ADAM10

Functionⁱ

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, PubMed:29224781). 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). Mediates the proteolytic cleavage of LAG3, leading to release the secreted form of LAG3 (By similarity). May regulate the EFNA5-EPHA3 signaling (PubMed:16239146).By similarity10 Publications

Catalytic activityⁱ

Endopeptidase of broad specificity.
10 Publications
Manual assertion based on experiment inⁱ
- Ref.6
  "ADAM10-mediated cleavage of L1 adhesion molecule at the cell surface and in released membrane vesicles."
  Gutwein P., Mechtersheimer S., Riedle S., Stoeck A., Gast D., Joumaa S., Zentgraf H., Fogel M., Altevogt P.
  FASEB J. 17:292-294(2003) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
- Ref.7
  "The disintegrins ADAM10 and TACE contribute to the constitutive and phorbol ester-regulated normal cleavage of the cellular prion protein."
  Vincent B., Paitel E., Saftig P., Frobert Y., Hartmann D., De Strooper B., Grassi J., Lopez-Perez E., Checler F.
  J. Biol. Chem. 276:37743-37746(2001) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY.
- Ref.9
  "Platelet-activating factor receptor and ADAM10 mediate responses to Staphylococcus aureus in epithelial cells."
  Lemjabbar H., Basbaum C.
  Nat. Med. 8:41-46(2002) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION.
- Ref.10
  "Adam meets Eph: an ADAM substrate recognition module acts as a molecular switch for ephrin cleavage in trans."
  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.
  Cell 123:291-304(2005) [PubMed] [Europe PMC] [Abstract]
  Cited for: IDENTIFICATION IN A COMPLEX WITH EFNA5 AND EPHA3, FUNCTION IN EFNA5-EPHA3 SIGNALING, CATALYTIC ACTIVITY.
- Ref.12
  "The Fas ligand intracellular domain is released by ADAM10 and SPPL2a cleavage in T-cells."
  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.
  Cell Death Differ. 14:1678-1687(2007) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION IN CLEAVAGE OF FASLG.
- Ref.13
  "Substrate requirements for SPPL2b-dependent regulated intramembrane proteolysis."
  Martin L., Fluhrer R., Haass C.
  J. Biol. Chem. 284:5662-5670(2009) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION IN CLEAVAGE OF ITM2B.
- Ref.17
  "Junctional adhesion molecule-C is a soluble mediator of angiogenesis."
  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.
  J. Immunol. 185:1777-1785(2010) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION IN CLEAVAGE OF JAM3.
- Ref.19
  "Ectodomain shedding and autocleavage of the cardiac membrane protease corin."
  Jiang J., Wu S., Wang W., Chen S., Peng J., Zhang X., Wu Q.
  J. Biol. Chem. 286:10066-10072(2011) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION IN CLEAVAGE OF CORIN.
- Ref.24
  "TspanC8 tetraspanins differentially regulate the cleavage of ADAM10 substrates, Notch activation and ADAM10 membrane compartmentalization."
  Jouannet S., Saint-Pol J., Fernandez L., Nguyen V., Charrin S., Boucheix C., Brou C., Milhiet P.E., Rubinstein E.
  Cell. Mol. Life Sci. 73:1895-1915(2016) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH TSPAN5; TSPAN14; TSPAN15 AND TSPAN33.
- Ref.30
  "Structural basis for regulated proteolysis by the alpha-secretase ADAM10."
  Seegar T.C.M., Killingsworth L.B., Saha N., Meyer P.A., Patra D., Zimmerman B., Janes P.W., Rubinstein E., Nikolov D.B., Skiniotis G., Kruse A.C., Blacklow S.C.
  Cell 171:1638-1648.E7(2017) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 214-654 IN COMPLEX WITH ZINC, CATALYTIC ACTIVITY, FUNCTION, MUTAGENESIS OF GLU-384, GLYCOSYLATION AT ASN-278, DISULFIDE BOND, ACTIVE SITE.
EC:3.4.24.81

Cofactorⁱ

Zn²⁺1 PublicationNote: Binds 1 zinc ion per subunit.1 Publication

Activity regulationⁱ

Catalytically inactive when the propeptide is intact and associated with the mature enzyme (By similarity). The disintegrin and cysteine-rich regions modulate access of substrates to exerts an inhibitory effect on the cleavage of ADAM10 substrates (PubMed:29224781).By similarity1 Publication

Sites

Feature key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	173	Zinc; in inhibited formBy similarity	1
Metal bindingⁱ	383	Zinc; via tele nitrogen; catalyticCombined sources2 Publications	1
Active siteⁱ	384	1 Publication	1
Metal bindingⁱ	387	Zinc; via tele nitrogen; catalyticCombined sources1 Publication	1
Metal bindingⁱ	393	Zinc; via tele nitrogen; catalyticCombined sources2 Publications	1

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Hydrolase, Metalloprotease, Protease
Biological process	Notch signaling pathway
Ligand	Metal-binding, Zinc

Enzyme and pathway databases

BioCycⁱ	MetaCyc:ENSG00000137845-MONOMER
BRENDAⁱ	3.4.24.81 2681
Reactomeⁱ	R-HSA-1442490 Collagen degradation R-HSA-1474228 Degradation of the extracellular matrix R-HSA-177929 Signaling by EGFR R-HSA-2122948 Activated NOTCH1 Transmits Signal to the Nucleus R-HSA-2644606 Constitutive Signaling by NOTCH1 PEST Domain Mutants R-HSA-2660826 Constitutive Signaling by NOTCH1 t(7;9)(NOTCH1:M1580_K2555) Translocation Mutant R-HSA-2691232 Constitutive Signaling by NOTCH1 HD Domain Mutants R-HSA-2894862 Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants R-HSA-2979096 NOTCH2 Activation and Transmission of Signal to the Nucleus R-HSA-381426 Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) R-HSA-3928665 EPH-ephrin mediated repulsion of cells R-HSA-6798695 Neutrophil degranulation R-HSA-8957275 Post-translational protein phosphorylation R-HSA-9013507 NOTCH3 Activation and Transmission of Signal to the Nucleus R-HSA-9013700 NOTCH4 Activation and Transmission of Signal to the Nucleus R-HSA-977225 Amyloid fiber formation
SignaLinkⁱ	O14672
SIGNORⁱ	O14672

Protein family/group databases

MEROPS protease database More...MEROPSⁱ	M12.210
TCDBⁱ	8.A.77.1.4 the sheddase (sheddase) family

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Disintegrin and metalloproteinase domain-containing protein 10 (EC:3.4.24.817 Publications) Short name: ADAM 10 Alternative name(s): CDw156 Kuzbanian protein homolog Mammalian disintegrin-metalloprotease CD_antigen: CD156c
Gene namesⁱ	Name:ADAM10 Synonyms:KUZ, MADM
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 15

Organism-specific databases

Human Gene Nomenclature Database More...HGNCⁱ	HGNC:188 ADAM10
MIMⁱ	602192 gene
neXtProtⁱ	NX_O14672

Topology

Feature key	Position(s)	DescriptionActions	Length
Topological domainⁱ	20 – 672	ExtracellularSequence analysisAdd BLAST	653
Transmembraneⁱ	673 – 693	HelicalSequence analysisAdd BLAST	21
Topological domainⁱ	694 – 748	CytoplasmicSequence analysisAdd BLAST	55

Keywords - Cellular componentⁱ

Cell membrane, Golgi apparatus, Membrane

Pathology & Biotechⁱ

Involvement in diseaseⁱ

Reticulate acropigmentation of Kitamura (RAK)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

Related information in OMIM

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱVAR_070907	139	P → S in RAK. 1 PublicationCorresponds to variant dbSNP:rs483352912EnsemblClinVar.		1
Natural variantⁱVAR_070910	524	C → Y in RAK. 1 PublicationCorresponds to variant dbSNP:rs483352916EnsemblClinVar.		1

Alzheimer disease 18 (AD18)2 Publications

Disease susceptibility is associated with variations affecting the gene represented in this entry.

Disease descriptionA 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.

Related information in OMIM

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱVAR_070908	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. 2 PublicationsCorresponds to variant dbSNP:rs61751103Ensembl.		1
Natural variantⁱVAR_070909	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. 2 PublicationsCorresponds to variant dbSNP:rs145518263EnsemblClinVar.		1

Mutagenesis

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Mutagenesisⁱ	384	E → A: Abrogates APP cleavage. Reduces Notch signaling. 1 Publication		1

