GenomeNet

Database: UniProt
Entry: Q9UKQ2
LinkDB: Q9UKQ2
Original site: Q9UKQ2 
ID   ADA28_HUMAN             Reviewed;         775 AA.
AC   Q9UKQ2; B2RMV5; Q9Y339; Q9Y3S0;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 3.
DT   13-FEB-2019, entry version 174.
DE   RecName: Full=Disintegrin and metalloproteinase domain-containing protein 28;
DE            Short=ADAM 28;
DE            EC=3.4.24.-;
DE   AltName: Full=Epididymal metalloproteinase-like, disintegrin-like, and cysteine-rich protein II;
DE            Short=eMDC II;
DE   AltName: Full=Metalloproteinase-like, disintegrin-like, and cysteine-rich protein L;
DE            Short=MDC-L;
DE   Flags: Precursor;
GN   Name=ADAM28; Synonyms=ADAM23, MDCL;
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] (ISOFORMS 1 AND 2), AND VARIANT MET-765.
RC   TISSUE=Lymph node;
RX   PubMed=10506182; DOI=10.1074/jbc.274.41.29251;
RA   Roberts C.M., Tani P.H., Bridges L.C., Laszik Z., Bowditch R.D.;
RT   "MDC-L, a novel metalloprotease disintegrin cysteine-rich protein
RT   family member expressed by human lymphocytes.";
RL   J. Biol. Chem. 274:29251-29259(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT MET-765.
RC   TISSUE=Epididymis;
RX   PubMed=10587367; DOI=10.1093/molehr/5.12.1127;
RA   Jury J.A., Perry A.C., Hall L.;
RT   "Identification, sequence analysis and expression of transcripts
RT   encoding a putative metalloproteinase, eMDC II, in human and macaque
RT   epididymis.";
RL   Mol. Hum. Reprod. 5:1127-1134(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16421571; DOI=10.1038/nature04406;
RA   Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
RA   Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
RA   Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA   Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
RA   Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
RA   DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
RA   Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
RA   Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA   Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA   Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
RA   O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
RA   Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
RA   Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
RA   Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
RA   Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
RA   Lander E.S.;
RT   "DNA sequence and analysis of human chromosome 8.";
RL   Nature 439:331-335(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT MET-765.
RA   Mural R.J., Istrail S., Sutton 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT MET-765.
RC   TISSUE=Brain;
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   [6]
RP   VARIANTS GLU-65; GLU-134; GLU-450; PHE-482 AND ASP-502.
RX   PubMed=21618342; DOI=10.1002/humu.21477;
RA   Wei X., Moncada-Pazos A., Cal S., Soria-Valles C., Gartner J.,
RA   Rudloff U., Lin J.C., Rosenberg S.A., Lopez-Otin C., Samuels Y.;
RT   "Analysis of the disintegrin-metalloproteinases family reveals ADAM29
RT   and ADAM7 are often mutated in melanoma.";
RL   Hum. Mutat. 32:E2148-E2175(2011).
CC   -!- FUNCTION: May play a role in the adhesive and proteolytic events
CC       that occur during lymphocyte emigration or may function in
CC       ectodomain shedding of lymphocyte surface target proteins, such as
CC       FASL and CD40L. May be involved in sperm maturation.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I
CC       membrane protein.
CC   -!- SUBCELLULAR LOCATION: Isoform 2: Secreted.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=MDC-LM;
CC         IsoId=Q9UKQ2-1; Sequence=Displayed;
CC       Name=2; Synonyms=MDC-LS;
CC         IsoId=Q9UKQ2-2; Sequence=VSP_005486, VSP_005487;
CC   -!- TISSUE SPECIFICITY: Expressed predominantly in secondary lymphoid
CC       tissues, such as lymph node, spleen, small intestine, stomach,
CC       colon, appendix and trachea. The lymphocyte population is
CC       responsible for expression of this protein in these tissues.
CC       Isoform 2 is expressed preferentially in spleen.
