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Q13444 (ADA15_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 157. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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):
Metalloprotease RGD disintegrin protein
Metalloproteinase-like, disintegrin-like, and cysteine-rich protein 15
Short name=MDC-15
Metargidin
Gene names
Name:ADAM15
Synonyms:MDC15
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length863 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. 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. Ref.3 Ref.18 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24

Cofactor

Binds 1 zinc ion per subunit By similarity.

Enzyme regulation

Inhibited by hydroxamate-type metalloproteinase inhibitors such as marimastat. Inhibited by metalloproteinase inhibitor 2 (TIMP-2) and TIMP-3 at nanomolar concentrations. Not significantly inhibited by TIMP-1 at concentrations of up to 100 nM. Not activated by PMA or ionomycin. Ref.25

Subunit structure

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 By similarity. Interacts specifically with Src family protein-tyrosine kinases (PTKs). Interacts with SH3PXD2A. Interacts with ITAGV-ITGB1. Interacts with GRB2, HCK, ITSN1, ITSN2, LYN, MAPK1, MAPK3, NCF1, NCK1, nephrocystin, PTK6, SNX33, LCK and SRC. Ref.5 Ref.13 Ref.14 Ref.15 Ref.17 Ref.19 Ref.26

Subcellular location

Endomembrane system; Single-pass type I membrane protein. Cell junctionadherens junction. Cell projectionciliumflagellum By similarity. Cytoplasmic vesiclesecretory vesicleacrosome By similarity. 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 By similarity. Ref.16

Tissue specificity

Expressed in colon and small intestine. Expressed in airway smooth muscle and glomerular mesangial cells (at protein level). Ubiquitously expressed. Overexpressed in atherosclerotic lesions. Constitutively expressed in cultured endothelium and smooth muscle. Expressed in chondrocytes. Expressed in airway smooth muscle and glomerular mesangial cells. Ref.3 Ref.12 Ref.18 Ref.21

Domain

The cytoplasmic domain is required for SH3GL2- and SNX9-binding.

Disintegrin domain binds to integrin alphaV-beta3.

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 By similarity.

Phosphorylation increases association with PTKs.

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
Polymorphism
   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 electronic annotation. Source: Ensembl

cell-matrix adhesion

Traceable author statement Ref.13. Source: ProtInc

collagen catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

extracellular matrix disassembly

Traceable author statement. Source: Reactome

extracellular matrix organization

Traceable author statement. Source: Reactome

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

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionSH3 domain binding

Inferred from physical interaction Ref.14. Source: BHF-UCL

metalloendopeptidase activity

Inferred from electronic annotation. Source: InterPro

metallopeptidase activity

Inferred from direct assay PubMed 12777399. Source: BHF-UCL

protein binding

Inferred from physical interaction Ref.14Ref.17PubMed 16374509. Source: IntAct

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 13 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13444-1)

Also known as: 6b;

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: Q13444-2)

The sequence of this isoform differs from the canonical sequence as follows:
     760-808: Missing.
Isoform 3 (identifier: Q13444-3)

Also known as: 6a;

The sequence of this isoform differs from the canonical sequence as follows:
     760-760: Missing.
Isoform 4 (identifier: Q13444-4)

Also known as: 4a;

The sequence of this isoform differs from the canonical sequence as follows:
     785-808: Missing.
Isoform 5 (identifier: Q13444-5)

The sequence of this isoform differs from the canonical sequence as follows:
     760-784: Missing.
Isoform 6 (identifier: Q13444-6)

Also known as: 7b;

The sequence of this isoform differs from the canonical sequence as follows:
     809-863: SQGPAKPPPPRKPLPADPQGRCPSGDLPGPGAGIPPLVVPSRPAPPPPTVSSLYL → VTVGGEKGTASPPT
Isoform 7 (identifier: Q13444-7)

Also known as: 7a;

The sequence of this isoform differs from the canonical sequence as follows:
     760-760: Missing.
     809-863: SQGPAKPPPPRKPLPADPQGRCPSGDLPGPGAGIPPLVVPSRPAPPPPTVSSLYL → VTVGGEKGTASPPT
Isoform 8 (identifier: Q13444-8)

The sequence of this isoform differs from the canonical sequence as follows:
     760-784: Missing.
     809-863: SQGPAKPPPPRKPLPADPQGRCPSGDLPGPGAGIPPLVVPSRPAPPPPTVSSLYL → VTVGGEKGTASPPT
Isoform 9 (identifier: Q13444-9)

Also known as: 3a;

The sequence of this isoform differs from the canonical sequence as follows:
     737-796: AAQSGPSERP...LADRPNPPTR → LVLSASRPPL...CPAQGLESRP
     797-863: Missing.
Isoform 10 (identifier: Q13444-10)

Also known as: 1;

The sequence of this isoform differs from the canonical sequence as follows:
     736-772: RAAQSGPSERPGPPQRALLARGTKQASALSFPAPPSR → SLRGQPSPHPQGSHCLPTPRAGAHRVTCPAQGLESRP
     773-863: Missing.
Isoform 11 (identifier: Q13444-11)

The sequence of this isoform differs from the canonical sequence as follows:
     94-387: Missing.
     760-808: Missing.
Isoform 12 (identifier: Q13444-12)

The sequence of this isoform differs from the canonical sequence as follows:
     26-26: I → IVLSWGVLGPA
     760-808: Missing.
Note: No experimental confirmation available.
Isoform 13 (identifier: Q13444-13)

The sequence of this isoform differs from the canonical sequence as follows:
     27-87: GGTEEQQAES...DSHILELLQN → VSACNVEAPQ...ISQLASKRCF
     641-649: CIDHRCQRV → SSLGGQDQV
     650-863: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Propeptide18 – 206189 By similarity
PRO_0000029082
Chain207 – 863657Disintegrin and metalloproteinase domain-containing protein 15
PRO_0000029083

Regions

Topological domain207 – 696490Extracellular Potential
Transmembrane697 – 71721Helical; Potential
Topological domain718 – 863146Cytoplasmic Potential
Domain213 – 414202Peptidase M12B
Domain421 – 50888Disintegrin
Domain657 – 68529EGF-like
Motif177 – 1848Cysteine switch By similarity
Motif484 – 4863Cell attachment site Potential
Motif815 – 8217SH3-binding Potential
Motif850 – 8567SH3-binding Potential
Compositional bias509 – 656148Cys-rich

Sites

Active site3491 By similarity
Metal binding1791Zinc; in inhibited form By similarity
Metal binding3481Zinc; catalytic By similarity
Metal binding3521Zinc; catalytic By similarity
Metal binding3581Zinc; catalytic By similarity

Amino acid modifications

Modified residue7151Phosphotyrosine; by HCK and LCK Ref.17
Modified residue7351Phosphotyrosine; by HCK and LCK Ref.17
Glycosylation2371N-linked (GlcNAc...) Potential
Glycosylation3891N-linked (GlcNAc...) Potential
Glycosylation3921N-linked (GlcNAc...) Potential
Glycosylation6061N-linked (GlcNAc...) Potential
Glycosylation6111N-linked (GlcNAc...) Potential
Disulfide bond323 ↔ 409 By similarity
Disulfide bond365 ↔ 393 By similarity
Disulfide bond367 ↔ 376 By similarity
Disulfide bond480 ↔ 500 By similarity
Disulfide bond657 ↔ 667 By similarity
Disulfide bond661 ↔ 673 By similarity
Disulfide bond675 ↔ 684 By similarity

Natural variations

Alternative sequence261I → IVLSWGVLGPA in isoform 12.
VSP_044695
Alternative sequence27 – 8761GGTEE…ELLQN → VSACNVEAPQVALRSSRQSQ RRPRGSPWSPRSFRTISQLA SKRCF in isoform 13.
VSP_055143
Alternative sequence94 – 387294Missing in isoform 11.
VSP_039524
Alternative sequence641 – 6499CIDHRCQRV → SSLGGQDQV in isoform 13.
VSP_055144
Alternative sequence650 – 863214Missing in isoform 13.
VSP_055145
Alternative sequence736 – 77237RAAQS…APPSR → SLRGQPSPHPQGSHCLPTPR AGAHRVTCPAQGLESRP in isoform 10.
VSP_039525
Alternative sequence737 – 79660AAQSG…NPPTR → LVLSASRPPLPGRCRLTLCP RDSSLRGQPSPHPQGSHCLP TPRAGAHRVTCPAQGLESRP in isoform 9.
VSP_039526
Alternative sequence760 – 80849Missing in isoform 2, isoform 11 and isoform 12.
VSP_039527
Alternative sequence760 – 78425Missing in isoform 5 and isoform 8.
VSP_039528
Alternative sequence7601Missing in isoform 3 and isoform 7.
VSP_039529
Alternative sequence773 – 86391Missing in isoform 10.
VSP_039530
Alternative sequence785 – 80824Missing in isoform 4.
VSP_039531
Alternative sequence797 – 86367Missing in isoform 9.
VSP_039532
Alternative sequence809 – 86355SQGPA…SSLYL → VTVGGEKGTASPPT in isoform 6, isoform 7 and isoform 8.
VSP_039533
Natural variant1911K → T. Ref.1 Ref.2 Ref.4 Ref.6 Ref.7 Ref.8 Ref.11
Corresponds to variant rs6427128 [ dbSNP | Ensembl ].
VAR_060315
Natural variant2161E → K. Ref.8
Corresponds to variant rs115753757 [ dbSNP | Ensembl ].
VAR_068970
Natural variant2941P → H.
Corresponds to variant rs2306122 [ dbSNP | Ensembl ].
VAR_060316
Natural variant5021P → Q.
Corresponds to variant rs17093828 [ dbSNP | Ensembl ].
VAR_054339

Experimental info

Mutagenesis484 – 4852RG → SV: Reduces ADAM15-mediated T-cell aggregation. Ref.22
Sequence conflict811I → V in BAG52157. Ref.9
Sequence conflict1041G → C in BAG59890. Ref.8
Sequence conflict1911K → T in BAG59890. Ref.8
Sequence conflict2861H → Y in BAG59477. Ref.8
Sequence conflict6491V → A in BAG52157. Ref.9
Sequence conflict7141S → G in AAC50404. Ref.2
Sequence conflict8401A → P in AAC51112. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (6b) [UniParc].

Last modified July 13, 2010. Version 4.
Checksum: 004936E9182629CA

FASTA86392,959
        10         20         30         40         50         60 
MRLALLWALG LLGAGSPLPS WPLPNIGGTE EQQAESEKAP REPLEPQVLQ DDLPISLKKV 

        70         80         90        100        110        120 
LQTSLPEPLR IKLELDGDSH ILELLQNREL VPGRPTLVWY QPDGTRVVSE GHTLENCCYQ 

       130        140        150        160        170        180 
GRVRGYAGSW VSICTCSGLR GLVVLTPERS YTLEQGPGDL QGPPIISRIQ DLHLPGHTCA 

       190        200        210        220        230        240 
LSWRESVHTQ KPPEHPLGQR HIRRRRDVVT ETKTVELVIV ADHSEAQKYR DFQHLLNRTL 

       250        260        270        280        290        300 
EVALLLDTFF RPLNVRVALV GLEAWTQRDL VEISPNPAVT LENFLHWRRA HLLPRLPHDS 

       310        320        330        340        350        360 
AQLVTGTSFS GPTVGMAIQN SICSPDFSGG VNMDHSTSIL GVASSIAHEL GHSLGLDHDL 