Keywords - Diseaseⁱ

Alzheimer disease, Amyloidosis, Disease mutation, Neurodegeneration

Organism-specific databases

DisGeNET More...DisGeNETⁱ	102
MalaCards human disease database More...MalaCardsⁱ	ADAM10
MIMⁱ	615537 phenotype 615590 phenotype
Open Targets More...OpenTargetsⁱ	ENSG00000137845
Orphanetⁱ	178307 Reticulate acropigmentation of Kitamura
PharmGKBⁱ	PA24505

Chemistry databases

ChEMBLⁱ	CHEMBL5028
Drug and drug target database More...DrugBankⁱ	DB04991 XL784
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYⁱ	1658

Polymorphism and mutation databases

BioMutaⁱ	ADAM10

BioMutaⁱ

ADAM10

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Length
Signal peptideⁱ	1 – 19	Sequence analysisAdd BLAST	19
PropeptideⁱPRO_0000029066	20 – 213	By similarityAdd BLAST	194
ChainⁱPRO_0000029067	214 – 748	Disintegrin and metalloproteinase domain-containing protein 10Add BLAST	535

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Disulfide bondⁱ	222 ↔ 313	Combined sources1 Publication
Glycosylationⁱ	267	N-linked (GlcNAc...) asparagineSequence analysis	1
Glycosylationⁱ	278	N-linked (GlcNAc...) asparagineCombined sources4 Publications	1
Disulfide bondⁱ	344 ↔ 451	Combined sources1 Publication
Disulfide bondⁱ	399 ↔ 435	Combined sources1 Publication
Glycosylationⁱ	439	N-linked (GlcNAc...) asparagineSequence analysis	1
Disulfide bondⁱ	460 ↔ 495	Combined sources1 Publication
Disulfide bondⁱ	471 ↔ 484	Combined sources1 Publication
Disulfide bondⁱ	473 ↔ 479	Combined sources1 Publication
Disulfide bondⁱ	483 ↔ 515	Combined sources1 Publication
Disulfide bondⁱ	503 ↔ 511	Combined sources1 Publication
Disulfide bondⁱ	510 ↔ 536	Combined sources1 Publication
Disulfide bondⁱ	524 ↔ 543	Combined sources1 Publication
Disulfide bondⁱ	530 ↔ 562	Combined sources1 Publication
Glycosylationⁱ	551	N-linked (GlcNAc...) asparagineSequence analysis	1
Disulfide bondⁱ	555 ↔ 567	Combined sources1 Publication
Disulfide bondⁱ	572 ↔ 598	Combined sources1 Publication
Disulfide bondⁱ	580 ↔ 607	Combined sources1 Publication
Disulfide bondⁱ	582 ↔ 597	Combined sources1 Publication
Disulfide bondⁱ	594 ↔ 639	Combined sources1 Publication
Disulfide bondⁱ	632 ↔ 645	Combined sources1 Publication
Modified residueⁱ	719	Phosphothreonine; by FAM20CCombined sources1 Publication	1

Post-translational modificationⁱ

The precursor is cleaved by furin and PCSK7.By similarity

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Siteⁱ	213 – 214	Cleavage; by furin and PCSK7By similarity		2

Keywords - PTMⁱ

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein, Zymogen

Proteomic databases

EPDⁱ	O14672
jPOSTⁱ	O14672
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	O14672
PaxDbⁱ	O14672
PeptideAtlas More...PeptideAtlasⁱ	O14672
PRIDEⁱ	O14672
ProteomicsDBⁱ	48162

PTM databases

GlyConnectⁱ	1178
iPTMnetⁱ	O14672
PhosphoSitePlusⁱ	O14672
SwissPalmⁱ	O14672

Miscellaneous databases

PMAP-CutDBⁱ	O14672

PMAP-CutDBⁱ

O14672

Expressionⁱ

Tissue specificityⁱ

Expressed in spleen, lymph node, thymus, peripheral blood leukocyte, bone marrow, cartilage, chondrocytes and fetal liver.2 Publications

Inductionⁱ

In osteoarthritis affected-cartilage.

Gene expression databases

Bgeeⁱ	ENSG00000137845 Expressed in 242 organ(s), highest expression level in testis
ExpressionAtlasⁱ	O14672 baseline and differential
Genevisibleⁱ	O14672 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	CAB001709 HPA050670

HPAⁱ

CAB001709
HPA050670

Interactionⁱ

Subunit structureⁱ

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).

