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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) (Metalloproteinase-like, disintegrin-like, and cysteine-rich protein L) (MDC-L)

 ADA28_HUMAN             Reviewed;         775 AA.
Q9UKQ2; B2RMV5; Q9Y339; Q9Y3S0;
20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 3.
22-NOV-2017, entry version 167.
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;
AltName: Full=Metalloproteinase-like, disintegrin-like, and cysteine-rich protein L;
Short=MDC-L;
Flags: Precursor;
Name=ADAM28; Synonyms=ADAM23, MDCL;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANT MET-765.
TISSUE=Lymph node;
PubMed=10506182; DOI=10.1074/jbc.274.41.29251;
Roberts C.M., Tani P.H., Bridges L.C., Laszik Z., Bowditch R.D.;
"MDC-L, a novel metalloprotease disintegrin cysteine-rich protein
family member expressed by human lymphocytes.";
J. Biol. Chem. 274:29251-29259(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT MET-765.
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16421571; DOI=10.1038/nature04406;
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT MET-765.
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT MET-765.
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
VARIANTS GLU-65; GLU-134; GLU-450; PHE-482 AND ASP-502.
PubMed=21618342; DOI=10.1002/humu.21477;
Wei X., Moncada-Pazos A., Cal S., Soria-Valles C., Gartner J.,
Rudloff U., Lin J.C., Rosenberg S.A., Lopez-Otin C., Samuels Y.;
"Analysis of the disintegrin-metalloproteinases family reveals ADAM29
and ADAM7 are often mutated in melanoma.";
Hum. Mutat. 32:E2148-E2175(2011).
-!- 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: Isoform 1: Cell membrane; Single-pass type I
membrane protein.
-!- SUBCELLULAR LOCATION: Isoform 2: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=MDC-LM;
IsoId=Q9UKQ2-1; Sequence=Displayed;
Name=2; Synonyms=MDC-LS;
IsoId=Q9UKQ2-2; Sequence=VSP_005486, VSP_005487;
-!- TISSUE SPECIFICITY: Expressed predominantly in secondary lymphoid
tissues, such as lymph node, spleen, small intestine, stomach,
colon, appendix and trachea. The lymphocyte population is
responsible for expression of this protein in these tissues.
Isoform 2 is expressed preferentially in spleen.
-!- 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; AF137334; AAD25099.1; -; mRNA.
EMBL; AF137335; AAD25100.1; -; mRNA.
EMBL; AJ242015; CAB42085.1; -; mRNA.
EMBL; AC044891; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC120193; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471080; EAW63609.1; -; Genomic_DNA.
EMBL; BC136478; AAI36479.1; -; mRNA.
CCDS; CCDS34865.1; -. [Q9UKQ2-1]
CCDS; CCDS47830.1; -. [Q9UKQ2-2]
RefSeq; NP_001291280.1; NM_001304351.1.
RefSeq; NP_055080.2; NM_014265.5. [Q9UKQ2-1]
RefSeq; NP_068547.2; NM_021777.4. [Q9UKQ2-2]
UniGene; Hs.174030; -.
UniGene; Hs.388903; -.
ProteinModelPortal; Q9UKQ2; -.
SMR; Q9UKQ2; -.
BioGrid; 116072; 1.
IntAct; Q9UKQ2; 1.
STRING; 9606.ENSP00000265769; -.
DrugBank; DB02996; 2-(Thiomethylene)-4-Methylpentanoic Acid.
DrugBank; DB03880; Batimastat.
DrugBank; DB02215; Furoyl-Leucine.
DrugBank; DB02255; GM6001.
DrugBank; DB02046; N-[(Furan-2-Yl)Carbonyl]-(S)-Leucyl-(R)-[1-Amino-2(1h-Indol-3-Yl)Ethyl]-Phosphonic Acid.
DrugBank; DB03088; Pyroglutamic Acid.
MEROPS; M12.224; -.
TCDB; 8.A.77.1.3; the sheddase (sheddase) family.
iPTMnet; Q9UKQ2; -.
PhosphoSitePlus; Q9UKQ2; -.
BioMuta; ADAM28; -.
DMDM; 317373485; -.
PaxDb; Q9UKQ2; -.
PeptideAtlas; Q9UKQ2; -.
PRIDE; Q9UKQ2; -.
Ensembl; ENST00000265769; ENSP00000265769; ENSG00000042980. [Q9UKQ2-1]
Ensembl; ENST00000437154; ENSP00000393699; ENSG00000042980. [Q9UKQ2-2]
GeneID; 10863; -.
KEGG; hsa:10863; -.
UCSC; uc003xdx.4; human. [Q9UKQ2-1]
CTD; 10863; -.
DisGeNET; 10863; -.
EuPathDB; HostDB:ENSG00000042980.12; -.
GeneCards; ADAM28; -.
H-InvDB; HIX0034262; -.
HGNC; HGNC:206; ADAM28.
HPA; HPA074034; -.
MIM; 606188; gene.
neXtProt; NX_Q9UKQ2; -.
OpenTargets; ENSG00000042980; -.
PharmGKB; PA24523; -.
eggNOG; KOG3607; Eukaryota.
eggNOG; ENOG410XX2M; LUCA.
GeneTree; ENSGT00760000118888; -.
HOGENOM; HOG000230883; -.
HOVERGEN; HBG006978; -.
InParanoid; Q9UKQ2; -.
KO; K08614; -.
OMA; TSPQIMD; -.
OrthoDB; EOG091G01NX; -.
PhylomeDB; Q9UKQ2; -.
TreeFam; TF314733; -.
ChiTaRS; ADAM28; human.
GeneWiki; ADAM28; -.
GenomeRNAi; 10863; -.
PRO; PR:Q9UKQ2; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000042980; -.
CleanEx; HS_ADAM23; -.
CleanEx; HS_ADAM28; -.
ExpressionAtlas; Q9UKQ2; baseline and differential.
Genevisible; Q9UKQ2; HS.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
GO; GO:0008237; F:metallopeptidase activity; IDA:BHF-UCL.
GO; GO:0007283; P:spermatogenesis; TAS:ProtInc.
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_sf.
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;
Alternative splicing; Cell membrane;
Cleavage on pair of basic residues; Complete proteome; Disulfide bond;
EGF-like domain; Glycoprotein; Hydrolase; Membrane; Metal-binding;
Metalloprotease; Polymorphism; Protease; Reference proteome; Secreted;
Signal; Transmembrane; Transmembrane helix; Zinc; Zymogen.
SIGNAL 1 18 {ECO:0000255}.
PROPEP 19 198 {ECO:0000250}.
/FTId=PRO_0000029128.
CHAIN 199 775 Disintegrin and metalloproteinase domain-
containing protein 28.
/FTId=PRO_0000029129.
TOPO_DOM 199 665 Extracellular. {ECO:0000255}.
TRANSMEM 666 686 Helical. {ECO:0000255}.
TOPO_DOM 687 775 Cytoplasmic. {ECO:0000255}.
DOMAIN 204 399 Peptidase M12B. {ECO:0000255|PROSITE-
ProRule:PRU00276}.
DOMAIN 407 493 Disintegrin. {ECO:0000255|PROSITE-
ProRule:PRU00068}.
DOMAIN 625 657 EGF-like. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
MOTIF 167 174 Cysteine switch. {ECO:0000250}.
COMPBIAS 494 628 Cys-rich.
ACT_SITE 340 340 {ECO:0000255|PROSITE-ProRule:PRU00276,
ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 169 169 Zinc; in inhibited form. {ECO:0000250}.
METAL 339 339 Zinc; catalytic. {ECO:0000250}.
METAL 343 343 Zinc; catalytic. {ECO:0000250}.
METAL 349 349 Zinc; catalytic. {ECO:0000250}.
CARBOHYD 268 268 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 275 275 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 557 557 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 602 602 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 628 628 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 315 394 {ECO:0000250}.
DISULFID 354 378 {ECO:0000250}.
DISULFID 356 361 {ECO:0000250}.
DISULFID 465 485 {ECO:0000250}.
DISULFID 629 639 {ECO:0000250}.
DISULFID 633 645 {ECO:0000250}.
DISULFID 647 656 {ECO:0000250}.
VAR_SEQ 524 540 TEVADKSCYNRNEGGSK -> RRTNPFPCACAKENHFR
(in isoform 2).
{ECO:0000303|PubMed:10506182}.
/FTId=VSP_005486.
VAR_SEQ 541 775 Missing (in isoform 2).
{ECO:0000303|PubMed:10506182}.
/FTId=VSP_005487.
VARIANT 65 65 G -> E (in a cutaneous metastatic
melanoma sample; somatic mutation).
{ECO:0000269|PubMed:21618342}.
/FTId=VAR_066317.
VARIANT 134 134 G -> E (in a cutaneous metastatic
melanoma sample; somatic mutation;
dbSNP:rs267601860).
{ECO:0000269|PubMed:21618342}.
/FTId=VAR_066318.
VARIANT 219 219 R -> M (in dbSNP:rs9314282).
/FTId=VAR_057067.
VARIANT 226 226 E -> D (in dbSNP:rs17736699).
/FTId=VAR_057068.
VARIANT 450 450 G -> E (in a cutaneous metastatic
melanoma sample; somatic mutation;
dbSNP:rs267601862).
{ECO:0000269|PubMed:21618342}.
/FTId=VAR_066319.
VARIANT 482 482 S -> F (in a cutaneous metastatic
melanoma sample; somatic mutation).
{ECO:0000269|PubMed:21618342}.
/FTId=VAR_066320.
VARIANT 493 493 N -> S (in dbSNP:rs7001647).
/FTId=VAR_057069.
VARIANT 502 502 G -> D (in a cutaneous metastatic
melanoma sample; somatic mutation;
dbSNP:rs267601864).
{ECO:0000269|PubMed:21618342}.
/FTId=VAR_066321.
VARIANT 593 593 T -> K (in dbSNP:rs36041430).
/FTId=VAR_057070.
VARIANT 604 604 T -> P (in dbSNP:rs35617826).
/FTId=VAR_057071.
VARIANT 684 684 M -> I (in dbSNP:rs7829965).
/FTId=VAR_057072.
VARIANT 765 765 V -> M (in dbSNP:rs7814768).
{ECO:0000269|PubMed:10506182,
ECO:0000269|PubMed:10587367,
ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.4}.
/FTId=VAR_024596.
CONFLICT 513 513 Q -> R (in Ref. 1; AAD25099/AAD25100).
{ECO:0000305}.
CONFLICT 774 774 K -> E (in Ref. 1; AAD25099).
{ECO:0000305}.
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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