GenomeNet

Database: UniProt
Entry: Q9UKJ8
LinkDB: Q9UKJ8
Original site: Q9UKJ8 
ID   ADA21_HUMAN             Reviewed;         722 AA.
AC   Q9UKJ8; O43507; Q2VPC6; Q32MR0;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 2.
DT   10-APR-2019, entry version 171.
DE   RecName: Full=Disintegrin and metalloproteinase domain-containing protein 21;
DE            Short=ADAM 21;
DE            EC=3.4.24.-;
DE   Flags: Precursor;
GN   Name=ADAM21;
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 [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   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 181-722.
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).
CC   -!- FUNCTION: May be involved in sperm maturation and/or
CC       fertilization. May also be involved in epithelia functions
CC       associated with establishing and maintaining gradients of ions or
CC       nutrients.
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   -!- 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.
DR   EMBL; AF158644; AAD55255.1; -; Genomic_DNA.
DR   EMBL; AL357153; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL391223; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC109024; AAI09025.1; -; mRNA.
DR   EMBL; BC109025; AAI09026.1; -; mRNA.
DR   EMBL; AF029900; AAC52042.1; -; mRNA.
DR   CCDS; CCDS9804.1; -.
DR   RefSeq; NP_003804.2; NM_003813.3.
DR   UniGene; Hs.178748; -.
DR   ProteinModelPortal; Q9UKJ8; -.
DR   SMR; Q9UKJ8; -.
DR   BioGrid; 114283; 32.
DR   IntAct; Q9UKJ8; 2.
DR   STRING; 9606.ENSP00000474385; -.
DR   MEROPS; M12.234; -.
DR   iPTMnet; Q9UKJ8; -.
DR   PhosphoSitePlus; Q9UKJ8; -.
DR   BioMuta; ADAM21; -.
DR   DMDM; 296434388; -.
DR   PaxDb; Q9UKJ8; -.
DR   PeptideAtlas; Q9UKJ8; -.
DR   PRIDE; Q9UKJ8; -.
DR   ProteomicsDB; 84810; -.
DR   Ensembl; ENST00000603540; ENSP00000474385; ENSG00000139985.
DR   GeneID; 8747; -.
DR   KEGG; hsa:8747; -.
DR   UCSC; uc001xmd.4; human.
DR   CTD; 8747; -.
DR   EuPathDB; HostDB:ENSG00000139985.6; -.
DR   GeneCards; ADAM21; -.
DR   H-InvDB; HIX0037649; -.
DR   HGNC; HGNC:200; ADAM21.
DR   HPA; HPA059016; -.
DR   MIM; 603713; gene.
DR   neXtProt; NX_Q9UKJ8; -.
DR   OpenTargets; ENSG00000139985; -.
DR   PharmGKB; PA24517; -.
DR   eggNOG; KOG3607; Eukaryota.
DR   eggNOG; ENOG410XX2M; LUCA.
DR   GeneTree; ENSGT00940000162712; -.
DR   HOGENOM; HOG000230883; -.
DR   HOVERGEN; HBG006978; -.
DR   InParanoid; Q9UKJ8; -.
DR   KO; K08610; -.
DR   OMA; GKICIHK; -.
DR   OrthoDB; 162519at2759; -.
DR   PhylomeDB; Q9UKJ8; -.
DR   TreeFam; TF314733; -.
DR   Reactome; R-HSA-1300644; Interaction With The Zona Pellucida.
DR   GenomeRNAi; 8747; -.
DR   PRO; PR:Q9UKJ8; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   Bgee; ENSG00000139985; Expressed in 64 organ(s), highest expression level in sperm.
DR   Genevisible; Q9UKJ8; HS.
DR   GO; GO:0030424; C:axon; IEA:Ensembl.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
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; IPR013032; EGF-like_CS.
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; PS01186; EGF_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    196       {ECO:0000255}.
FT                                /FTId=PRO_0000029108.
FT   CHAIN       197    722       Disintegrin and metalloproteinase domain-
FT                                containing protein 21.
FT                                /FTId=PRO_0000029109.
FT   TOPO_DOM    197    681       Extracellular. {ECO:0000255}.
FT   TRANSMEM    682    702       Helical. {ECO:0000255}.
