(data stored in ACNUC30567 zone)

HOGENOM: HS14_PE955

ID   HS14_PE955                           STANDARD;      PRT;   776 AA.
AC   HS14_PE955; O43506; Q6GTZ1; Q9UKJ9;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Disintegrin and metalloproteinase domain-containing protein
DE   20; Short=ADAM 20; EC=3.4.24 -;Flags: Precursor; (HS14.PE955).
GN   Name=ADAM20;
OS   HOMO SAPIENS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Primates; Haplorrhini; Simiiformes; Catarrhini;
OC   Hominoidea; Hominidae; Homininae; Homo.
OX   NCBI_TaxID=9606;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS HS14.PE955.
CC       Homo sapiens chromosome 14 GRCh37  sequence 1..107289540 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:ADA20_HUMAN
CC   -!- FUNCTION: May be involved in sperm maturation and/or
CC       fertilization.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (Potential).
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   -!- SIMILARITY: Contains 1 disintegrin domain.
CC   -!- SIMILARITY: Contains 1 EGF-like domain.
CC   -!- SIMILARITY: Contains 1 peptidase M12B domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH25378.2; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC       Sequence=AAH25378.2; Type=Erroneous initiation;
CC       Sequence=EAW81037.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC   -!- GENE_FAMILY: HOG000230883 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Homo_sapiens;ENSG00000134007;ENST00000256389;ENSP00000256389.
DR   EMBL; AF029899; - ;
DR   EMBL; AF158643; - ;
DR   EMBL; AL357153; - ;
DR   EMBL; BC025378; - ;
DR   EMBL; CH471061; - ;
DR   UniProtKB/Swiss-Prot; O43506; Q6GTZ1; Q9UKJ9; -.
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   IPI; IPI00306205; -.
DR   RefSeq; NP_003805.3; NM_003814.4.
DR   UniGene; Hs.177984; -.
DR   ProteinModelPortal; O43506; -.
DR   SMR; O43506; 202-670.
DR   STRING; O43506; -.
DR   MEROPS; M12.218; -.
DR   PRIDE; O43506; -.
DR   Ensembl; ENST00000256389; ENSP00000256389; ENSG00000134007.
DR   GeneID; 8748; -.
DR   KEGG; hsa:8748; -.
DR   CTD; 8748; -.
DR   GeneCards; GC14M051157; -.
DR   H-InvDB; HIX0202085; -.
DR   HGNC; HGNC:199; ADAM20.
DR   MIM; 603712; gene.
DR   neXtProt; NX_O43506; -.
DR   PharmGKB; PA24516; -.
DR   eggNOG; prNOG15722; -.
DR   GeneTree; ENSGT00590000082741; -.
DR   InParanoid; O43506; -.
DR   OrthoDB; EOG4XWFX8; -.
DR   PhylomeDB; O43506; -.
DR   ArrayExpress; O43506; -.
DR   Bgee; O43506; -.
DR   CleanEx; HS_ADAM20; -.
DR   Genevestigator; O43506; -.
DR   GermOnline; ENSG00000134007; Homo sapiens.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   GO; GO:0007338; P:single fertilization; TAS:ProtInc.
DR   InterPro; IPR006586; ADAM_Cys-rich.
DR   InterPro; IPR001762; Blood-coag_inhib_Disintegrin.
DR   InterPro; IPR018358; Disintegrin_CS.
DR   InterPro; IPR024079; MetalloPept_cat_dom.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   InterPro; IPR002870; Peptidase_M12B_N.
DR   Gene3D; G3DSA:4.10.70.10; Blood-coag_inhib_Disintegrin; 1.
DR   Gene3D; G3DSA:3.40.390.10; G3DSA:3.40.390.10; 1.
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; Disintegrin; 1.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS00546; CYSTEINE_SWITCH; FALSE_NEG.
DR   PROSITE; PS00427; DISINTEGRIN_1; 1.
DR   PROSITE; PS50214; DISINTEGRIN_2; 1.
DR   PROSITE; PS00022; EGF_1; FALSE_NEG.
DR   PROSITE; PS01186; EGF_2; FALSE_NEG.
DR   PROSITE; PS50026; EGF_3; FALSE_NEG.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
DR   HOGENOMDNA; HS14.PE955; -.
KW   ENSG000001340071755old_1320000031; ENSP000002563897901old_1320000031;
KW   AF029899; AF158643; AL357153; BC025378; CH471061;
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.
SQ   SEQUENCE   776 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MVQLHQDTDP QIPKGQPCTL NSSEGGARPA VPHTLFSSAL DRWLHNDSFI 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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