ADAM15 ADAM metallopeptidase domain 15 [Homo sapiens (human)] - Gene

Summary

Official Symbol: ADAM15provided by HGNC
Official Full Name: ADAM metallopeptidase domain 15provided by HGNC
Primary source: HGNC:HGNC:193
See related: Ensembl:ENSG00000143537 MIM:605548; AllianceGenome:HGNC:193
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Homo sapiens
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as: MDC15
Summary: The protein encoded by this gene is a member of the ADAM (a disintegrin and metalloproteinase) protein family. ADAM family members are type I transmembrane glycoproteins known to be involved in cell adhesion and proteolytic ectodomain processing of cytokines and adhesion molecules. This protein contains multiple functional domains including a zinc-binding metalloprotease domain, a disintegrin-like domain, as well as a EGF-like domain. Through its disintegrin-like domain, this protein specifically interacts with the integrin beta chain, beta 3. It also interacts with Src family protein-tyrosine kinases in a phosphorylation-dependent manner, suggesting that this protein may function in cell-cell adhesion as well as in cellular signaling. Multiple alternatively spliced transcript variants encoding distinct isoforms have been observed. [provided by RefSeq, Jul 2008]
Expression: Ubiquitous expression in skin (RPKM 41.3), esophagus (RPKM 32.4) and 25 other tissues See more
Orthologs: mouse all
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Genomic context

Location:: 1q21.3

Exon count:: 24

Annotation release	Status	Assembly	Chr	Location
RS_2024_08	current	GRCh38.p14 (GCF_000001405.40)	1	NC_000001.11 (155051316..155062775)
RS_2024_08	current	T2T-CHM13v2.0 (GCF_009914755.1)	1	NC_060925.1 (154190701..154202162)
RS_2024_09	previous assembly	GRCh37.p13 (GCF_000001405.25)	1	NC_000001.10 (155023792..155035251)

Chromosome 1 - NC_000001.11 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Loss of cancer cell-derived ADAM15 alters the tumor microenvironment in colorectal tumors.
Title: Loss of cancer cell-derived ADAM15 alters the tumor microenvironment in colorectal tumors.
Loss of ADAM15 Exacerbates Transition to Decompensated Myocardial Hypertrophy and Dilation Through Activation of the Calcineurin Pathway.
Title: Loss of ADAM15 Exacerbates Transition to Decompensated Myocardial Hypertrophy and Dilation Through Activation of the Calcineurin Pathway.
ADAM15 correlates with prognosis, immune infiltration and apoptosis in hepatocellular carcinoma.
Title: ADAM15 correlates with prognosis, immune infiltration and apoptosis in hepatocellular carcinoma.
A Novel Pro-Inflammatory Mechanosensing Pathway Orchestrated by the Disintegrin Metalloproteinase ADAM15 in Synovial Fibroblasts.
Title: A Novel Pro-Inflammatory Mechanosensing Pathway Orchestrated by the Disintegrin Metalloproteinase ADAM15 in Synovial Fibroblasts.
ADAM15 expression is increased in lung CD8(+) T cells, macrophages, and bronchial epithelial cells in patients with COPD and is inversely related to airflow obstruction.
Title: ADAM15 expression is increased in lung CD8(+) T cells, macrophages, and bronchial epithelial cells in patients with COPD and is inversely related to airflow obstruction.
ADAM15 Participates in Tick-Borne Encephalitis Virus Replication.
Title: ADAM15 Participates in Tick-Borne Encephalitis Virus Replication.
ADAM15 mediates upregulation of Claudin-1 expression in breast cancer cells.
Title: ADAM15 mediates upregulation of Claudin-1 expression in breast cancer cells.
ADAM (a Disintegrin and Metalloproteinase) 15 Deficiency Exacerbates Ang II (Angiotensin II)-Induced Aortic Remodeling Leading to Abdominal Aortic Aneurysm.
Title: ADAM (a Disintegrin and Metalloproteinase) 15 Deficiency Exacerbates Ang II (Angiotensin II)-Induced Aortic Remodeling Leading to Abdominal Aortic Aneurysm.
The absence of ADAM15 at low shear stress or static conditions may therefore lead to increased endothelial damage.
Title: The metalloproteinase ADAM15 is upregulated by shear stress and promotes survival of endothelial cells.
The data show that ADAM15 plays a role in rheumatoid arthritis angiogenesis, suggesting that ADAM15 might be a potential target in inflammatory diseases such as rheumatoid arthritis.
Title: A Disintegrin and Metalloprotease 15 is Expressed on Rheumatoid Arthritis Synovial Tissue Endothelial Cells and may Mediate Angiogenesis.

