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O88839

- ADA15_MOUSE

UniProt

O88839 - ADA15_MOUSE

Protein

Disintegrin and metalloproteinase domain-containing protein 15

Gene

Adam15

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 157 (01 Oct 2014)
      Sequence version 2 (14 Nov 2003)
      Previous versions | rss
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    Functioni

    Active metalloproteinase with gelatinolytic and collagenolytic activity. Plays a role in the wound healing process. Mediates both heterotypic intraepithelial cell/T-cell interactions and homotypic T-cell aggregation. Inhibits beta-1 integrin-mediated cell adhesion and migration of airway smooth muscle cells. Suppresses cell motility on or towards fibronectin possibly by driving alpha-v/beta-1 integrin (ITAGV-ITGB1) cell surface expression via ERK1/2 inactivation. Cleaves E-cadherin in response to growth factor deprivation. Plays a role in glomerular cell migration By similarity. Plays a role in pathological neovascularization. May play a role in cartilage remodeling. May be proteolytically processed, during sperm epididymal maturation and the acrosome reaction. May play a role in sperm-egg binding through its disintegrin domain. Interactions with egg membrane could be mediated via binding between the disintegrin-like domain to one or more integrin receptors on the egg.By similarity4 Publications

    Cofactori

    Binds 1 zinc ion per subunit.Curated

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi179 – 1791Zinc; in inhibited formBy similarity
    Sitei289 – 2902Cleavage; by furinSequence Analysis
    Metal bindingi349 – 3491Zinc; catalyticSequence Analysis
    Active sitei350 – 3501PROSITE-ProRule annotation
    Metal bindingi353 – 3531Zinc; catalyticSequence Analysis
    Metal bindingi359 – 3591Zinc; catalyticSequence Analysis

    GO - Molecular functioni

    1. metalloendopeptidase activity Source: InterPro
    2. protein binding Source: BHF-UCL
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. angiogenesis Source: UniProtKB-KW
    2. cardiac epithelial to mesenchymal transition Source: MGI
    3. cell adhesion Source: UniProtKB-KW
    4. collagen catabolic process Source: UniProtKB-KW
    5. tissue regeneration Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Biological processi

    Angiogenesis, Cell adhesion, Collagen degradation

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_199052. Degradation of the extracellular matrix.

    Protein family/group databases

    MEROPSiM12.215.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Disintegrin and metalloproteinase domain-containing protein 15 (EC:3.4.24.-)
    Short name:
    ADAM 15
    Alternative name(s):
    AD56
    Metalloprotease RGD disintegrin protein
    Metalloproteinase-like, disintegrin-like, and cysteine-rich protein 15
    Short name:
    MDC-15
    Metargidin
    Gene namesi
    Name:Adam15
    Synonyms:Mdc15
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 3

    Organism-specific databases

    MGIiMGI:1333882. Adam15.

    Subcellular locationi

    Endomembrane system 1 Publication; Single-pass type I membrane protein 1 Publication. Cell junctionadherens junction By similarity. Cell projectionciliumflagellum 1 Publication. Cytoplasmic vesiclesecretory vesicleacrosome 1 Publication
    Note: The majority of the protein is localized in a perinuclear compartment which may correspond to the trans-Golgi network or the late endosome. The pro-protein is the major detectable form on the cell surface, whereas the majority of the protein in the cell is processed.

