GenomeNet

Database: UniProt
Entry: Q9R159
LinkDB: Q9R159
Original site: Q9R159 
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   16-JAN-2019, entry version 142.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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
RT   spermatogenesis 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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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
CC       protein.
CC   -!- TISSUE SPECIFICITY: Expressed specifically in testis.
CC   -!- DEVELOPMENTAL STAGE: Adult levels are reached by day 25 after
CC       birth.
CC   -!- DOMAIN: The conserved cysteine present in the cysteine-switch
CC       motif binds the catalytic zinc ion, thus inhibiting the enzyme.
CC       The dissociation of the cysteine from the zinc ion upon the
CC       activation-peptide release activates the enzyme.
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   UniGene; Mm.483208; -.
DR   ProteinModelPortal; Q9R159; -.
DR   SMR; Q9R159; -.
DR   STRING; 10090.ENSMUSP00000094420; -.
DR   MEROPS; M12.228; -.
DR   PaxDb; Q9R159; -.
DR   PRIDE; Q9R159; -.
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   eggNOG; ENOG410XX2M; LUCA.
DR   HOGENOM; HOG000230883; -.
DR   HOVERGEN; HBG006978; -.
DR   InParanoid; Q9R159; -.
DR   KO; K08612; -.
DR   OrthoDB; 162519at2759; -.
DR   PhylomeDB; Q9R159; -.
DR   TreeFam; TF314733; -.
DR   PRO; PR:Q9R159; -.
DR   Proteomes; UP000000589; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0007275; P:multicellular organism development; 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; IPR013032; EGF-like_CS.
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   Complete proteome; Developmental protein; Differentiation;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Hydrolase; Membrane;
KW   Metal-binding; Metalloprotease; Protease; Reference proteome; Signal;
KW   Spermatogenesis; Transmembrane; Transmembrane helix; Zinc; Zymogen.
FT   SIGNAL        1     50       {ECO:0000255}.
FT   PROPEP       51    213       {ECO:0000250}.
FT                                /FTId=PRO_0000029124.
FT   CHAIN       214    760       Disintegrin and metalloproteinase domain-
FT                                containing protein 25.
FT                                /FTId=PRO_0000029125.
FT   TOPO_DOM    214    706       Extracellular. {ECO:0000255}.
FT   TRANSMEM    707    727       Helical. {ECO:0000255}.
FT   TOPO_DOM    728    760       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      221    413       Peptidase M12B. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00276}.
FT   DOMAIN      419    505       Disintegrin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00068}.
FT   DOMAIN      660    676       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   MOTIF       186    193       Cysteine switch. {ECO:0000250}.
FT   COMPBIAS    506    659       Cys-rich.
FT   ACT_SITE    356    356       {ECO:0000255|PROSITE-ProRule:PRU00276,
FT                                ECO:0000255|PROSITE-ProRule:PRU10095}.
FT   METAL       188    188       Zinc; in inhibited form. {ECO:0000250}.
FT   METAL       355    355       Zinc; catalytic. {ECO:0000250}.
FT   METAL       359    359       Zinc; catalytic. {ECO:0000250}.
FT   METAL       365    365       Zinc; catalytic. {ECO:0000250}.
FT   CARBOHYD    154    154       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    164    164       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    239    239       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    240    240       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    391    391       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    690    690       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    694    694       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    336    406       {ECO:0000250}.
FT   DISULFID    370    392       {ECO:0000250}.
FT   DISULFID    372    377       {ECO:0000250}.
FT   DISULFID    477    497       {ECO:0000250}.
FT   DISULFID    647    658       {ECO:0000250}.
FT   DISULFID    652    664       {ECO:0000250}.
FT   DISULFID    666    675       {ECO:0000250}.
FT   CONFLICT      4      4       T -> R (in Ref. 2; BAB30321).
FT                                {ECO:0000305}.
FT   CONFLICT     13     13       A -> T (in Ref. 2; BAB30321).
FT                                {ECO:0000305}.
FT   CONFLICT     33     33       L -> V (in Ref. 2; BAB30321).
FT                                {ECO:0000305}.
FT   CONFLICT     44     44       R -> W (in Ref. 2; BAB30321).
FT                                {ECO:0000305}.
FT   CONFLICT    174    174       H -> Q (in Ref. 2; BAB30321).
FT                                {ECO:0000305}.
FT   CONFLICT    374    374       T -> R (in Ref. 2; BAB30321).
FT                                {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
//
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