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O88839 (ADA15_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 155. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Disintegrin and metalloproteinase domain-containing protein 15

Short name=ADAM 15
EC=3.4.24.-
Alternative name(s):
AD56
Metalloprotease RGD disintegrin protein
Metalloproteinase-like, disintegrin-like, and cysteine-rich protein 15
Short name=MDC-15
Metargidin
Gene names
Name:Adam15
Synonyms:Mdc15
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length864 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5 Ref.7 Ref.8 Ref.9

Cofactor

Binds 1 zinc ion per subunit Potential.

Subunit structure

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. Ref.6 Ref.7

Subcellular location

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. Ref.5

Tissue specificity

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. Ref.5 Ref.10

Developmental stage

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. Ref.8 Ref.10

Induction

By hypoxic stimulus in retina (at protein level). Up-regulated by VEGF in retina. Ref.8 Ref.10

Domain

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.

Post-translational modification

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. Ref.1

May be partially sialylated.

Phosphorylation increases association with PTKs By similarity.

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.

Sequence similarities

Contains 1 disintegrin domain.

Contains 1 EGF-like domain.

Contains 1 peptidase M12B domain.

Ontologies

Keywords
   Biological processAngiogenesis
Cell adhesion
Collagen degradation
   Cellular componentCell junction
Cell projection
Cytoplasmic vesicle
Membrane
   Coding sequence diversityAlternative splicing
   DomainEGF-like domain
SH3-binding
Signal
Transmembrane
Transmembrane helix
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Phosphoprotein
Zymogen
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processangiogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

cardiac epithelial to mesenchymal transition

Inferred from mutant phenotype PubMed 19156209. Source: MGI

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

collagen catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

tissue regeneration

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentacrosomal vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

adherens junction

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell projection

Inferred from electronic annotation. Source: UniProtKB-KW

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionmetalloendopeptidase activity

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction Ref.6. Source: BHF-UCL

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O88839-1)

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.
Isoform 2 (identifier: O88839-2)

Also known as: ADAM15v1;

The sequence of this isoform differs from the canonical sequence as follows:
     761-785: Missing.
Isoform 3 (identifier: O88839-3)

Also known as: ADAM15;

The sequence of this isoform differs from the canonical sequence as follows:
     761-809: Missing.
Isoform 4 (identifier: O88839-4)

The sequence of this isoform differs from the canonical sequence as follows:
     415-830: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Propeptide18 – 207190 Probable
PRO_0000029084
Chain208 – 864657Disintegrin and metalloproteinase domain-containing protein 15
PRO_0000029085

Regions

Topological domain208 – 696489Extracellular Potential
Transmembrane697 – 71721Helical; Potential
Topological domain718 – 864147Cytoplasmic Potential
Domain214 – 415202Peptidase M12B
Domain422 – 50988Disintegrin
Domain658 – 68629EGF-like
Motif177 – 1848Cysteine switch By similarity
Motif816 – 8227SH3-binding Potential
Motif851 – 8577SH3-binding Potential
Compositional bias510 – 657148Cys-rich
Compositional bias699 – 71214Poly-Leu

Sites

Active site3501 Potential
Metal binding1791Zinc; in inhibited form By similarity
Metal binding3491Zinc; catalytic Potential
Metal binding3531Zinc; catalytic Potential
Metal binding3591Zinc; catalytic Potential
Site289 – 2902Cleavage; by furin Potential

Amino acid modifications

Modified residue7161Phosphotyrosine; by HCK and LCK By similarity
Modified residue7361Phosphotyrosine; by HCK and LCK By similarity
Glycosylation2381N-linked (GlcNAc...) Potential
Glycosylation3901N-linked (GlcNAc...) Potential
Glycosylation3931N-linked (GlcNAc...) Potential
Glycosylation6071N-linked (GlcNAc...) Potential
Glycosylation6121N-linked (GlcNAc...) Potential
Disulfide bond324 ↔ 410 By similarity
Disulfide bond366 ↔ 394 By similarity
Disulfide bond368 ↔ 377 By similarity
Disulfide bond481 ↔ 501 By similarity
Disulfide bond658 ↔ 668 By similarity
Disulfide bond662 ↔ 674 By similarity
Disulfide bond676 ↔ 685 By similarity

