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Disintegrin and metalloproteinase domain-containing protein 10 (ADAM 10) (EC 3.4.24.81) (CDw156) (Kuzbanian protein homolog) (Mammalian disintegrin-metalloprotease) (CD antigen CD156c)

 ADA10_HUMAN             Reviewed;         748 AA.
O14672; B4DU28; Q10742; Q92650;
28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
22-NOV-2017, entry version 181.
RecName: Full=Disintegrin and metalloproteinase domain-containing protein 10;
Short=ADAM 10;
EC=3.4.24.81 {ECO:0000269|PubMed:11477090, ECO:0000269|PubMed:11786905, ECO:0000269|PubMed:12475894, ECO:0000269|PubMed:16239146, ECO:0000269|PubMed:17557115, ECO:0000269|PubMed:19114711, ECO:0000269|PubMed:20592283};
AltName: Full=CDw156;
AltName: Full=Kuzbanian protein homolog;
AltName: Full=Mammalian disintegrin-metalloprotease;
AltName: CD_antigen=CD156c;
Flags: Precursor;
Name=ADAM10; Synonyms=KUZ, MADM;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF
216-237.
PubMed=9305925; DOI=10.1074/jbc.272.39.24588;
Rosendahl M.S., Ko S.C., Long D.L., Brewer M.T., Rosenzweig B.,
Hedl E., Anderson L., Pyle S.M., Moreland J., Meyers M.A., Kohno T.,
Lyons D., Lichenstein H.S.;
"Identification and characterization of a pro-tumor necrosis factor-
alpha-processing enzyme from the ADAM family of zinc
metalloproteases.";
J. Biol. Chem. 272:24588-24593(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 109-748 (ISOFORM 1).
PubMed=8694785; DOI=10.1042/bj3170045;
Howard L., Mitchell S., Lu X., Griffiths S., Glynn P.;
"Molecular cloning of MADM: a catalytically active mammalian
disintegrin-metalloprotease expressed in various cell types.";
Biochem. J. 317:45-50(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16572171; DOI=10.1038/nature04601;
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R.,
Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
Nusbaum C.;
"Analysis of the DNA sequence and duplication history of human
chromosome 15.";
Nature 440:671-675(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
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.,
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
TISSUE SPECIFICITY.
PubMed=9016778; DOI=10.1006/bbrc.1996.5957;
McKie N., Edwards T., Dallas D.J., Houghton A., Stringer B.,
Graham R., Russell G., Croucher P.I.;
"Expression of members of a novel membrane linked metalloproteinase
family (ADAM) in human articular chondrocytes.";
Biochem. Biophys. Res. Commun. 230:335-339(1997).
[6]
FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
PubMed=12475894; DOI=10.1096/fj.02-0430fje;
Gutwein P., Mechtersheimer S., Riedle S., Stoeck A., Gast D.,
Joumaa S., Zentgraf H., Fogel M., Altevogt P.;
"ADAM10-mediated cleavage of L1 adhesion molecule at the cell surface
and in released membrane vesicles.";
FASEB J. 17:292-294(2003).
[7]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=11477090; DOI=10.1074/jbc.M105677200;
Vincent B., Paitel E., Saftig P., Frobert Y., Hartmann D.,
De Strooper B., Grassi J., Lopez-Perez E., Checler F.;
"The disintegrins ADAM10 and TACE contribute to the constitutive and
phorbol ester-regulated normal cleavage of the cellular prion
protein.";
J. Biol. Chem. 276:37743-37746(2001).
[8]
TISSUE SPECIFICITY.
PubMed=11511685; DOI=10.1177/002215540104900910;
Chubinskaya S., Mikhail R., Deutsch A., Tindal M.H.;
"ADAM-10 protein is present in human articular cartilage primarily in
the membrane-bound form and is upregulated in osteoarthritis and in
response to IL-1alpha in bovine nasal cartilage.";
J. Histochem. Cytochem. 49:1165-1176(2001).
[9]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=11786905; DOI=10.1038/nm0102-41;
Lemjabbar H., Basbaum C.;
"Platelet-activating factor receptor and ADAM10 mediate responses to
Staphylococcus aureus in epithelial cells.";
Nat. Med. 8:41-46(2002).
