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Q61824

- ADA12_MOUSE

UniProt

Q61824 - ADA12_MOUSE

Protein

Disintegrin and metalloproteinase domain-containing protein 12

Gene

Adam12

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 2 (03 Oct 2012)
      Previous versions | rss
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    Functioni

    Involved in skeletal muscle regeneration, specifically at the onset of cell fusion. Also involved in macrophage-derived giant cells (MGC) and osteoclast formation from mononuclear precursors.

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi177 – 1771Zinc; in inhibited formBy similarity
    Metal bindingi348 – 3481Zinc; catalyticBy similarity
    Active sitei349 – 3491PROSITE-ProRule annotation
    Metal bindingi352 – 3521Zinc; catalyticBy similarity
    Metal bindingi358 – 3581Zinc; catalyticBy similarity

    GO - Molecular functioni

    1. metalloendopeptidase activity Source: InterPro
    2. protein binding Source: IntAct
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cell adhesion Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Biological processi

    Cell adhesion

    Keywords - Ligandi

    Metal-binding, Zinc

    Protein family/group databases

    MEROPSiM12.212.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Disintegrin and metalloproteinase domain-containing protein 12 (EC:3.4.24.-)
    Short name:
    ADAM 12
    Alternative name(s):
    Meltrin-alpha
    Gene namesi
    Name:Adam12
    Synonyms:Mltna
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:105378. Adam12.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. mitochondrion Source: Ensembl
    3. nucleus Source: Ensembl
    4. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3131Sequence AnalysisAdd
    BLAST
    Propeptidei32 – 205174By similarityPRO_0000029080Add
    BLAST
    Chaini206 – 903698Disintegrin and metalloproteinase domain-containing protein 12PRO_0000029081Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi112 – 1121N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi147 – 1471N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi157 – 1571N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi182 – 1821N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi185 – 1851N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi323 ↔ 409By similarity
    Disulfide bondi365 ↔ 393By similarity
    Disulfide bondi367 ↔ 376By similarity
    Glycosylationi450 – 4501N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi480 ↔ 500By similarity
    Glycosylationi649 – 6491N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi658 ↔ 668By similarity
    Disulfide bondi662 ↔ 674By similarity
    Disulfide bondi676 ↔ 685By similarity
    Modified residuei901 – 9011Phosphotyrosine; by SRC1 Publication

    Post-translational modificationi

    The precursor is cleaved by a furin endopeptidase.By similarity

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein, Zymogen

    Proteomic databases

    PRIDEiQ61824.

    PTM databases

    PhosphoSiteiQ61824.

    Expressioni

    Tissue specificityi

    Expressed during early developing mesenchymal cells that give rise to skeletal muscle, bones and visceral organs. Not expressed in adult normal muscle but expressed in regenerating muscle.1 Publication

    Inductioni

    At the onset of myoblast fusion.

    Gene expression databases

    ArrayExpressiQ61824.
    GenevestigatoriQ61824.

    Interactioni

    Subunit structurei

    Interacts with alpha-actinin-2 and with syndecans. Interacts with SH3PXD2A. Interacts with FST3. Interacts with GNB2L1/RACK1; the interaction is required for PKC-dependent translocation of ADAM12 to the cell membrane By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ACTN2P356093EBI-77785,EBI-77797From a different organism.

    Protein-protein interaction databases

    IntActiQ61824. 1 interaction.
    MINTiMINT-154663.

    Structurei

    3D structure databases

    ProteinModelPortaliQ61824.
    SMRiQ61824. Positions 211-688.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini206 – 706501ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini728 – 903176CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei707 – 72721HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini212 – 414203Peptidase M12BPROSITE-ProRule annotationAdd
    BLAST
    Domaini422 – 50887DisintegrinPROSITE-ProRule annotationAdd
    BLAST
    Domaini654 – 68633EGF-likePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi175 – 1828Cysteine switchBy similarity
    Motifi824 – 8307SH3-binding; class II
    Motifi830 – 8378SH3-binding; class I
    Motifi846 – 8527SH3-binding; class II
    Motifi852 – 8587SH3-binding; class I
    Motifi881 – 8877SH3-binding; class I

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi509 – 653145Cys-richAdd
    BLAST

    Domaini

    The first 30 amino acids of the cytoplasmic domain contain a major binding site to alpha-actinin-2. This interaction is necessary to promote muscle cell fusion.
    The cysteine-rich domain supports cell adhesion through syndecans and triggers signaling events that lead to beta-1 integrin-dependent cell spreading. In carcinoma cells the binding of this domain to syndecans does not allow the integrin-mediated cell spreading By similarity.By similarity
    The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.

    Sequence similaritiesi

    Contains 1 disintegrin domain.PROSITE-ProRule annotation
    Contains 1 EGF-like domain.PROSITE-ProRule annotation
    Contains 1 peptidase M12B domain.PROSITE-ProRule annotation

    Keywords - Domaini

    EGF-like domain, SH3-binding, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG294463.
    GeneTreeiENSGT00740000114848.
    HOGENOMiHOG000230883.
    HOVERGENiHBG006978.
    InParanoidiQ61824.
    KOiK06835.
    OMAiPPFCDKF.
    OrthoDBiEOG7F7W89.
    TreeFamiTF314733.

    Family and domain databases

    Gene3Di3.40.390.10. 1 hit.
    4.10.70.10. 1 hit.
    InterProiIPR006586. ADAM_Cys-rich.
    IPR001762. Blood-coag_inhib_Disintegrin.
    IPR018358. Disintegrin_CS.
    IPR000742. EG-like_dom.
    IPR024079. MetalloPept_cat_dom.
    IPR001590. Peptidase_M12B.
    IPR002870. Peptidase_M12B_N.
    [Graphical view]
    PfamiPF08516. ADAM_CR. 1 hit.
    PF00200. Disintegrin. 1 hit.
    PF01562. Pep_M12B_propep. 1 hit.
    PF01421. Reprolysin. 1 hit.
    [Graphical view]
    PRINTSiPR00289. DISINTEGRIN.
    SMARTiSM00608. ACR. 1 hit.
    SM00050. DISIN. 1 hit.
    [Graphical view]
    SUPFAMiSSF57552. SSF57552. 1 hit.
    PROSITEiPS50215. ADAM_MEPRO. 1 hit.
    PS00427. DISINTEGRIN_1. 1 hit.
    PS50214. DISINTEGRIN_2. 1 hit.
    PS50026. EGF_3. 1 hit.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q61824-1 [UniParc]FASTAAdd to Basket

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    MAERPARRAP PARALLLALA GALLAPRAAR GMSLWDQRGT YEVARASLLS    50
    KDPGIPGQSI PAKDHPDVLT VQLQLESRDL ILSLERNEGL IANGFTETHY 100
    LQDGTDVSLT RNHTDHCYYH GHVQGDAASV VSLSTCSGLR GLIMFENKTY 150
    SLEPMKNTTD SYKLVPAESM TNIQGLCGSQ HNKSNLTMED VSPGTSQMRA 200
    RRHKRETLKM TKYVELVIVA DNREFQRQGK DLEKVKQRLI EIANHVDKFY 250
    RPLNIRIVLV GVEVWNDIDK CSISQDPFTS LHEFLDWRKI KLLPRKSHDN 300
    AQLISGVYFQ GTTIGMAPIM SMCTAEQSGG VVMDHSDSPL GAAVTLAHEL 350
    GHNFGMNHDT LERGCSCRMA AEKGGCIMNP STGFPFPMVF SSCSRKDLEA 400
    SLEKGMGMCL FNLPEVKQAF GGRKCGNGYV EEGEECDCGE PEECTNRCCN 450
    ATTCTLKPDA VCAHGQCCED CQLKPPGTAC RGSSNSCDLP EFCTGTAPHC 500
    PANVYLHDGH PCQGVDGYCY NGICQTHEQQ CVTLWGPGAK PAPGICFERV 550
    NSAGDPYGNC GKDSKSAFAK CELRDAKCGK IQCQGGASRP VIGTNAVSIE 600
    TNIPQQEGGR ILCRGTHVYL GDDMPDPGLV LAGTKCAEGK ICLNRRCQNI 650
    SVFGVHKCAM QCHGRGVCNN RKNCHCEAHW APPFCDKFGF GGSTDSGPIR 700
    QADNQGLTVG ILVSILCLLA AGFVVYLKRK TLMRLLFTHK KTTMEKLRCV 750
    HPSRTPSGPH LGQAHHTPGK GLLMNRAPHF NTPKDRHSLK CQNMDISRPL 800
    DARAVPQLQS PQRVLLPLHQ TPRAPSGPAR PLPASPAVRQ AQGIRKPSPP 850
    QKPLPADPLS RTSRLTSALV RTPGQQEPGH RPAPIRPAPK HQVPRPSHNA 900
    YIK 903
    Length:903
    Mass (Da):98,504
    Last modified:October 3, 2012 - v2
    Checksum:iB6A1D0816E4A73FC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti40 – 401T → A in BAA08912. (PubMed:7566181)Curated
    Sequence conflicti138 – 1381G → D in BAA08912. (PubMed:7566181)Curated
    Sequence conflicti280 – 2801S → R in BAA08912. (PubMed:7566181)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D50411 mRNA. Translation: BAA08912.1.
    AC125372 Genomic DNA. No translation available.
    AC126676 Genomic DNA. No translation available.
    AC140055 Genomic DNA. No translation available.
    CCDSiCCDS21938.1.
    PIRiS60257.
    RefSeqiNP_031426.2. NM_007400.2.
    UniGeneiMm.439714.

    Genome annotation databases

    EnsembliENSMUST00000067680; ENSMUSP00000065213; ENSMUSG00000054555.
    GeneIDi11489.
    KEGGimmu:11489.
    UCSCiuc009kdo.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D50411 mRNA. Translation: BAA08912.1 .
    AC125372 Genomic DNA. No translation available.
    AC126676 Genomic DNA. No translation available.
    AC140055 Genomic DNA. No translation available.
    CCDSi CCDS21938.1.
    PIRi S60257.
    RefSeqi NP_031426.2. NM_007400.2.
    UniGenei Mm.439714.

    3D structure databases

    ProteinModelPortali Q61824.
    SMRi Q61824. Positions 211-688.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q61824. 1 interaction.
    MINTi MINT-154663.

    Protein family/group databases

    MEROPSi M12.212.

    PTM databases

    PhosphoSitei Q61824.

    Proteomic databases

    PRIDEi Q61824.

    Protocols and materials databases

    DNASUi 11489.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000067680 ; ENSMUSP00000065213 ; ENSMUSG00000054555 .
    GeneIDi 11489.
    KEGGi mmu:11489.
    UCSCi uc009kdo.2. mouse.

    Organism-specific databases

    CTDi 8038.
    MGIi MGI:105378. Adam12.

    Phylogenomic databases

    eggNOGi NOG294463.
    GeneTreei ENSGT00740000114848.
    HOGENOMi HOG000230883.
    HOVERGENi HBG006978.
    InParanoidi Q61824.
    KOi K06835.
    OMAi PPFCDKF.
    OrthoDBi EOG7F7W89.
    TreeFami TF314733.

    Miscellaneous databases

    ChiTaRSi ADAM12. mouse.
    NextBioi 278856.
    PROi Q61824.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q61824.
    Genevestigatori Q61824.

    Family and domain databases

    Gene3Di 3.40.390.10. 1 hit.
    4.10.70.10. 1 hit.
    InterProi IPR006586. ADAM_Cys-rich.
    IPR001762. Blood-coag_inhib_Disintegrin.
    IPR018358. Disintegrin_CS.
    IPR000742. EG-like_dom.
    IPR024079. MetalloPept_cat_dom.
    IPR001590. Peptidase_M12B.
    IPR002870. Peptidase_M12B_N.
    [Graphical view ]
    Pfami PF08516. ADAM_CR. 1 hit.
    PF00200. Disintegrin. 1 hit.
    PF01562. Pep_M12B_propep. 1 hit.
    PF01421. Reprolysin. 1 hit.
    [Graphical view ]
    PRINTSi PR00289. DISINTEGRIN.
    SMARTi SM00608. ACR. 1 hit.
    SM00050. DISIN. 1 hit.
    [Graphical view ]
    SUPFAMi SSF57552. SSF57552. 1 hit.
    PROSITEi PS50215. ADAM_MEPRO. 1 hit.
    PS00427. DISINTEGRIN_1. 1 hit.
    PS50214. DISINTEGRIN_2. 1 hit.
    PS50026. EGF_3. 1 hit.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A metalloprotease-disintegrin participating in myoblast fusion."
      Yagami-Hiromasa T., Sato T., Kurisaki T., Kamijo K., Nabeshima Y., Fujisawa-Sehara A.
      Nature 377:652-656(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Embryonic fibroblast.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. "Spatially- and temporally-restricted expression of meltrin alpha (ADAM12) and beta (ADAM19) in mouse embryo."
      Kurisaki T., Masuda A., Osumi N., Nabeshima Y., Fujisawa-Sehara A.
      Mech. Dev. 73:211-215(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    4. "Binding of ADAM12, a marker of skeletal muscle regeneration, to the muscle-specific actin-binding protein, alpha-actinin-2, is required for myoblast fusion."
      Galliano M.-F., Huet C., Frygelius J., Polgren A., Wewer U.M., Engvall E.
      J. Biol. Chem. 275:13933-13939(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ALPHA-ACTININ-2.
    5. "Meltrin alpha cytoplasmic domain interacts with SH3 domains of Src and Grb2 and is phosphorylated by v-Src."
      Suzuki A., Kadota N., Hara T., Nakagami Y., Izumi T., Takenawa T., Sabe H., Endo T.
      Oncogene 19:5842-5850(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-901.

    Entry informationi

    Entry nameiADA12_MOUSE
    AccessioniPrimary (citable) accession number: Q61824
    Secondary accession number(s): F8VQN4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 31, 2002
    Last sequence update: October 3, 2012
    Last modified: October 1, 2014
    This is version 136 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Marker of skeletal muscle regeneration.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3