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O88839

- ADA15_MOUSE

UniProt

O88839 - ADA15_MOUSE

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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

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. 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
Complete GO annotation...

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. cell junction Source: UniProtKB-KW
  2. cell projection Source: UniProtKB-KW
  3. cytoplasmic vesicle Source: UniProtKB-KW
  4. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

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

MaxQBiO88839.
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.
GeneTreeiENSGT00760000118888.
HOVERGENiHBG006978.
InParanoidiO88839.
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

        10         20         30         40         50
MRLALLWALG LLGAGSPRPS PPLPNIGGTE EEQQASPERT LSGSMESRVV
60 70 80 90 100
QDSPPMSLAD VLQTGLPEAL RISLELDSES HVLELLQNRD LIPGRPTLVW
110 120 130 140 150
YQPDGTRMVS EGYSLENCCY RGRVQGHPSS WVSLCACSGI RGLIVLSPER
160 170 180 190 200
GYTLELGPGD LQRPVISRIQ DHLLLGHTCA PSWHASVPTR AGPDLLLEQH
210 220 230 240 250
HAHRLKRDVV TETKIVELVI VADNSEVRKY PDFQQLLNRT LEAALLLDTF
260 270 280 290 300
FQPLNVRVAL VGLEAWTQHN LIEMSSNPAV LLDNFLRWRR TDLLPRLPHD
310 320 330 340 350
SAQLVTVTSF SGPMVGMAIQ NSICSPDFSG GVNMDHSTSI LGVASSIAHE
360 370 380 390 400
LGHSLGLDHD SPGHSCPCPG PAPAKSCIME ASTDFLPGLN FSNCSRQALE
410 420 430 440 450
KALLEGMGSC LFERQPSLAP MSSLCGNMFV DPGEQCDCGF PDECTDPCCD
460 470 480 490 500
HFTCQLRPGA QCASDGPCCQ NCKLHPAGWL CRPPTDDCDL PEFCPGDSSQ
510 520 530 540 550
CPSDIRLGDG EPCASGEAVC MHGRCASYAR QCQSLWGPGA QPAAPLCLQT
560 570 580 590 600
ANTRGNAFGS CGRSPGGSYM PCAPRDVMCG QLQCQWGRSQ PLLGSVQDRL
610 620 630 640 650
SEVLEANGTQ LNCSWVDLDL GNDVAQPLLA LPGTACGPGL VCIGHRCQPV
660 670 680 690 700
DLLGAQECRR KCHGHGVCDS SGHCRCEEGW APPDCMTQLK ATSSLTTGLL
710 720 730 740 750
LSLLLLLVLV LLGASYWHRA RLHQRLCQLK GSSCQYRAPQ SCPPERPGPP
760 770 780 790 800
QRAQQMTGTK QASVVSFPVP PSRPLPPNPV PKKLQAALAD RSNPPTRPLP
810 820 830 840 850
ADPVVRRPKS QGPTKPPPPR KPLPANPQGQ HPPGDLPGPG DGSLPLVVPS
860
RPAPPPPAAS SLYL
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

MaxQBi O88839.
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 ENSGT00760000118888.
HOVERGENi HBG006978.
InParanoidi O88839.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 158 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