GenomeNet

Database: UniProt
Entry: Q95194
LinkDB: Q95194
Original site: Q95194 
ID   ADA18_MACFA             Reviewed;         746 AA.
AC   Q95194;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   10-APR-2019, entry version 90.
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: Precursor;
GN   Name=ADAM18; Synonyms=TMDC3;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RX   PubMed=9665629; DOI=10.1093/molehr/4.5.429;
RA   Frayne J., Jury J.A., Barker H.L., Perry A.C.F., Jones R., Hall L.;
RT   "Macaque MDC family of proteins: sequence analysis, tissue
RT   distribution and processing in the male reproductive tract.";
RL   Mol. Hum. Reprod. 4:429-437(1998).
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
CC       protein.
CC   -!- TISSUE SPECIFICITY: Expressed predominantly in adult and
CC       prepubertal testis.
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. {ECO:0000250}.
CC   -!- PTM: The prodomain and the metalloprotease-like domain are cleaved
CC       during the epididymal maturation of the spermatozoa.
DR   EMBL; Y08617; CAA69909.1; -; mRNA.
DR   UniGene; Mfa.611; -.
DR   ProteinModelPortal; Q95194; -.
DR   SMR; Q95194; -.
DR   STRING; 9541.XP_005563194.1; -.
DR   MEROPS; M12.957; -.
DR   PRIDE; Q95194; -.
DR   HOVERGEN; HBG103628; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; 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   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; 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;
KW   EGF-like domain; Glycoprotein; Membrane; Signal; Spermatogenesis;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     16       {ECO:0000255}.
FT   PROPEP       17    183       {ECO:0000255}.
FT                                /FTId=PRO_0000029098.
FT   CHAIN       184    746       Disintegrin and metalloproteinase domain-
FT                                containing protein 18.
FT                                /FTId=PRO_0000029099.
FT   TOPO_DOM    177    687       Extracellular. {ECO:0000255}.
FT   TRANSMEM    688    708       Helical. {ECO:0000255}.
FT   TOPO_DOM    709    746       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      184    381       Peptidase M12B. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00276}.
FT   DOMAIN      390    479       Disintegrin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00068}.
FT   DOMAIN      620    654       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   COMPBIAS    480    619       Cys-rich.
FT   CARBOHYD     36     36       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    122    122       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    149    149       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    156    156       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    177    177       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    294    294       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    359    359       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    465    465       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    611    611       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    625    625       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    293    376       {ECO:0000250}.
FT   DISULFID    335    360       {ECO:0000250}.
FT   DISULFID    337    342       {ECO:0000250}.
FT   DISULFID    450    471       {ECO:0000250}.
FT   DISULFID    624    636       {ECO:0000250}.
FT   DISULFID    630    642       {ECO:0000250}.
FT   DISULFID    644    653       {ECO:0000250}.
SQ   SEQUENCE   746 AA;  84449 MW;  1D8C7E9071502E30 CRC64;
     MFFLLALLTE LGRLQAHVGS EGIFLHVTVP RKILSNDSEV SERKMIYIIT IDGQPYTLHL
     RKQSFLPQNF LVYTYNEAGS LHSESPYFMM HCHYQGYAAE FPNSFVTLSI CSGLRGFLQF
     ENVSYGIEPL ESSARFEHII YQMKNNDPNV SILAENYSHI WQKDQSYKVP LNSQKKNLSK
     LLPQYLEIYI IVEKALYDYM GSEMMAVTQK IVQVIGLVNT MFTQFRLTVT LSSLELWSNE
     NQISTSGDAD DILQRFLAWK RDYLILRPHD IAYLLVYRKH PKYVGATFPG TICNESYDAG
     IAMYPDAIDL EGFSVIIAQL LGLNVGLTYD DITQCFCLRA TCIMNHEAMS ARGIKIFSNC
     SMHDYRYFVS KFEAKCLQKL SNLQPLHQNQ PVCGNGILES NEECDCGNKK ECQFKKCCDY
     NTCKLKGSVK CGSGPCCTSK CELSIVGTPC RKSVDPECDF TEYCNGTSSD CVPDTYALNG
     HLCKLGTAYC YNGQCQTTDN QCAKIFGKGA QGAPFACFKE VNSLHETSEN CGFKNSQPLP
     CERKDVLCGK LACVQPHKNA YKSDIQYTVY SYIQDHVCVS IATGSSMRSD GTDNAYVADG
     TMCGPEMYCV NKTCRKVHLT GYNCNTTTKC KGKGICNNFG NCQCFPGHKP PDCKFQFGSP
     GGSIDDGNFQ KSDEFYTEKG YNAHWNNWFI LSFYIVLPFF IIFTIVIFKR NEIRKLCNRE
     NTELIHPLYQ KAMMWNINIA QNFRSK
//
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