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Q9Y2P5

- S27A5_HUMAN

UniProt

Q9Y2P5 - S27A5_HUMAN

Protein

Bile acyl-CoA synthetase

Gene

SLC27A5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    Functioni

    Acyl-CoA synthetase involved in bile acid metabolism. Proposed to catalyze the first step in the conjugation of C24 bile acids (choloneates) to glycine and taurine before excretion into bile canaliculi by activating them to their CoA thioesters. Seems to activate secondary bile acids entering the liver from the enterohepatic circulation. In vitro, also activates 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanate (THCA), the C27 precursor of cholic acid deriving from the de novo synthesis from cholesterol.2 Publications

    Catalytic activityi

    ATP + cholate + CoA = AMP + diphosphate + choloyl-CoA.
    ATP + (25R)-3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestan-26-oate + CoA = AMP + diphosphate + (25R)-3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi292 – 30312AMPSequence AnalysisAdd
    BLAST

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. catalytic activity Source: InterPro
    3. cholate-CoA ligase activity Source: UniProtKB-EC
    4. fatty acid transporter activity Source: Ensembl
    5. very long-chain fatty acid-CoA ligase activity Source: UniProtKB

    GO - Biological processi

    1. bile acid and bile salt transport Source: Reactome
    2. bile acid biosynthetic process Source: UniProtKB
    3. bile acid metabolic process Source: Reactome
    4. ketone body biosynthetic process Source: Ensembl
    5. plasma membrane long-chain fatty acid transport Source: Ensembl
    6. small molecule metabolic process Source: Reactome
    7. triglyceride mobilization Source: Ensembl
    8. very long-chain fatty acid metabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_11041. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
    REACT_11042. Recycling of bile acids and salts.
    REACT_11053. Synthesis of bile acids and bile salts via 24-hydroxycholesterol.

    Protein family/group databases

    TCDBi4.C.1.1.13. the proposed fatty acid transporter (fat) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bile acyl-CoA synthetase (EC:6.2.1.7)
    Short name:
    BACS
    Alternative name(s):
    Bile acid-CoA ligase
    Short name:
    BA-CoA ligase
    Short name:
    BAL
    Cholate--CoA ligase
    Fatty acid transport protein 5
    Short name:
    FATP-5
    Fatty-acid-coenzyme A ligase, very long-chain 3
    Solute carrier family 27 member 5
    Very long-chain acyl-CoA synthetase homolog 2
    Short name:
    VLCS-H2
    Short name:
    VLCSH2
    Very long-chain acyl-CoA synthetase-related protein
    Short name:
    VLACS-related
    Short name:
    VLACSR
    Gene namesi
    Name:SLC27A5
    Synonyms:ACSB, ACSVL6, FACVL3, FATP5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:10999. SLC27A5.

    Subcellular locationi

    Endoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein 1 Publication

    GO - Cellular componenti

    1. basal plasma membrane Source: Ensembl
    2. endoplasmic reticulum Source: UniProtKB
    3. endoplasmic reticulum membrane Source: Reactome
    4. integral component of endoplasmic reticulum membrane Source: UniProtKB
    5. protein complex Source: Ensembl

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA35873.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 690690Bile acyl-CoA synthetasePRO_0000193213Add
    BLAST

    Proteomic databases

    PaxDbiQ9Y2P5.
    PRIDEiQ9Y2P5.

    PTM databases

    PhosphoSiteiQ9Y2P5.

    Expressioni

    Tissue specificityi

    Predominantly expressed in liver.1 Publication

    Gene expression databases

    ArrayExpressiQ9Y2P5.
    BgeeiQ9Y2P5.
    CleanExiHS_SLC27A5.
    GenevestigatoriQ9Y2P5.

    Organism-specific databases

    HPAiCAB056160.
    HPA007292.