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: Pro-domain removal and maturation may be, at least in part,
CC       autocatalytic. {ECO:0000250}.
DR   EMBL; AF137334; AAD25099.1; -; mRNA.
DR   EMBL; AF137335; AAD25100.1; -; mRNA.
DR   EMBL; AJ242015; CAB42085.1; -; mRNA.
DR   EMBL; AC044891; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC120193; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471080; EAW63609.1; -; Genomic_DNA.
DR   EMBL; BC136478; AAI36479.1; -; mRNA.
DR   CCDS; CCDS34865.1; -. [Q9UKQ2-1]
DR   CCDS; CCDS47830.1; -. [Q9UKQ2-2]
DR   RefSeq; NP_001291280.1; NM_001304351.1.
DR   RefSeq; NP_055080.2; NM_014265.5. [Q9UKQ2-1]
DR   RefSeq; NP_068547.2; NM_021777.4. [Q9UKQ2-2]
DR   UniGene; Hs.174030; -.
DR   UniGene; Hs.388903; -.
DR   ProteinModelPortal; Q9UKQ2; -.
DR   SMR; Q9UKQ2; -.
DR   BioGrid; 116072; 1.
DR   IntAct; Q9UKQ2; 1.
DR   STRING; 9606.ENSP00000265769; -.
DR   DrugBank; DB02996; 2-(Thiomethylene)-4-Methylpentanoic Acid.
DR   DrugBank; DB03880; Batimastat.
DR   DrugBank; DB02215; Furoyl-Leucine.
DR   DrugBank; DB02255; GM6001.
DR   DrugBank; DB02046; N-[(Furan-2-Yl)Carbonyl]-(S)-Leucyl-(R)-[1-Amino-2(1h-Indol-3-Yl)Ethyl]-Phosphonic Acid.
DR   DrugBank; DB03088; Pyroglutamic Acid.
DR   MEROPS; M12.224; -.
DR   TCDB; 8.A.77.1.3; the sheddase (sheddase) family.
DR   iPTMnet; Q9UKQ2; -.
DR   PhosphoSitePlus; Q9UKQ2; -.
DR   BioMuta; ADAM28; -.
DR   DMDM; 317373485; -.
DR   jPOST; Q9UKQ2; -.
DR   PaxDb; Q9UKQ2; -.
DR   PeptideAtlas; Q9UKQ2; -.
DR   PRIDE; Q9UKQ2; -.
DR   ProteomicsDB; 84834; -.
DR   ProteomicsDB; 84835; -. [Q9UKQ2-2]
DR   Ensembl; ENST00000265769; ENSP00000265769; ENSG00000042980. [Q9UKQ2-1]
DR   Ensembl; ENST00000437154; ENSP00000393699; ENSG00000042980. [Q9UKQ2-2]
DR   GeneID; 10863; -.
DR   KEGG; hsa:10863; -.
DR   UCSC; uc003xdx.4; human. [Q9UKQ2-1]
DR   CTD; 10863; -.
DR   DisGeNET; 10863; -.
DR   EuPathDB; HostDB:ENSG00000042980.12; -.
DR   GeneCards; ADAM28; -.
DR   H-InvDB; HIX0034262; -.
DR   HGNC; HGNC:206; ADAM28.
DR   HPA; HPA074034; -.
DR   MIM; 606188; gene.
DR   neXtProt; NX_Q9UKQ2; -.
DR   OpenTargets; ENSG00000042980; -.
DR   PharmGKB; PA24523; -.
DR   eggNOG; KOG3607; Eukaryota.
DR   eggNOG; ENOG410XX2M; LUCA.
DR   GeneTree; ENSGT00940000156716; -.
DR   HOGENOM; HOG000230883; -.
DR   HOVERGEN; HBG006978; -.
DR   InParanoid; Q9UKQ2; -.
DR   KO; K08614; -.
DR   OMA; YYQGHII; -.
