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Q8BH59

- CMC1_MOUSE

UniProt

Q8BH59 - CMC1_MOUSE

Protein

Calcium-binding mitochondrial carrier protein Aralar1

Gene

Slc25a12

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
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    Functioni

    Catalyzes the calcium-dependent exchange of cytoplasmic glutamate with mitochondrial aspartate across the mitochondrial inner membrane. May have a function in the urea cycle By similarity.By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi65 – 76121PROSITE-ProRule annotationAdd
    BLAST
    Calcium bindingi99 – 110122PROSITE-ProRule annotationAdd
    BLAST
    Calcium bindingi170 – 181123PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. calcium ion binding Source: UniProtKB
    2. L-aspartate transmembrane transporter activity Source: UniProtKB
    3. L-glutamate transmembrane transporter activity Source: UniProtKB

    GO - Biological processi

    1. aspartate transport Source: UniProtKB
    2. L-glutamate transport Source: UniProtKB
    3. malate-aspartate shuttle Source: UniProtKB
    4. response to calcium ion Source: UniProtKB

    Keywords - Biological processi

    Transport

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_199101. Mitochondrial protein import.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Calcium-binding mitochondrial carrier protein Aralar1
    Alternative name(s):
    Mitochondrial aspartate glutamate carrier 1
    Solute carrier family 25 member 12
    Gene namesi
    Name:Slc25a12
    Synonyms:Aralar1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:1926080. Slc25a12.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. mitochondrial inner membrane Source: MGI
    3. mitochondrion Source: UniProtKB

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion inner membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 677676Calcium-binding mitochondrial carrier protein Aralar1PRO_0000090599Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ8BH59.
    PaxDbiQ8BH59.
    PRIDEiQ8BH59.

    PTM databases

    PhosphoSiteiQ8BH59.

    Expressioni

    Gene expression databases

    BgeeiQ8BH59.
    GenevestigatoriQ8BH59.

    Interactioni

    Protein-protein interaction databases

    BioGridi219664. 4 interactions.
    IntActiQ8BH59. 8 interactions.
    MINTiMINT-1843325.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8BH59.
    SMRiQ8BH59. Positions 19-285, 330-602.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei330 – 34718Helical; Name=1Sequence AnalysisAdd
    BLAST
    Transmembranei391 – 41020Helical; Name=2Sequence AnalysisAdd
    BLAST
    Transmembranei434 – 44714Helical; Name=3Sequence AnalysisAdd
    BLAST
    Transmembranei483 – 50220Helical; Name=4Sequence AnalysisAdd
    BLAST
    Transmembranei522 – 53918Helical; Name=5Sequence AnalysisAdd
    BLAST
    Transmembranei579 – 59820Helical; Name=6Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini40 – 8546EF-hand 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini86 – 12136EF-hand 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini122 – 15635EF-hand 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini157 – 19236EF-hand 4PROSITE-ProRule annotationAdd
    BLAST
    Repeati324 – 41693Solcar 1Add
    BLAST
    Repeati424 – 50885Solcar 2Add
    BLAST
    Repeati516 – 60489Solcar 3Add
    BLAST

    Sequence similaritiesi

    Contains 4 EF-hand domains.PROSITE-ProRule annotation
    Contains 3 Solcar repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG292991.
    GeneTreeiENSGT00530000062944.
    HOGENOMiHOG000180633.
    HOVERGENiHBG005350.
    InParanoidiA2BFG0.
    KOiK15105.
    OMAiFESVLCT.
    OrthoDBiEOG70GMF1.
    PhylomeDBiQ8BH59.
    TreeFamiTF313209.