By similarity3 Publications

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	106616, 39 interactors
Database of interacting proteins More...DIPⁱ	DIP-39889N
IntActⁱ	O14672, 12 interactors
Molecular INTeraction database More...MINTⁱ	O14672
STRINGⁱ	9606.ENSP00000260408

Chemistry databases

BindingDBⁱ

O14672

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	219 – 228	Combined sources	10
Helixⁱ	230 – 236	Combined sources	7
Helixⁱ	239 – 258	Combined sources	20
Beta strandⁱ	269 – 277	Combined sources	9
Helixⁱ	280 – 284	Combined sources	5
Helixⁱ	297 – 305	Combined sources	9
Beta strandⁱ	313 – 322	Combined sources	10
Helixⁱ	324 – 326	Combined sources	3
Beta strandⁱ	329 – 331	Combined sources	3
Beta strandⁱ	336 – 338	Combined sources	3
Beta strandⁱ	348 – 350	Combined sources	3
Beta strandⁱ	359 – 367	Combined sources	9
Helixⁱ	374 – 388	Combined sources	15
Turnⁱ	397 – 399	Combined sources	3
Helixⁱ	401 – 403	Combined sources	3
Helixⁱ	407 – 411	Combined sources	5
Helixⁱ	428 – 430	Combined sources	3
Helixⁱ	434 – 447	Combined sources	14
Helixⁱ	448 – 450	Combined sources	3
Beta strandⁱ	462 – 464	Combined sources	3
Turnⁱ	476 – 478	Combined sources	3
Turnⁱ	491 – 495	Combined sources	5
Turnⁱ	505 – 507	Combined sources	3
Beta strandⁱ	509 – 511	Combined sources	3
Beta strandⁱ	523 – 525	Combined sources	3
Beta strandⁱ	529 – 531	Combined sources	3
Beta strandⁱ	553 – 555	Combined sources	3
Turnⁱ	556 – 559	Combined sources	4
Beta strandⁱ	560 – 563	Combined sources	4
Beta strandⁱ	566 – 569	Combined sources	4
Helixⁱ	571 – 575	Combined sources	5
Beta strandⁱ	577 – 580	Combined sources	4
Beta strandⁱ	597 – 600	Combined sources	4
Helixⁱ	604 – 606	Combined sources	3
Helixⁱ	614 – 617	Combined sources	4
Beta strandⁱ	630 – 632	Combined sources	3
Turnⁱ	633 – 636	Combined sources	4
Beta strandⁱ	637 – 639	Combined sources	3
Beta strandⁱ	645 – 647	Combined sources	3

Show more details

3D structure databases

SMRⁱ	O14672
ModBaseⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	220 – 456	Peptidase M12BPROSITE-ProRule annotationAdd BLAST		237
Domainⁱ	457 – 551	DisintegrinPROSITE-ProRule annotationAdd BLAST		95

Motif

Feature key	Position(s)	DescriptionActions	Length
Motifⁱ	171 – 178	Cysteine switchBy similarity	8
Motifⁱ	708 – 715	SH3-bindingSequence analysis	8
Motifⁱ	722 – 728	SH3-bindingSequence analysis	7

Compositional bias

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Compositional biasⁱ	555 – 673	Cys-richCuratedAdd BLAST		119

Domainⁱ

The propeptide keeps the metalloprotease in a latent form via a cysteine switch mechanism. This mechanism may be mediated by a highly conserved cysteine (Cys-173) in the propeptide, which interacts and neutralizes the zinc-coordinating HEXGHXXGXXHD catalytic core of the metalloprotease domain. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.By similarity

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).By similarity1 Publication

Keywords - Domainⁱ

SH3-binding, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGⁱ	KOG3658 Eukaryota ENOG410XQWB LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00940000160579
HOGENOMⁱ	HOG000008148
InParanoidⁱ	O14672
KEGG Orthology (KO) More...KOⁱ	K06704
OMAⁱ	EGFIQTH
Database of Orthologous Groups More...OrthoDBⁱ	162519at2759
PhylomeDBⁱ	O14672
TreeFamⁱ	TF352021

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd04270 ZnMc_TACE_like, 1 hit
Gene3Dⁱ	3.40.390.10, 1 hit 4.10.70.10, 1 hit
InterProⁱ	View protein in InterPro IPR034025 ADAM10_ADAM17 IPR027053 ADAM_10 IPR001762 Disintegrin_dom IPR036436 Disintegrin_dom_sf IPR024079 MetalloPept_cat_dom_sf IPR001590 Peptidase_M12B IPR002870 Peptidase_M12B_N
PANTHERⁱ	PTHR45702:SF4 PTHR45702:SF4, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00200 Disintegrin, 1 hit PF01562 Pep_M12B_propep, 1 hit
SMARTⁱ	View protein in SMART SM00050 DISIN, 1 hit
SUPFAMⁱ	SSF57552 SSF57552, 1 hit
PROSITEⁱ	View protein in PROSITE PS50215 ADAM_MEPRO, 1 hit PS50214 DISINTEGRIN_2, 1 hit PS00142 ZINC_PROTEASE, 1 hit