[10]
IDENTIFICATION IN A COMPLEX WITH EFNA5 AND EPHA3, FUNCTION IN
EFNA5-EPHA3 SIGNALING, AND CATALYTIC ACTIVITY.
PubMed=16239146; DOI=10.1016/j.cell.2005.08.014;
Janes P.W., Saha N., Barton W.A., Kolev M.V., Wimmer-Kleikamp S.H.,
Nievergall E., Blobel C.P., Himanen J.P., Lackmann M., Nikolov D.B.;
"Adam meets Eph: an ADAM substrate recognition module acts as a
molecular switch for ephrin cleavage in trans.";
Cell 123:291-304(2005).
[11]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-278.
TISSUE=Platelet;
PubMed=16263699; DOI=10.1074/mcp.M500324-MCP200;
Lewandrowski U., Moebius J., Walter U., Sickmann A.;
"Elucidation of N-glycosylation sites on human platelet proteins: a
glycoproteomic approach.";
Mol. Cell. Proteomics 5:226-233(2006).
[12]
FUNCTION IN CLEAVAGE OF FASLG.
PubMed=17557115; DOI=10.1038/sj.cdd.4402175;
Kirkin V., Cahuzac N., Guardiola-Serrano F., Huault S., Luckerath K.,
Friedmann E., Novac N., Wels W.S., Martoglio B., Hueber A.O.,
Zornig M.;
"The Fas ligand intracellular domain is released by ADAM10 and SPPL2a
cleavage in T-cells.";
Cell Death Differ. 14:1678-1687(2007).
[13]
FUNCTION IN CLEAVAGE OF ITM2B.
PubMed=19114711; DOI=10.1074/jbc.M807485200;
Martin L., Fluhrer R., Haass C.;
"Substrate requirements for SPPL2b-dependent regulated intramembrane
proteolysis.";
J. Biol. Chem. 284:5662-5670(2009).
[14]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-278.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[15]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-278.
TISSUE=Leukemic T-cell;
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[16]
INTERACTION WITH NGF.
PubMed=20164177; DOI=10.1074/jbc.M110.100479;
Wijeyewickrema L.C., Gardiner E.E., Gladigau E.L., Berndt M.C.,
Andrews R.K.;
"Nerve growth factor inhibits metalloproteinase-disintegrins and
blocks ectodomain shedding of platelet glycoprotein VI.";
J. Biol. Chem. 285:11793-11799(2010).
[17]
FUNCTION IN CLEAVAGE OF JAM3.
PubMed=20592283; DOI=10.4049/jimmunol.1000556;
Rabquer B.J., Amin M.A., Teegala N., Shaheen M.K., Tsou P.S.,
Ruth J.H., Lesch C.A., Imhof B.A., Koch A.E.;
"Junctional adhesion molecule-C is a soluble mediator of
angiogenesis.";
J. Immunol. 185:1777-1785(2010).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[19]
FUNCTION IN CLEAVAGE OF CORIN.
PubMed=21288900; DOI=10.1074/jbc.M110.185082;
Jiang J., Wu S., Wang W., Chen S., Peng J., Zhang X., Wu Q.;
"Ectodomain shedding and autocleavage of the cardiac membrane protease
corin.";
J. Biol. Chem. 286:10066-10072(2011).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-719, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-719, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[22]
PHOSPHORYLATION AT THR-719.
PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
Pinna L.A., Pagliarini D.J., Dixon J.E.;
"A single kinase generates the majority of the secreted
phosphoproteome.";
Cell 161:1619-1632(2015).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[24]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND INTERACTION
WITH TSPAN5; TSPAN14; TSPAN15 AND TSPAN33.