    GO - Cellular componenti

    1. acrosomal vesicle Source: UniProtKB-SubCell
    2. adherens junction Source: UniProtKB-SubCell
    3. cell projection Source: UniProtKB-KW
    4. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cell junction, Cell projection, Cytoplasmic vesicle, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi482 – 4821R → A: Reduced binding to CHO cells expressing ITAG9-ITGB1. 1 Publication
    Mutagenesisi489 – 4891D → A: Reduced binding to CHO cells expressing ITAG9-ITGB1. 1 Publication
    Mutagenesisi490 – 4901L → A: Reduced binding to CHO cells expressing ITAG9-ITGB1. 1 Publication
    Mutagenesisi491 – 4911P → A: Reduced binding to CHO cells expressing ITAG9-ITGB1. 1 Publication
    Mutagenesisi492 – 4921E → A: Reduced binding to CHO cells expressing ITAG9-ITGB1. 1 Publication
    Mutagenesisi493 – 4931F → A: Reduced binding to CHO cells expressing ITAG9-ITGB1. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1717Sequence AnalysisAdd
    BLAST
    Propeptidei18 – 207190CuratedPRO_0000029084Add
    BLAST
    Chaini208 – 864657Disintegrin and metalloproteinase domain-containing protein 15PRO_0000029085Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi238 – 2381N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi324 ↔ 410By similarity
    Disulfide bondi366 ↔ 394By similarity
    Disulfide bondi368 ↔ 377By similarity
    Glycosylationi390 – 3901N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi393 – 3931N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi481 ↔ 501By similarity
    Glycosylationi607 – 6071N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi612 – 6121N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi658 ↔ 668By similarity
    Disulfide bondi662 ↔ 674By similarity
    Disulfide bondi676 ↔ 685By similarity
    Modified residuei716 – 7161Phosphotyrosine; by HCK and LCKBy similarity
    Modified residuei736 – 7361Phosphotyrosine; by HCK and LCKBy similarity

    Post-translational modificationi

    The precursor is cleaved by a furin endopeptidase. An additional membrane proximal site of cleavage affects a small percentage of the proteins and results in disulfide-linked fragments. The prodomain is apparently cleaved in several positions that are N-terminal of the furin cleavage site.1 Publication
    May be partially sialylated.
    Phosphorylation increases association with PTKs.By similarity

    Keywords - PTMi

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

    Proteomic databases

    PaxDbiO88839.
    PRIDEiO88839.

    PTM databases

    PhosphoSiteiO88839.

    Expressioni

    Tissue specificityi

    Expressed moderately in pericytes of retina. Expressed in testis and in spermatozoa from the caput, corpus, and cauda epididymis, as well as in non-capacitated and acrosome-reacted sperm (at protein level). Highly expressed in heart, brain, lung, and kidney. Expressed at lower levels in spleen, liver, testis and muscle.2 Publications

    Developmental stagei

    At E13.5, strongly expressed in the developing vasculature of the endocardium. At P17, expressed throughout the retina (at protein level). At E9.5 and thereafter, prominently expressed in the vasculature, including in ventral and dorsal aorta and the caudal artery. In developing heart, detected in endocardium and blood vessels of the ventricle, bulbus arteriosus, and atrium. Also highly expressed in hypertrophic cells of the developing bone. In adult, expressed prominently in brain, including in hippocampus, cerebellum, pons, thalamus, cortex, and olfactory bulb.2 Publications

    Inductioni

    By hypoxic stimulus in retina (at protein level). Up-regulated by VEGF in retina.2 Publications

    Gene expression databases

    BgeeiO88839.
    GenevestigatoriO88839.

    Interactioni

    Subunit structurei

    Interacts specifically with Src family protein-tyrosine kinases (PTKs) By similarity. Interacts with ITAGV-ITGB3 (vitronectin receptor). Interacts with SH3GL2 and SNX9; this interaction occurs preferentially with ADAM15 precursor, rather than the processed form, suggesting it occurs in a secretory pathway compartment prior to the medial Golgi. Interacts with ITAG9-ITGB1. Interacts with SH3PXD2A By similarity. Interacts with ITAGV-ITGB1. Interacts with GRB2, HCK, ITSN1, ITSN2, LYN, MAPK1, MAPK3, NCF1, NCK1, nephrocystin, PTK6, SNX33, LCK and SRC By similarity.By similarity

    Protein-protein interaction databases

    IntActiO88839. 3 interactions.
    MINTiMINT-4996290.