Sequences (2+)ⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 2 described isoforms and 7 potential isoforms that are computationally mapped.Show all Align All

Isoform 1 (identifier: O14672-1) [UniParc]FASTA Add to basket

This isoform has been chosen as the canonicalⁱ sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MVLLRVLILL LSWAAGMGGQ YGNPLNKYIR HYEGLSYNVD SLHQKHQRAK 
        60         70         80         90        100
RAVSHEDQFL RLDFHAHGRH FNLRMKRDTS LFSDEFKVET SNKVLDYDTS 
       110        120        130        140        150
HIYTGHIYGE EGSFSHGSVI DGRFEGFIQT RGGTFYVEPA ERYIKDRTLP 
       160        170        180        190        200
FHSVIYHEDD INYPHKYGPQ GGCADHSVFE RMRKYQMTGV EEVTQIPQEE 
       210        220        230        240        250
HAANGPELLR KKRTTSAEKN TCQLYIQTDH LFFKYYGTRE AVIAQISSHV 
       260        270        280        290        300
KAIDTIYQTT DFSGIRNISF MVKRIRINTT ADEKDPTNPF RFPNIGVEKF 
       310        320        330        340        350
LELNSEQNHD DYCLAYVFTD RDFDDGVLGL AWVGAPSGSS GGICEKSKLY 
       360        370        380        390        400
SDGKKKSLNT GIITVQNYGS HVPPKVSHIT FAHEVGHNFG SPHDSGTECT 
       410        420        430        440        450
PGESKNLGQK ENGNYIMYAR ATSGDKLNNN KFSLCSIRNI SQVLEKKRNN 
       460        470        480        490        500
CFVESGQPIC GNGMVEQGEE CDCGYSDQCK DECCFDANQP EGRKCKLKPG 
       510        520        530        540        550
KQCSPSQGPC CTAQCAFKSK SEKCRDDSDC AREGICNGFT ALCPASDPKP 
       560        570        580        590        600
NFTDCNRHTQ VCINGQCAGS ICEKYGLEEC TCASSDGKDD KELCHVCCMK 
       610        620        630        640        650
KMDPSTCAST GSVQWSRHFS GRTITLQPGS PCNDFRGYCD VFMRCRLVDA 
       660        670        680        690        700
DGPLARLKKA IFSPELYENI AEWIVAHWWA VLLMGIALIM LMAGFIKICS 
       710        720        730        740 
VHTPSSNPKL PPPKPLPGTL KRRRPPQPIQ QPQRQRPRES YQMGHMRR

Length:748

Mass (Da):84,142

Last modified:January 1, 1998 - v1

Checksum:ⁱ0881E65B17022A71

GO

Isoform 2 (identifier: O14672-2) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
19-319: Missing.

« Hide

        10         20         30         40         50
MVLLRVLILL LSWAAGMGDR DFDDGVLGLA WVGAPSGSSG GICEKSKLYS 
        60         70         80         90        100
DGKKKSLNTG IITVQNYGSH VPPKVSHITF AHEVGHNFGS PHDSGTECTP 
       110        120        130        140        150
GESKNLGQKE NGNYIMYARA TSGDKLNNNK FSLCSIRNIS QVLEKKRNNC 
       160        170        180        190        200
FVESGQPICG NGMVEQGEEC DCGYSDQCKD ECCFDANQPE GRKCKLKPGK 
       210        220        230        240        250
QCSPSQGPCC TAQCAFKSKS EKCRDDSDCA REGICNGFTA LCPASDPKPN 
       260        270        280        290        300
FTDCNRHTQV CINGQCAGSI CEKYGLEECT CASSDGKDDK ELCHVCCMKK 
       310        320        330        340        350
MDPSTCASTG SVQWSRHFSG RTITLQPGSP CNDFRGYCDV FMRCRLVDAD 
       360        370        380        390        400
GPLARLKKAI FSPELYENIA EWIVAHWWAV LLMGIALIML MAGFIKICSV 
       410        420        430        440 
HTPSSNPKLP PPKPLPGTLK RRRPPQPIQQ PQRQRPRESY QMGHMRR

Note: No experimental confirmation available.

Show »

Length:447

Mass (Da):49,047

Checksum:ⁱAAD95BF5D660C7D8

GO

Computationally mapped potential isoform sequencesⁱ

There are 7 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

H0YNC5	H0YNC5_HUMAN	Disintegrin and metalloproteinase d... Disintegrin and metalloproteinase domain-containing protein 10	ADAM10	148	Annotation score:
B5MC71	B5MC71_HUMAN	Disintegrin and metalloproteinase d... Disintegrin and metalloproteinase domain-containing protein 10	ADAM10	71	Annotation score:
H0YK87	H0YK87_HUMAN	Disintegrin and metalloproteinase d... Disintegrin and metalloproteinase domain-containing protein 10	ADAM10	115	Annotation score:
C9J9B4	C9J9B4_HUMAN	Disintegrin and metalloproteinase d... Disintegrin and metalloproteinase domain-containing protein 10	ADAM10	125	Annotation score:
H3BS53	H3BS53_HUMAN	Disintegrin and metalloproteinase d... Disintegrin and metalloproteinase domain-containing protein 10	ADAM10	58	Annotation score:
H0YK32	H0YK32_HUMAN	Disintegrin and metalloproteinase d... Disintegrin and metalloproteinase domain-containing protein 10	ADAM10	38	Annotation score:
A0A087WYG1	A0A087WYG1_HUMAN	Disintegrin and metalloproteinase d... Disintegrin and metalloproteinase domain-containing protein 10	ADAM10	59	Annotation score:

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	162	N → SERLKLRLRKLMSLELWTSC CLPCALLLHSWKKAVNSHCL YFKDFWGFSEIY in CAA88463 (PubMed:8694785).Curated	1
Sequence conflictⁱ	212	K → R in CAA88463 (PubMed:8694785).Curated	1
Sequence conflictⁱ	296	G → S in CAA88463 (PubMed:8694785).Curated	1

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_070907	139	P → S in RAK. 1 PublicationCorresponds to variant dbSNP:rs483352912EnsemblClinVar.	1
Natural variantⁱVAR_070908	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. 2 PublicationsCorresponds to variant dbSNP:rs61751103Ensembl.	1
Natural variantⁱVAR_066309	176	H → Y in a cutaneous metastatic melanoma sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs267604273Ensembl.	1
Natural variantⁱVAR_070909	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. 2 PublicationsCorresponds to variant dbSNP:rs145518263EnsemblClinVar.	1
Natural variantⁱVAR_070910	524	C → Y in RAK. 1 PublicationCorresponds to variant dbSNP:rs483352916EnsemblClinVar.	1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_056401	19 – 319	Missing in isoform 2. 1 PublicationAdd BLAST		301

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF009615 mRNA Translation: AAC51766.1 AK300472 mRNA Translation: BAG62190.1 AC018904 Genomic DNA No translation available. AC091046 Genomic DNA No translation available. Z48579 mRNA Translation: CAA88463.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS10167.1 [O14672-1]
NCBI Reference Sequences More...RefSeqⁱ	NP_001101.1, NM_001110.3 [O14672-1]

Genome annotation databases

Ensemblⁱ	ENST00000260408; ENSP00000260408; ENSG00000137845 [O14672-1]
GeneIDⁱ	102
KEGGⁱ	hsa:102
UCSC genome browser More...UCSCⁱ	uc002afd.3 human [O14672-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
O14672	ADAM metallopeptidase domain 10, isoform CRA_b		HUMAN		748	UniRef100_O14672
Disintegrin and metalloproteinase domain-containing protein 10		MACMU		748
ADAM metallopeptidase domain 10		PANTR		748
Uncharacterized protein		CERAT		748
Uncharacterized protein		PANPA		748
+4
O14672-2	Disintegrin and metalloproteinase domain-containing protein 10 (Fragment)		HUMAN		148	UniRef100_O14672-2
ADAM10 isoform 10 (Fragment)		PONAB		148
ADAM10 isoform 9 (Fragment)		PANTR		148