FT   TOPO_DOM    703    722       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      208    398       Peptidase M12B. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00276}.
FT   DOMAIN      406    492       Disintegrin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00068}.
FT   DOMAIN      634    663       EGF-like.
FT   MOTIF       171    178       Cysteine switch. {ECO:0000250}.
FT   COMPBIAS    213    216       Poly-Val.
FT   COMPBIAS    493    633       Cys-rich.
FT   ACT_SITE    342    342       {ECO:0000255|PROSITE-ProRule:PRU00276,
FT                                ECO:0000255|PROSITE-ProRule:PRU10095}.
FT   METAL       173    173       Zinc; in inhibited form. {ECO:0000250}.
FT   METAL       341    341       Zinc; catalytic. {ECO:0000255}.
FT   METAL       345    345       Zinc; catalytic. {ECO:0000255}.
FT   METAL       351    351       Zinc; catalytic. {ECO:0000255}.
FT   CARBOHYD    164    164       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    227    227       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    377    377       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    437    437       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    478    478       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    546    546       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    600    600       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    316    393       {ECO:0000250}.
FT   DISULFID    356    378       {ECO:0000250}.
FT   DISULFID    358    363       {ECO:0000250}.
FT   DISULFID    464    484       {ECO:0000250}.
FT   DISULFID    634    645       {ECO:0000250}.
FT   DISULFID    639    651       {ECO:0000250}.
FT   DISULFID    653    662       {ECO:0000250}.
FT   CONFLICT     95     95       D -> E (in Ref. 1; AAD55255 and 3;
FT                                AAI09025/AAI09026). {ECO:0000305}.
FT   CONFLICT    117    117       A -> G (in Ref. 1; AAD55255 and 3;
FT                                AAI09025/AAI09026). {ECO:0000305}.
FT   CONFLICT    161    161       I -> V (in Ref. 1; AAD55255 and 3;
FT                                AAI09025/AAI09026). {ECO:0000305}.
FT   CONFLICT    181    181       A -> G (in Ref. 3; AAC52042).
FT                                {ECO:0000305}.
FT   CONFLICT    247    247       K -> Q (in Ref. 1; AAD55255 and 3;
FT                                AAI09025/AAI09026). {ECO:0000305}.
FT   CONFLICT    345    345       H -> Y (in Ref. 3; AAC52042).
FT                                {ECO:0000305}.
SQ   SEQUENCE   722 AA;  80834 MW;  4D18503812A6C02F CRC64;
     MAVDGTLVYI RVTLLLLWLG VFLSISGYCQ AGPSQHFTSP EVVIPLKVIS RGRSAKAPGW
     LSYSLRFGGQ KHVVHMRVKK LLVSRHLPVF TYTDDRALLE DQLFIPDDCY YHGYVEAAPE
     SLVVFSACFG GFRGVLKISG LTYEIEPIRH SATFEHLVYK INSNETQFPA MRCGLTEKEV
     ARQQLEFEEA ENSALEPKSA GDWWTHAWFL ELVVVVNHDF FIYSQSNISK VQEDVFLVVN
     IVDSMYKQLG TYIILIGIEI WNQGNVFPMT SIEQVLNDFS QWKQISLSQL QHDAAHMFIK
     NSLISILGLA YVAGICRPPI DCGVDNFQGD TWSLFANTVA HELGHTLGMQ HDEEFCFCGE
     RGCIMNTFRV PAEKFTNCSY ADFMKTTLNQ GSCLHNPPRL GEIFMLKRCG NGVVEREEQC
     DCGSVQQCEQ DACCLLNCTL RPGAACAFGL CCKDCKFMPS GELCRQEVNE CDLPEWCNGT
     SHQCPEDRYV QDGIPCSDSA YCYQKRCNNH DQHCREIFGK DAKSASQNCY KEINSQGNRF
     GHCGINGTTY LKCHISDVFC GRVQCENVRD IPLLQDHFTL QHTHINGVTC WGIDYHLRMN
     ISDIGEVKDG TVCGPGKICI HKKCVSLSVL SHVCLPETCN MKGICNNKHH CHCGYGWSPP
     YCQHRGYGGS IDSGPASAKR GVFLPLIVIP SLSVLTFLFT VGLLMYLRQC SGPKETKAHS
     SG
//
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