PubMed=26686862; DOI=10.1007/s00018-015-2111-z;
Jouannet S., Saint-Pol J., Fernandez L., Nguyen V., Charrin S.,
Boucheix C., Brou C., Milhiet P.E., Rubinstein E.;
"TspanC8 tetraspanins differentially regulate the cleavage of ADAM10
substrates, Notch activation and ADAM10 membrane
compartmentalization.";
Cell. Mol. Life Sci. 73:1895-1915(2016).
[25]
INTERACTION WITH TSPAN14, AND DOMAIN.
PubMed=26668317; DOI=10.1074/jbc.M115.703058;
Noy P.J., Yang J., Reyat J.S., Matthews A.L., Charlton A.E.,
Furmston J., Rogers D.A., Rainger G.E., Tomlinson M.G.;
"TspanC8 tetraspanins and A disintegrin and metalloprotease 10
(ADAM10) interact via their extracellular regions: evidence for
distinct binding mechanisms for different TspanC8 proteins.";
J. Biol. Chem. 291:3145-3157(2016).
[26]
VARIANTS AD18 HIS-170 AND GLY-181, AND CHARACTERIZATION OF VARIANTS
AD18 HIS-170 AND GLY-181.
PubMed=19608551; DOI=10.1093/hmg/ddp323;
Kim M., Suh J., Romano D., Truong M.H., Mullin K., Hooli B.,
Norton D., Tesco G., Elliott K., Wagner S.L., Moir R.D., Becker K.D.,
Tanzi R.E.;
"Potential late-onset Alzheimer's disease-associated mutations in the
ADAM10 gene attenuate {alpha}-secretase activity.";
Hum. Mol. Genet. 18:3987-3996(2009).
[27]
VARIANT TYR-176.
PubMed=21618342; DOI=10.1002/humu.21477;
Wei X., Moncada-Pazos A., Cal S., Soria-Valles C., Gartner J.,
Rudloff U., Lin J.C., Rosenberg S.A., Lopez-Otin C., Samuels Y.;
"Analysis of the disintegrin-metalloproteinases family reveals ADAM29
and ADAM7 are often mutated in melanoma.";
Hum. Mutat. 32:E2148-E2175(2011).
[28]
VARIANTS RAK SER-139 AND TYR-524.
PubMed=23666529; DOI=10.1093/hmg/ddt207;
Kono M., Sugiura K., Suganuma M., Hayashi M., Takama H., Suzuki T.,
Matsunaga K., Tomita Y., Akiyama M.;
"Whole-exome sequencing identifies ADAM10 mutations as a cause of
reticulate acropigmentation of Kitamura, a clinical entity distinct
from Dowling-Degos disease.";
Hum. Mol. Genet. 22:3524-3533(2013).
[29]
CHARACTERIZATION OF VARIANTS AD18 HIS-170 AND GLY-181.
PubMed=24055016; DOI=10.1016/j.neuron.2013.08.035;
Suh J., Choi S.H., Romano D.M., Gannon M.A., Lesinski A.N., Kim D.Y.,
Tanzi R.E.;
"ADAM10 missense mutations potentiate beta-amyloid accumulation by
impairing prodomain chaperone function.";
Neuron 80:385-401(2013).
-!- FUNCTION: Cleaves the membrane-bound precursor of TNF-alpha at
'76-Ala-|-Val-77' to its mature soluble form. Responsible for the
proteolytical release of soluble JAM3 from endothelial cells
surface (PubMed:20592283). Responsible for the proteolytic release
of several other cell-surface proteins, including heparin-binding
epidermal growth-like factor, ephrin-A2, CD44, CDH2 and for
constitutive and regulated alpha-secretase cleavage of amyloid
precursor protein (APP) (PubMed:26686862, PubMed:11786905).
Contributes to the normal cleavage of the cellular prion protein
(PubMed:11477090). Involved in the cleavage of the adhesion
molecule L1 at the cell surface and in released membrane vesicles,
suggesting a vesicle-based protease activity (PubMed:12475894).