    Structurei

    3D structure databases

    ProteinModelPortaliO88839.
    SMRiO88839. Positions 208-687.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini208 – 696489ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini718 – 864147CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei697 – 71721HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini214 – 415202Peptidase M12BPROSITE-ProRule annotationAdd
    BLAST
    Domaini422 – 50988DisintegrinPROSITE-ProRule annotationAdd
    BLAST
    Domaini658 – 68629EGF-likePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi177 – 1848Cysteine switchBy similarity
    Motifi816 – 8227SH3-bindingSequence Analysis
    Motifi851 – 8577SH3-bindingSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi510 – 657148Cys-richAdd
    BLAST
    Compositional biasi699 – 71214Poly-LeuAdd
    BLAST

    Domaini

    The cytoplasmic domain is required for SH3GL2- and SNX9-binding.
    Disintegrin domain binds to integrin alphaV-beta3.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.
    HOVERGENiHBG006978.
    InParanoidiQ3UE21.
    KOiK06836.
    OMAiHGVCDSN.
    OrthoDBiEOG7F7W89.
    PhylomeDBiO88839.
    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.
    IPR000742. EG-like_dom.
    IPR013032. EGF-like_CS.
    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]
    SMARTiSM00608. ACR. 1 hit.
    SM00050. DISIN. 1 hit.
    SM00181. EGF. 1 hit.
    [Graphical view]
    SUPFAMiSSF57552. SSF57552. 1 hit.
    PROSITEiPS50215. ADAM_MEPRO. 1 hit.
    PS50214. DISINTEGRIN_2. 1 hit.
    PS01186. EGF_2. 1 hit.
    PS50026. EGF_3. 1 hit.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O88839-1) [UniParc]FASTAAdd to Basket

    Also known as: ADAM15v2

    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

    MRLALLWALG LLGAGSPRPS PPLPNIGGTE EEQQASPERT LSGSMESRVV    50
    QDSPPMSLAD VLQTGLPEAL RISLELDSES HVLELLQNRD LIPGRPTLVW 100
    YQPDGTRMVS EGYSLENCCY RGRVQGHPSS WVSLCACSGI RGLIVLSPER 150
    GYTLELGPGD LQRPVISRIQ DHLLLGHTCA PSWHASVPTR AGPDLLLEQH 200
    HAHRLKRDVV TETKIVELVI VADNSEVRKY PDFQQLLNRT LEAALLLDTF 250
    FQPLNVRVAL VGLEAWTQHN LIEMSSNPAV LLDNFLRWRR TDLLPRLPHD 300
    SAQLVTVTSF SGPMVGMAIQ NSICSPDFSG GVNMDHSTSI LGVASSIAHE 350
    LGHSLGLDHD SPGHSCPCPG PAPAKSCIME ASTDFLPGLN FSNCSRQALE 400
    KALLEGMGSC LFERQPSLAP MSSLCGNMFV DPGEQCDCGF PDECTDPCCD 450
    HFTCQLRPGA QCASDGPCCQ NCKLHPAGWL CRPPTDDCDL PEFCPGDSSQ 500
    CPSDIRLGDG EPCASGEAVC MHGRCASYAR QCQSLWGPGA QPAAPLCLQT 550
    ANTRGNAFGS CGRSPGGSYM PCAPRDVMCG QLQCQWGRSQ PLLGSVQDRL 600
    SEVLEANGTQ LNCSWVDLDL GNDVAQPLLA LPGTACGPGL VCIGHRCQPV 650
    DLLGAQECRR KCHGHGVCDS SGHCRCEEGW APPDCMTQLK ATSSLTTGLL 700
    LSLLLLLVLV LLGASYWHRA RLHQRLCQLK GSSCQYRAPQ SCPPERPGPP 750
    QRAQQMTGTK QASVVSFPVP PSRPLPPNPV PKKLQAALAD RSNPPTRPLP 800
    ADPVVRRPKS QGPTKPPPPR KPLPANPQGQ HPPGDLPGPG DGSLPLVVPS 850
    RPAPPPPAAS SLYL 864
    Length:864
    Mass (Da):92,664
    Last modified:November 14, 2003 - v2
    Checksum:iB1CBEB923463BB15
    GO
    Isoform 2 (identifier: O88839-2) [UniParc]FASTAAdd to Basket

    Also known as: ADAM15v1

    The sequence of this isoform differs from the canonical sequence as follows:
         761-785: Missing.