    Interactioni

    Protein-protein interaction databases

    BioGridi116191. 1 interaction.
    STRINGi9606.ENSP00000263093.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Y2P5.
    SMRiQ9Y2P5. Positions 117-651.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 3030Cytoplasmic1 PublicationAdd
    BLAST
    Topological domaini77 – 690614Cytoplasmic1 PublicationAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei31 – 5121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei56 – 7621HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0318.
    HOGENOMiHOG000044189.
    HOVERGENiHBG005642.
    InParanoidiQ9Y2P5.
    KOiK08748.
    OMAiSEISAKW.
    OrthoDBiEOG7W6WKB.
    PhylomeDBiQ9Y2P5.
    TreeFamiTF313430.

    Family and domain databases

    InterProiIPR025110. AMP-bd_C.
    IPR020845. AMP-binding_CS.
    IPR000873. AMP-dep_Synth/Lig.
    [Graphical view]
    PfamiPF00501. AMP-binding. 1 hit.
    PF13193. AMP-binding_C. 1 hit.
    [Graphical view]
    PROSITEiPS00455. AMP_BINDING. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9Y2P5-1) [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

    MGVRQQLALL LLLLLLLWGL GQPVWPVAVA LTLRWLLGDP TCCVLLGLAM    50
    LARPWLGPWV PHGLSLAAAA LALTLLPARL PPGLRWLPAD VIFLAKILHL 100
    GLKIRGCLSR QPPDTFVDAF ERRARAQPGR ALLVWTGPGA GSVTFGELDA 150
    RACQAAWALK AELGDPASLC AGEPTALLVL ASQAVPALCM WLGLAKLGCP 200
    TAWINPHGRG MPLAHSVLSS GARVLVVDPD LRESLEEILP KLQAENIRCF 250
    YLSHTSPTPG VGALGAALDA APSHPVPADL RAGITWRSPA LFIYTSGTTG 300
    LPKPAILTHE RVLQMSKMLS LSGATADDVV YTVLPLYHVM GLVVGILGCL 350
    DLGATCVLAP KFSTSCFWDD CRQHGVTVIL YVGELLRYLC NIPQQPEDRT 400
    HTVRLAMGNG LRADVWETFQ QRFGPIRIWE VYGSTEGNMG LVNYVGRCGA 450
    LGKMSCLLRM LSPFELVQFD MEAAEPVRDN QGFCIPVGLG EPGLLLTKVV 500
    SQQPFVGYRG PRELSERKLV RNVRQSGDVY YNTGDVLAMD REGFLYFRDR 550
    LGDTFRWKGE NVSTHEVEGV LSQVDFLQQV NVYGVCVPGC EGKVGMAAVQ 600
    LAPGQTFDGE KLYQHVRAWL PAYATPHFIR IQDAMEVTST FKLMKTRLVR 650
    EGFNVGIVVD PLFVLDNRAQ SFRPLTAEMY QAVCEGTWRL 690
    Length:690
    Mass (Da):75,385
    Last modified:November 1, 1999 - v1
    Checksum:i011313424D794546
    GO
    Isoform 2 (identifier: Q9Y2P5-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         146-229: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:606
    Mass (Da):66,846
    Checksum:i4A49B281561FF8D6
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti50 – 501M → T.
    Corresponds to variant rs35350976 [ dbSNP | Ensembl ].
    VAR_048243
    Natural varianti53 – 531R → W.
    Corresponds to variant rs34415062 [ dbSNP | Ensembl ].
    VAR_048244

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei146 – 22984Missing in isoform 2. 1 PublicationVSP_055810Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF064255 mRNA. Translation: AAD29444.1.
    AK123036 mRNA. Translation: BAG53858.1.
    AK298446 mRNA. Translation: BAG60663.1.
    AC012313 Genomic DNA. No translation available.
    CH471135 Genomic DNA. Translation: EAW72601.1.
    CCDSiCCDS12983.1.
    RefSeqiNP_036386.1. NM_012254.2.
    UniGeneiHs.292177.

    Genome annotation databases

    EnsembliENST00000263093; ENSP00000263093; ENSG00000083807. [Q9Y2P5-1]
    ENST00000601355; ENSP00000470368; ENSG00000083807. [Q9Y2P5-2]
    GeneIDi10998.
    KEGGihsa:10998.
    UCSCiuc002qtc.2. human.