Submit: New GeneRIF Correction See all GeneRIFs (63)

Phenotypes

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Find tests for this gene in the NIH Genetic Testing Registry (GTR)

Review eQTL and phenotype association data in this region using PheGenI

EBI GWAS Catalog

Description
Identification of 23 new prostate cancer susceptibility loci using the iCOGS custom genotyping array. EBI GWAS Catalog EBI GWAS CatalogPubMed

Variation

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See variants in ClinVar

See studies and variants in dbVar

See Variation Viewer (GRCh37.p13)

See Variation Viewer (GRCh38)

HIV-1 interactions

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Replication interactions

Interaction	Pubs
Knockdown of ADAM metallopeptidase domain 15 (ADAM15) by siRNA inhibits HIV-1 replication in MAGI-CCR5 cells	PubMed

Go to the HIV-1, Human Interaction Database

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Readthrough ADAM15-EFNA4

Readthrough gene: ADAM15-EFNA4, Included gene: EFNA4

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables SH3 domain binding	IPI Inferred from Physical Interaction more info	PubMed
enables immunoglobulin receptor binding	IPI Inferred from Physical Interaction more info	PubMed
enables integrin binding	IBA Inferred from Biological aspect of Ancestor more info
enables integrin binding	IMP Inferred from Mutant Phenotype more info	PubMed
enables metal ion binding	IEA Inferred from Electronic Annotation more info
enables metalloendopeptidase activity	IBA Inferred from Biological aspect of Ancestor more info
enables metalloendopeptidase activity	TAS Traceable Author Statement more info
enables metallopeptidase activity	IDA Inferred from Direct Assay more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed

Process	Evidence Code	Pubs
involved_in angiogenesis	IEA Inferred from Electronic Annotation more info
NOT involved_in apoptotic process	IDA Inferred from Direct Assay more info	PubMed
involved_in cardiac epithelial to mesenchymal transition	IEA Inferred from Electronic Annotation more info
involved_in cell-matrix adhesion	TAS Traceable Author Statement more info	PubMed
involved_in cellular response to phorbol 13-acetate 12-myristate	IDA Inferred from Direct Assay more info	PubMed
involved_in collagen catabolic process	IEA Inferred from Electronic Annotation more info
involved_in extracellular matrix disassembly	TAS Traceable Author Statement more info
involved_in immune response to tumor cell	IDA Inferred from Direct Assay more info	PubMed
involved_in innate immune response	IBA Inferred from Biological aspect of Ancestor more info
involved_in innate immune response	IDA Inferred from Direct Assay more info	PubMed
involved_in integrin-mediated signaling pathway	IBA Inferred from Biological aspect of Ancestor more info
involved_in integrin-mediated signaling pathway	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in male gonad development	IEA Inferred from Electronic Annotation more info
involved_in negative regulation of cell growth	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in negative regulation of cell migration	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in negative regulation of cell-matrix adhesion	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in negative regulation of receptor binding	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in proteolysis	IBA Inferred from Biological aspect of Ancestor more info
involved_in response to hypobaric hypoxia	IEA Inferred from Electronic Annotation more info
involved_in tissue regeneration	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
located_in acrosomal vesicle	IEA Inferred from Electronic Annotation more info
located_in adherens junction	IEA Inferred from Electronic Annotation more info
located_in cell surface	IDA Inferred from Direct Assay more info	PubMed
located_in extracellular exosome	IDA Inferred from Direct Assay more info	PubMed
is_active_in extracellular space	IBA Inferred from Biological aspect of Ancestor more info
located_in motile cilium	IEA Inferred from Electronic Annotation more info
located_in plasma membrane	TAS Traceable Author Statement more info

General protein information

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Preferred Names: disintegrin and metalloproteinase domain-containing protein 15

Names: MDC-15; a disintegrin and metalloproteinase domain 15 (metargidin); metalloprotease RGD disintegrin protein; metalloproteinase-like, disintegrin-like, and cysteine-rich protein 15

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

Genomic

NG_029667.1 RefSeqGene

Range

5031..16490

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001261464.2 → NP_001248393.1 disintegrin and metalloproteinase domain-containing protein 15 isoform 7 preproprotein

Status: REVIEWED

Description

Transcript Variant: This variant (7) lacks two alternate in-frame exons in the 3' coding region compared to variant 6. The resulting protein (isoform 7) is shorter compared to isoform 6.

Source sequence(s)

AK296925, AL451085, AL691442, BM971880

Consensus CDS

CCDS58031.1

UniProtKB/TrEMBL

B7Z390

Related

ENSP00000432927.1, ENST00000531455.5

Conserved Domains (5) summary

smart00050
Location:440 → 514

DISIN; Homologues of snake disintegrins

smart00608
Location:518 → 659

ACR; ADAM Cysteine-Rich Domain

cd04269
Location:223 → 421

ZnMc_adamalysin_II_like; Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom zinc endopeptidase. This subfamily contains other snake venom metalloproteinases, as well as membrane-anchored metalloproteases belonging to the ADAM family. ...

pfam01421
Location:223 → 423

Reprolysin; Reprolysin (M12B) family zinc metalloprotease

pfam01562
Location:72 → 164

Pep_M12B_propep; Reprolysin family propeptide
NM_001261465.2 → NP_001248394.1 disintegrin and metalloproteinase domain-containing protein 15 isoform 8 preproprotein

Status: REVIEWED

Description

Transcript Variant: This variant (8) lacks two alternate in-frame exons in the 3' coding region compared to variant 6. The resulting protein (isoform 8) is shorter compared to isoform 6.

Source sequence(s)

AL691442, AY560595, BM971880

Consensus CDS

CCDS58032.1

UniProtKB/TrEMBL

B7Z390

Related

ENSP00000357397.3, ENST00000368412.7

Conserved Domains (5) summary

smart00050
Location:430 → 504

DISIN; Homologues of snake disintegrins

smart00608
Location:508 → 649

ACR; ADAM Cysteine-Rich Domain

cd04269
Location:213 → 411

ZnMc_adamalysin_II_like; Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom zinc endopeptidase. This subfamily contains other snake venom metalloproteinases, as well as membrane-anchored metalloproteases belonging to the ADAM family. ...

pfam01421
Location:213 → 413

Reprolysin; Reprolysin (M12B) family zinc metalloprotease

pfam01562
Location:62 → 154

Pep_M12B_propep; Reprolysin family propeptide
NM_001261466.2 → NP_001248395.1 disintegrin and metalloproteinase domain-containing protein 15 isoform 9 preproprotein

Status: REVIEWED

Description

Transcript Variant: This variant (9) has multiple differences in the 5' coding region and differs in the 3' coding region and UTR compared to variant 6. The resulting protein (isoform 9) is shorter and has a distinct C-terminus compared to isoform 6.

Source sequence(s)

AK297468, AL451085, AL691442, AW290953

Consensus CDS

CCDS60282.1

UniProtKB/Swiss-Prot

Q13444

Related

ENSP00000476000.1, ENST00000447332.3

Conserved Domains (5) summary

smart00050
Location:414 → 488

DISIN; Homologues of snake disintegrins

smart00608
Location:492 → 624

ACR; ADAM Cysteine-Rich Domain

cd04269
Location:197 → 395

ZnMc_adamalysin_II_like; Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom zinc endopeptidase. This subfamily contains other snake venom metalloproteinases, as well as membrane-anchored metalloproteases belonging to the ADAM family. ...

pfam01421
Location:197 → 397

Reprolysin; Reprolysin (M12B) family zinc metalloprotease

pfam01562
Location:72 → 138

Pep_M12B_propep; Reprolysin family propeptide
NM_003815.5 → NP_003806.3 disintegrin and metalloproteinase domain-containing protein 15 isoform 2 preproprotein

See identical proteins and their annotated locations for NP_003806.3

Status: REVIEWED

Description

Transcript Variant: This variant (2) lacks two in-frame coding exons compared to variant 6. The resulting isoform (2) lacks an internal region, as compared to the longest isoform (6).

