ADA20_HUMAN
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 03-AUG-2022, entry version 188.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 metalloproteases
RT 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) genes
RT 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., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., 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., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: May be involved in sperm maturation and/or 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 protein.
CC -!- TISSUE SPECIFICITY: Testis specific.
CC -!- DOMAIN: A tripeptide motif (VGE) within disintegrin-like domain could
CC be involved in the binding to egg integrin receptor and thus could
CC mediate sperm/egg binding.
CC -!- DOMAIN: The cysteine-rich domain encodes putative cell-fusion peptides,
CC which could be involved in sperm-egg fusion.
CC -!- DOMAIN: The conserved cysteine present in the cysteine-switch motif
CC binds the catalytic zinc ion, thus inhibiting the enzyme. The
CC dissociation of the cysteine from the zinc ion upon the activation-
CC peptide release activates the enzyme.
CC -!- PTM: Has no obvious cleavage site for furin endopeptidase, suggesting
CC 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=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH25378.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=EAW81037.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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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 AlphaFoldDB; O43506; -.
DR SMR; O43506; -.
DR BioGRID; 114284; 1.
DR IntAct; O43506; 1.
DR MINT; O43506; -.
DR STRING; 9606.ENSP00000256389; -.
DR MEROPS; M12.218; -.
DR GlyGen; O43506; 6 sites.
DR iPTMnet; O43506; -.
DR PhosphoSitePlus; O43506; -.
DR BioMuta; ADAM20; -.
DR MassIVE; O43506; -.
DR PaxDb; O43506; -.
DR PeptideAtlas; O43506; -.
DR PRIDE; O43506; -.
DR Antibodypedia; 25132; 174 antibodies from 24 providers.
DR DNASU; 8748; -.
DR Ensembl; ENST00000256389.5; ENSP00000256389.3; ENSG00000134007.5.
DR GeneID; 8748; -.
DR KEGG; hsa:8748; -.
DR MANE-Select; ENST00000256389.5; ENSP00000256389.3; NM_003814.5; NP_003805.4.
DR UCSC; uc001xme.4; human.
DR CTD; 8748; -.
DR DisGeNET; 8748; -.
DR GeneCards; ADAM20; -.
DR HGNC; HGNC:199; ADAM20.
DR HPA; ENSG00000134007; Group enriched (brain, testis).
DR MIM; 603712; gene.
DR neXtProt; NX_O43506; -.
DR OpenTargets; ENSG00000134007; -.
DR PharmGKB; PA24516; -.
DR VEuPathDB; HostDB:ENSG00000134007; -.
DR eggNOG; KOG3607; Eukaryota.
DR GeneTree; ENSGT00940000161067; -.
DR HOGENOM; CLU_012714_4_0_1; -.
DR InParanoid; O43506; -.
DR OrthoDB; 162519at2759; -.
DR PhylomeDB; O43506; -.
DR TreeFam; TF314733; -.
DR PathwayCommons; O43506; -.
DR Reactome; R-HSA-2534343; Interaction With Cumulus Cells And The Zona Pellucida.
DR SignaLink; O43506; -.
DR BioGRID-ORCS; 8748; 8 hits in 1064 CRISPR screens.
DR ChiTaRS; ADAM20; human.
DR GenomeRNAi; 8748; -.
DR Pharos; O43506; Tdark.
DR PRO; PR:O43506; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; O43506; protein.
DR Bgee; ENSG00000134007; Expressed in sperm and 35 other tissues.
DR ExpressionAtlas; O43506; baseline and differential.
DR Genevisible; O43506; HS.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:1990913; C:sperm head plasma membrane; IBA:GO_Central.
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:0008584; P:male gonad development; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 Disulfide bond; EGF-like domain; Glycoprotein; Hydrolase; Membrane;
KW Metal-binding; Metalloprotease; Protease; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Zinc; Zymogen.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT PROPEP 32..206
FT /evidence="ECO:0000255"
FT /id="PRO_0000029106"
FT CHAIN 207..726
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein 20"
FT /id="PRO_0000029107"
FT TOPO_DOM 207..693
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 694..714
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 715..726
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 207..400
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 407..493
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DOMAIN 635..663
FT /note="EGF-like"
FT MOTIF 171..178
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT ACT_SITE 343
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /note="in inhibited form"
FT /evidence="ECO:0000250"
FT BINDING 342
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255"
FT BINDING 346
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255"
FT BINDING 352
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 378
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 438
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 479
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 587
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 317..394
FT /evidence="ECO:0000250"
FT DISULFID 357..379
FT /evidence="ECO:0000250"
FT DISULFID 359..364
FT /evidence="ECO:0000250"
FT DISULFID 465..485
FT /evidence="ECO:0000250"
FT DISULFID 635..646
FT /evidence="ECO:0000250"
FT DISULFID 640..652
FT /evidence="ECO:0000250"
FT DISULFID 654..663
FT /evidence="ECO:0000250"
FT VARIANT 19
FT /note="F -> L (in dbSNP:rs1059166)"
FT /evidence="ECO:0000269|PubMed:9469942"
FT /id="VAR_047311"
FT CONFLICT 109
FT /note="C -> W (in Ref. 1; AAC52041)"
FT /evidence="ECO:0000305"
FT CONFLICT 637
FT /note="P -> R (in Ref. 1; AAC52041)"
FT /evidence="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