Protein	Similar proteins		Species	Score	Length	Source
O14672	Disintegrin and metalloproteinase domain-containing protein 10	)	BOVIN		748	UniRef90_O14672
ADAM metallopeptidase domain 10, isoform CRA_b		HUMAN		748
Disintegrin and metalloproteinase domain-containing protein 10		MACMU		748
ADAM metallopeptidase domain 10		PANTR		748
Uncharacterized protein		CERAT		748
+110
O14672-2	Disintegrin and metalloproteinase domain-containing protein 10 (Fragment)		HUMAN		148	UniRef90_O14672-2
ADAM10 isoform 10 (Fragment)		PONAB		148
ADAM10 isoform 9 (Fragment)		PANTR		148
A disintegrin and metalloproteinase domain-containing protein 10		PIG		447
ADAM metallopeptidase domain 10		Agassiz's desert tortoise		418
+1

Protein	Similar proteins		Species	Score	Length	Source
O14672	Disintegrin and metalloproteinase domain-containing protein 10	)	BOVIN		748	UniRef50_O14672
Disintegrin and metalloproteinase domain-containing protein 10		XENLA		749
Disintegrin and metalloproteinase domain-containing protein 10		RAT		749
Disintegrin and metalloproteinase domain-containing protein 10		MOUSE		749
Disintegrin and metalloproteinase domain-containing protein 10		PIG		748
+611
O14672-2	Disintegrin and metalloproteinase domain-containing protein 10 (Fragment)		HUMAN		148	UniRef50_O14672-2
ADAM10 isoform 10 (Fragment)		PONAB		148
ADAM10 isoform 9 (Fragment)		PANTR		148
A disintegrin and metalloproteinase domain-containing protein 10		PIG		447
ADAM metallopeptidase domain 10		Agassiz's desert tortoise		418
+4

Cross-referencesⁱ

Web resourcesⁱ

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF009615 mRNA Translation: AAC51766.1 AK300472 mRNA Translation: BAG62190.1 AC018904 Genomic DNA No translation available. AC091046 Genomic DNA No translation available. Z48579 mRNA Translation: CAA88463.1
CCDSⁱ	CCDS10167.1 [O14672-1]
RefSeqⁱ	NP_001101.1, NM_001110.3 [O14672-1]

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1M1I	model	-	A	207-453	[»]
	6BDZ	X-ray	3.10	A	220-654	[»]
	6BE6	X-ray	2.80	A/B/C/D	214-654	[»]
SMRⁱ	O14672
ModBaseⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	106616, 39 interactors
DIPⁱ	DIP-39889N
IntActⁱ	O14672, 12 interactors
MINTⁱ	O14672
STRINGⁱ	9606.ENSP00000260408

Chemistry databases

BindingDBⁱ	O14672
ChEMBLⁱ	CHEMBL5028
DrugBankⁱ	DB04991 XL784
GuidetoPHARMACOLOGYⁱ	1658

Protein family/group databases

MEROPSⁱ	M12.210
TCDBⁱ	8.A.77.1.4 the sheddase (sheddase) family

PTM databases

GlyConnectⁱ	1178
iPTMnetⁱ	O14672
PhosphoSitePlusⁱ	O14672
SwissPalmⁱ	O14672

Polymorphism and mutation databases

BioMutaⁱ	ADAM10

BioMutaⁱ

ADAM10

Proteomic databases

EPDⁱ	O14672
jPOSTⁱ	O14672
MaxQBⁱ	O14672
PaxDbⁱ	O14672
PeptideAtlasⁱ	O14672
PRIDEⁱ	O14672
ProteomicsDBⁱ	48162

Protocols and materials databases

ABCDⁱ	O14672
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000260408; ENSP00000260408; ENSG00000137845 [O14672-1]
GeneIDⁱ	102
KEGGⁱ	hsa:102
UCSCⁱ	uc002afd.3 human [O14672-1]

Organism-specific databases

CTDⁱ	102
DisGeNETⁱ	102
GeneCardsⁱ	ADAM10
HGNCⁱ	HGNC:188 ADAM10
HPAⁱ	CAB001709 HPA050670
MalaCardsⁱ	ADAM10
MIMⁱ	602192 gene 615537 phenotype 615590 phenotype
neXtProtⁱ	NX_O14672
OpenTargetsⁱ	ENSG00000137845
Orphanetⁱ	178307 Reticulate acropigmentation of Kitamura
PharmGKBⁱ	PA24505
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG3658 Eukaryota ENOG410XQWB LUCA
GeneTreeⁱ	ENSGT00940000160579
HOGENOMⁱ	HOG000008148
InParanoidⁱ	O14672
KOⁱ	K06704
OMAⁱ	EGFIQTH
OrthoDBⁱ	162519at2759
PhylomeDBⁱ	O14672
TreeFamⁱ	TF352021

