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Q61824

- ADA12_MOUSE

UniProt

Q61824 - ADA12_MOUSE

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Protein

Disintegrin and metalloproteinase domain-containing protein 12

Gene

Adam12

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi177 – 1771Zinc; in inhibited formBy similarity
Metal bindingi348 – 3481Zinc; catalyticBy similarity
Active sitei349 – 3491PROSITE-ProRule annotation
Metal bindingi352 – 3521Zinc; catalyticBy similarity
Metal bindingi358 – 3581Zinc; catalyticBy similarity

GO - Molecular functioni

  1. metalloendopeptidase activity Source: InterPro
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. cell adhesion Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_242976. Signaling by EGFR.

Protein family/group databases

MEROPSiM12.212.

Names & Taxonomyi

Protein namesi
Recommended name:
Disintegrin and metalloproteinase domain-containing protein 12 (EC:3.4.24.-)
Short name:
ADAM 12
Alternative name(s):
Meltrin-alpha
Gene namesi
Name:Adam12
Synonyms:Mltna
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:105378. Adam12.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini206 – 706501ExtracellularSequence AnalysisAdd
BLAST
Transmembranei707 – 72721HelicalSequence AnalysisAdd
BLAST
Topological domaini728 – 903176CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3131Sequence AnalysisAdd
BLAST
Propeptidei32 – 205174By similarityPRO_0000029080Add
BLAST
Chaini206 – 903698Disintegrin and metalloproteinase domain-containing protein 12PRO_0000029081Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi112 – 1121N-linked (GlcNAc...)Sequence Analysis
Glycosylationi147 – 1471N-linked (GlcNAc...)Sequence Analysis
Glycosylationi157 – 1571N-linked (GlcNAc...)Sequence Analysis
Glycosylationi182 – 1821N-linked (GlcNAc...)Sequence Analysis
Glycosylationi185 – 1851N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi323 ↔ 409By similarity
Disulfide bondi365 ↔ 393By similarity
Disulfide bondi367 ↔ 376By similarity
Glycosylationi450 – 4501N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi480 ↔ 500By similarity
Glycosylationi649 – 6491N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi658 ↔ 668By similarity
Disulfide bondi662 ↔ 674By similarity
Disulfide bondi676 ↔ 685By similarity
Modified residuei901 – 9011Phosphotyrosine; by SRC1 Publication

Post-translational modificationi

The precursor is cleaved by a furin endopeptidase.By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein, Zymogen

Proteomic databases

PRIDEiQ61824.

PTM databases

PhosphoSiteiQ61824.

Expressioni

Tissue specificityi

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.1 Publication

Inductioni

At the onset of myoblast fusion.

Gene expression databases

ExpressionAtlasiQ61824. baseline and differential.
GenevestigatoriQ61824.

Interactioni

Subunit structurei

Interacts with alpha-actinin-2 and with syndecans. Interacts with SH3PXD2A. Interacts with FST3. Interacts with GNB2L1/RACK1; the interaction is required for PKC-dependent translocation of ADAM12 to the cell membrane (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
ACTN2P356093EBI-77785,EBI-77797From a different organism.

Protein-protein interaction databases

IntActiQ61824. 1 interaction.
MINTiMINT-154663.

Structurei

3D structure databases

ProteinModelPortaliQ61824.
SMRiQ61824. Positions 211-688.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini212 – 414203Peptidase M12BPROSITE-ProRule annotationAdd
BLAST
Domaini422 – 50887DisintegrinPROSITE-ProRule annotationAdd
BLAST
Domaini654 – 68633EGF-likePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi175 – 1828Cysteine switchBy similarity
Motifi824 – 8307SH3-binding; class II
Motifi830 – 8378SH3-binding; class I
Motifi846 – 8527SH3-binding; class II
Motifi852 – 8587SH3-binding; class I
Motifi881 – 8877SH3-binding; class I

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi509 – 653145Cys-richAdd
BLAST

Domaini

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.
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).By similarity
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.