Controls also the proteolytic processing of Notch and mediates
lateral inhibition during neurogenesis (By similarity).
Responsible for the FasL ectodomain shedding and for the
generation of the remnant ADAM10-processed FasL (FasL APL)
transmembrane form (PubMed:17557115). Also cleaves the ectodomain
of the integral membrane proteins CORIN and ITM2B
(PubMed:19114711, PubMed:21288900). May regulate the EFNA5-EPHA3
signaling (PubMed:16239146). {ECO:0000250|UniProtKB:O35598,
ECO:0000269|PubMed:11477090, ECO:0000269|PubMed:11786905,
ECO:0000269|PubMed:12475894, ECO:0000269|PubMed:16239146,
ECO:0000269|PubMed:17557115, ECO:0000269|PubMed:19114711,
ECO:0000269|PubMed:20592283, ECO:0000269|PubMed:21288900,
ECO:0000269|PubMed:26686862}.
-!- CATALYTIC ACTIVITY: Endopeptidase of broad specificity.
{ECO:0000269|PubMed:11477090, ECO:0000269|PubMed:11786905,
ECO:0000269|PubMed:12475894, ECO:0000269|PubMed:16239146,
ECO:0000269|PubMed:17557115, ECO:0000269|PubMed:19114711,
ECO:0000269|PubMed:20592283, ECO:0000269|PubMed:21288900,
ECO:0000269|PubMed:26686862}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000250|UniProtKB:P78325};
Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P78325};
-!- SUBUNIT: Interacts with EPHA2 (By similarity). Forms a ternary
EFNA5-EPHA3-ADAM10 complex mediating EFNA5 extracellular domain
shedding by ADAM10 which regulates the EFNA5-EPHA3 complex
internalization and function, the cleavage occurs in trans, with
ADAM10 and its substrate being on the membranes of opposing cells
(PubMed:16239146). Interacts with NGF in a divalent cation-
dependent manner (PubMed:20164177). Interacts with TSPAN14; the
interaction promotes ADAM10 maturation and cell surface expression
(PubMed:26668317, PubMed:26686862). Interacts with TSPAN5,
TSPAN10, TSPAN15, TSPAN17 and TSPAN33; these interactions regulate
ADAM10 substrate specificity (PubMed:26686862).
{ECO:0000250|UniProtKB:O35598, ECO:0000269|PubMed:16239146,
ECO:0000269|PubMed:20164177, ECO:0000269|PubMed:26668317}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26686862};
Single-pass type I membrane protein {ECO:0000305}. Golgi apparatus
membrane {ECO:0000269|PubMed:12475894}; Single-pass type I
membrane protein {ECO:0000305}. Note=Is localized in the plasma
membrane but is predominantly expressed in the Golgi apparatus and
in released membrane vesicles derived likely from the Golgi.
{ECO:0000269|PubMed:12475894}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O14672-1; Sequence=Displayed;
Name=2;
IsoId=O14672-2; Sequence=VSP_056401;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in spleen, lymph node, thymus,
peripheral blood leukocyte, bone marrow, cartilage, chondrocytes
and fetal liver. {ECO:0000269|PubMed:11511685,
ECO:0000269|PubMed:9016778}.
-!- INDUCTION: In osteoarthritis affected-cartilage.
-!- DOMAIN: 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.
-!- DOMAIN: The Cys-rich region C-terminal to the disintegrin domain
functions as a substrate-recognition module, it recognizes the
EFNA5-EPHA3 Complex but not the individual proteins (By
similarity). Both Cys-rich and stalk region are necessary for
interaction with TSPAN5, TSPAN10, TSPAN14, TSPAN17, TSPAN33
(PubMed:26668317). Stalk region is sufficient for interaction with
TSPAN15 (By similarity). {ECO:0000250|UniProtKB:O35598,
ECO:0000250|UniProtKB:Q10741, ECO:0000269|PubMed:26668317}.