Source sequence(s)

AY518542, BC014566, U41767

Consensus CDS

CCDS1084.1

UniProtKB/TrEMBL

Q59GF2

Related

ENSP00000271836.6, ENST00000271836.10

Conserved Domains (5) summary

smart00050
Location:430 → 504

DISIN; Homologues of snake disintegrins

smart00608
Location:508 → 649

ACR; ADAM Cysteine-Rich Domain

cd04269
Location:213 → 411

ZnMc_adamalysin_II_like; Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom zinc endopeptidase. This subfamily contains other snake venom metalloproteinases, as well as membrane-anchored metalloproteases belonging to the ADAM family. ...

pfam01421
Location:213 → 413

Reprolysin; Reprolysin (M12B) family zinc metalloprotease

pfam01562
Location:62 → 154

Pep_M12B_propep; Reprolysin family propeptide
NM_207191.3 → NP_997074.1 disintegrin and metalloproteinase domain-containing protein 15 isoform 1 preproprotein

See identical proteins and their annotated locations for NP_997074.1

Status: REVIEWED

Description

Transcript Variant: This variant (1) lacks three exons in the coding region compared to variant 6, one of which causes a translation frameshift. The resulting isoform (1) has a distinct and shorter C-terminus, as compared to the longest isoform (6).

Source sequence(s)

AY518542, AY560593, BM971880

Consensus CDS

CCDS1088.1

UniProtKB/TrEMBL

B7Z390

Related

ENSP00000353892.4, ENST00000360674.8

Conserved Domains (5) summary

smart00050
Location:430 → 504

DISIN; Homologues of snake disintegrins

smart00608
Location:508 → 649

ACR; ADAM Cysteine-Rich Domain

cd04269
Location:213 → 411

ZnMc_adamalysin_II_like; Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom zinc endopeptidase. This subfamily contains other snake venom metalloproteinases, as well as membrane-anchored metalloproteases belonging to the ADAM family. ...

pfam01421
Location:213 → 413

Reprolysin; Reprolysin (M12B) family zinc metalloprotease

pfam01562
Location:62 → 154

Pep_M12B_propep; Reprolysin family propeptide
NM_207194.3 → NP_997077.1 disintegrin and metalloproteinase domain-containing protein 15 isoform 3 preproprotein

See identical proteins and their annotated locations for NP_997077.1

Status: REVIEWED

Description

Transcript Variant: This variant (3) lacks an in-frame coding exon compared to variant 6. The resulting isoform (3) lacks an internal region, as compared to the longest isoform 6.

Source sequence(s)

AY518542, AY560593, AY560596, U41767

Consensus CDS

CCDS1085.1

UniProtKB/TrEMBL

Q59GF2

Related

ENSP00000348227.2, ENST00000355956.6

Conserved Domains (5) summary

smart00050
Location:430 → 504

DISIN; Homologues of snake disintegrins

smart00608
Location:508 → 649

ACR; ADAM Cysteine-Rich Domain

cd04269
Location:213 → 411

ZnMc_adamalysin_II_like; Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom zinc endopeptidase. This subfamily contains other snake venom metalloproteinases, as well as membrane-anchored metalloproteases belonging to the ADAM family. ...

pfam01421
Location:213 → 413

Reprolysin; Reprolysin (M12B) family zinc metalloprotease

pfam01562
Location:62 → 154

Pep_M12B_propep; Reprolysin family propeptide
NM_207195.3 → NP_997078.1 disintegrin and metalloproteinase domain-containing protein 15 isoform 4 preproprotein

See identical proteins and their annotated locations for NP_997078.1

Status: REVIEWED

Description

Transcript Variant: This variant (4) lacks two in-frame coding exons compared to variant 6. The resulting isoform (4) lacks an internal region, as compared to the longest isoform (6).

Source sequence(s)

AY518542, AY560593, AY560597, U41767

Consensus CDS

CCDS1086.1

UniProtKB/TrEMBL

Q59GF2

Related

ENSP00000352226.4, ENST00000359280.8

Conserved Domains (5) summary

smart00050
Location:430 → 504

DISIN; Homologues of snake disintegrins

smart00608
Location:508 → 649

ACR; ADAM Cysteine-Rich Domain

cd04269
Location:213 → 411

ZnMc_adamalysin_II_like; Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom zinc endopeptidase. This subfamily contains other snake venom metalloproteinases, as well as membrane-anchored metalloproteases belonging to the ADAM family. ...

pfam01421
Location:213 → 413

Reprolysin; Reprolysin (M12B) family zinc metalloprotease

pfam01562
Location:62 → 154

Pep_M12B_propep; Reprolysin family propeptide
NM_207196.3 → NP_997079.1 disintegrin and metalloproteinase domain-containing protein 15 isoform 5 preproprotein

See identical proteins and their annotated locations for NP_997079.1

Status: REVIEWED

Description

Transcript Variant: This variant (5) uses an alternative splice site within the coding region compared to variant 6. The translation frame remains the same. The resulting isoform (5) lacks an amino acid, as compared to the longest isoform (6).