       370        380        390        400        410        420 
PGNSCPCPGP APAKTCIMEA STDFLPGLNF SNCSRRALEK ALLDGMGSCL FERLPSLPPM 

       430        440        450        460        470        480 
AAFCGNMFVE PGEQCDCGFL DDCVDPCCDS LTCQLRPGAQ CASDGPCCQN CQLRPSGWQC 

       490        500        510        520        530        540 
RPTRGDCDLP EFCPGDSSQC PPDVSLGDGE PCAGGQAVCM HGRCASYAQQ CQSLWGPGAQ 

       550        560        570        580        590        600 
PAAPLCLQTA NTRGNAFGSC GRNPSGSYVS CTPRDAICGQ LQCQTGRTQP LLGSIRDLLW 

       610        620        630        640        650        660 
ETIDVNGTEL NCSWVHLDLG SDVAQPLLTL PGTACGPGLV CIDHRCQRVD LLGAQECRSK 

       670        680        690        700        710        720 
CHGHGVCDSN RHCYCEEGWA PPDCTTQLKA TSSLTTGLLL SLLVLLVLVM LGASYWYRAR 

       730        740        750        760        770        780 
LHQRLCQLKG PTCQYRAAQS GPSERPGPPQ RALLARGTKQ ASALSFPAPP SRPLPPDPVS 

       790        800        810        820        830        840 
KRLQAELADR PNPPTRPLPA DPVVRSPKSQ GPAKPPPPRK PLPADPQGRC PSGDLPGPGA 

       850        860 
GIPPLVVPSR PAPPPPTVSS LYL 

« Hide

Isoform 2 [UniParc].

Checksum: C6A297D51BED277E
Show »

FASTA81487,744
Isoform 3 (6a) [UniParc].

Checksum: C39147754DD6B63C
Show »

FASTA86292,831
Isoform 4 (4a) [UniParc].

Checksum: 3B5F7590EFE0EBC1
Show »

FASTA83990,383
Isoform 5 [UniParc].

Checksum: 22637515284E16E8
Show »

FASTA83890,320
Isoform 6 (7b) [UniParc].

Checksum: 2C01760368BEAF58
Show »

FASTA82288,779
Isoform 7 (7a) [UniParc].

Checksum: 574AC60AD10ACFCE
Show »

FASTA82188,651
Isoform 8 [UniParc].

Checksum: 402644A60C8BB7A3
Show »

FASTA79786,140
Isoform 9 (3a) [UniParc].

Checksum: 7C808DCF0D1C296A
Show »

FASTA79686,311
Isoform 10 (1) [UniParc].

Checksum: 3EE4998C8EDCF958
Show »

FASTA77283,664
Isoform 11 [UniParc].

Checksum: 601F3874454899A0
Show »

FASTA52055,446
Isoform 12 [UniParc].

Checksum: 84B3BF611CBF9E9D
Show »

FASTA82488,724
Isoform 13 [UniParc].

Checksum: 6C412A20B4E83369
Show »