-!- PTM: The precursor is cleaved by a furin endopeptidase.
{ECO:0000250}.
-!- DISEASE: Reticulate acropigmentation of Kitamura (RAK)
[MIM:615537]: A rare cutaneous pigmentation disorder characterized
by reticulate, slightly depressed, sharply demarcated brown
macules without hypopigmentation, affecting the dorsa of the hands
and feet and appearing in the first or second decade of life. The
macules gradually darken and extend to the proximal regions of the
extremities. The manifestations tend to progress until middle age,
after which progression of the eruptions stops. The pigmentary
augmentation is found on the flexor aspects of the wrists, neck,
patella and olecranon. Other features include breaks in the
epidermal ridges on the palms and fingers, palmoplantar pits,
occasionally plantar keratoderma, and partial alopecia.
{ECO:0000269|PubMed:23666529}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Alzheimer disease 18 (AD18) [MIM:615590]: A late-onset
form of Alzheimer disease. Alzheimer disease is a
neurodegenerative disorder characterized by progressive dementia,
loss of cognitive abilities, and deposition of fibrillar amyloid
proteins as intraneuronal neurofibrillary tangles, extracellular
amyloid plaques and vascular amyloid deposits. The major
constituents of these plaques are neurotoxic amyloid-beta protein
40 and amyloid-beta protein 42, that are produced by the
proteolysis of the transmembrane APP protein. The cytotoxic C-
terminal fragments (CTFs) and the caspase-cleaved products, such
as C31, are also implicated in neuronal death.
{ECO:0000269|PubMed:19608551, ECO:0000269|PubMed:24055016}.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/ADAM10ID44397ch15q21.html";
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EMBL; AF009615; AAC51766.1; -; mRNA.
EMBL; AK300472; BAG62190.1; -; mRNA.
EMBL; AC018904; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC091046; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z48579; CAA88463.1; -; mRNA.
CCDS; CCDS10167.1; -. [O14672-1]
RefSeq; NP_001101.1; NM_001110.3. [O14672-1]
UniGene; Hs.172028; -.
UniGene; Hs.578508; -.
UniGene; Hs.745136; -.
PDB; 1M1I; Model; -; A=207-453.
PDBsum; 1M1I; -.
ProteinModelPortal; O14672; -.
SMR; O14672; -.
BioGrid; 106616; 35.
DIP; DIP-39889N; -.
IntAct; O14672; 10.
MINT; MINT-5000775; -.
STRING; 9606.ENSP00000260408; -.
BindingDB; O14672; -.
ChEMBL; CHEMBL5028; -.
DrugBank; DB04991; XL784.
GuidetoPHARMACOLOGY; 1658; -.
MEROPS; M12.210; -.
TCDB; 8.A.77.1.4; the sheddase (sheddase) family.
iPTMnet; O14672; -.
PhosphoSitePlus; O14672; -.
SwissPalm; O14672; -.
EPD; O14672; -.
MaxQB; O14672; -.
PaxDb; O14672; -.
PeptideAtlas; O14672; -.
PRIDE; O14672; -.
Ensembl; ENST00000260408; ENSP00000260408; ENSG00000137845. [O14672-1]
GeneID; 102; -.
KEGG; hsa:102; -.
UCSC; uc002afd.3; human. [O14672-1]
CTD; 102; -.
DisGeNET; 102; -.
EuPathDB; HostDB:ENSG00000137845.14; -.
GeneCards; ADAM10; -.
HGNC; HGNC:188; ADAM10.
HPA; CAB001709; -.
HPA; HPA050670; -.
MalaCards; ADAM10; -.
MIM; 602192; gene.
MIM; 615537; phenotype.
MIM; 615590; phenotype.
neXtProt; NX_O14672; -.
OpenTargets; ENSG00000137845; -.
Orphanet; 178307; Reticulate acropigmentation of Kitamura.
PharmGKB; PA24505; -.
eggNOG; KOG3658; Eukaryota.
eggNOG; ENOG410XQWB; LUCA.
GeneTree; ENSGT00670000097974; -.
HOGENOM; HOG000008148; -.
HOVERGEN; HBG050455; -.
InParanoid; O14672; -.
KO; K06704; -.
OMA; EGFIQTH; -.
OrthoDB; EOG091G01J4; -.
PhylomeDB; O14672; -.
TreeFam; TF352021; -.
BioCyc; MetaCyc:ENSG00000137845-MONOMER; -.
BRENDA; 3.4.24.81; 2681.
Reactome; R-HSA-1442490; Collagen degradation.
Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
Reactome; R-HSA-177929; Signaling by EGFR.
Reactome; R-HSA-1980148; Signaling by NOTCH3.
Reactome; R-HSA-1980150; Signaling by NOTCH4.
Reactome; R-HSA-2122948; Activated NOTCH1 Transmits Signal to the Nucleus.
Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants.
Reactome; R-HSA-2660826; Constitutive Signaling by NOTCH1 t(7;9)(NOTCH1:M1580_K2555) Translocation Mutant.
Reactome; R-HSA-2691232; Constitutive Signaling by NOTCH1 HD Domain Mutants.
Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
Reactome; R-HSA-2979096; NOTCH2 Activation and Transmission of Signal to the Nucleus.
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-HSA-3928665; EPH-ephrin mediated repulsion of cells.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
SignaLink; O14672; -.
ChiTaRS; ADAM10; human.
GeneWiki; ADAM10; -.
GenomeRNAi; 102; -.
PMAP-CutDB; O14672; -.
PRO; PR:O14672; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000137845; -.
CleanEx; HS_ADAM10; -.
ExpressionAtlas; O14672; baseline and differential.
Genevisible; O14672; HS.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0005798; C:Golgi-associated vesicle; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0097038; C:perinuclear endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
GO; GO:0097197; C:tetraspanin-enriched microdomain; IDA:UniProtKB.
GO; GO:0004175; F:endopeptidase activity; ISS:UniProtKB.
GO; GO:0005178; F:integrin binding; NAS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004222; F:metalloendopeptidase activity; IMP:UniProtKB.
GO; GO:0008237; F:metallopeptidase activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB.
GO; GO:0005102; F:receptor binding; NAS:UniProtKB.
GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
GO; GO:0007267; P:cell-cell signaling; NAS:UniProtKB.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0051089; P:constitutive protein ectodomain proteolysis; IDA:UniProtKB.
GO; GO:0048013; P:ephrin receptor signaling pathway; TAS:Reactome.
GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome.
GO; GO:0001701; P:in utero embryonic development; ISS:UniProtKB.
GO; GO:0007229; P:integrin-mediated signaling pathway; NAS:UniProtKB.
GO; GO:0006509; P:membrane protein ectodomain proteolysis; IDA:UniProtKB.
GO; GO:0042117; P:monocyte activation; IMP:BHF-UCL.
GO; GO:0007162; P:negative regulation of cell adhesion; IDA:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0007220; P:Notch receptor processing; TAS:Reactome.
GO; GO:0007219; P:Notch signaling pathway; ISS:UniProtKB.
GO; GO:0051088; P:PMA-inducible membrane protein ectodomain proteolysis; IMP:BHF-UCL.
GO; GO:0030307; P:positive regulation of cell growth; IMP:BHF-UCL.
GO; GO:0030335; P:positive regulation of cell migration; IMP:BHF-UCL.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:BHF-UCL.
GO; GO:0010820; P:positive regulation of T cell chemotaxis; IMP:BHF-UCL.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
GO; GO:0016485; P:protein processing; IEA:Ensembl.
GO; GO:0034612; P:response to tumor necrosis factor; IDA:BHF-UCL.
CDD; cd04270; ZnMc_TACE_like; 1.
Gene3D; 3.40.390.10; -; 1.
Gene3D; 4.10.70.10; -; 1.
InterPro; IPR034025; ADAM10_ADAM17.