Enzyme and pathway databases

BioCycⁱ	MetaCyc:ENSG00000137845-MONOMER
BRENDAⁱ	3.4.24.81 2681
Reactomeⁱ	R-HSA-1442490 Collagen degradation R-HSA-1474228 Degradation of the extracellular matrix R-HSA-177929 Signaling by EGFR R-HSA-2122948 Activated NOTCH1 Transmits Signal to the Nucleus R-HSA-2644606 Constitutive Signaling by NOTCH1 PEST Domain Mutants R-HSA-2660826 Constitutive Signaling by NOTCH1 t(7;9)(NOTCH1:M1580_K2555) Translocation Mutant R-HSA-2691232 Constitutive Signaling by NOTCH1 HD Domain Mutants R-HSA-2894862 Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants R-HSA-2979096 NOTCH2 Activation and Transmission of Signal to the Nucleus R-HSA-381426 Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) R-HSA-3928665 EPH-ephrin mediated repulsion of cells R-HSA-6798695 Neutrophil degranulation R-HSA-8957275 Post-translational protein phosphorylation R-HSA-9013507 NOTCH3 Activation and Transmission of Signal to the Nucleus R-HSA-9013700 NOTCH4 Activation and Transmission of Signal to the Nucleus R-HSA-977225 Amyloid fiber formation
SignaLinkⁱ	O14672
SIGNORⁱ	O14672

Miscellaneous databases

ChiTaRSⁱ	ADAM10 human
GeneWikiⁱ	ADAM10
GenomeRNAiⁱ	102
PMAP-CutDBⁱ	O14672
Protein Ontology More...PROⁱ	PR:O14672
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000137845 Expressed in 242 organ(s), highest expression level in testis
ExpressionAtlasⁱ	O14672 baseline and differential
Genevisibleⁱ	O14672 HS

Family and domain databases

CDDⁱ	cd04270 ZnMc_TACE_like, 1 hit
Gene3Dⁱ	3.40.390.10, 1 hit 4.10.70.10, 1 hit
InterProⁱ	View protein in InterPro IPR034025 ADAM10_ADAM17 IPR027053 ADAM_10 IPR001762 Disintegrin_dom IPR036436 Disintegrin_dom_sf IPR024079 MetalloPept_cat_dom_sf IPR001590 Peptidase_M12B IPR002870 Peptidase_M12B_N
PANTHERⁱ	PTHR45702:SF4 PTHR45702:SF4, 1 hit
Pfamⁱ	View protein in Pfam PF00200 Disintegrin, 1 hit PF01562 Pep_M12B_propep, 1 hit
SMARTⁱ	View protein in SMART SM00050 DISIN, 1 hit
SUPFAMⁱ	SSF57552 SSF57552, 1 hit
PROSITEⁱ	View protein in PROSITE PS50215 ADAM_MEPRO, 1 hit PS50214 DISINTEGRIN_2, 1 hit PS00142 ZINC_PROTEASE, 1 hit
ProtoNetⁱ	Search...
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	ADA10_HUMAN
Accessionⁱ	O14672Primary (citable) accession number: O14672 Secondary accession number(s): B4DU28, Q10742, Q92650
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	February 28, 2003
	Last sequence update:	January 1, 1998
	Last modified:	July 3, 2019
	This is version 197 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any 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.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Human cell differentiation molecules
CD nomenclature of surface proteins of human leucocytes and list of entries
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
Human chromosome 15
Human chromosome 15: entries, gene names and cross-references to MIM
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations

UniProtKB

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Supporting data

UniProtKB - O14672 (ADA10_HUMAN)

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Disintegrin and metalloproteinase domain-containing protein 10

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

Protein family/group databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Plasma membrane

Golgi apparatus

Endoplasmic reticulum

Extracellular region or secreted

Golgi apparatus

Nucleus

Plasma Membrane

Other locations

Topology

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Keywords - Diseasei

Organism-specific databases

Chemistry databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Sites

Keywords - PTMi

Proteomic databases

PTM databases

Miscellaneous databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Motif

Compositional bias

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

Protein family/group databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Your basket is currently empty. ⁱ

Functionⁱ

Catalytic activityⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

Keywords - Diseaseⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Keywords - Domainⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