FASTA63368,256

References

« Hide 'large scale' references
[1]"Metargidin, a membrane-anchored metalloprotease-disintegrin protein with an RGD integrin binding sequence."
Kraetzschmar J., Lum L., Blobel C.P.
J. Biol. Chem. 271:4593-4596(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT THR-191.
Tissue: Mammary carcinoma.
[2]"Expression of a disintegrin-like protein in cultured human vascular cells and in vivo."
Herren B., Raines E.W., Ross R.
FASEB J. 11:173-180(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT THR-191.
Tissue: Umbilical vein.
[3]"ADAM-15 inhibits wound healing in human intestinal epithelial cell monolayers."
Charrier L., Yan Y., Driss A., Laboisse C.L., Sitaraman S.V., Merlin D.
Am. J. Physiol. 288:G346-G353(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 10), FUNCTION, TISSUE SPECIFICITY, ALTERNATIVE SPLICING (ISOFORM 2).
[4]"ADAM15 gene structure and differential alternative exon use in human tissues."
Kleino I., Ortiz R.M., Huovila A.P.
BMC Mol. Biol. 8:90-90(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3; 4; 5; 6; 7; 8; 9; 10), VARIANT THR-191.
[5]"Distinct functions of natural ADAM-15 cytoplasmic domain variants in human mammary carcinoma."
Zhong J.L., Poghosyan Z., Pennington C.J., Scott X., Handsley M.M., Warn A., Gavrilovic J., Honert K., Kruger A., Span P.N., Sweep F.C., Edwards D.R.
Mol. Cancer Res. 6:383-394(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 4 AND 10), ALTERNATIVE SPLICING, INTERACTION WITH GRB2; MAPK1; MAPK3; NCK1; PTK6; SH3PXD2A AND SRC.
[6]"Characterization of human ADAM15 gene and promoter, and evidence for alternative exon use."
Karkkainen I., Ortiz R.M., Huovila A.-P.J.
Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6; 7; 8 AND 9), VARIANT THR-191.
[7]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT THR-191.
[8]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 12 AND 13), VARIANTS THR-191 AND LYS-216.
Tissue: Tongue.
[9]"Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y. expand/collapse author list , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 11).
Tissue: Embryo.
[10]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]"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 2), VARIANT THR-191.
Tissue: Kidney.
[12]"Expression of members of a novel membrane linked metalloproteinase family (ADAM) in human articular chondrocytes."
McKie N., Edwards T., Dallas D.J., Houghton A., Stringer B., Graham R., Russell G., Croucher P.I.
Biochem. Biophys. Res. Commun. 230:335-339(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[13]"Specific interaction of the recombinant disintegrin-like domain of MDC-15 (metargidin, ADAM-15) with integrin alphavbeta3."
Zhang X.P., Kamata T., Yokoyama K., Puzon-McLaughlin W., Takada Y.
J. Biol. Chem. 273:7345-7350(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH INTEGRIN ALPHAV-BETA3.
[14]"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 SH3GL2 AND SNX9.
[15]"Interaction of metargidin (ADAM-15) with alphavbeta3 and alpha5beta1 integrins on different haemopoietic cells."
Nath D., Slocombe P.M., Stephens P.E., Warn A., Hutchinson G.R., Yamada K.M., Docherty A.J., Murphy G.
J. Cell Sci. 112:579-587(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH INTEGRIN ALPHAV-BETA3 AND INTEGRIN ALPHA5-BETA1.
[16]"ADAM15 is an adherens junction molecule whose surface expression can be driven by VE-cadherin."
Ham C., Levkau B., Raines E.W., Herren B.
Exp. Cell Res. 279:239-247(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[17]"Phosphorylation-dependent interactions between ADAM15 cytoplasmic domain and Src family protein-tyrosine kinases."
Poghosyan Z., Robbins S.M., Houslay M.D., Webster A., Murphy G., Edwards D.R.
J. Biol. Chem. 277:4999-5007(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-715 AND TYR-735, INTERACTION WITH GRB2; LCK AND HCK.
[18]"The role of ADAM 15 in glomerular mesangial cell migration."
Martin J., Eynstone L.V., Davies M., Williams J.D., Steadman R.
