GenomeNet

Database: UniProt
Entry: Q9R157
LinkDB: Q9R157
Original site: Q9R157 
ID   ADA18_MOUSE             Reviewed;         719 AA.
AC   Q9R157; Q60621; Q80Y08;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   13-FEB-2019, entry version 148.
DE   RecName: Full=Disintegrin and metalloproteinase domain-containing protein 18;
DE            Short=ADAM 18;
DE   AltName: Full=Disintegrin and metalloproteinase domain-containing protein 27;
DE            Short=ADAM 27;
DE   AltName: Full=Transmembrane metalloproteinase-like, disintegrin-like, and cysteine-rich protein III;
DE            Short=tMDC III;
DE   Flags: Precursor;
GN   Name=Adam18; Synonyms=Adam27, Dtgn3, Tmdc3;
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].
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   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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 405-453.
RC   STRAIN=BALB/cJ;
RX   PubMed=8146185; DOI=10.1073/pnas.91.7.2748;
RA   Weskamp G., Blobel C.P.;
RT   "A family of cellular proteins related to snake venom disintegrins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:2748-2751(1994).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Sperm surface membrane protein that may be involved in
CC       spermatogenesis and fertilization. This is a non catalytic
CC       metalloprotease-like protein.
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 16 after
CC       birth.
CC   -!- DOMAIN: A tripeptide motif (ECD) within disintegrin-like domain
CC       could be involved in the binding to egg integrin receptor and thus
CC       could mediate sperm/egg binding.
CC   -!- PTM: The prodomain and the metalloprotease-like domain are cleaved
CC       during the epididymal maturation of the spermatozoa.
CC       {ECO:0000250}.
DR   EMBL; AF167405; AAD48844.1; -; mRNA.
DR   EMBL; BC051136; AAH51136.2; -; mRNA.
DR   EMBL; U06148; AAA18427.1; -; mRNA.
DR   CCDS; CCDS22195.1; -.
DR   PIR; I48946; I48946.
DR   RefSeq; NP_034214.2; NM_010084.2.
DR   UniGene; Mm.89943; -.
DR   ProteinModelPortal; Q9R157; -.
DR   SMR; Q9R157; -.
DR   STRING; 10090.ENSMUSP00000033957; -.
DR   MEROPS; M12.958; -.
DR   iPTMnet; Q9R157; -.
DR   PhosphoSitePlus; Q9R157; -.
DR   PaxDb; Q9R157; -.
DR   PRIDE; Q9R157; -.
DR   Ensembl; ENSMUST00000033957; ENSMUSP00000033957; ENSMUSG00000031552.
DR   GeneID; 13524; -.
DR   KEGG; mmu:13524; -.
DR   UCSC; uc009lfb.2; mouse.
DR   CTD; 8749; -.
DR   MGI; MGI:105986; Adam18.
DR   eggNOG; KOG3607; Eukaryota.
DR   eggNOG; ENOG410XX2M; LUCA.
DR   GeneTree; ENSGT00940000162281; -.
DR   HOGENOM; HOG000230883; -.
DR   HOVERGEN; HBG103628; -.
DR   InParanoid; Q9R157; -.
DR   KO; K16909; -.
DR   OrthoDB; 162519at2759; -.
DR   TreeFam; TF314733; -.
DR   PRO; PR:Q9R157; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   Bgee; ENSMUSG00000031552; Expressed in 20 organ(s), highest expression level in testis.
DR   ExpressionAtlas; Q9R157; baseline and differential.
DR   Genevisible; Q9R157; MM.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005178; F:integrin binding; ISS:MGI.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
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; 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   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; PS50026; EGF_3; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Developmental protein; Differentiation;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Membrane;
KW   Reference proteome; Signal; Spermatogenesis; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     19       {ECO:0000255}.
FT   PROPEP       20    179       {ECO:0000255}.
FT                                /FTId=PRO_0000029100.
FT   CHAIN       180    719       Disintegrin and metalloproteinase domain-
FT                                containing protein 18.
FT                                /FTId=PRO_0000029101.
FT   TOPO_DOM    173    683       Extracellular. {ECO:0000255}.
FT   TRANSMEM    684    704       Helical. {ECO:0000255}.
FT   TOPO_DOM    705    719       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      180    378       Peptidase M12B. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00276}.
FT   DOMAIN      387    476       Disintegrin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00068}.
FT   DOMAIN      616    650       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   COMPBIAS    477    615       Cys-rich.
FT   CARBOHYD     61     61       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     75     75       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    121    121       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    152    152       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    173    173       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    244    244       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    331    331       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    356    356       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    405    405       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    607    607       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    614    614       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    621    621       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    289    373       {ECO:0000250}.
FT   DISULFID    332    357       {ECO:0000250}.
FT   DISULFID    334    339       {ECO:0000250}.
FT   DISULFID    447    468       {ECO:0000250}.
FT   DISULFID    620    632       {ECO:0000250}.
FT   DISULFID    626    638       {ECO:0000250}.
FT   DISULFID    640    649       {ECO:0000250}.
FT   CONFLICT    145    145       D -> N (in Ref. 1; AAD48844).
FT                                {ECO:0000305}.
FT   CONFLICT    159    159       I -> T (in Ref. 1; AAD48844).
FT                                {ECO:0000305}.
FT   CONFLICT    169    169       E -> D (in Ref. 1; AAD48844).
FT                                {ECO:0000305}.
FT   CONFLICT    276    276       R -> H (in Ref. 1; AAD48844).
FT                                {ECO:0000305}.
FT   CONFLICT    386    386       N -> K (in Ref. 1; AAD48844).
FT                                {ECO:0000305}.
FT   CONFLICT    577    577       I -> V (in Ref. 1; AAD48844).
FT                                {ECO:0000305}.
SQ   SEQUENCE   719 AA;  79210 MW;  9CD092E12625DA6D CRC64;
     MPLLFILAEL AMLFARLDSE GICLHITVPQ KIEPRKGGDA EGKVTYVITI DGKPYSLHLR
     NHSFLSQNFL VYTYNETGSL YSDSSHFLAH CHYRGYVDEV PNSIVTLSIC SGLRGFLQLE
     NVSYGIEPLE SSARFEHIVY QVKSDSSMLA GNDSHVWQID QLDKGHFNEQ DKNHSQLLPQ
     SLKLHIIVGK FLFDYMGSDI MAITQKIFQI IGLVNAMLTQ LKLSVVLASL ELWSDKNHIS
     TDGNATDILQ RLLDWKRDYL TLQSNEITHL LIYRRRPKYI GAASPGEICS KSYVAGVGMY
     PEDIGLEGFS VVITQLIGLH IGLTYDDNIR NCSCPSAPCI MQQGALSSSG KKTFSNCSLH
     DYMHYVSNFD TQCLGDLSNV HVLQPNQAVC GNGIMEAGEE CDCGNETECQ FKECCDHETC
     RLKGSAQCGS GACCMPTCEL SASGTPCRKA VDPECDFTEY CDGSSSHCVP DTFALNGHLC
     RLGSAYCYNG RCQALNDQCV SLFGKGSQGA SYACFEKVNS PRENLANCDS KDSYSVPCGQ
     QDVLCGKLAC FRPPKNYKSP SQSVVYSYVH DSVCLSILPG LSMRSDGRDS AYVADGTVCG
     PQMYCINGTC KEVNFTGNDC NATKKCKGNG ICNNFGNCQC FPDYRPPDCN LQIGSPGGSI
     DDGNTLRTES AFATKRLSKN EDSWVILGFF IFLPFIVTFL VGIMKRNERK IVPQGEHKI
//
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