ADA24_MOUSE
ID ADA24_MOUSE Reviewed; 761 AA.
AC Q9R160; A6H683; E9QL68;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Disintegrin and metalloproteinase domain-containing protein 24;
DE Short=ADAM 24;
DE EC=3.4.24.-;
DE AltName: Full=Testase-1;
DE Flags: Precursor;
GN Name=Adam24;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RX PubMed=10395895; DOI=10.1016/s0378-1119(99)00208-5;
RA Zhu G.-Z., Lin Y., Myles D.G., Primakoff P.;
RT "Identification of four novel ADAMs with potential roles in spermatogenesis
RT and fertilization.";
RL Gene 234:227-237(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP CHARACTERIZATION.
RX PubMed=11309208; DOI=10.1242/jcs.114.9.1787;
RA Zhu G.-Z., Myles D.G., Primakoff P.;
RT "Testase 1 (ADAM 24) a plasma membrane-anchored sperm protease implicated
RT in sperm function during epididymal maturation or fertilization.";
RL J. Cell Sci. 114:1787-1794(2001).
CC -!- FUNCTION: Plasma membrane protease present on mature sperm that may be
CC involved in sperm function during epididymal maturation and/or
CC fertilization.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed exclusively in testis and more
CC specifically on the surface of mature sperm. Localized to the
CC equatorial region of the plasma membrane of cauda epididymal sperm.
CC -!- DEVELOPMENTAL STAGE: Adult levels are reached by day 20 after birth.
CC -!- DOMAIN: The conserved cysteine present in the cysteine-switch motif
CC binds the catalytic zinc ion, thus inhibiting the enzyme. The
CC dissociation of the cysteine from the zinc ion upon the activation-
CC peptide release activates the enzyme.
CC -!- PTM: The prodomain is removed during sperm passage through the caput
CC epididymis after the protein has reached the cell surface. Not
CC processed in the secretory pathway.
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DR EMBL; AF167402; AAD48841.1; -; mRNA.
DR EMBL; AC158915; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC145785; AAI45786.1; -; mRNA.
DR CCDS; CCDS22255.1; -.
DR RefSeq; NP_034216.3; NM_010086.5.
DR RefSeq; XP_006509324.1; XM_006509261.1.
DR AlphaFoldDB; Q9R160; -.
DR SMR; Q9R160; -.
DR MEROPS; M12.227; -.
DR GlyGen; Q9R160; 6 sites.
DR iPTMnet; Q9R160; -.
DR PhosphoSitePlus; Q9R160; -.
DR PaxDb; Q9R160; -.
DR PRIDE; Q9R160; -.
DR ProteomicsDB; 285757; -.
DR DNASU; 13526; -.
DR Ensembl; ENSMUST00000051614; ENSMUSP00000050727; ENSMUSG00000046723.
DR GeneID; 13526; -.
DR KEGG; mmu:13526; -.
DR UCSC; uc009lnb.1; mouse.
DR CTD; 13526; -.
DR MGI; MGI:105984; Adam24.
DR VEuPathDB; HostDB:ENSMUSG00000046723; -.
DR eggNOG; KOG3607; Eukaryota.
DR GeneTree; ENSGT00940000162672; -.
DR HOGENOM; CLU_012714_4_0_1; -.
DR InParanoid; Q9R160; -.
DR OMA; IQQCAKD; -.
DR OrthoDB; 162519at2759; -.
DR PhylomeDB; Q9R160; -.
DR TreeFam; TF314733; -.
DR BioGRID-ORCS; 13526; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q9R160; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9R160; protein.
DR Bgee; ENSMUSG00000046723; Expressed in spermatid and 16 other tissues.
DR Genevisible; Q9R160; MM.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:1990913; C:sperm head plasma membrane; IDA:MGI.
DR GO; GO:0005178; F:integrin binding; ISS:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; ISS:MGI.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0008584; P:male gonad development; IBA:GO_Central.
DR GO; GO:0060468; P:prevention of polyspermy; IMP:MGI.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR Gene3D; 4.10.70.10; -; 1.
DR InterPro; IPR033953; ADAM24.
DR InterPro; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR018358; Disintegrin_CS.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR034027; Reprolysin_adamalysin.
