ADA18_MACFA
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 03-AUG-2022, entry version 100.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC 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 distribution and
RT 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 protein.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in adult and prepubertal
CC testis.
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.
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DR EMBL; Y08617; CAA69909.1; -; mRNA.
DR AlphaFoldDB; Q95194; -.
DR SMR; Q95194; -.
DR STRING; 9541.XP_005563194.1; -.
DR MEROPS; M12.957; -.
DR eggNOG; KOG3607; Eukaryota.
DR Proteomes; UP000233100; 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: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; 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; EGF-like domain;
KW Glycoprotein; Membrane; Reference proteome; Signal; Spermatogenesis;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT PROPEP 17..183
FT /evidence="ECO:0000255"
FT /id="PRO_0000029098"
FT CHAIN 184..746
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein 18"
FT /id="PRO_0000029099"
FT TOPO_DOM 177..687
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 688..708
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 709..746
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 184..381
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 390..479
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DOMAIN 620..654
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 359
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 611
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 625
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 293..376
FT /evidence="ECO:0000250"
FT DISULFID 335..360
FT /evidence="ECO:0000250"
FT DISULFID 337..342
FT /evidence="ECO:0000250"
FT DISULFID 450..471
FT /evidence="ECO:0000250"
FT DISULFID 624..636
FT /evidence="ECO:0000250"
FT DISULFID 630..642
FT /evidence="ECO:0000250"
FT DISULFID 644..653
FT /evidence="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