    Show »
    Length:839
    Mass (Da):90,002
    Checksum:i0C61FAA9B79B8123
    GO
    Isoform 3 (identifier: O88839-3) [UniParc]FASTAAdd to Basket

    Also known as: ADAM15

    The sequence of this isoform differs from the canonical sequence as follows:
         761-809: Missing.

    Show »
    Length:815
    Mass (Da):87,425
    Checksum:iC064BD3B7347D19B
    GO
    Isoform 4 (identifier: O88839-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         415-830: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:448
    Mass (Da):48,417
    Checksum:i37FEB93BD3704400
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti21 – 222PP → RR in BAA88903. (PubMed:13679040)Curated
    Sequence conflicti51 – 511Q → H in BAE29090. (PubMed:16141072)Curated
    Sequence conflicti73 – 731S → P in BAE41564. (PubMed:16141072)Curated
    Sequence conflicti443 – 4431E → Q in BAA88903. (PubMed:13679040)Curated
    Sequence conflicti459 – 4591G → E in BAA88903. (PubMed:13679040)Curated
    Sequence conflicti564 – 5652SP → T in BAA88903. (PubMed:13679040)Curated
    Sequence conflicti654 – 6541G → E in BAA88903. (PubMed:13679040)Curated
    Sequence conflicti660 – 6601R → S in BAA88903. (PubMed:13679040)Curated
    Sequence conflicti703 – 7031L → R in BAA88903. (PubMed:13679040)Curated
    Sequence conflicti712 – 7121L → R in BAA88903. (PubMed:13679040)Curated
    Sequence conflicti729 – 7291L → R in BAA88903. (PubMed:13679040)Curated
    Sequence conflicti830 – 8301Q → R in BAE41564. (PubMed:16141072)Curated
    Sequence conflicti846 – 8461L → S in BAA88903. (PubMed:13679040)Curated
    Sequence conflicti852 – 8543PAP → AAS in BAA88903. (PubMed:13679040)Curated
    Sequence conflicti859 – 8591A → P in BAA88903. (PubMed:13679040)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei415 – 830416Missing in isoform 4. 1 PublicationVSP_008879Add
    BLAST
    Alternative sequencei761 – 80949Missing in isoform 3. 2 PublicationsVSP_008881Add
    BLAST
    Alternative sequencei761 – 78525Missing in isoform 2. CuratedVSP_008880Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF006196 mRNA. Translation: AAC61896.1.
    AB022089 Genomic DNA. Translation: BAA88903.1.
    AK048901 mRNA. Translation: BAC33485.1.
    AK149796 mRNA. Translation: BAE29090.1.
    AK151804 mRNA. Translation: BAE30703.1.
    AK152725 mRNA. Translation: BAE31447.1.
    AK170101 mRNA. Translation: BAE41564.1.
    BC009132 mRNA. Translation: AAH09132.1.
    EF506571 mRNA. Translation: ABP73662.1.
    CCDSiCCDS17502.1. [O88839-1]
    CCDS17503.1. [O88839-3]
    RefSeqiNP_001032811.2. NM_001037722.2. [O88839-1]
    NP_033744.1. NM_009614.2. [O88839-3]
    XP_006500981.1. XM_006500918.1. [O88839-2]
    UniGeneiMm.274049.
    Mm.470104.