DR   OrthoDB; 162519at2759; -.
DR   PhylomeDB; Q9UKQ2; -.
DR   TreeFam; TF314733; -.
DR   ChiTaRS; ADAM28; human.
DR   GeneWiki; ADAM28; -.
DR   GenomeRNAi; 10863; -.
DR   PRO; PR:Q9UKQ2; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   Bgee; ENSG00000042980; Expressed in 181 organ(s), highest expression level in caput epididymis.
DR   ExpressionAtlas; Q9UKQ2; baseline and differential.
DR   Genevisible; Q9UKQ2; HS.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
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; IDA:BHF-UCL.
DR   GO; GO:0007283; P:spermatogenesis; 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; IPR000742; EGF-like_dom.
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; PS50026; EGF_3; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell membrane;
KW   Cleavage on pair of basic residues; Complete proteome; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Hydrolase; Membrane; Metal-binding;
KW   Metalloprotease; Polymorphism; Protease; Reference proteome; Secreted;
KW   Signal; Transmembrane; Transmembrane helix; Zinc; Zymogen.
FT   SIGNAL        1     18       {ECO:0000255}.
FT   PROPEP       19    198       {ECO:0000250}.
FT                                /FTId=PRO_0000029128.
FT   CHAIN       199    775       Disintegrin and metalloproteinase domain-
FT                                containing protein 28.
FT                                /FTId=PRO_0000029129.
FT   TOPO_DOM    199    665       Extracellular. {ECO:0000255}.
FT   TRANSMEM    666    686       Helical. {ECO:0000255}.
FT   TOPO_DOM    687    775       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      204    399       Peptidase M12B. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00276}.
FT   DOMAIN      407    493       Disintegrin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00068}.
FT   DOMAIN      625    657       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   MOTIF       167    174       Cysteine switch. {ECO:0000250}.
FT   COMPBIAS    494    628       Cys-rich.
FT   ACT_SITE    340    340       {ECO:0000255|PROSITE-ProRule:PRU00276,
FT                                ECO:0000255|PROSITE-ProRule:PRU10095}.
FT   METAL       169    169       Zinc; in inhibited form. {ECO:0000250}.
FT   METAL       339    339       Zinc; catalytic. {ECO:0000250}.
FT   METAL       343    343       Zinc; catalytic. {ECO:0000250}.
FT   METAL       349    349       Zinc; catalytic. {ECO:0000250}.
FT   CARBOHYD    268    268       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    275    275       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    557    557       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    602    602       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    628    628       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    315    394       {ECO:0000250}.
FT   DISULFID    354    378       {ECO:0000250}.
FT   DISULFID    356    361       {ECO:0000250}.
FT   DISULFID    465    485       {ECO:0000250}.
FT   DISULFID    629    639       {ECO:0000250}.
FT   DISULFID    633    645       {ECO:0000250}.
FT   DISULFID    647    656       {ECO:0000250}.
FT   VAR_SEQ     524    540       TEVADKSCYNRNEGGSK -> RRTNPFPCACAKENHFR
FT                                (in isoform 2).
FT                                {ECO:0000303|PubMed:10506182}.
FT                                /FTId=VSP_005486.
FT   VAR_SEQ     541    775       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:10506182}.
FT                                /FTId=VSP_005487.
FT   VARIANT      65     65       G -> E (in a cutaneous metastatic
FT                                melanoma sample; somatic mutation).
FT                                {ECO:0000269|PubMed:21618342}.
FT                                /FTId=VAR_066317.
FT   VARIANT     134    134       G -> E (in a cutaneous metastatic
FT                                melanoma sample; somatic mutation;
FT                                dbSNP:rs267601860).
FT                                {ECO:0000269|PubMed:21618342}.
FT                                /FTId=VAR_066318.
FT   VARIANT     219    219       R -> M (in dbSNP:rs9314282).
FT                                /FTId=VAR_057067.
FT   VARIANT     226    226       E -> D (in dbSNP:rs17736699).
