ADA28_MACFA
ID ADA28_MACFA Reviewed; 776 AA.
AC Q9XSL6;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 110.
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 Flags: Precursor;
GN Name=ADAM28;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 encoding a
RT putative metalloproteinase, eMDC II, in human and macaque epididymis.";
RL Mol. Hum. Reprod. 5:1127-1134(1999).
CC -!- FUNCTION: May play a role in the adhesive and proteolytic events that
CC occur during lymphocyte emigration or may function in ectodomain
CC shedding of lymphocyte surface target proteins, such as FASL and CD40L.
CC 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: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in epididymis and at lower
CC levels in lung.
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: Pro-domain removal and maturation may be, at least in part,
CC autocatalytic. {ECO:0000250}.
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DR EMBL; AJ242014; CAB42090.1; -; mRNA.
DR RefSeq; NP_001306280.1; NM_001319351.1.
DR AlphaFoldDB; Q9XSL6; -.
DR SMR; Q9XSL6; -.
DR STRING; 9541.XP_005562910.1; -.
DR MEROPS; M12.224; -.
DR GeneID; 102143721; -.
DR CTD; 10863; -.
DR eggNOG; KOG3607; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; 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 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..19
FT /evidence="ECO:0000255"
FT PROPEP 20..193
FT /evidence="ECO:0000250"
FT /id="PRO_0000029130"
FT CHAIN 194..776
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein 28"
FT /id="PRO_0000029131"
FT TOPO_DOM 194..666
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 667..687
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 688..776
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 204..400
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 408..494
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DOMAIN 626..658
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 691..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 746..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 168..175
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT COMPBIAS 691..705
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 341
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 170
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 340
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 344
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 350
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 558
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 603
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 629
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 315..395
FT /evidence="ECO:0000250"
FT DISULFID 355..379
FT /evidence="ECO:0000250"
FT DISULFID 357..362
FT /evidence="ECO:0000250"
FT DISULFID 466..486
FT /evidence="ECO:0000250"
FT DISULFID 630..640
FT /evidence="ECO:0000250"
FT DISULFID 634..646
FT /evidence="ECO:0000250"
FT DISULFID 648..657
FT /evidence="ECO:0000250"
SQ SEQUENCE 776 AA; 87214 MW; 08AAFE834B37F19F CRC64;
MLQALLTVSL LLSPVPVSAI KELPGVKKYE VVYPIRLHPL HKREVKEPEQ QEQFETELKY
KMTVNGKIAV LYLKKNKNLL APGYTETYYN STGKEITTSP QIMDDCYYQG HIINEKDSDA
SISTCRGLRG YFSQGNQRYF IEPLSPIHRD GQEHALFKYD PEEKNYDSTC GTDGVLWVHD
LQNIARPATR LVKLNDGKVQ KHEKYIEYYL VLDNGEFKKY NENQDEIRKR VFEMANYVNM
LYKKLNTHVA LVGMEIWTDE DKINITPNAS FTLENFSKWR GSVLPRRKRH DIAQLITATE
FAGMTVGLAF MSTMCSPYHS VGVVQDHSDN LLRVAGTMAH EMGHNFGMFH DNYSCKCPST
ICVMDKALSF YIPTDFSSCS RVSYDKFFED KLSNCLFNAP LPTDIISTPI CGNQMVEMGE
DCDCGTSEEC TNICCDAKTC KIKAGFQCTS GECCEKCQFK KAGMVCRPAK DECDLPEMCD
GKSGNCPDDR FRANGFPCHH GKGYCLMGAC PTLQEQCTEL WGPGTKVADQ SCYNRNEGGS
KYGYCRRVDD TLIPCKTNDT MCGKLFCQGG SDNLPWKGRI VTFLTCKTFD PEDTSEEIGM
VANGTKCGHN KVCINAECVD IEKAYKSTNC SSKCKGHAVC DHELQCQCEE GWSPPDCDDS
SVVFYFSIVV AVLFPVAVIS LVVAIVIRQQ SSREKQKKDQ RPLSTTGTRP HKQKRKPQMV
KAVQPQEMSQ MKLHVYDLPV EGNEPPASFL ISKPDFSPPP IPAPRSSSFL DSNPKA