Sequence similaritiesi

Contains 1 disintegrin domain.PROSITE-ProRule annotation
Contains 1 EGF-like domain.PROSITE-ProRule annotation
Contains 1 peptidase M12B domain.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, SH3-binding, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG294463.
GeneTreeiENSGT00760000118888.
HOGENOMiHOG000230883.
HOVERGENiHBG006978.
InParanoidiQ61824.
KOiK06835.
OMAiPPFCDKF.
OrthoDBiEOG7F7W89.
TreeFamiTF314733.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
4.10.70.10. 1 hit.
InterProiIPR006586. ADAM_Cys-rich.
IPR001762. Blood-coag_inhib_Disintegrin.
IPR018358. Disintegrin_CS.
IPR000742. EG-like_dom.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR002870. Peptidase_M12B_N.
[Graphical view]
PfamiPF08516. ADAM_CR. 1 hit.
PF00200. Disintegrin. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
[Graphical view]
PRINTSiPR00289. DISINTEGRIN.
SMARTiSM00608. ACR. 1 hit.
SM00050. DISIN. 1 hit.
[Graphical view]
SUPFAMiSSF57552. SSF57552. 1 hit.
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS00427. DISINTEGRIN_1. 1 hit.
PS50214. DISINTEGRIN_2. 1 hit.
PS50026. EGF_3. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q61824-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAERPARRAP PARALLLALA GALLAPRAAR GMSLWDQRGT YEVARASLLS
60 70 80 90 100
KDPGIPGQSI PAKDHPDVLT VQLQLESRDL ILSLERNEGL IANGFTETHY
110 120 130 140 150
LQDGTDVSLT RNHTDHCYYH GHVQGDAASV VSLSTCSGLR GLIMFENKTY
160 170 180 190 200
SLEPMKNTTD SYKLVPAESM TNIQGLCGSQ HNKSNLTMED VSPGTSQMRA
210 220 230 240 250
RRHKRETLKM TKYVELVIVA DNREFQRQGK DLEKVKQRLI EIANHVDKFY
260 270 280 290 300
RPLNIRIVLV GVEVWNDIDK CSISQDPFTS LHEFLDWRKI KLLPRKSHDN
310 320 330 340 350
AQLISGVYFQ GTTIGMAPIM SMCTAEQSGG VVMDHSDSPL GAAVTLAHEL
360 370 380 390 400
GHNFGMNHDT LERGCSCRMA AEKGGCIMNP STGFPFPMVF SSCSRKDLEA
410 420 430 440 450
SLEKGMGMCL FNLPEVKQAF GGRKCGNGYV EEGEECDCGE PEECTNRCCN
460 470 480 490 500
ATTCTLKPDA VCAHGQCCED CQLKPPGTAC RGSSNSCDLP EFCTGTAPHC
510 520 530 540 550
PANVYLHDGH PCQGVDGYCY NGICQTHEQQ CVTLWGPGAK PAPGICFERV
560 570 580 590 600
NSAGDPYGNC GKDSKSAFAK CELRDAKCGK IQCQGGASRP VIGTNAVSIE
610 620 630 640 650
TNIPQQEGGR ILCRGTHVYL GDDMPDPGLV LAGTKCAEGK ICLNRRCQNI
660 670 680 690 700
SVFGVHKCAM QCHGRGVCNN RKNCHCEAHW APPFCDKFGF GGSTDSGPIR
710 720 730 740 750
QADNQGLTVG ILVSILCLLA AGFVVYLKRK TLMRLLFTHK KTTMEKLRCV
760 770 780 790 800
HPSRTPSGPH LGQAHHTPGK GLLMNRAPHF NTPKDRHSLK CQNMDISRPL
810 820 830 840 850
DARAVPQLQS PQRVLLPLHQ TPRAPSGPAR PLPASPAVRQ AQGIRKPSPP
860 870 880 890 900
QKPLPADPLS RTSRLTSALV RTPGQQEPGH RPAPIRPAPK HQVPRPSHNA

YIK
Length:903
Mass (Da):98,504
Last modified:October 3, 2012 - v2
Checksum:iB6A1D0816E4A73FC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti40 – 401T → A in BAA08912. (PubMed:7566181)Curated
Sequence conflicti138 – 1381G → D in BAA08912. (PubMed:7566181)Curated
Sequence conflicti280 – 2801S → R in BAA08912. (PubMed:7566181)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D50411 mRNA. Translation: BAA08912.1.
AC125372 Genomic DNA. No translation available.
AC126676 Genomic DNA. No translation available.
AC140055 Genomic DNA. No translation available.
CCDSiCCDS21938.1.
PIRiS60257.
RefSeqiNP_031426.2. NM_007400.2.
UniGeneiMm.439714.

