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Reviewed, UniProtKB/Swiss-Prot O43506 (ADA20_HUMAN)

Last modified December 16, 2008. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    ADAM 20
    EC=3.4.24.-
Alternative name(s):
    A disintegrin and metalloproteinase domain 20
Gene names
Name: ADAM20
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length726 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

May be involved in sperm maturation and/or fertilization.

Cofactor

Binds 1 zinc ion per subunit Potential.

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Testis specific.

Domain

A tripeptide motif (VGE) within disintegrin-like domain could be involved in the binding to egg integrin receptor and thus could mediate sperm/egg binding.

The cysteine-rich domain encodes putative cell-fusion peptides, which could be involved in sperm-egg fusion.

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

Has no obvious cleavage site for furin endopeptidase, suggesting that the proteolytic processing is regulated.

Miscellaneous

May be the functional equivalent of ADAM 1/fertilin alpha which is a pseudogene in human.

Sequence similarities

Contains 1 disintegrin domain.

Contains 1 EGF-like domain.

Contains 1 peptidase M12B domain.

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Ontologies

Keywords

   Cellular componentMembrane
   DomainEGF-like domain
Signal
Transmembrane
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMGlycoprotein
Zymogen

Gene Ontology (GO)

   Biological processproteolysis

Inferred from electronic annotation. Source: InterPro

single fertilization Ref.1

Traceable author statement. Source: ProtInc

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionmetalloendopeptidase activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Potential
Propeptide32 – 206175 Potential
PRO_0000029106
Chain207 – 726520ADAM 20
PRO_0000029107

Regions

Topological domain207 – 693487Extracellular Potential
Transmembrane694 – 71421 Potential
Topological domain715 – 72612Cytoplasmic Potential
Domain207 – 400194Peptidase M12B
Domain407 – 49387Disintegrin
Domain635 – 66329EGF-like
Motif171 – 1788Cysteine switch By similarity
Compositional bias494 – 634141Cys-rich

Sites

Active site3431 Potential
Metal binding1731Zinc; in inhibited form By similarity
Metal binding3421Zinc; catalytic Potential
Metal binding3461Zinc; catalytic Potential
Metal binding3521Zinc; catalytic Potential

Amino acid modifications

Glycosylation1911N-linked (GlcNAc...) Potential
Glycosylation2261N-linked (GlcNAc...) Potential
Glycosylation3781N-linked (GlcNAc...) Potential
Glycosylation4381N-linked (GlcNAc...) Potential
Glycosylation4791N-linked (GlcNAc...) Potential
Glycosylation5871N-linked (GlcNAc...) Potential
Disulfide bond317 ↔ 394 By similarity
Disulfide bond357 ↔ 379 By similarity
Disulfide bond359 ↔ 364 By similarity
Disulfide bond465 ↔ 485 By similarity
Disulfide bond635 ↔ 646 By similarity
Disulfide bond640 ↔ 652 By similarity
Disulfide bond654 ↔ 663 By similarity

Natural variations

Natural variant191F → L: dbSNP rs1059166. Ref.1
VAR_047311

Experimental info

Sequence conflict1091C → W in AAC52041. Ref.1
Sequence conflict6371P → R in AAC52041. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
O43506-1 [UniParc].

Last modified November 25, 2008. Version 2.
Checksum: 7DB864FA1796A9B0

FASTA72681,603
        10         20         30         40         50         60 
MAVGEPLVHI RVTLLLLWFG MFLSISGHSQ ARPSQYFTSP EVVIPLKVIS RGRGAKAPGW 

        70         80         90        100        110        120 
LSYSLRFGGQ RYIVHMRVNK LLFAAHLPVF TYTEQHALLQ DQPFIQDDCY YHGYVEGVPE 

       130        140        150        160        170        180 
SLVALSTCSG GFLGMLQIND LVYEIKPISV SATFEHLVYK IDSDDTQFPP MRCGLTEEKI 

       190        200        210        220        230        240 
AHQMELQLSY NFTLKQSSFV GWWTHQRFVE LVVVVDNIRY LFSQSNATTV QHEVFNVVNI 

       250        260        270        280        290        300 
VDSFYHPLEV DVILTGIDIW TASNPLPTSG DLDNVLEDFS IWKNYNLNNR LQHDVAHLFI 

       310        320        330        340        350        360 
KDTQGMKLGV AYVKGICQNP FNTGVDVFED NRLVVFAITL GHELGHNLGM QHDTQWCVCE 

       370        380        390        400        410        420 
LQWCIMHAYR KVTTKFSNCS YAQYWDSTIS SGLCIQPPPY PGNIFRLKYC GNLVVEEGEE 

       430        440        450        460        470        480 
CDCGTIRQCA KDPCCLLNCT LHPGAACAFG ICCKDCKFLP SGTLCRQQVG ECDLPEWCNG 

       490        500        510        520        530        540 
TSHQCPDDVY VQDGISCNVN AFCYEKTCNN HDIQCKEIFG QDARSASQSC YQEINTQGNR 

       550        560        570        580        590        600 
FGHCGIVGTT YVKCWTPDIM CGRVQCENVG VIPNLIEHST VQQFHLNDTT CWGTDYHLGM 

       610        620        630        640        650        660 
AIPDIGEVKD GTVCGPEKIC IRKKCASMVH LSQACQPKTC NMRGICNNKQ HCHCNHEWAP 

       670        680        690        700        710        720 
PYCKDKGYGG SADSGPPPKN NMEGLNVMGK LRYLSLLCLL PLVAFLLFCL HVLFKKRTKS 


KEDEEG

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References

« Hide 'large scale' references
[1]"ADAM 20 and 21; two novel human testis-specific membrane metalloproteases with similarity to fertilin-alpha."
Hooft van Huijsduijnen R.
Gene 206:273-282(1998) [PubMed: 9469942] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LEU-19.
Tissue: Testis.
[2]"The identification of seven metalloproteinase-disintegrin (ADAM) genes from genomic libraries."
Poindexter K., Nelson N., DuBose R.F., Black R.A., Cerretti D.P.
Gene 237:61-70(1999) [PubMed: 10524237] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The DNA sequence and analysis of human chromosome 14."
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. expand/collapse author list , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
Nature 421:601-607(2003) [PubMed: 12508121] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.

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Cross-references

Sequence databases

AF029899 mRNA. Translation: AAC52041.1.
AF158643 Genomic DNA. Translation: AAD55254.1.
AL357153 Genomic DNA. No translation available.
CH471061 Genomic DNA. Translation: EAW81037.1. Different initiation.
BC025378 mRNA. Translation: AAH25378.2. Different initiation.
RefSeqNP_003805.3.
UniGeneHs.177984

3D structure databases

HSSPHSSP built from PDB template 1FVL based on UniProtKB P18619.
ModBaseSearch...

Protein family/group databases

MEROPSM12.218.

Genome annotation databases

EnsemblENSG00000134007. Homo sapiens. [Contig view]
GeneID8748.
KEGGhsa:8748.

Organism-specific databases

GeneCardsGC14M070058.
HGNCHGNC:199. ADAM20.
MIM603712. gene.
PharmGKBPA24516.
GenAtlasSearch...

Phylogenomic databases

HOVERGENO43506.

Gene expression databases

ArrayExpressO43506.
CleanExHS_ADAM20.
GermOnlineENSG00000134007. Homo sapiens.

Family and domain databases

InterProIPR006586. ADAM_cysteine.
IPR001762. Blood-coag_inhib_Disintegrin.
IPR000742. EGF_3.
IPR013032. EGF_like_reg_CS.
IPR001818. Pept_M10A_M12B.
IPR006025. Pept_M_Zn_BS.
IPR001590. Peptidase_M12B.
IPR002870. Peptidase_M12B_N.
[Graphical view]
Gene3DG3DSA:4.10.70.10. Blood-coag_inhib_Disintegrin. 1 hit.
PfamPF08516. ADAM_CR. 1 hit.
PF00200. Disintegrin. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
[Graphical view]
PRINTSPR00289. DISINTEGRIN.
ProDomPD000664. Disintegrin. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00608. ACR. 1 hit.
SM00050. DISIN. 1 hit.
[Graphical view]
PROSITEPS50215. ADAM_MEPRO. 1 hit.
PS00546. CYSTEINE_SWITCH. False negative.
PS00427. DISINTEGRIN_1. 1 hit.
PS50214. DISINTEGRIN_2. 1 hit.
PS00022. EGF_1. False negative.
PS01186. EGF_2. False negative.
PS50026. EGF_3. False negative.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

SOURCESearch...

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Entry information

Entry nameADA20_HUMAN
AccessionPrimary (citable) accession number: O43506
Secondary accession number(s): Q6GTZ1, Q9UKJ9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: November 25, 2008
Last modified: December 16, 2008
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

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

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents