ADA25_MOUSE
ID ADA25_MOUSE Reviewed; 760 AA.
AC Q9R159; Q9D4E4;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Disintegrin and metalloproteinase domain-containing protein 25;
DE Short=ADAM 25;
DE EC=3.4.24.-;
DE AltName: Full=Testase-2;
DE Flags: Precursor;
GN Name=Adam25;
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 MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
CC -!- FUNCTION: Sperm surface membrane protein that may be involved in
CC spermatogenesis and 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 -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed specifically in testis.
CC -!- DEVELOPMENTAL STAGE: Adult levels are reached by day 25 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.
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DR EMBL; AF167403; AAD48842.1; -; mRNA.
DR EMBL; AK016581; BAB30321.1; -; mRNA.
DR CCDS; CCDS22256.1; -.
DR RefSeq; NP_035911.2; NM_011781.3.
DR AlphaFoldDB; Q9R159; -.
DR SMR; Q9R159; -.
DR BioGRID; 204716; 8.
DR STRING; 10090.ENSMUSP00000094420; -.
DR MEROPS; M12.228; -.
DR GlyGen; Q9R159; 7 sites.
DR PaxDb; Q9R159; -.
DR PRIDE; Q9R159; -.
DR ProteomicsDB; 285549; -.
DR DNASU; 23793; -.
DR GeneID; 23793; -.
DR KEGG; mmu:23793; -.
DR UCSC; uc009lnc.1; mouse.
DR CTD; 23793; -.
DR MGI; MGI:1345157; Adam25.
DR eggNOG; KOG3607; Eukaryota.
DR InParanoid; Q9R159; -.
DR OrthoDB; 162519at2759; -.
DR PhylomeDB; Q9R159; -.
DR TreeFam; TF314733; -.
DR Reactome; R-MMU-2534343; Interaction With Cumulus Cells And The Zona Pellucida.
DR BioGRID-ORCS; 23793; 0 hits in 51 CRISPR screens.
DR PRO; PR:Q9R159; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9R159; protein.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
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; IBA:GO_Central.
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: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; IPR006586; ADAM_Cys-rich.
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 Pfam; PF08516; ADAM_CR; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR PRINTS; PR00289; DISINTEGRIN.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00050; DISIN; 1.
DR SUPFAM; SSF57552; SSF57552; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 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 2: Evidence at transcript 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..50
FT /evidence="ECO:0000255"
FT PROPEP 51..213
FT /evidence="ECO:0000250"
FT /id="PRO_0000029124"
FT CHAIN 214..760
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein 25"
FT /id="PRO_0000029125"
FT TOPO_DOM 214..706
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 707..727
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 728..760
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 221..413
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 419..505
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DOMAIN 660..676
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 738..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 186..193
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT COMPBIAS 742..760
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 356
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 188
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 355
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 359
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 365
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 690
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 694
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 336..406
FT /evidence="ECO:0000250"
FT DISULFID 370..392
FT /evidence="ECO:0000250"
FT DISULFID 372..377
FT /evidence="ECO:0000250"
FT DISULFID 477..497
FT /evidence="ECO:0000250"
FT DISULFID 647..658
FT /evidence="ECO:0000250"
FT DISULFID 652..664
FT /evidence="ECO:0000250"
FT DISULFID 666..675
FT /evidence="ECO:0000250"
FT CONFLICT 4
FT /note="T -> R (in Ref. 2; BAB30321)"
FT /evidence="ECO:0000305"
FT CONFLICT 13
FT /note="A -> T (in Ref. 2; BAB30321)"
FT /evidence="ECO:0000305"
FT CONFLICT 33
FT /note="L -> V (in Ref. 2; BAB30321)"
FT /evidence="ECO:0000305"
FT CONFLICT 44
FT /note="R -> W (in Ref. 2; BAB30321)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="H -> Q (in Ref. 2; BAB30321)"
FT /evidence="ECO:0000305"
FT CONFLICT 374
FT /note="T -> R (in Ref. 2; BAB30321)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 760 AA; 86128 MW; 674B73933F7FD070 CRC64;
MQTTQRASSF AAAEDNIAMD KAVVYTRIPH LYLWLEILNI LSSRPLTGYA QHTSLPEVVI
PLRVTGNRPM WAMGWLTYSL HFGGQKHFIH IKAKKFLVSR LFSVFTYTKQ GALHKDQPYV
QNDCYYHGHM DGDPESMVAI TTCYGGFQGI LQINGTVYEI KPKNLSSTFE HLVHKMDSEE
TELLPMRCAL TEEIARQMKL QQNENPTLMQ SHYEGWWTHK SFLDLALVVE RERIRYHNNN
TSRVLVEVFT IINIINNIYE TLDVELVLLG VEMWNERNHV QVRSIEELLD EFCMWKARSL
NFRIPNDIAH IFVNHEFGIY LGLAYIGSVC VPSHNCGVDR LLGGNLFYFG RIIAHEMGHN
LGMEHDSSSC TCGTKICLMA PADNGIPKFS NCSYSYYWAT YATAKCMRKE KKSKGILRGK
LCGDGVVDDG EQCDCGSAKS CADDPCCKPS CTLKDGAACA FGLCCLYCQI MPAGTVCRQE
VNECDLPEWC NGHSHKCPND VYLLDGSPCR DGGYCYEKRC NNRDEQCKQI FGKEARSADH
SCYRELNTQG DRFGNCGVIR DAYLRCHDPD ILCGRVQCEN VAHIPFLRDH STVHWTHLNG
VTCWGTDYHF GMTIPDIGIV KDGTDCGPEH VCINKKCVSK SIWRSQCSPK TCNMKGVCNN
LHHCHCNLGW DPPHCLKSGL GGSIDSGPPN YTENYTEKKH KKSIGLVILF WILFACFSVL
FIVFLFFLRS YVELPMSEEP KVPTPENKED TNEVMNTETE
