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Protein

Disintegrin and metalloproteinase domain-containing protein 24

Gene

Adam24

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

Functioni

Plasma membrane protease present on mature sperm that may be involved in sperm function during epididymal maturation and/or fertilization.

Cofactori

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi174Zinc; in inhibited formBy similarity1
Metal bindingi342Zinc; catalyticBy similarity1
Active sitei343PROSITE-ProRule annotation1
Metal bindingi346Zinc; catalyticBy similarity1
Metal bindingi352Zinc; catalyticBy similarity1

GO - Molecular functioni

  • integrin binding Source: MGI
  • metal ion binding Source: UniProtKB-KW
  • metalloendopeptidase activity Source: InterPro
  • metallopeptidase activity Source: MGI

GO - Biological processi

  • cell differentiation Source: UniProtKB-KW
  • multicellular organism development Source: UniProtKB-KW
  • prevention of polyspermy Source: MGI
  • spermatogenesis Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Differentiation, Spermatogenesis

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM12.227.

Names & Taxonomyi

Protein namesi
Recommended name:
Disintegrin and metalloproteinase domain-containing protein 24 (EC:3.4.24.-)
Short name:
ADAM 24
Alternative name(s):
Testase-1
Gene namesi
Name:Adam24
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:105984. Adam24.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini35 – 697ExtracellularSequence analysisAdd BLAST663
Transmembranei698 – 718HelicalSequence analysisAdd BLAST21
Topological domaini719 – 761CytoplasmicSequence analysisAdd BLAST43

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 34Sequence analysisAdd BLAST34
PropeptideiPRO_000002912235 – 200By similarityAdd BLAST166
ChainiPRO_0000029123201 – 761Disintegrin and metalloproteinase domain-containing protein 24Add BLAST561

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi140N-linked (GlcNAc...)Sequence analysis1
Glycosylationi227N-linked (GlcNAc...)Sequence analysis1
Glycosylationi301N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi323 ↔ 393By similarity
Disulfide bondi357 ↔ 379By similarity
Disulfide bondi359 ↔ 364By similarity
Glycosylationi378N-linked (GlcNAc...)Sequence analysis1
Glycosylationi390N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi465 ↔ 485By similarity
Glycosylationi479N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi635 ↔ 646By similarity
Disulfide bondi640 ↔ 652By similarity
Disulfide bondi654 ↔ 663By similarity

Post-translational modificationi

The prodomain is removed during sperm passage through the caput epididymis after the protein has reached the cell surface. Not processed in the secretory pathway.

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiQ9R160.
PRIDEiQ9R160.

PTM databases

iPTMnetiQ9R160.
PhosphoSitePlusiQ9R160.

Expressioni

Tissue specificityi

Expressed exclusively in testis and more specifically on the surface of mature sperm. Localized to the equatorial region of the plasma membrane of cauda epididymal sperm.

Developmental stagei

Adult levels are reached by day 20 after birth.

Gene expression databases

BgeeiENSMUSG00000046723.
GenevisibleiQ9R160. MM.

Interactioni

Subunit structurei

Monomer.

GO - Molecular functioni

  • integrin binding Source: MGI

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000050727.

Structurei

3D structure databases

ProteinModelPortaliQ9R160.
SMRiQ9R160.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini208 – 400Peptidase M12BPROSITE-ProRule annotationAdd BLAST193
Domaini406 – 493DisintegrinPROSITE-ProRule annotationAdd BLAST88
Domaini631 – 664EGF-likePROSITE-ProRule annotationAdd BLAST34

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi172 – 179Cysteine switchBy similarity8

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi494 – 630Cys-richAdd BLAST137

Domaini

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, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3607. Eukaryota.
ENOG410XX2M. LUCA.
GeneTreeiENSGT00760000118888.
HOGENOMiHOG000230883.
HOVERGENiHBG006978.
InParanoidiQ9R160.
KOiK08611.
OMAiTIGHIVA.
OrthoDBiEOG091G03BZ.
TreeFamiTF314733.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
4.10.70.10. 1 hit.
InterProiIPR033953. ADAM24.
IPR006586. ADAM_Cys-rich.
IPR018358. Disintegrin_CS.
IPR001762. Disintegrin_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR002870. Peptidase_M12B_N.
[Graphical view]
PANTHERiPTHR11905:SF118. PTHR11905:SF118. 1 hit.
PfamiPF08516. ADAM_CR. 1 hit.
PF00200. Disintegrin. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
[Graphical view]
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.
PS01186. EGF_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.