    Polymorphism databases

    DMDMi74739456.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF064255 mRNA. Translation: AAD29444.1 .
    AK123036 mRNA. Translation: BAG53858.1 .
    AK298446 mRNA. Translation: BAG60663.1 .
    AC012313 Genomic DNA. No translation available.
    CH471135 Genomic DNA. Translation: EAW72601.1 .
    CCDSi CCDS12983.1.
    RefSeqi NP_036386.1. NM_012254.2.
    UniGenei Hs.292177.

    3D structure databases

    ProteinModelPortali Q9Y2P5.
    SMRi Q9Y2P5. Positions 117-651.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116191. 1 interaction.
    STRINGi 9606.ENSP00000263093.

    Chemistry

    ChEMBLi CHEMBL5196.

    Protein family/group databases

    TCDBi 4.C.1.1.13. the proposed fatty acid transporter (fat) family.

    PTM databases

    PhosphoSitei Q9Y2P5.

    Polymorphism databases

    DMDMi 74739456.

    Proteomic databases

    PaxDbi Q9Y2P5.
    PRIDEi Q9Y2P5.

    Protocols and materials databases

    DNASUi 10998.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000263093 ; ENSP00000263093 ; ENSG00000083807 . [Q9Y2P5-1 ]
    ENST00000601355 ; ENSP00000470368 ; ENSG00000083807 . [Q9Y2P5-2 ]
    GeneIDi 10998.
    KEGGi hsa:10998.
    UCSCi uc002qtc.2. human.

    Organism-specific databases

    CTDi 10998.
    GeneCardsi GC19M058990.
    HGNCi HGNC:10999. SLC27A5.
    HPAi CAB056160.
    HPA007292.
    MIMi 603314. gene.
    neXtProti NX_Q9Y2P5.
    PharmGKBi PA35873.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0318.
    HOGENOMi HOG000044189.
    HOVERGENi HBG005642.
    InParanoidi Q9Y2P5.
    KOi K08748.
    OMAi SEISAKW.
    OrthoDBi EOG7W6WKB.
    PhylomeDBi Q9Y2P5.
    TreeFami TF313430.

    Enzyme and pathway databases

    Reactomei REACT_11041. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
    REACT_11042. Recycling of bile acids and salts.
    REACT_11053. Synthesis of bile acids and bile salts via 24-hydroxycholesterol.

    Miscellaneous databases

    GeneWikii SLC27A5.
    GenomeRNAii 10998.
    NextBioi 41783.
    PROi Q9Y2P5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y2P5.
    Bgeei Q9Y2P5.
    CleanExi HS_SLC27A5.
    Genevestigatori Q9Y2P5.

    Family and domain databases

    InterProi IPR025110. AMP-bd_C.
    IPR020845. AMP-binding_CS.
    IPR000873. AMP-dep_Synth/Lig.
    [Graphical view ]
    Pfami PF00501. AMP-binding. 1 hit.
    PF13193. AMP-binding_C. 1 hit.
    [Graphical view ]
    PROSITEi PS00455. AMP_BINDING. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human liver-specific very-long-chain acyl-coenzyme A synthetase: cDNA cloning and characterization of a second enzymatically active protein."
      Steinberg S.J., Wang S.J., McGuinness M.C., Watkins P.A.
      Mol. Genet. Metab. 68:32-42(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Liver.
    3. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The human liver-specific homolog of very long-chain acyl-CoA synthetase is cholate:CoA ligase."
      Steinberg S.J., Mihalik S.J., Kim D.G., Cuebas D.A., Watkins P.A.
      J. Biol. Chem. 275:15605-15608(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY.
    6. "Participation of two members of the very long-chain acyl-CoA synthetase family in bile acid synthesis and recycling."
      Mihalik S.J., Steinberg S.J., Pei Z., Park J., Kim do G., Heinzer A.K., Dacremont G., Wanders R.J., Cuebas D.A., Smith K.D., Watkins P.A.
      J. Biol. Chem. 277:24771-24779(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, TOPOLOGY.

    Entry informationi

    Entry nameiS27A5_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y2P5
    Secondary accession number(s): B3KVP6, B4DPQ1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 22, 2005
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 100 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3