GenomeNet

Database: UniProt
Entry: O43506
LinkDB: O43506
Original site: O43506 
ID   ADA20_HUMAN             Reviewed;         726 AA.
AC   O43506; Q6GTZ1; Q9UKJ9;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 2.
DT   13-FEB-2019, entry version 171.
DE   RecName: Full=Disintegrin and metalloproteinase domain-containing protein 20;
DE            Short=ADAM 20;
DE            EC=3.4.24.-;
DE   Flags: Precursor;
GN   Name=ADAM20;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LEU-19.
RC   TISSUE=Testis;
RX   PubMed=9469942; DOI=10.1016/S0378-1119(97)00597-0;
RA   Hooft van Huijsduijnen R.;
RT   "ADAM 20 and 21; two novel human testis-specific membrane
RT   metalloproteases with similarity to fertilin-alpha.";
RL   Gene 206:273-282(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10524237; DOI=10.1016/S0378-1119(99)00302-9;
RA   Poindexter K., Nelson N., DuBose R.F., Black R.A., Cerretti D.P.;
RT   "The identification of seven metalloproteinase-disintegrin (ADAM)
RT   genes from genomic libraries.";
RL   Gene 237:61-70(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12508121; DOI=10.1038/nature01348;
RA   Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA   Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA   Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
RA   Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
RA   Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
RA   Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
RA   Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
RA   Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
RA   Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
RA   Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
RA   Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
RA   Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
RA   Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
RA   Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA   Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA   Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
RA   Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
RA   Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
RA   Quetier F., Waterston R., Hood L., Weissenbach J.;
RT   "The DNA sequence and analysis of human chromosome 14.";
RL   Nature 421:601-607(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May be involved in sperm maturation and/or
CC       fertilization.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000305};
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: Testis specific.
CC   -!- DOMAIN: A tripeptide motif (VGE) within disintegrin-like domain
CC       could be involved in the binding to egg integrin receptor and thus
CC       could mediate sperm/egg binding.
CC   -!- DOMAIN: The cysteine-rich domain encodes putative cell-fusion
CC       peptides, which could be involved in sperm-egg fusion.
CC   -!- DOMAIN: The conserved cysteine present in the cysteine-switch
CC       motif binds the catalytic zinc ion, thus inhibiting the enzyme.
CC       The dissociation of the cysteine from the zinc ion upon the
CC       activation-peptide release activates the enzyme.
CC   -!- PTM: Has no obvious cleavage site for furin endopeptidase,
CC       suggesting that the proteolytic processing is regulated.
CC   -!- MISCELLANEOUS: May be the functional equivalent of ADAM 1/fertilin
CC       alpha which is a pseudogene in human.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH25378.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
CC       Sequence=AAH25378.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=EAW81037.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
DR   EMBL; AF029899; AAC52041.1; -; mRNA.
DR   EMBL; AF158643; AAD55254.1; -; Genomic_DNA.
DR   EMBL; AL357153; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471061; EAW81037.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BC025378; AAH25378.2; ALT_INIT; mRNA.
DR   CCDS; CCDS32111.1; -.
DR   RefSeq; NP_003805.3; NM_003814.4.
DR   RefSeq; XP_005268208.1; XM_005268151.3.
DR   UniGene; Hs.177984; -.
DR   ProteinModelPortal; O43506; -.
DR   SMR; O43506; -.
DR   IntAct; O43506; 1.
DR   MINT; O43506; -.
DR   STRING; 9606.ENSP00000256389; -.
DR   MEROPS; M12.218; -.
DR   iPTMnet; O43506; -.
DR   PhosphoSitePlus; O43506; -.
DR   BioMuta; ADAM20; -.
DR   jPOST; O43506; -.
DR   PaxDb; O43506; -.
DR   PeptideAtlas; O43506; -.
DR   PRIDE; O43506; -.
DR   ProteomicsDB; 48999; -.
DR   DNASU; 8748; -.
DR   Ensembl; ENST00000256389; ENSP00000256389; ENSG00000134007.
DR   GeneID; 8748; -.
DR   KEGG; hsa:8748; -.
DR   UCSC; uc001xme.4; human.
DR   CTD; 8748; -.
DR   DisGeNET; 8748; -.
DR   EuPathDB; HostDB:ENSG00000134007.3; -.
DR   GeneCards; ADAM20; -.
DR   HGNC; HGNC:199; ADAM20.
DR   HPA; HPA059377; -.
DR   MIM; 603712; gene.
DR   neXtProt; NX_O43506; -.
DR   PharmGKB; PA24516; -.
DR   eggNOG; KOG3607; Eukaryota.
DR   eggNOG; ENOG410XX2M; LUCA.
DR   HOGENOM; HOG000230883; -.
DR   HOVERGEN; HBG006978; -.
DR   InParanoid; O43506; -.
DR   KO; K08609; -.
DR   OrthoDB; 162519at2759; -.
DR   PhylomeDB; O43506; -.
DR   TreeFam; TF314733; -.
DR   Reactome; R-HSA-1300644; Interaction With The Zona Pellucida.
DR   GenomeRNAi; 8748; -.
DR   PRO; PR:O43506; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   Bgee; ENSG00000134007; Expressed in 31 organ(s), highest expression level in sperm.
DR   Genevisible; O43506; HS.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008237; F:metallopeptidase activity; TAS:ProtInc.
DR   GO; GO:0007339; P:binding of sperm to zona pellucida; TAS:Reactome.
DR   GO; GO:0007338; P:single fertilization; TAS:ProtInc.
DR   CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR   Gene3D; 3.40.390.10; -; 1.
DR   Gene3D; 4.10.70.10; -; 1.
DR   InterPro; IPR006586; ADAM_Cys-rich.
DR   InterPro; IPR018358; Disintegrin_CS.
DR   InterPro; IPR001762; Disintegrin_dom.
DR   InterPro; IPR036436; Disintegrin_dom_sf.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   InterPro; IPR002870; Peptidase_M12B_N.
DR   InterPro; IPR034027; Reprolysin_adamalysin.
DR   Pfam; PF08516; ADAM_CR; 1.
DR   Pfam; PF00200; Disintegrin; 1.
DR   Pfam; PF01562; Pep_M12B_propep; 1.
DR   Pfam; PF01421; Reprolysin; 1.
DR   PRINTS; PR00289; DISINTEGRIN.
DR   SMART; SM00608; ACR; 1.
DR   SMART; SM00050; DISIN; 1.
DR   SUPFAM; SSF57552; SSF57552; 1.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS00427; DISINTEGRIN_1; 1.
DR   PROSITE; PS50214; DISINTEGRIN_2; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Disulfide bond; EGF-like domain; Glycoprotein;
KW   Hydrolase; Membrane; Metal-binding; Metalloprotease; Protease;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix; Zinc;
KW   Zymogen.
FT   SIGNAL        1     31       {ECO:0000255}.
FT   PROPEP       32    206       {ECO:0000255}.
FT                                /FTId=PRO_0000029106.
FT   CHAIN       207    726       Disintegrin and metalloproteinase domain-
FT                                containing protein 20.
FT                                /FTId=PRO_0000029107.
FT   TOPO_DOM    207    693       Extracellular. {ECO:0000255}.
FT   TRANSMEM    694    714       Helical. {ECO:0000255}.
FT   TOPO_DOM    715    726       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      207    400       Peptidase M12B. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00276}.
FT   DOMAIN      407    493       Disintegrin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00068}.
FT   DOMAIN      635    663       EGF-like.
FT   MOTIF       171    178       Cysteine switch. {ECO:0000250}.
FT   COMPBIAS    494    634       Cys-rich.
FT   ACT_SITE    343    343       {ECO:0000255|PROSITE-ProRule:PRU00276,
FT                                ECO:0000255|PROSITE-ProRule:PRU10095}.
FT   METAL       173    173       Zinc; in inhibited form. {ECO:0000250}.
FT   METAL       342    342       Zinc; catalytic. {ECO:0000255}.
FT   METAL       346    346       Zinc; catalytic. {ECO:0000255}.
FT   METAL       352    352       Zinc; catalytic. {ECO:0000255}.
FT   CARBOHYD    191    191       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    226    226       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    378    378       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    438    438       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    479    479       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    587    587       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    317    394       {ECO:0000250}.
FT   DISULFID    357    379       {ECO:0000250}.
FT   DISULFID    359    364       {ECO:0000250}.
FT   DISULFID    465    485       {ECO:0000250}.
FT   DISULFID    635    646       {ECO:0000250}.
FT   DISULFID    640    652       {ECO:0000250}.
FT   DISULFID    654    663       {ECO:0000250}.
FT   VARIANT      19     19       F -> L (in dbSNP:rs1059166).
FT                                {ECO:0000269|PubMed:9469942}.
FT                                /FTId=VAR_047311.
FT   CONFLICT    109    109       C -> W (in Ref. 1; AAC52041).
FT                                {ECO:0000305}.
FT   CONFLICT    637    637       P -> R (in Ref. 1; AAC52041).
FT                                {ECO:0000305}.
SQ   SEQUENCE   726 AA;  81603 MW;  7DB864FA1796A9B0 CRC64;
     MAVGEPLVHI RVTLLLLWFG MFLSISGHSQ ARPSQYFTSP EVVIPLKVIS RGRGAKAPGW
     LSYSLRFGGQ RYIVHMRVNK LLFAAHLPVF TYTEQHALLQ DQPFIQDDCY YHGYVEGVPE
     SLVALSTCSG GFLGMLQIND LVYEIKPISV SATFEHLVYK IDSDDTQFPP MRCGLTEEKI
     AHQMELQLSY NFTLKQSSFV GWWTHQRFVE LVVVVDNIRY LFSQSNATTV QHEVFNVVNI
     VDSFYHPLEV DVILTGIDIW TASNPLPTSG DLDNVLEDFS IWKNYNLNNR LQHDVAHLFI
     KDTQGMKLGV AYVKGICQNP FNTGVDVFED NRLVVFAITL GHELGHNLGM QHDTQWCVCE
     LQWCIMHAYR KVTTKFSNCS YAQYWDSTIS SGLCIQPPPY PGNIFRLKYC GNLVVEEGEE
     CDCGTIRQCA KDPCCLLNCT LHPGAACAFG ICCKDCKFLP SGTLCRQQVG ECDLPEWCNG
     TSHQCPDDVY VQDGISCNVN AFCYEKTCNN HDIQCKEIFG QDARSASQSC YQEINTQGNR
     FGHCGIVGTT YVKCWTPDIM CGRVQCENVG VIPNLIEHST VQQFHLNDTT CWGTDYHLGM
     AIPDIGEVKD GTVCGPEKIC IRKKCASMVH LSQACQPKTC NMRGICNNKQ HCHCNHEWAP
     PYCKDKGYGG SADSGPPPKN NMEGLNVMGK LRYLSLLCLL PLVAFLLFCL HVLFKKRTKS
     KEDEEG
//
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