Source sequence(s)

AY518542, AY560593, AY560598, U41767

Consensus CDS

CCDS44236.1

UniProtKB/TrEMBL

Q59GF2

Related

ENSP00000403843.2, ENST00000449910.6

Conserved Domains (5) summary

smart00050
Location:430 → 504

DISIN; Homologues of snake disintegrins

smart00608
Location:508 → 649

ACR; ADAM Cysteine-Rich Domain

cd04269
Location:213 → 411

ZnMc_adamalysin_II_like; Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom zinc endopeptidase. This subfamily contains other snake venom metalloproteinases, as well as membrane-anchored metalloproteases belonging to the ADAM family. ...

pfam01421
Location:213 → 413

Reprolysin; Reprolysin (M12B) family zinc metalloprotease

pfam01562
Location:62 → 154

Pep_M12B_propep; Reprolysin family propeptide
NM_207197.3 → NP_997080.1 disintegrin and metalloproteinase domain-containing protein 15 isoform 6 preproprotein

See identical proteins and their annotated locations for NP_997080.1

Status: REVIEWED

Description

Transcript Variant: This variant (6) encodes the longest isoform (6).

Source sequence(s)

AY518542, AY560593, AY560599, U41767

Consensus CDS

CCDS1087.1

UniProtKB/Swiss-Prot

B3KQU5, B4DLB5, B4DMH8, E9PN65, Q13444, Q13493, Q53XQ0, Q5SR68, Q5SR69, Q6R267, Q71S61, Q71S62, Q71S63, Q71S64, Q71S65, Q71S66, Q71S67, Q71S68, Q71S69, Q96C78, U3KQL5

UniProtKB/TrEMBL

Q59GF2

Related

ENSP00000349436.2, ENST00000356955.7

Conserved Domains (5) summary

smart00050
Location:430 → 504

DISIN; Homologues of snake disintegrins

smart00608
Location:508 → 649

ACR; ADAM Cysteine-Rich Domain

cd04269
Location:213 → 411

ZnMc_adamalysin_II_like; Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom zinc endopeptidase. This subfamily contains other snake venom metalloproteinases, as well as membrane-anchored metalloproteases belonging to the ADAM family. ...

pfam01421
Location:213 → 413

Reprolysin; Reprolysin (M12B) family zinc metalloprotease

pfam01562
Location:62 → 154

Pep_M12B_propep; Reprolysin family propeptide

RNA

NR_048577.2 RNA Sequence

Status: REVIEWED

Description

Transcript Variant: This variant (10) uses two alternate splice sites in 3' exons compared to variant 6. This variant is represented as non-coding because the use of the 5'-most supported translational start codon, as used in variant 1, renders the transcript a candidate for nonsense-mediated mRNA decay (NMD).

Source sequence(s)

AL691442, AY560600, BM971880
NR_048578.2 RNA Sequence

Status: REVIEWED

Description

Transcript Variant: This variant (11) uses an alternate splice site in a 3' exon compared to variant 6. This variant is represented as non-coding because the use of the 5'-most supported translational start codon, as used in variant 1, renders the transcript a candidate for nonsense-mediated mRNA decay (NMD).

Source sequence(s)

AL691442, AY560601, BM971880

Related

ENST00000526491.5
NR_048579.2 RNA Sequence

Status: REVIEWED

Description

Transcript Variant: This variant (12) lacks an exon and uses an alternate splice site in a 3' exon compared to variant 6. This variant is represented as non-coding because the use of the 5'-most supported translational start codon, as used in variant 1, renders the transcript a candidate for nonsense-mediated mRNA decay (NMD).

Source sequence(s)

AL691442, AY576417, BM971880

Related

ENST00000529473.5