FT                                /FTId=VAR_057068.
FT   VARIANT     450    450       G -> E (in a cutaneous metastatic
FT                                melanoma sample; somatic mutation;
FT                                dbSNP:rs267601862).
FT                                {ECO:0000269|PubMed:21618342}.
FT                                /FTId=VAR_066319.
FT   VARIANT     482    482       S -> F (in a cutaneous metastatic
FT                                melanoma sample; somatic mutation).
FT                                {ECO:0000269|PubMed:21618342}.
FT                                /FTId=VAR_066320.
FT   VARIANT     493    493       N -> S (in dbSNP:rs7001647).
FT                                /FTId=VAR_057069.
FT   VARIANT     502    502       G -> D (in a cutaneous metastatic
FT                                melanoma sample; somatic mutation;
FT                                dbSNP:rs267601864).
FT                                {ECO:0000269|PubMed:21618342}.
FT                                /FTId=VAR_066321.
FT   VARIANT     593    593       T -> K (in dbSNP:rs36041430).
FT                                /FTId=VAR_057070.
FT   VARIANT     604    604       T -> P (in dbSNP:rs35617826).
FT                                /FTId=VAR_057071.
FT   VARIANT     684    684       M -> I (in dbSNP:rs7829965).
FT                                /FTId=VAR_057072.
FT   VARIANT     765    765       V -> M (in dbSNP:rs7814768).
FT                                {ECO:0000269|PubMed:10506182,
FT                                ECO:0000269|PubMed:10587367,
FT                                ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|Ref.4}.
FT                                /FTId=VAR_024596.
FT   CONFLICT    513    513       Q -> R (in Ref. 1; AAD25099/AAD25100).
FT                                {ECO:0000305}.
FT   CONFLICT    774    774       K -> E (in Ref. 1; AAD25099).
FT                                {ECO:0000305}.
SQ   SEQUENCE   775 AA;  87148 MW;  895E0985840F971C CRC64;
     MLQGLLPVSL LLSVAVSAIK ELPGVKKYEV VYPIRLHPLH KREAKEPEQQ EQFETELKYK
     MTINGKIAVL YLKKNKNLLA PGYTETYYNS TGKEITTSPQ IMDDCYYQGH ILNEKVSDAS
     ISTCRGLRGY FSQGDQRYFI EPLSPIHRDG QEHALFKYNP DEKNYDSTCG MDGVLWAHDL
     QQNIALPATK LVKLKDRKVQ EHEKYIEYYL VLDNGEFKRY NENQDEIRKR VFEMANYVNM
     LYKKLNTHVA LVGMEIWTDK DKIKITPNAS FTLENFSKWR GSVLSRRKRH DIAQLITATE
     LAGTTVGLAF MSTMCSPYSV GVVQDHSDNL LRVAGTMAHE MGHNFGMFHD DYSCKCPSTI
     CVMDKALSFY IPTDFSSCSR LSYDKFFEDK LSNCLFNAPL PTDIISTPIC GNQLVEMGED
     CDCGTSEECT NICCDAKTCK IKATFQCALG ECCEKCQFKK AGMVCRPAKD ECDLPEMCNG
     KSGNCPDDRF QVNGFPCHHG KGHCLMGTCP TLQEQCTELW GPGTEVADKS CYNRNEGGSK
     YGYCRRVDDT LIPCKANDTM CGKLFCQGGS DNLPWKGRIV TFLTCKTFDP EDTSQEIGMV
     ANGTKCGDNK VCINAECVDI EKAYKSTNCS SKCKGHAVCD HELQCQCEEG WIPPDCDDSS
     VVFHFSIVVG VLFPMAVIFV VVAMVIRHQS SREKQKKDQR PLSTTGTRPH KQKRKPQMVK
     AVQPQEMSQM KPHVYDLPVE GNEPPASFHK DTNALPPTVF KDNPVSTPKD SNPKA
//
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