Genome annotation databases

EnsembliENSMUST00000067680; ENSMUSP00000065213; ENSMUSG00000054555.
GeneIDi11489.
KEGGimmu:11489.
UCSCiuc009kdo.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D50411 mRNA. Translation: BAA08912.1 .
AC125372 Genomic DNA. No translation available.
AC126676 Genomic DNA. No translation available.
AC140055 Genomic DNA. No translation available.
CCDSi CCDS21938.1.
PIRi S60257.
RefSeqi NP_031426.2. NM_007400.2.
UniGenei Mm.439714.

3D structure databases

ProteinModelPortali Q61824.
SMRi Q61824. Positions 211-688.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q61824. 1 interaction.
MINTi MINT-154663.

Protein family/group databases

MEROPSi M12.212.

PTM databases

PhosphoSitei Q61824.

Proteomic databases

PRIDEi Q61824.

Protocols and materials databases

DNASUi 11489.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000067680 ; ENSMUSP00000065213 ; ENSMUSG00000054555 .
GeneIDi 11489.
KEGGi mmu:11489.
UCSCi uc009kdo.2. mouse.

Organism-specific databases

CTDi 8038.
MGIi MGI:105378. Adam12.

Phylogenomic databases

eggNOGi NOG294463.
GeneTreei ENSGT00760000118888.
HOGENOMi HOG000230883.
HOVERGENi HBG006978.
InParanoidi Q61824.
KOi K06835.
OMAi PPFCDKF.
OrthoDBi EOG7F7W89.
TreeFami TF314733.

Enzyme and pathway databases

Reactomei REACT_242976. Signaling by EGFR.

Miscellaneous databases

ChiTaRSi Adam12. mouse.
NextBioi 278856.
PROi Q61824.
SOURCEi Search...

Gene expression databases

ExpressionAtlasi Q61824. baseline and differential.
Genevestigatori Q61824.

Family and domain databases

Gene3Di 3.40.390.10. 1 hit.
4.10.70.10. 1 hit.
InterProi IPR006586. ADAM_Cys-rich.
IPR001762. Blood-coag_inhib_Disintegrin.
IPR018358. Disintegrin_CS.
IPR000742. EG-like_dom.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR002870. Peptidase_M12B_N.
[Graphical view ]
Pfami PF08516. ADAM_CR. 1 hit.
PF00200. Disintegrin. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
[Graphical view ]
PRINTSi PR00289. DISINTEGRIN.
SMARTi SM00608. ACR. 1 hit.
SM00050. DISIN. 1 hit.
[Graphical view ]
SUPFAMi SSF57552. SSF57552. 1 hit.
PROSITEi PS50215. ADAM_MEPRO. 1 hit.
PS00427. DISINTEGRIN_1. 1 hit.
PS50214. DISINTEGRIN_2. 1 hit.
PS50026. EGF_3. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A metalloprotease-disintegrin participating in myoblast fusion."
    Yagami-Hiromasa T., Sato T., Kurisaki T., Kamijo K., Nabeshima Y., Fujisawa-Sehara A.
    Nature 377:652-656(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Embryonic fibroblast.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "Spatially- and temporally-restricted expression of meltrin alpha (ADAM12) and beta (ADAM19) in mouse embryo."
    Kurisaki T., Masuda A., Osumi N., Nabeshima Y., Fujisawa-Sehara A.
    Mech. Dev. 73:211-215(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  4. "Binding of ADAM12, a marker of skeletal muscle regeneration, to the muscle-specific actin-binding protein, alpha-actinin-2, is required for myoblast fusion."
    Galliano M.-F., Huet C., Frygelius J., Polgren A., Wewer U.M., Engvall E.
    J. Biol. Chem. 275:13933-13939(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ALPHA-ACTININ-2.
  5. "Meltrin alpha cytoplasmic domain interacts with SH3 domains of Src and Grb2 and is phosphorylated by v-Src."
    Suzuki A., Kadota N., Hara T., Nakagami Y., Izumi T., Takenawa T., Sabe H., Endo T.
    Oncogene 19:5842-5850(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-901.

Entry informationi

Entry nameiADA12_MOUSE
AccessioniPrimary (citable) accession number: Q61824
Secondary accession number(s): F8VQN4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: October 3, 2012
Last modified: November 26, 2014
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Marker of skeletal muscle regeneration.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3