C., Hameister H., Boerchers T., Spener F.
      Gene 215:123-130(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 129/SvJ.
    3. "Cloning and chromosomal location of the murine Keratinocyte lipid-binding protein gene."
      Hertzel A.V., Bernlohr D.A.
      Gene 221:235-243(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "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].
      Strain: C57BL/6J.
      Tissue: Stomach.
    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].
      Tissue: Mammary tumor.
    6. Lubec G., Klug S.
      Submitted (MAR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 13-24, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Hippocampus.

    Entry informationi

    Entry nameiFABP5_MOUSE
    AccessioniPrimary (citable) accession number: Q05816
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 128 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3