J. Biol. Chem. 277:33683-33689(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[19]"The adaptor protein fish associates with members of the ADAMs family and localizes to podosomes of Src-transformed cells."
Abram C.L., Seals D.F., Pass I., Salinsky D., Maurer L., Roth T.M., Courtneidge S.A.
J. Biol. Chem. 278:16844-16851(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SH3PXD2A.
[20]"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.
[21]"Inhibition of airway smooth muscle adhesion and migration by the disintegrin domain of ADAM-15."
Lu D., Xie S., Sukkar M.B., Lu X., Scully M.F., Chung K.F.
Am. J. Respir. Cell Mol. Biol. 37:494-500(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[22]"ADAM-15/metargidin mediates homotypic aggregation of human T lymphocytes and heterotypic interactions of T lymphocytes with intestinal epithelial cells."
Charrier L., Yan Y., Nguyen H.T., Dalmasso G., Laboisse C.L., Gewirtz A.T., Sitaraman S.V., Merlin D.
J. Biol. Chem. 282:16948-16958(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF 484-ARG-GLY-485.
[23]"ADAM15 suppresses cell motility by driving integrin alpha5beta1 cell surface expression via Erk inactivation."
Chen Q., Meng L.H., Zhu C.H., Lin L.P., Lu H., Ding J.
Int. J. Biochem. Cell Biol. 40:2164-2173(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[24]"The ectodomain shedding of E-cadherin by ADAM15 supports ErbB receptor activation."
Najy A.J., Day K.C., Day M.L.
J. Biol. Chem. 283:18393-18401(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[25]"Characterization of the catalytic activity of the membrane-anchored metalloproteinase ADAM15 in cell-based assays."
Maretzky T., Yang G., Ouerfelli O., Overall C.M., Worpenberg S., Hassiepen U., Eder J., Blobel C.P.
Biochem. J. 420:105-113(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION.
[26]"Alternative splicing of ADAM15 regulates its interactions with cellular SH3 proteins."
Kleino I., Ortiz R.M., Yritys M., Huovila A.P., Saksela K.
J. Cell. Biochem. 108:877-885(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HCK; ITSN1; ITSN2; LYN; NCF1; NEPHROCYSTIN; SH3PXD2A; SNX33; SNX9 AND SRC.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U41767 mRNA. Translation: AAC50404.1.
U46005 mRNA. Translation: AAC51112.1.
AY518542 mRNA. Translation: AAR99331.1.
AF314227 Genomic DNA. Translation: AAM44189.1.
AF314227 Genomic DNA. Translation: AAS48590.1.
AF314227 Genomic DNA. Translation: AAS48591.1.
AF314227 Genomic DNA. Translation: AAS48592.1.
AF314227 Genomic DNA. Translation: AAS48593.1.
AF314227 Genomic DNA. Translation: AAS48594.1.
AF314227 Genomic DNA. Translation: AAS48595.1.
AF314227 Genomic DNA. Translation: AAS48596.1.
AF314227 Genomic DNA. Translation: AAS48597.1.
AF314227 Genomic DNA. Translation: AAS72298.1.
AY560593 mRNA. Translation: AAS72991.1.
AY560594 mRNA. Translation: AAS72992.1.
AY560595 mRNA. Translation: AAS72993.1.
AY560596 mRNA. Translation: AAS72994.1.
AY560597 mRNA. Translation: AAS72995.1.
AY560598 mRNA. Translation: AAS72996.1.
AY560599 mRNA. Translation: AAS72997.1.
AY560600 mRNA. Translation: AAS72998.1.
AY560601 mRNA. Translation: AAS72999.1.
AY576417 mRNA. Translation: AAS73000.1.
BT009764 mRNA. Translation: AAP88766.1.
AK296925 mRNA. Translation: BAG59477.1.
AK297468 mRNA. Translation: BAG59890.1.
AK075498 mRNA. Translation: BAG52157.1.
AL451085, AL691442 Genomic DNA. Translation: CAI13273.1.
AL451085, AL691442 Genomic DNA. Translation: CAI13274.1.
AL691442, AL451085 Genomic DNA. Translation: CAI15327.1.
AL691442, AL451085 Genomic DNA. Translation: CAI15328.1.
BC014566 mRNA. Translation: AAH14566.1.
CCDSCCDS1084.1. [Q13444-2]
CCDS1085.1. [Q13444-4]
CCDS1086.1. [Q13444-5]
CCDS1087.1. [Q13444-1]
CCDS1088.1. [Q13444-10]
CCDS44236.1. [Q13444-3]
CCDS58031.1. [Q13444-12]
CCDS58032.1. [Q13444-9]
PIRG02390.
RefSeqNP_001248393.1. NM_001261464.1. [Q13444-12]
NP_001248394.1. NM_001261465.1. [Q13444-9]
NP_003806.3. NM_003815.4. [Q13444-2]
NP_997074.1. NM_207191.2. [Q13444-10]
NP_997077.1. NM_207194.2. [Q13444-4]
NP_997078.1. NM_207195.2. [Q13444-5]
NP_997079.1. NM_207196.2. [Q13444-3]
NP_997080.1. NM_207197.2. [Q13444-1]
UniGeneHs.312098.

3D structure databases

ProteinModelPortalQ13444.
SMRQ13444. Positions 213-646.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114287. 27 interactions.
IntActQ13444. 27 interactions.
MINTMINT-108799.
STRING9606.ENSP00000349436.

Chemistry

ChEMBLCHEMBL2331050.

Protein family/group databases

MEROPSM12.215.

PTM databases

PhosphoSiteQ13444.

Polymorphism databases

DMDM300669614.

Proteomic databases

MaxQBQ13444.
PaxDbQ13444.
PRIDEQ13444.

Protocols and materials databases

DNASU8751.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000271836; ENSP00000271836; ENSG00000143537. [Q13444-2]
ENST00000355956; ENSP00000348227; ENSG00000143537. [Q13444-4]
ENST00000356955; ENSP00000349436; ENSG00000143537. [Q13444-1]
ENST00000359280; ENSP00000352226; ENSG00000143537. [Q13444-5]
ENST00000360674; ENSP00000353892; ENSG00000143537. [Q13444-10]
ENST00000368412; ENSP00000357397; ENSG00000143537. [Q13444-9]
ENST00000368413; ENSP00000357398; ENSG00000143537. [Q13444-11]
ENST00000447332; ENSP00000476000; ENSG00000143537.
ENST00000449910; ENSP00000403843; ENSG00000143537. [Q13444-3]
ENST00000526491; ENSP00000432347; ENSG00000143537. [Q13444-6]
ENST00000529473; ENSP00000434227; ENSG00000143537. [Q13444-8]
ENST00000531455; ENSP00000432927; ENSG00000143537. [Q13444-12]
GeneID8751.
KEGGhsa:8751.
UCSCuc001fgr.2. human. [Q13444-1]
uc001fgs.2. human. [Q13444-9]
uc001fgt.2. human. [Q13444-3]
uc001fgu.2. human. [Q13444-5]
uc001fgv.2. human. [Q13444-4]
uc001fgw.2. human. [Q13444-2]
uc001fgx.2. human. [Q13444-10]

Organism-specific databases

CTD8751.
GeneCardsGC01P155023.
HGNCHGNC:193. ADAM15.
HPAHPA011633.
MIM605548. gene.
neXtProtNX_Q13444.
PharmGKBPA24510.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG294463.
HOGENOMHOG000230884.
HOVERGENHBG006978.
KOK06836.
OMAHGVCDSN.
OrthoDBEOG7F7W89.
PhylomeDBQ13444.
TreeFamTF314733.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressQ13444.
BgeeQ13444.
CleanExHS_ADAM15.
GenevestigatorQ13444.

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

GeneWikiADAM15.
GenomeRNAi8751.
NextBio32829.
PROQ13444.
SOURCESearch...

Entry information

Entry nameADA15_HUMAN
AccessionPrimary (citable) accession number: Q13444
Secondary accession number(s): B3KQU5 expand/collapse secondary AC list , B4DLB5, B4DMH8, E9PN65, Q13493, Q53XQ0, Q5SR68, Q5SR69, Q6R267, Q71S61, Q71S62, Q71S63, Q71S64, Q71S65, Q71S66, Q71S67, Q71S68, Q71S69, Q96C78, U3KQL5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: July 13, 2010
Last modified: July 9, 2014
This is version 157 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM