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Disintegrin and metalloproteinase domain-containing protein 12 (ADAM 12) (EC 3.4.24.-) (Meltrin-alpha)

 ADA12_MOUSE             Reviewed;         903 AA.
Q61824; F8VQN4;
31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
03-OCT-2012, sequence version 2.
12-SEP-2018, entry version 169.
RecName: Full=Disintegrin and metalloproteinase domain-containing protein 12;
Short=ADAM 12;
EC=3.4.24.-;
AltName: Full=Meltrin-alpha;
Flags: Precursor;
Name=Adam12; Synonyms=Mltna;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Embryonic fibroblast;
PubMed=7566181; DOI=10.1038/377652a0;
Yagami-Hiromasa T., Sato T., Kurisaki T., Kamijo K., Nabeshima Y.,
Fujisawa-Sehara A.;
"A metalloprotease-disintegrin participating in myoblast fusion.";
Nature 377:652-656(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
TISSUE SPECIFICITY.
PubMed=9622634; DOI=10.1016/S0925-4773(98)00043-4;
Kurisaki T., Masuda A., Osumi N., Nabeshima Y., Fujisawa-Sehara A.;
"Spatially- and temporally-restricted expression of meltrin alpha
(ADAM12) and beta (ADAM19) in mouse embryo.";
Mech. Dev. 73:211-215(1998).
[4]
INTERACTION WITH ALPHA-ACTININ-2.
PubMed=10788519; DOI=10.1074/jbc.275.18.13933;
Galliano M.-F., Huet C., Frygelius J., Polgren A., Wewer U.M.,
Engvall E.;
"Binding of ADAM12, a marker of skeletal muscle regeneration, to the
muscle-specific actin-binding protein, alpha-actinin-2, is required
for myoblast fusion.";
J. Biol. Chem. 275:13933-13939(2000).
[5]
PHOSPHORYLATION AT TYR-901.
PubMed=11127814; DOI=10.1038/sj.onc.1203986;
Suzuki A., Kadota N., Hara T., Nakagami Y., Izumi T., Takenawa T.,
Sabe H., Endo T.;
"Meltrin alpha cytoplasmic domain interacts with SH3 domains of Src
and Grb2 and is phosphorylated by v-Src.";
Oncogene 19:5842-5850(2000).
-!- FUNCTION: Involved in skeletal muscle regeneration, specifically
at the onset of cell fusion. Also involved in macrophage-derived
giant cells (MGC) and osteoclast formation from mononuclear
precursors.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- SUBUNIT: Interacts with alpha-actinin-2 and with syndecans.
Interacts with SH3PXD2A. Interacts with FST3. Interacts with
RACK1; the interaction is required for PKC-dependent translocation
of ADAM12 to the cell membrane (By similarity). {ECO:0000250}.
-!- INTERACTION:
P35609:ACTN2 (xeno); NbExp=3; IntAct=EBI-77785, EBI-77797;
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- TISSUE SPECIFICITY: Expressed during early developing mesenchymal
cells that give rise to skeletal muscle, bones and visceral
organs. Not expressed in adult normal muscle but expressed in
regenerating muscle. {ECO:0000269|PubMed:9622634}.
-!- INDUCTION: At the onset of myoblast fusion.
-!- DOMAIN: The first 30 amino acids of the cytoplasmic domain contain
a major binding site to alpha-actinin-2. This interaction is
necessary to promote muscle cell fusion.
-!- DOMAIN: The cysteine-rich domain supports cell adhesion through
syndecans and triggers signaling events that lead to beta-1
integrin-dependent cell spreading. In carcinoma cells the binding
of this domain to syndecans does not allow the integrin-mediated
cell spreading (By similarity). {ECO:0000250}.
-!- 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: The precursor is cleaved by a furin endopeptidase.
{ECO:0000250}.
-!- MISCELLANEOUS: Marker of skeletal muscle regeneration.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; D50411; BAA08912.1; -; mRNA.
EMBL; AC125372; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC126676; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC140055; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS21938.1; -.
PIR; S60257; S60257.
RefSeq; NP_031426.2; NM_007400.2.
UniGene; Mm.439714; -.
ProteinModelPortal; Q61824; -.
SMR; Q61824; -.
IntAct; Q61824; 1.
MINT; Q61824; -.
STRING; 10090.ENSMUSP00000065213; -.
MEROPS; M12.212; -.
iPTMnet; Q61824; -.
PhosphoSitePlus; Q61824; -.
PaxDb; Q61824; -.
PRIDE; Q61824; -.
DNASU; 11489; -.
Ensembl; ENSMUST00000067680; ENSMUSP00000065213; ENSMUSG00000054555.
GeneID; 11489; -.
KEGG; mmu:11489; -.
UCSC; uc009kdo.2; mouse.
CTD; 8038; -.
MGI; MGI:105378; Adam12.
eggNOG; KOG3607; Eukaryota.
eggNOG; ENOG410XX2M; LUCA.
GeneTree; ENSGT00910000144014; -.
HOGENOM; HOG000230883; -.
HOVERGEN; HBG006978; -.
InParanoid; Q61824; -.
KO; K06835; -.
OMA; FTSLHEF; -.
OrthoDB; EOG091G01NX; -.
TreeFam; TF314733; -.
BRENDA; 3.4.24.B10; 3474.
Reactome; R-MMU-8941237; Invadopodia formation.
ChiTaRS; Adam12; mouse.
PRO; PR:Q61824; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000054555; Expressed in 239 organ(s), highest expression level in decidua.
ExpressionAtlas; Q61824; baseline and differential.
Genevisible; Q61824; MM.
GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
GO; GO:0017124; F:SH3 domain binding; ISO:MGI.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
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; 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; PS50026; EGF_3; 1.
PROSITE; PS00142; ZINC_PROTEASE; 1.
1: Evidence at protein level;
Cell adhesion; Cleavage on pair of basic residues; Complete proteome;
Disulfide bond; EGF-like domain; Glycoprotein; Hydrolase; Membrane;
Metal-binding; Metalloprotease; Phosphoprotein; Protease;
Reference proteome; SH3-binding; Signal; Transmembrane;
Transmembrane helix; Zinc; Zymogen.
SIGNAL 1 31 {ECO:0000255}.
PROPEP 32 205 {ECO:0000250}.
/FTId=PRO_0000029080.
CHAIN 206 903 Disintegrin and metalloproteinase domain-
containing protein 12.
/FTId=PRO_0000029081.
TOPO_DOM 206 706 Extracellular. {ECO:0000255}.
TRANSMEM 707 727 Helical. {ECO:0000255}.
TOPO_DOM 728 903 Cytoplasmic. {ECO:0000255}.
DOMAIN 212 414 Peptidase M12B. {ECO:0000255|PROSITE-
ProRule:PRU00276}.
DOMAIN 422 508 Disintegrin. {ECO:0000255|PROSITE-
ProRule:PRU00068}.
DOMAIN 654 686 EGF-like. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
MOTIF 175 182 Cysteine switch. {ECO:0000250}.
MOTIF 824 830 SH3-binding; class II.
MOTIF 830 837 SH3-binding; class I.
MOTIF 846 852 SH3-binding; class II.
MOTIF 852 858 SH3-binding; class I.
MOTIF 881 887 SH3-binding; class I.
COMPBIAS 509 653 Cys-rich.
ACT_SITE 349 349 {ECO:0000255|PROSITE-ProRule:PRU00276,
ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 177 177 Zinc; in inhibited form. {ECO:0000250}.
METAL 348 348 Zinc; catalytic. {ECO:0000250}.
METAL 352 352 Zinc; catalytic. {ECO:0000250}.
METAL 358 358 Zinc; catalytic. {ECO:0000250}.
MOD_RES 901 901 Phosphotyrosine; by SRC.
{ECO:0000305|PubMed:11127814}.
CARBOHYD 112 112 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 147 147 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 157 157 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 182 182 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 185 185 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 450 450 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 649 649 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 323 409 {ECO:0000250}.
DISULFID 365 393 {ECO:0000250}.
DISULFID 367 376 {ECO:0000250}.
DISULFID 480 500 {ECO:0000250}.
DISULFID 658 668 {ECO:0000250}.
DISULFID 662 674 {ECO:0000250}.
DISULFID 676 685 {ECO:0000250}.
CONFLICT 40 40 T -> A (in Ref. 1; BAA08912).
{ECO:0000305}.
CONFLICT 138 138 G -> D (in Ref. 1; BAA08912).
{ECO:0000305}.
CONFLICT 280 280 S -> R (in Ref. 1; BAA08912).
{ECO:0000305}.
SEQUENCE 903 AA; 98504 MW; B6A1D0816E4A73FC CRC64;
MAERPARRAP PARALLLALA GALLAPRAAR GMSLWDQRGT YEVARASLLS KDPGIPGQSI
PAKDHPDVLT VQLQLESRDL ILSLERNEGL IANGFTETHY LQDGTDVSLT RNHTDHCYYH
GHVQGDAASV VSLSTCSGLR GLIMFENKTY SLEPMKNTTD SYKLVPAESM TNIQGLCGSQ
HNKSNLTMED VSPGTSQMRA RRHKRETLKM TKYVELVIVA DNREFQRQGK DLEKVKQRLI
EIANHVDKFY RPLNIRIVLV GVEVWNDIDK CSISQDPFTS LHEFLDWRKI KLLPRKSHDN
AQLISGVYFQ GTTIGMAPIM SMCTAEQSGG VVMDHSDSPL GAAVTLAHEL GHNFGMNHDT
LERGCSCRMA AEKGGCIMNP STGFPFPMVF SSCSRKDLEA SLEKGMGMCL FNLPEVKQAF
GGRKCGNGYV EEGEECDCGE PEECTNRCCN ATTCTLKPDA VCAHGQCCED CQLKPPGTAC
RGSSNSCDLP EFCTGTAPHC PANVYLHDGH PCQGVDGYCY NGICQTHEQQ CVTLWGPGAK
PAPGICFERV NSAGDPYGNC GKDSKSAFAK CELRDAKCGK IQCQGGASRP VIGTNAVSIE
TNIPQQEGGR ILCRGTHVYL GDDMPDPGLV LAGTKCAEGK ICLNRRCQNI SVFGVHKCAM
QCHGRGVCNN RKNCHCEAHW APPFCDKFGF GGSTDSGPIR QADNQGLTVG ILVSILCLLA
AGFVVYLKRK TLMRLLFTHK KTTMEKLRCV HPSRTPSGPH LGQAHHTPGK GLLMNRAPHF
NTPKDRHSLK CQNMDISRPL DARAVPQLQS PQRVLLPLHQ TPRAPSGPAR PLPASPAVRQ
AQGIRKPSPP QKPLPADPLS RTSRLTSALV RTPGQQEPGH RPAPIRPAPK HQVPRPSHNA
YIK


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