    Genome annotation databases

    EnsembliENSMUST00000029676; ENSMUSP00000029676; ENSMUSG00000028041. [O88839-1]
    ENSMUST00000074582; ENSMUSP00000074167; ENSMUSG00000028041. [O88839-3]
    ENSMUST00000107446; ENSMUSP00000103070; ENSMUSG00000028041. [O88839-4]
    ENSMUST00000107448; ENSMUSP00000103072; ENSMUSG00000028041. [O88839-2]
    ENSMUST00000184651; ENSMUSP00000139147; ENSMUSG00000028041. [O88839-1]
    GeneIDi11490.
    KEGGimmu:11490.
    UCSCiuc008pyv.1. mouse. [O88839-1]
    uc008pyw.1. mouse. [O88839-3]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF006196 mRNA. Translation: AAC61896.1 .
    AB022089 Genomic DNA. Translation: BAA88903.1 .
    AK048901 mRNA. Translation: BAC33485.1 .
    AK149796 mRNA. Translation: BAE29090.1 .
    AK151804 mRNA. Translation: BAE30703.1 .
    AK152725 mRNA. Translation: BAE31447.1 .
    AK170101 mRNA. Translation: BAE41564.1 .
    BC009132 mRNA. Translation: AAH09132.1 .
    EF506571 mRNA. Translation: ABP73662.1 .
    CCDSi CCDS17502.1. [O88839-1 ]
    CCDS17503.1. [O88839-3 ]
    RefSeqi NP_001032811.2. NM_001037722.2. [O88839-1 ]
    NP_033744.1. NM_009614.2. [O88839-3 ]
    XP_006500981.1. XM_006500918.1. [O88839-2 ]
    UniGenei Mm.274049.
    Mm.470104.

    3D structure databases

    ProteinModelPortali O88839.
    SMRi O88839. Positions 208-687.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi O88839. 3 interactions.
    MINTi MINT-4996290.

    Protein family/group databases

    MEROPSi M12.215.

    PTM databases

    PhosphoSitei O88839.

    Proteomic databases

    PaxDbi O88839.
    PRIDEi O88839.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000029676 ; ENSMUSP00000029676 ; ENSMUSG00000028041 . [O88839-1 ]
    ENSMUST00000074582 ; ENSMUSP00000074167 ; ENSMUSG00000028041 . [O88839-3 ]
    ENSMUST00000107446 ; ENSMUSP00000103070 ; ENSMUSG00000028041 . [O88839-4 ]
    ENSMUST00000107448 ; ENSMUSP00000103072 ; ENSMUSG00000028041 . [O88839-2 ]
    ENSMUST00000184651 ; ENSMUSP00000139147 ; ENSMUSG00000028041 . [O88839-1 ]
    GeneIDi 11490.
    KEGGi mmu:11490.
    UCSCi uc008pyv.1. mouse. [O88839-1 ]
    uc008pyw.1. mouse. [O88839-3 ]

    Organism-specific databases

    CTDi 8751.
    MGIi MGI:1333882. Adam15.

    Phylogenomic databases

    eggNOGi NOG294463.
    GeneTreei ENSGT00740000114848.
    HOVERGENi HBG006978.
    InParanoidi Q3UE21.
    KOi K06836.
    OMAi HGVCDSN.
    OrthoDBi EOG7F7W89.
    PhylomeDBi O88839.
    TreeFami TF314733.

    Enzyme and pathway databases

    Reactomei REACT_199052. Degradation of the extracellular matrix.

    Miscellaneous databases

    NextBioi 278860.
    PROi O88839.
    SOURCEi Search...

    Gene expression databases

    Bgeei O88839.
    Genevestigatori O88839.

    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.
    IPR000742. EG-like_dom.
    IPR013032. EGF-like_CS.
    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 ]
    SMARTi SM00608. ACR. 1 hit.
    SM00050. DISIN. 1 hit.
    SM00181. EGF. 1 hit.
    [Graphical view ]
    SUPFAMi SSF57552. SSF57552. 1 hit.
    PROSITEi PS50215. ADAM_MEPRO. 1 hit.
    PS50214. DISINTEGRIN_2. 1 hit.
    PS01186. EGF_2. 1 hit.
    PS50026. EGF_3. 1 hit.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Intracellular maturation of the mouse metalloprotease disintegrin MDC15."
      Lum L., Reid M.S., Blobel C.P.
      J. Biol. Chem. 273:26236-26247(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), PROTEOLYTIC PROCESSING.
      Tissue: Lung.
    2. "Structure and expression of the murine ADAM 15 gene and its splice variants, and difference of interaction between their cytoplasmic domains and Src family proteins."
      Shimizu E., Yasui A., Matsuura K., Hijiya N., Higuchi Y., Yamamoto S.
      Biochem. Biophys. Res. Commun. 309:779-785(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2 AND 3).
      Tissue: Myeloid and Myeloma.
    3. "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 3).
      Strain: C57BL/6J and NOD.
      Tissue: Bone marrow macrophage, Cerebellum and Dendritic cell.
    4. "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 4).
      Tissue: Mammary gland.
    5. "Presence, processing, and localization of mouse ADAM15 during sperm maturation and the role of its disintegrin domain during sperm-egg binding."
      Pasten-Hidalgo K., Hernandez-Rivas R., Roa-Espitia A.L., Sanchez-Gutierrez M., Martinez-Perez F., Monrroy A.O., Hernandez-Gonzalez E.O., Mujica A.
      Reproduction 136:41-51(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 207-694 (ISOFORMS 1/2/3), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Testis.
    6. "Interaction of the metalloprotease disintegrins MDC9 and MDC15 with two SH3 domain-containing proteins, endophilin I and SH3PX1."
      Howard L., Nelson K.K., Maciewicz R.A., Blobel C.P.
      J. Biol. Chem. 274:31693-31699(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ENDOPHILIN I AND SNX9.
    7. "Functional classification of ADAMs based on a conserved motif for binding to integrin alpha 9beta 1: implications for sperm-egg binding and other cell interactions."
      Eto K., Huet C., Tarui T., Kupriyanov S., Liu H.Z., Puzon-McLaughlin W., Zhang X.P., Sheppard D., Engvall E., Takada Y.
      J. Biol. Chem. 277:17804-17810(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH INTEGRIN ALPHAV-BETA3 AND ALPHA9-BETA1, MUTAGENESIS OF ARG-482; ASP-489; LEU-490; PRO-491; GLU-492 AND PHE-493.
    8. Cited for: FUNCTION, DEVELOPMENTAL STAGE, INDUCTION.
    9. "Homeostatic effects of the metalloproteinase disintegrin ADAM15 in degenerative cartilage remodeling."
      Bohm B.B., Aigner T., Roy B., Brodie T.A., Blobel C.P., Burkhardt H.
      Arthritis Rheum. 52:1100-1109(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "An Adam15 amplification loop promotes vascular endothelial growth factor-induced ocular neovascularization."
      Xie B., Shen J., Dong A., Swaim M., Hackett S.F., Wyder L., Worpenberg S., Barbieri S., Campochiaro P.A.
      FASEB J. 22:2775-2783(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION.

    Entry informationi

    Entry nameiADA15_MOUSE
    AccessioniPrimary (citable) accession number: O88839
    Secondary accession number(s): A4ZYV2
    , Q3TDN7, Q3U7C2, Q3UE21, Q8C7Z0, Q91VS9, Q9QYL2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 2001
    Last sequence update: November 14, 2003
    Last modified: October 1, 2014
    This is version 157 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Mice targeted for deletion of the first 27 amino acids of the ADAM15 N-terminal sequence are viable and fertile, showing no major developmental defects and displaying normal mortality or morbidity. These mutant mice, however, exhibit significantly reduced ischemia-induced retinal neovascularization, choroidal neovascularization at rupture sites in Bruch's membrane, and VEGF-induced subretinal neovascularization, and develop significantly smaller tumors following implantation of B16F0 melanoma cells. Aging mutant mice exhibit accelerated development of osteoarthritic lesions in knee joints.

    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