DR PANTHER; PTHR11905:SF118; PTHR11905:SF118; 1.
DR Pfam; PF08516; ADAM_CR; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00050; DISIN; 1.
DR SUPFAM; SSF57552; SSF57552; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS00427; DISINTEGRIN_1; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Differentiation; Disulfide bond; EGF-like domain;
KW Glycoprotein; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Signal; Spermatogenesis; Transmembrane;
KW Transmembrane helix; Zinc; Zymogen.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT PROPEP 35..200
FT /evidence="ECO:0000250"
FT /id="PRO_0000029122"
FT CHAIN 201..761
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein 24"
FT /id="PRO_0000029123"
FT TOPO_DOM 35..697
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 698..718
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 719..761
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 208..400
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 406..493
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DOMAIN 631..664
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 725..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 172..179
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT COMPBIAS 729..743
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 343
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /note="in inhibited form"
FT /evidence="ECO:0000250"
FT BINDING 342
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 346
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 352
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 378
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 479
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 323..393
FT /evidence="ECO:0000250"
FT DISULFID 357..379
FT /evidence="ECO:0000250"
FT DISULFID 359..364
FT /evidence="ECO:0000250"
FT DISULFID 465..485
FT /evidence="ECO:0000250"
FT DISULFID 635..646
FT /evidence="ECO:0000250"
FT DISULFID 640..652
FT /evidence="ECO:0000250"
FT DISULFID 654..663
FT /evidence="ECO:0000250"
FT CONFLICT 162
FT /note="I -> L (in Ref. 1; AAD48841 and 3; AAI45786)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="A -> E (in Ref. 1; AAD48841 and 3; AAI45786)"
FT /evidence="ECO:0000305"
FT CONFLICT 454
FT /note="R -> H (in Ref. 1; AAD48841 and 3; AAI45786)"
FT /evidence="ECO:0000305"
FT CONFLICT 603
FT /note="A -> T (in Ref. 1; AAD48841 and 3; AAI45786)"
FT /evidence="ECO:0000305"
FT CONFLICT 622
FT /note="A -> D (in Ref. 1; AAD48841 and 3; AAI45786)"
FT /evidence="ECO:0000305"
FT CONFLICT 735..737
FT /note="EER -> GET (in Ref. 1; AAD48841 and 3; AAI45786)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 761 AA; 85054 MW; 60F5A903262A3184 CRC64;
MVAMSEALVH ARITLLQAWL RMLLFSSVWP PTWCAEYKGP PETVKPLRVI VSSKDMSLAG
WMSYSLYFGG QRHIISMKSK NFLESRQLPV FTYNDQGVLF EDRPFVQNDC YYLGFVDGDL
ESMAALTTCF GGFQGILQIN DTAYEIKPKS PSSTFEHLLY KIDSEKTQLR PMRCGLTDEE
IAGQVRLQEN GKSTRMQSIY GSWWSHGLYI KLALVIDHEQ YLYRKKNTSL VIRDVLSIMQ
GINLFLLSVD INVVLLGLTI WTNGNPIPVQ DIYALLPAFC TWKGTNLDSQ IPYDIAHLFV
NYTFSNYFGI AYVGTVCDKT FGCGIDSIAE DDFLTIGHIV AHEIGHNLGM SHDGILCTCG
EESCLMSATM DSSQKLSNCS YEVLWAHMIN KSCIHREPRP SDIFQLKVCG NGIVEEGEQC
DCGSSENCRR NRCCMPSCTL RSKAKCDTGL CCNRKCQIQP SGTLCRAREN ECDLPEWCNG
TSHECPEDLF VQDGTSCPGD GYCYEKRCNS HDVHCQRVFG QLAMKASDSC YKELNTRGDR
FGNCGFINNE YVRCEISDIL CGRIQCDKVG TLPILQNHYT IHWTHFNSVS CWSTDYHLGM
KIADLGDIKD GTNCGPQHVC IARKCVNKPS WVNDCTPETC NMKGVCNNKQ HCHCDVGWSP
PNCQETGTGG SIDSGSPGNE VYEDEVVSKK DAPEKPNVII WLLPIICVAV VLSVLFCLSG
ATKKSREAAA SQPAEERVKP PYEGAEPSYE TVKPPDEWAN P
