SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O88839

- ADA15_MOUSE

UniProt

O88839 - ADA15_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Disintegrin and metalloproteinase domain-containing protein 15
Gene
Adam15, Mdc15
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.4 Publications

Cofactori

Binds 1 zinc ion per subunit Reviewed prediction.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi179 – 1791Zinc; in inhibited form By similarity
Sitei289 – 2902Cleavage; by furin Reviewed prediction
Metal bindingi349 – 3491Zinc; catalytic Reviewed prediction
Active sitei350 – 3501 Reviewed prediction
Metal bindingi353 – 3531Zinc; catalytic Reviewed prediction
Metal bindingi359 – 3591Zinc; catalytic Reviewed prediction

GO - Molecular functioni

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

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; Single-pass type I membrane protein. Cell junctionadherens junction By similarity. Cell projectionciliumflagellum. Cytoplasmic vesiclesecretory vesicleacrosome
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.1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini208 – 696489Extracellular Reviewed prediction
Add
BLAST
Transmembranei697 – 71721Helical; Reviewed prediction
Add
BLAST
Topological domaini718 – 864147Cytoplasmic Reviewed prediction
Add
BLAST

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
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 – 1717 Reviewed prediction
Add
BLAST
Propeptidei18 – 207190 Inferred
PRO_0000029084Add
BLAST
Chaini208 – 864657Disintegrin and metalloproteinase domain-containing protein 15
PRO_0000029085Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi238 – 2381N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi324 ↔ 410 By similarity
Disulfide bondi366 ↔ 394 By similarity
Disulfide bondi368 ↔ 377 By similarity
Glycosylationi390 – 3901N-linked (GlcNAc...) Reviewed prediction
Glycosylationi393 – 3931N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi481 ↔ 501 By similarity
Glycosylationi607 – 6071N-linked (GlcNAc...) Reviewed prediction
Glycosylationi612 – 6121N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi658 ↔ 668 By similarity
Disulfide bondi662 ↔ 674 By similarity
Disulfide bondi676 ↔ 685 By similarity
Modified residuei716 – 7161Phosphotyrosine; by HCK and LCK By similarity
Modified residuei736 – 7361Phosphotyrosine; by HCK and LCK By 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.2 Publications

Protein-protein interaction databases

IntActiO88839. 3 interactions.
MINTiMINT-4996290.

Structurei

3D structure databases

ProteinModelPortaliO88839.
SMRiO88839. Positions 208-687.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini214 – 415202Peptidase M12B
Add
BLAST
Domaini422 – 50988Disintegrin
Add
BLAST
Domaini658 – 68629EGF-like
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi177 – 1848Cysteine switch By similarity
Motifi816 – 8227SH3-binding Reviewed prediction
Motifi851 – 8577SH3-binding Reviewed prediction

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi510 – 657148Cys-rich
Add
BLAST
Compositional biasi699 – 71214Poly-Leu
Add
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.
Contains 1 EGF-like domain.

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei415 – 830416Missing in isoform 4.
VSP_008879Add
BLAST
Alternative sequencei761 – 80949Missing in isoform 3.
VSP_008881Add
BLAST
Alternative sequencei761 – 78525Missing in isoform 2.
VSP_008880Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti21 – 222PP → RR in BAA88903. 1 Publication
Sequence conflicti51 – 511Q → H in BAE29090. 1 Publication
Sequence conflicti73 – 731S → P in BAE41564. 1 Publication
Sequence conflicti443 – 4431E → Q in BAA88903. 1 Publication
Sequence conflicti459 – 4591G → E in BAA88903. 1 Publication
Sequence conflicti564 – 5652SP → T in BAA88903. 1 Publication
Sequence conflicti654 – 6541G → E in BAA88903. 1 Publication
Sequence conflicti660 – 6601R → S in BAA88903. 1 Publication
Sequence conflicti703 – 7031L → R in BAA88903. 1 Publication
Sequence conflicti712 – 7121L → R in BAA88903. 1 Publication
Sequence conflicti729 – 7291L → R in BAA88903. 1 Publication
Sequence conflicti830 – 8301Q → R in BAE41564. 1 Publication
Sequence conflicti846 – 8461L → S in BAA88903. 1 Publication
Sequence conflicti852 – 8543PAP → AAS in BAA88903. 1 Publication
Sequence conflicti859 – 8591A → P in BAA88903. 1 Publication

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...

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

« 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: September 3, 2014
This is version 156 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

Similar proteinsi