ADA18_RAT
ID ADA18_RAT Reviewed; 445 AA.
AC P97776;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Disintegrin and metalloproteinase domain-containing protein 18;
DE Short=ADAM 18;
DE AltName: Full=Transmembrane metalloproteinase-like, disintegrin-like, and cysteine-rich protein III;
DE Short=tMDC III;
DE Flags: Fragment;
GN Name=Adam18; Synonyms=Tmdc3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Testis;
RX PubMed=9291465;
RX DOI=10.1002/(sici)1098-2795(199710)48:2<159::aid-mrd3>3.0.co;2-r;
RA Frayne J., Jury J.A., Barker H.L., Hall L.;
RT "Rat MDC family of proteins: sequence analysis, tissue distribution, and
RT expression in prepubertal and adult rat testis.";
RL Mol. Reprod. Dev. 48:159-167(1997).
CC -!- FUNCTION: Sperm surface membrane protein that may be involved in
CC spermatogenesis and fertilization. This is a non catalytic
CC metalloprotease-like protein (By similarity). {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 28 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. {ECO:0000250}.
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; Y11490; CAA72276.1; -; mRNA.
DR AlphaFoldDB; P97776; -.
DR SMR; P97776; -.
DR STRING; 10116.ENSRNOP00000023805; -.
DR MEROPS; M12.958; -.
DR GlyGen; P97776; 6 sites.
DR PaxDb; P97776; -.
DR UCSC; RGD:620405; rat.
DR RGD; 620405; Adam18.
DR eggNOG; KOG3607; Eukaryota.
DR InParanoid; P97776; -.
DR PhylomeDB; P97776; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 Gene3D; 3.40.390.10; -; 1.
DR Gene3D; 4.10.70.10; -; 1.
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 Pfam; PF08516; ADAM_CR; 1.
DR Pfam; PF00200; Disintegrin; 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; PS50026; EGF_3; 1.
PE 2: Evidence at transcript level;
KW Developmental protein; Differentiation; Disulfide bond; EGF-like domain;
KW Glycoprotein; Membrane; Reference proteome; Spermatogenesis; Transmembrane;
KW Transmembrane helix.
FT CHAIN <1..445
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein 18"
FT /id="PRO_0000078208"
FT TOPO_DOM <1..409
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 431..445
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN <1..106
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 113..202
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DOMAIN 342..376
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CARBOHYD 19
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 18..101
FT /evidence="ECO:0000250"
FT DISULFID 60..85
FT /evidence="ECO:0000250"
FT DISULFID 62..67
FT /evidence="ECO:0000250"
FT DISULFID 173..194
FT /evidence="ECO:0000250"
FT DISULFID 346..358
FT /evidence="ECO:0000250"
FT DISULFID 352..364
FT /evidence="ECO:0000250"
FT DISULFID 366..375
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 445 AA; 48200 MW; E6D4758377CDA84B CRC64;
IYRKHLKYIG ATSPGELCNE SYVAGVGTYP EDIGLEGLSM VITQLIGLHI GLTYDDVDNC
SCPRAPCIMQ PEALSSSGMK TFSNCSVHDY THYASKLDMQ CLGDLSNVLQ PKQSVCGNGI
VEGSEECDCG NETECQFKEC CNHETCKLKG SAQCGSGTCC TPKCELSAAG TPCRKAVDPE
CDFTEYCDGS SSHCVPDTFA LDGHLCRLGS AYCYNGRCQA LNDQCVSLFG KGSQGASYAC
FEKVNSQREN LANCDSKNSY SLPCGQKDVL CGKLACFRPN KNYKSSTQSV LYSYVHGSVC
LSIPPGLSMR SDGKDNAYVA DGTVCGPQMY CINGSCKEVN FTGNDCNAAK KCKGNGICNN
FGHCQCFPDY RPPDCNLQIG SPGGSIDDGN LLRTDSALAT KRLSQHADSW VILGFFIFLP
FIMTLFLGII KRNERKIVPQ KEQER