Natural variations

Alternative sequence415 – 830416Missing in isoform 4.
VSP_008879
Alternative sequence761 – 80949Missing in isoform 3.
VSP_008881
Alternative sequence761 – 78525Missing in isoform 2.
VSP_008880

Experimental info

Mutagenesis4821R → A: Reduced binding to CHO cells expressing ITAG9-ITGB1. Ref.7
Mutagenesis4891D → A: Reduced binding to CHO cells expressing ITAG9-ITGB1. Ref.7
Mutagenesis4901L → A: Reduced binding to CHO cells expressing ITAG9-ITGB1. Ref.7
Mutagenesis4911P → A: Reduced binding to CHO cells expressing ITAG9-ITGB1. Ref.7
Mutagenesis4921E → A: Reduced binding to CHO cells expressing ITAG9-ITGB1. Ref.7
Mutagenesis4931F → A: Reduced binding to CHO cells expressing ITAG9-ITGB1. Ref.7
Sequence conflict21 – 222PP → RR in BAA88903. Ref.2
Sequence conflict511Q → H in BAE29090. Ref.3
Sequence conflict731S → P in BAE41564. Ref.3
Sequence conflict4431E → Q in BAA88903. Ref.2
Sequence conflict4591G → E in BAA88903. Ref.2
Sequence conflict564 – 5652SP → T in BAA88903. Ref.2
Sequence conflict6541G → E in BAA88903. Ref.2
Sequence conflict6601R → S in BAA88903. Ref.2
Sequence conflict7031L → R in BAA88903. Ref.2
Sequence conflict7121L → R in BAA88903. Ref.2
Sequence conflict7291L → R in BAA88903. Ref.2
Sequence conflict8301Q → R in BAE41564. Ref.3
Sequence conflict8461L → S in BAA88903. Ref.2
Sequence conflict852 – 8543PAP → AAS in BAA88903. Ref.2
Sequence conflict8591A → P in BAA88903. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (ADAM15v2) [UniParc].

Last modified November 14, 2003. Version 2.
Checksum: B1CBEB923463BB15

FASTA86492,664
        10         20         30         40         50         60 
MRLALLWALG LLGAGSPRPS PPLPNIGGTE EEQQASPERT LSGSMESRVV QDSPPMSLAD 

        70         80         90        100        110        120 
VLQTGLPEAL RISLELDSES HVLELLQNRD LIPGRPTLVW YQPDGTRMVS EGYSLENCCY 

       130        140        150        160        170        180 
RGRVQGHPSS WVSLCACSGI RGLIVLSPER GYTLELGPGD LQRPVISRIQ DHLLLGHTCA 

       190        200        210        220        230        240 
PSWHASVPTR AGPDLLLEQH HAHRLKRDVV TETKIVELVI VADNSEVRKY PDFQQLLNRT 

       250        260        270        280        290        300 
LEAALLLDTF FQPLNVRVAL VGLEAWTQHN LIEMSSNPAV LLDNFLRWRR TDLLPRLPHD 

       310        320        330        340        350        360 
SAQLVTVTSF SGPMVGMAIQ NSICSPDFSG GVNMDHSTSI LGVASSIAHE LGHSLGLDHD 

       370        380        390        400        410        420 
SPGHSCPCPG PAPAKSCIME ASTDFLPGLN FSNCSRQALE KALLEGMGSC LFERQPSLAP 

       430        440        450        460        470        480 
MSSLCGNMFV DPGEQCDCGF PDECTDPCCD HFTCQLRPGA QCASDGPCCQ NCKLHPAGWL 

       490        500        510        520        530        540 
CRPPTDDCDL PEFCPGDSSQ CPSDIRLGDG EPCASGEAVC MHGRCASYAR QCQSLWGPGA 

       550        560        570        580        590        600 
QPAAPLCLQT ANTRGNAFGS CGRSPGGSYM PCAPRDVMCG QLQCQWGRSQ PLLGSVQDRL 

       610        620        630        640        650        660 
SEVLEANGTQ LNCSWVDLDL GNDVAQPLLA LPGTACGPGL VCIGHRCQPV DLLGAQECRR 

       670        680        690        700        710        720 
KCHGHGVCDS SGHCRCEEGW APPDCMTQLK ATSSLTTGLL LSLLLLLVLV LLGASYWHRA 

       730        740        750        760        770        780 
RLHQRLCQLK GSSCQYRAPQ SCPPERPGPP QRAQQMTGTK QASVVSFPVP PSRPLPPNPV 

       790        800        810        820        830        840 
PKKLQAALAD RSNPPTRPLP ADPVVRRPKS QGPTKPPPPR KPLPANPQGQ HPPGDLPGPG 

       850        860 
DGSLPLVVPS RPAPPPPAAS SLYL 

« Hide

Isoform 2 (ADAM15v1) [UniParc].

Checksum: 0C61FAA9B79B8123
Show »

FASTA83990,002
Isoform 3 (ADAM15) [UniParc].

Checksum: C064BD3B7347D19B
Show »

FASTA81587,425
Isoform 4 [UniParc].

Checksum: 37FEB93BD3704400
Show »

FASTA44848,417

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Potential role for ADAM15 in pathological neovascularization in mice."
Horiuchi K., Weskamp G., Lum L., Hammes H.P., Cai H., Brodie T.A., Ludwig T., Chiusaroli R., Baron R., Preissner K.T., Manova K., Blobel C.P.
Mol. Cell. Biol. 23:5614-5624(2003) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS17502.1. [O88839-1]
CCDS17503.1. [O88839-3]
RefSeqNP_001032811.2. NM_001037722.2. [O88839-1]
NP_033744.1. NM_009614.2. [O88839-3]
XP_006500981.1. XM_006500918.1. [O88839-2]
UniGeneMm.274049.
Mm.470104.

3D structure databases

ProteinModelPortalO88839.
SMRO88839. Positions 208-687.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO88839. 3 interactions.
MINTMINT-4996290.

Protein family/group databases

MEROPSM12.215.

PTM databases

PhosphoSiteO88839.

Proteomic databases

PaxDbO88839.
PRIDEO88839.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000029676; ENSMUSP00000029676; ENSMUSG00000028041. [O88839-1]
ENSMUST00000074582; ENSMUSP00000074167; ENSMUSG00000028041. [O88839-3]
ENSMUST00000107446; ENSMUSP00000103070; ENSMUSG00000028041. [O88839-4]
ENSMUST00000107448; ENSMUSP00000103072; ENSMUSG00000028041. [O88839-2]
ENSMUST00000184651; ENSMUSP00000139147; ENSMUSG00000028041. [O88839-1]
GeneID11490.
KEGGmmu:11490.
UCSCuc008pyv.1. mouse. [O88839-1]
uc008pyw.1. mouse. [O88839-3]

Organism-specific databases

CTD8751.
MGIMGI:1333882. Adam15.

Phylogenomic databases

eggNOGNOG294463.
GeneTreeENSGT00740000114848.
HOVERGENHBG006978.
InParanoidQ3UE21.
KOK06836.
OMAHGVCDSN.
OrthoDBEOG7F7W89.
PhylomeDBO88839.
TreeFamTF314733.

Gene expression databases

BgeeO88839.
GenevestigatorO88839.

Family and domain databases

Gene3D3.40.390.10. 1 hit.
4.10.70.10. 1 hit.
InterProIPR006586. 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]
PfamPF08516. ADAM_CR. 1 hit.
PF00200. Disintegrin. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
[Graphical view]
SMARTSM00608. ACR. 1 hit.
SM00050. DISIN. 1 hit.
SM00181. EGF. 1 hit.
[Graphical view]
SUPFAMSSF57552. SSF57552. 1 hit.
PROSITEPS50215. 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]
ProtoNetSearch...

Other

NextBio278860.
PROO88839.
SOURCESearch...

Entry information

Entry nameADA15_MOUSE
AccessionPrimary (citable) accession number: O88839
Secondary accession number(s): A4ZYV2 expand/collapse secondary AC list , Q3TDN7, Q3U7C2, Q3UE21, Q8C7Z0, Q91VS9, Q9QYL2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: November 14, 2003
Last modified: July 9, 2014
This is version 155 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot