O88839 (ADA15_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	864 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 junction › adherens junction By similarity. Cell projection › cilium › flagellum. Cytoplasmic vesicle › secretory vesicle › acrosome. 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 process	Angiogenesis Cell adhesion Collagen degradation
Cellular component	Cell junction Cell projection Cytoplasmic vesicle Membrane
Coding sequence diversity	Alternative splicing
Domain	EGF-like domain SH3-binding Signal Transmembrane Transmembrane helix
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Phosphoprotein Zymogen
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	angiogenesis 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 proteolysis Inferred from electronic annotation. Source: UniProtKB-KW tissue regeneration Inferred from electronic annotation. Source: Compara
Cellular_component	acrosomal 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 endomembrane system Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 17	17	Potential
	Propeptide	18 – 207	190	Probable		PRO_0000029084
	Chain	208 – 864	657	Disintegrin and metalloproteinase domain-containing protein 15		PRO_0000029085
Regions
	Topological domain	208 – 696	489	Extracellular Potential
	Transmembrane	697 – 717	21	Helical; Potential
	Topological domain	718 – 864	147	Cytoplasmic Potential
	Domain	214 – 415	202	Peptidase M12B
	Domain	422 – 509	88	Disintegrin
	Domain	658 – 686	29	EGF-like
	Motif	177 – 184	8	Cysteine switch By similarity
	Motif	816 – 822	7	SH3-binding Potential
	Motif	851 – 857	7	SH3-binding Potential
	Compositional bias	510 – 657	148	Cys-rich
	Compositional bias	699 – 712	14	Poly-Leu
Sites
	Active site	350	1	Potential
	Metal binding	179	1	Zinc; in inhibited form By similarity
	Metal binding	349	1	Zinc; catalytic Potential
	Metal binding	353	1	Zinc; catalytic Potential
	Metal binding	359	1	Zinc; catalytic Potential
	Site	289 – 290	2	Cleavage; by furin Potential
Amino acid modifications
	Modified residue	716	1	Phosphotyrosine; by HCK and LCK By similarity
	Modified residue	736	1	Phosphotyrosine; by HCK and LCK By similarity
	Glycosylation	238	1	N-linked (GlcNAc...) Potential
	Glycosylation	390	1	N-linked (GlcNAc...) Potential
	Glycosylation	393	1	N-linked (GlcNAc...) Potential
	Glycosylation	607	1	N-linked (GlcNAc...) Potential
	Glycosylation	612	1	N-linked (GlcNAc...) Potential
	Disulfide bond	324 ↔ 410		By similarity
	Disulfide bond	366 ↔ 394		By similarity
	Disulfide bond	368 ↔ 377		By similarity
	Disulfide bond	481 ↔ 501		By similarity
	Disulfide bond	658 ↔ 668		By similarity
	Disulfide bond	662 ↔ 674		By similarity
	Disulfide bond	676 ↔ 685		By similarity
Natural variations
	Alternative sequence	415 – 830	416	Missing in isoform 4.		VSP_008879
	Alternative sequence	761 – 809	49	Missing in isoform 3.		VSP_008881
	Alternative sequence	761 – 785	25	Missing in isoform 2.		VSP_008880
Experimental info
	Mutagenesis	482	1	R → A: Reduced binding to CHO cells expressing ITAG9-ITGB1. Ref.7
	Mutagenesis	489	1	D → A: Reduced binding to CHO cells expressing ITAG9-ITGB1. Ref.7
	Mutagenesis	490	1	L → A: Reduced binding to CHO cells expressing ITAG9-ITGB1. Ref.7
	Mutagenesis	491	1	P → A: Reduced binding to CHO cells expressing ITAG9-ITGB1. Ref.7
	Mutagenesis	492	1	E → A: Reduced binding to CHO cells expressing ITAG9-ITGB1. Ref.7
	Mutagenesis	493	1	F → A: Reduced binding to CHO cells expressing ITAG9-ITGB1. Ref.7
	Sequence conflict	21 – 22	2	PP → RR in BAA88903. Ref.2
	Sequence conflict	51	1	Q → H in BAE29090. Ref.3
	Sequence conflict	73	1	S → P in BAE41564. Ref.3
	Sequence conflict	443	1	E → Q in BAA88903. Ref.2
	Sequence conflict	459	1	G → E in BAA88903. Ref.2
	Sequence conflict	564 – 565	2	SP → T in BAA88903. Ref.2
	Sequence conflict	654	1	G → E in BAA88903. Ref.2
	Sequence conflict	660	1	R → S in BAA88903. Ref.2
	Sequence conflict	703	1	L → R in BAA88903. Ref.2
	Sequence conflict	712	1	L → R in BAA88903. Ref.2
	Sequence conflict	729	1	L → R in BAA88903. Ref.2
	Sequence conflict	830	1	Q → R in BAE41564. Ref.3
	Sequence conflict	846	1	L → S in BAA88903. Ref.2
	Sequence conflict	852 – 854	3	PAP → AAS in BAA88903. Ref.2
	Sequence conflict	859	1	A → P in BAA88903. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (ADAM15v2) [UniParc]. Last modified November 14, 2003. Version 2. Checksum: B1CBEB923463BB15	FASTA	864	92,664
	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
	Isoform 2 (ADAM15v1) [UniParc]. Checksum: 0C61FAA9B79B8123	FASTA	839	90,002
	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 AALADRSNPP TRPLPADPVV 790 800 810 820 830 RRPKSQGPTK PPPPRKPLPA NPQGQHPPGD LPGPGDGSLP LVVPSRPAPP PPAASSLYL
	Isoform 3 (ADAM15) [UniParc]. Checksum: C064BD3B7347D19B	FASTA	815	87,425
	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 SQGPTKPPPP RKPLPANPQG 790 800 810 QHPPGDLPGP GDGSLPLVVP SRPAPPPPAA SSLYL
	Isoform 4 [UniParc]. Checksum: 37FEB93BD3704400	FASTA	448	48,417
	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 LFERHPPGDL 430 440 PGPGDGSLPL VVPSRPAPPP PAASSLYL

References

	« Hide 'large scale' referencesShow '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. , 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.
IPI	IPI00123329. IPI00135185. IPI00378498. IPI00395062.
RefSeq	NP_001032811.2. NM_001037722.2. NP_033744.1. NM_009614.2.
UniGene	Mm.274049.
3D structure databases
ProteinModelPortal	O88839.
SMR	O88839. Positions 208-688.
ModBase	Search...
Protein-protein interaction databases
IntAct	O88839. 2 interactions.
MINT	MINT-4996290.
Protein family/group databases
MEROPS	M12.215.
PTM databases
PhosphoSite	O88839.
Proteomic databases
PaxDb	O88839.
PRIDE	O88839.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000029676; ENSMUSP00000029676; ENSMUSG00000028041. ENSMUST00000074582; ENSMUSP00000074167; ENSMUSG00000028041. ENSMUST00000107446; ENSMUSP00000103070; ENSMUSG00000028041. ENSMUST00000107448; ENSMUSP00000103072; ENSMUSG00000028041.
GeneID	11490.
KEGG	mmu:11490.
UCSC	uc008pyv.1. mouse. uc008pyw.1. mouse.
Organism-specific databases
CTD	8751.
MGI	MGI:1333882. Adam15.
Phylogenomic databases
eggNOG	NOG294463.
GeneTree	ENSGT00660000095090.
HOVERGEN	HBG006978.
InParanoid	Q3UE21.
KO	K06836.
OMA	GAQCASD.
OrthoDB	EOG479F6Q.
Gene expression databases
ArrayExpress	O88839.
Bgee	O88839.
Genevestigator	O88839.
GermOnline	ENSMUSG00000028041. Mus musculus.
Family and domain databases
Gene3D	3.40.390.10. 1 hit. 4.10.70.10. 1 hit.
InterPro	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]
Pfam	PF08516. ADAM_CR. 1 hit. PF00200. Disintegrin. 1 hit. PF01562. Pep_M12B_propep. 1 hit. PF01421. Reprolysin. 1 hit. [Graphical view]
SMART	SM00608. ACR. 1 hit. SM00050. DISIN. 1 hit. SM00181. EGF. 1 hit. [Graphical view]
SUPFAM	SSF57552. Disintegrin. 1 hit.
PROSITE	PS50215. ADAM_MEPRO. 1 hit. PS00546. CYSTEINE_SWITCH. False negative. PS00427. DISINTEGRIN_1. False negative. PS50214. DISINTEGRIN_2. 1 hit. PS00022. EGF_1. False negative. PS01186. EGF_2. 1 hit. PS50026. EGF_3. 1 hit. PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	278860.
SOURCE	Search...

Entry information

Entry name

ADA15_MOUSE

Accession

Primary (citable) accession number: O88839
Secondary accession number(s): A4ZYV2 , Q3TDN7, Q3U7C2, Q3UE21, Q8C7Z0, Q91VS9, Q9QYL2

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 2001
Last sequence update:	November 14, 2003
Last modified:	May 29, 2013
This is version 144 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program