ADA18_MOUSE
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 03-AUG-2022, entry version 164.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC 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 spermatogenesis
RT 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 project:
RT 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 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 protein.
CC -!- TISSUE SPECIFICITY: Expressed specifically in testis.
CC -!- DEVELOPMENTAL STAGE: Adult levels are reached by day 16 after birth.
CC -!- DOMAIN: A tripeptide motif (ECD) within disintegrin-like domain could
CC be involved in the binding to egg integrin receptor and thus could
CC mediate sperm/egg binding.
CC -!- PTM: The prodomain and the metalloprotease-like domain are cleaved
CC during the epididymal maturation of the spermatozoa. {ECO:0000250}.
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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 AlphaFoldDB; Q9R157; -.
DR SMR; Q9R157; -.
DR STRING; 10090.ENSMUSP00000033957; -.
DR MEROPS; M12.958; -.
DR GlyGen; Q9R157; 12 sites.
DR iPTMnet; Q9R157; -.
DR PhosphoSitePlus; Q9R157; -.
DR PaxDb; Q9R157; -.
DR PRIDE; Q9R157; -.
DR ProteomicsDB; 281936; -.
DR Antibodypedia; 23870; 40 antibodies from 8 providers.
DR DNASU; 13524; -.
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 VEuPathDB; HostDB:ENSMUSG00000031552; -.
DR eggNOG; KOG3607; Eukaryota.
DR GeneTree; ENSGT00940000162281; -.
DR InParanoid; Q9R157; -.
DR OMA; GPQMYCV; -.
DR OrthoDB; 162519at2759; -.
DR PhylomeDB; Q9R157; -.
DR TreeFam; TF314733; -.
DR BioGRID-ORCS; 13524; 1 hit in 73 CRISPR screens.
DR PRO; PR:Q9R157; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9R157; protein.
DR Bgee; ENSMUSG00000031552; Expressed in spermatocyte and 9 other tissues.
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:0007339; P:binding of sperm to zona pellucida; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
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 Developmental protein; Differentiation; Disulfide bond; EGF-like domain;
KW Glycoprotein; Membrane; Reference proteome; Signal; Spermatogenesis;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..179
FT /evidence="ECO:0000255"
FT /id="PRO_0000029100"
FT CHAIN 180..719
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein 18"
FT /id="PRO_0000029101"
FT TOPO_DOM 173..683
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 684..704
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 705..719
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 180..378
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 387..476
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DOMAIN 616..650
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 607
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 614
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 621
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 289..373
FT /evidence="ECO:0000250"
FT DISULFID 332..357
FT /evidence="ECO:0000250"
FT DISULFID 334..339
FT /evidence="ECO:0000250"
FT DISULFID 447..468
FT /evidence="ECO:0000250"
FT DISULFID 620..632
FT /evidence="ECO:0000250"
FT DISULFID 626..638
FT /evidence="ECO:0000250"
FT DISULFID 640..649
FT /evidence="ECO:0000250"
FT CONFLICT 145
FT /note="D -> N (in Ref. 1; AAD48844)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="I -> T (in Ref. 1; AAD48844)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="E -> D (in Ref. 1; AAD48844)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="R -> H (in Ref. 1; AAD48844)"
FT /evidence="ECO:0000305"
FT CONFLICT 386
FT /note="N -> K (in Ref. 1; AAD48844)"
FT /evidence="ECO:0000305"
FT CONFLICT 577
FT /note="I -> V (in Ref. 1; AAD48844)"
FT /evidence="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