InterPro; IPR027053; ADAM_10.
InterPro; IPR001762; Disintegrin_dom.
InterPro; IPR036436; Disintegrin_dom_sf.
InterPro; IPR024079; MetalloPept_cat_dom_sf.
InterPro; IPR001590; Peptidase_M12B.
InterPro; IPR002870; Peptidase_M12B_N.
PANTHER; PTHR11905:SF4; PTHR11905:SF4; 1.
Pfam; PF00200; Disintegrin; 1.
Pfam; PF01562; Pep_M12B_propep; 1.
SMART; SM00050; DISIN; 1.
SUPFAM; SSF57552; SSF57552; 1.
PROSITE; PS50215; ADAM_MEPRO; 1.
PROSITE; PS50214; DISINTEGRIN_2; 1.
PROSITE; PS00142; ZINC_PROTEASE; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Alzheimer disease; Amyloidosis;
Cell membrane; Cleavage on pair of basic residues; Complete proteome;
Direct protein sequencing; Disease mutation; Disulfide bond;
Glycoprotein; Golgi apparatus; Hydrolase; Membrane; Metal-binding;
Metalloprotease; Neurodegeneration; Notch signaling pathway;
Phosphoprotein; Polymorphism; Protease; Reference proteome;
SH3-binding; Signal; Transmembrane; Transmembrane helix; Zinc;
Zymogen.
SIGNAL 1 19 {ECO:0000255}.
PROPEP 20 213 {ECO:0000250|UniProtKB:Q10741}.
/FTId=PRO_0000029066.
CHAIN 214 748 Disintegrin and metalloproteinase domain-
containing protein 10.
/FTId=PRO_0000029067.
TOPO_DOM 20 672 Extracellular. {ECO:0000255}.
TRANSMEM 673 693 Helical. {ECO:0000255}.
TOPO_DOM 694 748 Cytoplasmic. {ECO:0000255}.
DOMAIN 220 456 Peptidase M12B. {ECO:0000255|PROSITE-
ProRule:PRU00276}.
DOMAIN 457 551 Disintegrin. {ECO:0000255|PROSITE-
ProRule:PRU00068}.
MOTIF 171 178 Cysteine switch. {ECO:0000250}.
MOTIF 708 715 SH3-binding. {ECO:0000255}.
MOTIF 722 728 SH3-binding. {ECO:0000255}.
COMPBIAS 555 673 Cys-rich.
ACT_SITE 384 384
METAL 173 173 Zinc; in inhibited form. {ECO:0000250}.
METAL 383 383 Zinc; catalytic.
{ECO:0000250|UniProtKB:P78325}.
METAL 387 387 Zinc; catalytic.
{ECO:0000250|UniProtKB:P78325}.
METAL 393 393 Zinc; catalytic.
{ECO:0000250|UniProtKB:P78325}.
MOD_RES 719 719 Phosphothreonine; by FAM20C.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:26091039}.
CARBOHYD 267 267 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 278 278 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16263699,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19349973}.
CARBOHYD 439 439 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 551 551 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 222 313 {ECO:0000250}.
DISULFID 344 451 {ECO:0000250}.
DISULFID 399 435 {ECO:0000250}.
DISULFID 484 515 {ECO:0000250|UniProtKB:Q10741}.
DISULFID 503 511 {ECO:0000250|UniProtKB:Q10741}.
DISULFID 524 543 {ECO:0000250|UniProtKB:Q10741}.
DISULFID 530 562 {ECO:0000250|UniProtKB:Q10741}.
DISULFID 555 567 {ECO:0000250|UniProtKB:Q10741}.
DISULFID 572 598 {ECO:0000250|UniProtKB:Q10741}.
DISULFID 580 607 {ECO:0000250|UniProtKB:Q10741}.
DISULFID 582 597 {ECO:0000250|UniProtKB:Q10741}.
DISULFID 594 639 {ECO:0000250|UniProtKB:Q10741}.
