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Disintegrin and metalloproteinase domain-containing protein 28 (ADAM 28) (EC 3.4.24.-) (Epididymal metalloproteinase-like, disintegrin-like, and cysteine-rich protein II) (eMDC II)

 ADA28_MACFA             Reviewed;         776 AA.
Q9XSL6;
20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
25-OCT-2017, entry version 98.
RecName: Full=Disintegrin and metalloproteinase domain-containing protein 28;
Short=ADAM 28;
EC=3.4.24.-;
AltName: Full=Epididymal metalloproteinase-like, disintegrin-like, and cysteine-rich protein II;
Short=eMDC II;
Flags: Precursor;
Name=ADAM28;
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
NCBI_TaxID=9541;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Epididymis;
PubMed=10587367; DOI=10.1093/molehr/5.12.1127;
Jury J.A., Perry A.C., Hall L.;
"Identification, sequence analysis and expression of transcripts
encoding a putative metalloproteinase, eMDC II, in human and macaque
epididymis.";
Mol. Hum. Reprod. 5:1127-1134(1999).
-!- FUNCTION: May play a role in the adhesive and proteolytic events
that occur during lymphocyte emigration or may function in
ectodomain shedding of lymphocyte surface target proteins, such as
FASL and CD40L. May be involved in sperm maturation.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- TISSUE SPECIFICITY: Expressed at high levels in epididymis and at
lower levels in lung.
-!- DOMAIN: The conserved cysteine present in the cysteine-switch
motif binds the catalytic zinc ion, thus inhibiting the enzyme.
The dissociation of the cysteine from the zinc ion upon the
activation-peptide release activates the enzyme.
-!- PTM: Pro-domain removal and maturation may be, at least in part,
autocatalytic. {ECO:0000250}.
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EMBL; AJ242014; CAB42090.1; -; mRNA.
RefSeq; NP_001306280.1; NM_001319351.1.
UniGene; Mfa.6649; -.
ProteinModelPortal; Q9XSL6; -.
SMR; Q9XSL6; -.
MEROPS; M12.224; -.
PRIDE; Q9XSL6; -.
GeneID; 102143721; -.
KEGG; mcf:102143721; -.
CTD; 10863; -.
HOVERGEN; HBG006978; -.
KO; K08614; -.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
CDD; cd04269; ZnMc_adamalysin_II_like; 1.
Gene3D; 3.40.390.10; -; 1.
Gene3D; 4.10.70.10; -; 1.
InterPro; IPR006586; ADAM_Cys-rich.
InterPro; IPR018358; Disintegrin_CS.
InterPro; IPR001762; Disintegrin_dom.
InterPro; IPR036436; Disintegrin_dom_sf.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR024079; MetalloPept_cat_dom.
InterPro; IPR001590; Peptidase_M12B.
InterPro; IPR002870; Peptidase_M12B_N.
InterPro; IPR034027; Reprolysin_adamalysin.
Pfam; PF08516; ADAM_CR; 1.
Pfam; PF00200; Disintegrin; 1.
Pfam; PF01562; Pep_M12B_propep; 1.
Pfam; PF01421; Reprolysin; 1.
PRINTS; PR00289; DISINTEGRIN.
SMART; SM00608; ACR; 1.
SMART; SM00050; DISIN; 1.
SUPFAM; SSF57552; SSF57552; 1.
PROSITE; PS50215; ADAM_MEPRO; 1.
PROSITE; PS00427; DISINTEGRIN_1; 1.
PROSITE; PS50214; DISINTEGRIN_2; 1.
PROSITE; PS01186; EGF_2; 1.
PROSITE; PS50026; EGF_3; 1.
PROSITE; PS00142; ZINC_PROTEASE; 1.
2: Evidence at transcript level;
Disulfide bond; EGF-like domain; Glycoprotein; Hydrolase; Membrane;
Metal-binding; Metalloprotease; Protease; Signal; Transmembrane;
Transmembrane helix; Zinc; Zymogen.
SIGNAL 1 19 {ECO:0000255}.
PROPEP 20 193 {ECO:0000250}.
/FTId=PRO_0000029130.
CHAIN 194 776 Disintegrin and metalloproteinase domain-
containing protein 28.
/FTId=PRO_0000029131.
TOPO_DOM 194 666 Extracellular. {ECO:0000255}.
TRANSMEM 667 687 Helical. {ECO:0000255}.
TOPO_DOM 688 776 Cytoplasmic. {ECO:0000255}.
DOMAIN 204 400 Peptidase M12B. {ECO:0000255|PROSITE-
ProRule:PRU00276}.
DOMAIN 408 494 Disintegrin. {ECO:0000255|PROSITE-
ProRule:PRU00068}.
DOMAIN 626 658 EGF-like. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
MOTIF 168 175 Cysteine switch. {ECO:0000250}.
COMPBIAS 495 629 Cys-rich.
ACT_SITE 341 341 {ECO:0000255|PROSITE-ProRule:PRU00276,
ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 170 170 Zinc; in inhibited form. {ECO:0000250}.
METAL 340 340 Zinc; catalytic. {ECO:0000250}.
METAL 344 344 Zinc; catalytic. {ECO:0000250}.
METAL 350 350 Zinc; catalytic. {ECO:0000250}.
CARBOHYD 268 268 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 275 275 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 352 352 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 558 558 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 603 603 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 629 629 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 315 395 {ECO:0000250}.
DISULFID 355 379 {ECO:0000250}.
DISULFID 357 362 {ECO:0000250}.
DISULFID 466 486 {ECO:0000250}.
DISULFID 630 640 {ECO:0000250}.
DISULFID 634 646 {ECO:0000250}.
DISULFID 648 657 {ECO:0000250}.
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


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