Q9R160-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVAMSEALVH ARITLLQAWL RMLLFSSVWP PTWCAEYKGP PETVKPLRVI
60 70 80 90 100
VSSKDMSLAG WMSYSLYFGG QRHIISMKSK NFLESRQLPV FTYNDQGVLF
110 120 130 140 150
EDRPFVQNDC YYLGFVDGDL ESMAALTTCF GGFQGILQIN DTAYEIKPKS
160 170 180 190 200
PSSTFEHLLY KIDSEKTQLR PMRCGLTDEE IAGQVRLQEN GKSTRMQSIY
210 220 230 240 250
GSWWSHGLYI KLALVIDHEQ YLYRKKNTSL VIRDVLSIMQ GINLFLLSVD
260 270 280 290 300
INVVLLGLTI WTNGNPIPVQ DIYALLPAFC TWKGTNLDSQ IPYDIAHLFV
310 320 330 340 350
NYTFSNYFGI AYVGTVCDKT FGCGIDSIAE DDFLTIGHIV AHEIGHNLGM
360 370 380 390 400
SHDGILCTCG EESCLMSATM DSSQKLSNCS YEVLWAHMIN KSCIHREPRP
410 420 430 440 450
SDIFQLKVCG NGIVEEGEQC DCGSSENCRR NRCCMPSCTL RSKAKCDTGL
460 470 480 490 500
CCNRKCQIQP SGTLCRAREN ECDLPEWCNG TSHECPEDLF VQDGTSCPGD
510 520 530 540 550
GYCYEKRCNS HDVHCQRVFG QLAMKASDSC YKELNTRGDR FGNCGFINNE
560 570 580 590 600
YVRCEISDIL CGRIQCDKVG TLPILQNHYT IHWTHFNSVS CWSTDYHLGM
610 620 630 640 650
KIADLGDIKD GTNCGPQHVC IARKCVNKPS WVNDCTPETC NMKGVCNNKQ
660 670 680 690 700
HCHCDVGWSP PNCQETGTGG SIDSGSPGNE VYEDEVVSKK DAPEKPNVII
710 720 730 740 750
WLLPIICVAV VLSVLFCLSG ATKKSREAAA SQPAEERVKP PYEGAEPSYE
760
TVKPPDEWAN P
Length:761
Mass (Da):85,054
Last modified:July 27, 2011 - v2
Checksum:i60F5A903262A3184
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti162I → L in AAD48841 (PubMed:10395895).Curated1
Sequence conflicti162I → L in AAI45786 (PubMed:15489334).Curated1
Sequence conflicti182A → E in AAD48841 (PubMed:10395895).Curated1
Sequence conflicti182A → E in AAI45786 (PubMed:15489334).Curated1
Sequence conflicti454R → H in AAD48841 (PubMed:10395895).Curated1
Sequence conflicti454R → H in AAI45786 (PubMed:15489334).Curated1
Sequence conflicti603A → T in AAD48841 (PubMed:10395895).Curated1
Sequence conflicti603A → T in AAI45786 (PubMed:15489334).Curated1
Sequence conflicti622A → D in AAD48841 (PubMed:10395895).Curated1
Sequence conflicti622A → D in AAI45786 (PubMed:15489334).Curated1
Sequence conflicti735 – 737EER → GET in AAD48841 (PubMed:10395895).Curated3
Sequence conflicti735 – 737EER → GET in AAI45786 (PubMed:15489334).Curated3

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF167402 mRNA. Translation: AAD48841.1.
AC158915 Genomic DNA. No translation available.
BC145785 mRNA. Translation: AAI45786.1.
CCDSiCCDS22255.1.
RefSeqiNP_034216.3. NM_010086.5.
XP_006509324.1. XM_006509261.1.
UniGeneiMm.67403.

Genome annotation databases

EnsembliENSMUST00000051614; ENSMUSP00000050727; ENSMUSG00000046723.
GeneIDi13526.
KEGGimmu:13526.
UCSCiuc009lnb.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF167402 mRNA. Translation: AAD48841.1.
AC158915 Genomic DNA. No translation available.
BC145785 mRNA. Translation: AAI45786.1.
CCDSiCCDS22255.1.
RefSeqiNP_034216.3. NM_010086.5.
XP_006509324.1. XM_006509261.1.
UniGeneiMm.67403.

3D structure databases

ProteinModelPortaliQ9R160.
SMRiQ9R160.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000050727.

Protein family/group databases

MEROPSiM12.227.

PTM databases

iPTMnetiQ9R160.
PhosphoSitePlusiQ9R160.

Proteomic databases

PaxDbiQ9R160.
PRIDEiQ9R160.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000051614; ENSMUSP00000050727; ENSMUSG00000046723.
GeneIDi13526.
KEGGimmu:13526.
UCSCiuc009lnb.1. mouse.

Organism-specific databases

CTDi13526.
MGIiMGI:105984. Adam24.

Phylogenomic databases

eggNOGiKOG3607. Eukaryota.
ENOG410XX2M. LUCA.
GeneTreeiENSGT00760000118888.
HOGENOMiHOG000230883.
HOVERGENiHBG006978.
InParanoidiQ9R160.
KOiK08611.
OMAiTIGHIVA.
OrthoDBiEOG091G03BZ.
TreeFamiTF314733.

Miscellaneous databases

PROiQ9R160.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000046723.
GenevisibleiQ9R160. MM.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
4.10.70.10. 1 hit.
InterProiIPR033953. ADAM24.
IPR006586. ADAM_Cys-rich.
IPR018358. Disintegrin_CS.
IPR001762. Disintegrin_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR002870. Peptidase_M12B_N.
[Graphical view]
PANTHERiPTHR11905:SF118. PTHR11905:SF118. 1 hit.
PfamiPF08516. ADAM_CR. 1 hit.
PF00200. Disintegrin. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
[Graphical view]
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.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiADA24_MOUSE
AccessioniPrimary (citable) accession number: Q9R160
Secondary accession number(s): A6H683, E9QL68
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: July 27, 2011
Last modified: November 30, 2016
This is version 136 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.