DISULFID 632 645 {ECO:0000250|UniProtKB:Q10741}.
VAR_SEQ 19 319 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056401.
VARIANT 139 139 P -> S (in RAK; dbSNP:rs483352912).
{ECO:0000269|PubMed:23666529}.
/FTId=VAR_070907.
VARIANT 170 170 Q -> H (in AD18; associated with disease
susceptibility; significantly attenuates
alpha-secretase activity of the enzyme;
shifts APP processing toward beta-
secretase-mediated cleavage resulting in
enhanced amyloid-beta plaque load and
reactive gliosis; dbSNP:rs61751103).
{ECO:0000269|PubMed:19608551,
ECO:0000269|PubMed:24055016}.
/FTId=VAR_070908.
VARIANT 176 176 H -> Y (in a cutaneous metastatic
melanoma sample; somatic mutation;
dbSNP:rs267604273).
{ECO:0000269|PubMed:21618342}.
/FTId=VAR_066309.
VARIANT 181 181 R -> G (in AD18; associated with disease
susceptibility; significantly attenuates
alpha-secretase activity of the enzyme;
shifts APP processing toward beta-
secretase-mediated cleavage resulting in
enhanced amyloid-beta plaque load and
reactive gliosis; dbSNP:rs145518263).
{ECO:0000269|PubMed:19608551,
ECO:0000269|PubMed:24055016}.
/FTId=VAR_070909.
VARIANT 524 524 C -> Y (in RAK; dbSNP:rs483352916).
{ECO:0000269|PubMed:23666529}.
/FTId=VAR_070910.
CONFLICT 162 162 N -> SERLKLRLRKLMSLELWTSCCLPCALLLHSWKKAVN
SHCLYFKDFWGFSEIY (in Ref. 2; CAA88463).
{ECO:0000305}.
CONFLICT 212 212 K -> R (in Ref. 2; CAA88463).
{ECO:0000305}.
CONFLICT 296 296 G -> S (in Ref. 2; CAA88463).
{ECO:0000305}.
SEQUENCE 748 AA; 84142 MW; 0881E65B17022A71 CRC64;
MVLLRVLILL LSWAAGMGGQ YGNPLNKYIR HYEGLSYNVD SLHQKHQRAK RAVSHEDQFL
RLDFHAHGRH FNLRMKRDTS LFSDEFKVET SNKVLDYDTS HIYTGHIYGE EGSFSHGSVI
DGRFEGFIQT RGGTFYVEPA ERYIKDRTLP FHSVIYHEDD INYPHKYGPQ GGCADHSVFE
RMRKYQMTGV EEVTQIPQEE HAANGPELLR KKRTTSAEKN TCQLYIQTDH LFFKYYGTRE
AVIAQISSHV KAIDTIYQTT DFSGIRNISF MVKRIRINTT ADEKDPTNPF RFPNIGVEKF
LELNSEQNHD DYCLAYVFTD RDFDDGVLGL AWVGAPSGSS GGICEKSKLY SDGKKKSLNT
GIITVQNYGS HVPPKVSHIT FAHEVGHNFG SPHDSGTECT PGESKNLGQK ENGNYIMYAR
ATSGDKLNNN KFSLCSIRNI SQVLEKKRNN CFVESGQPIC GNGMVEQGEE CDCGYSDQCK
DECCFDANQP EGRKCKLKPG KQCSPSQGPC CTAQCAFKSK SEKCRDDSDC AREGICNGFT
ALCPASDPKP NFTDCNRHTQ VCINGQCAGS ICEKYGLEEC TCASSDGKDD KELCHVCCMK
KMDPSTCAST GSVQWSRHFS GRTITLQPGS PCNDFRGYCD VFMRCRLVDA DGPLARLKKA
IFSPELYENI AEWIVAHWWA VLLMGIALIM LMAGFIKICS VHTPSSNPKL PPPKPLPGTL
KRRRPPQPIQ QPQRQRPRES YQMGHMRR


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