    Family and domain databases

    Gene3Di1.10.238.10. 2 hits.
    1.50.40.10. 1 hit.
    InterProiIPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    IPR002067. Mit_carrier.
    IPR018108. Mitochondrial_sb/sol_carrier.
    IPR023395. Mt_carrier_dom.
    [Graphical view]
    PfamiPF13405. EF-hand_6. 1 hit.
    PF00153. Mito_carr. 3 hits.
    [Graphical view]
    PRINTSiPR00926. MITOCARRIER.
    SMARTiSM00054. EFh. 3 hits.
    [Graphical view]
    SUPFAMiSSF103506. SSF103506. 1 hit.
    PROSITEiPS00018. EF_HAND_1. 1 hit.
    PS50222. EF_HAND_2. 2 hits.
    PS50920. SOLCAR. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q8BH59-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAVKVHTTKR GDPHELRNIF LQYASTEVDG EHYMTPEDFV QRYLGLYNDP    50
    NSNPKIVQLL AGVADQTKDG LISYQEFLAF ESVLCAPDSM FIVAFQLFDK 100
    SGNGEVTFEN VKEIFGQTII HHHIPFNWDC EFIRLHFGHN RKKHLNYVEF 150
    TQFLQELQLE HARQAFALKD KSKSGMISGL DFSDVMVTIR SHMLTPFVEE 200
    NLVSAAGGGT SHQVSFSYFN AFNSLLNNME LVRKIYSTLA GTRKDIEVTK 250
    EEFAQSAIRY GQVTPLEIDI LYQLADLYNA SGRLTLADIE RIAPLAEGAL 300
    PYNLAELQRQ QSPGLGRPIW LQIAESAYRF TLGSVAGAVG ATAVYPIDLV 350
    KTRMQNQRGT GSVVGELMYK NSFDCFKKVL RYEGFFGLYR GLIPQLIGVA 400
    PEKAIKLTVN DFVRDKFTKR DGSIPLPAEI LAGGCAGGSQ VIFTNPLEIV 450
    KIRLQVAGEI TTGPRVSALN VLQDLGLFGL YKGAKACFLR DIPFSAIYFP 500
    VYAHCKLLLA DENGRVGGIN LLTAGALAGV PAASLVTPAD VIKTRLQVAA 550
    RAGQTTYSGV VDCFRKILRE EGPSAFWKGT AARVFRSSPQ FGVTLVTYEL 600
    LQRWFYIDFG GLKPSGSEPT PKSRIADLPP ANPDHIGGYR LATATFAGIE 650
    NKFGLYLPKF KSPSVAVAQP KAAAAAQ 677
    Length:677
    Mass (Da):74,570
    Last modified:March 1, 2003 - v1
    Checksum:i488ABC7EB8227571
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK030595 mRNA. Translation: BAC27037.1.
    AK083156 mRNA. Translation: BAC38787.1.
    BX284624 Genomic DNA. Translation: CAM20071.1.
    BC060505 mRNA. Translation: AAH60505.1.
    CCDSiCCDS16113.1.
    RefSeqiNP_766024.1. NM_172436.3.
    UniGeneiMm.146696.
    Mm.30928.

    Genome annotation databases

    EnsembliENSMUST00000151937; ENSMUSP00000122103; ENSMUSG00000027010.
    GeneIDi78830.
    KEGGimmu:78830.
    UCSCiuc008kan.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK030595 mRNA. Translation: BAC27037.1 .
    AK083156 mRNA. Translation: BAC38787.1 .
    BX284624 Genomic DNA. Translation: CAM20071.1 .
    BC060505 mRNA. Translation: AAH60505.1 .
    CCDSi CCDS16113.1.
    RefSeqi NP_766024.1. NM_172436.3.
    UniGenei Mm.146696.
    Mm.30928.

    3D structure databases

    ProteinModelPortali Q8BH59.
    SMRi Q8BH59. Positions 19-285, 330-602.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 219664. 4 interactions.
    IntActi Q8BH59. 8 interactions.
    MINTi MINT-1843325.

    PTM databases

    PhosphoSitei Q8BH59.

    Proteomic databases

    MaxQBi Q8BH59.
    PaxDbi Q8BH59.
    PRIDEi Q8BH59.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000151937 ; ENSMUSP00000122103 ; ENSMUSG00000027010 .
    GeneIDi 78830.
    KEGGi mmu:78830.
    UCSCi uc008kan.1. mouse.

    Organism-specific databases

    CTDi 8604.
    MGIi MGI:1926080. Slc25a12.

    Phylogenomic databases

    eggNOGi NOG292991.
    GeneTreei ENSGT00530000062944.
    HOGENOMi HOG000180633.
    HOVERGENi HBG005350.
    InParanoidi A2BFG0.
    KOi K15105.
    OMAi FESVLCT.
    OrthoDBi EOG70GMF1.
    PhylomeDBi Q8BH59.
    TreeFami TF313209.

    Enzyme and pathway databases

    Reactomei REACT_199101. Mitochondrial protein import.

    Miscellaneous databases

    NextBioi 349608.
    PROi Q8BH59.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8BH59.
    Genevestigatori Q8BH59.

    Family and domain databases

    Gene3Di 1.10.238.10. 2 hits.
    1.50.40.10. 1 hit.
    InterProi IPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    IPR002067. Mit_carrier.
    IPR018108. Mitochondrial_sb/sol_carrier.
    IPR023395. Mt_carrier_dom.
    [Graphical view ]
    Pfami PF13405. EF-hand_6. 1 hit.
    PF00153. Mito_carr. 3 hits.
    [Graphical view ]
    PRINTSi PR00926. MITOCARRIER.
    SMARTi SM00054. EFh. 3 hits.
    [Graphical view ]
    SUPFAMi SSF103506. SSF103506. 1 hit.
    PROSITEi PS00018. EF_HAND_1. 1 hit.
    PS50222. EF_HAND_2. 2 hits.
    PS50920. SOLCAR. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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: Hippocampus and Pituitary.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    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].
      Tissue: Olfactory epithelium.
    4. Lubec G., Kang S.U.
      Submitted (APR-2007) to UniProtKB
      Strain: C57BL/6.
      Tissue: Brain.

    Entry informationi

    Entry nameiCMC1_MOUSE
    AccessioniPrimary (citable) accession number: Q8BH59
    Secondary accession number(s): A2BFG0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 24, 2004
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 109 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Binds calcium.By similarity

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, 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