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Database: UniProt
Entry: Q60472
LinkDB: Q60472
Original site: Q60472 
ID   ADAM5_CAVPO             Reviewed;         777 AA.
AC   Q60472;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JAN-2019, entry version 91.
DE   RecName: Full=Disintegrin and metalloproteinase domain-containing protein 5;
DE   Flags: Precursor;
GN   Name=ADAM5;
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia;
OC   Hystricomorpha; Caviidae; Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Testis;
RX   PubMed=7750654; DOI=10.1006/dbio.1995.1152;
RA   Wolfsberg T.G., Straight P.D., Gerena R.L., Huovila A.-P.,
RA   Primakoff P., Myles D.G., White J.M.;
RT   "ADAM, a widely distributed and developmentally regulated gene family
RT   encoding membrane proteins with a disintegrin and metalloprotease
RT   domain.";
RL   Dev. Biol. 169:378-383(1995).
CC   -!- FUNCTION: This is a non catalytic metalloprotease-like protein.
CC       May play a role in sperm-egg fusion (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with TEX101. {ECO:0000250|UniProtKB:Q3TTE0}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Detected in testis.
CC       {ECO:0000269|PubMed:7750654}.
CC   -!- PTM: Subject to proteolytic processing during epididymal transit
CC       of spermatozoa. {ECO:0000250}.
CC   -!- CAUTION: Not expected to have protease activity. {ECO:0000305}.
DR   EMBL; U22060; AAA74918.1; -; mRNA.
DR   PIR; I48100; I48100.
DR   RefSeq; NP_001166570.1; NM_001173099.1.
DR   ProteinModelPortal; Q60472; -.
DR   SMR; Q60472; -.
DR   MEROPS; M12.953; -.
DR   PRIDE; Q60472; -.
DR   GeneID; 100379225; -.
DR   HOVERGEN; HBG103628; -.
DR   InParanoid; Q60472; -.
DR   OrthoDB; 162519at2759; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
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; IPR013032; EGF-like_CS.
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; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Disulfide bond; EGF-like domain; Glycoprotein;
KW   Membrane; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     16       {ECO:0000255}.
FT   PROPEP       17    142       {ECO:0000255}.
FT                                /FTId=PRO_0000349298.
FT   CHAIN       143    777       Disintegrin and metalloproteinase domain-
FT                                containing protein 5.
FT                                /FTId=PRO_5000144556.
FT   TOPO_DOM     17    706       Extracellular. {ECO:0000255}.
FT   TRANSMEM    707    727       Helical. {ECO:0000255}.
FT   TOPO_DOM    728    777       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      185    382       Peptidase M12B. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00276}.
FT   DOMAIN      396    485       Disintegrin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00068}.
FT   DOMAIN      633    667       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   CARBOHYD     49     49       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    123    123       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    566    566       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    294    377       {ECO:0000250}.
FT   DISULFID    336    361       {ECO:0000250}.
FT   DISULFID    338    343       {ECO:0000250}.
FT   DISULFID    456    477       {ECO:0000250}.
FT   DISULFID    637    649       {ECO:0000250}.
FT   DISULFID    643    655       {ECO:0000250}.
FT   DISULFID    657    666       {ECO:0000250}.
SQ   SEQUENCE   777 AA;  87407 MW;  9A303C414AF25614 CRC64;
     MFLVLVLLTG LGRLYAGNNP RKTFVQTTVP ERISSVDTRR HLEHNVAYNI TLKGKSYVVR
     LKKESFLSSG SVIYFYDNRG VQRSQPLLPE MDCSYSGYVA GFPHSRVVFA TCLGLRGVIQ
     FENVSYAIEP LEVLSGFTHM IYEENNDNTH VPLFGKNNSY ARIHNLESQG RRSVHKTTVS
     KLSPRYIDMY IVVNKNLFDY LGSDIKTVTQ KIIQVIGLVN AMFTQLKLHV LISSIEIWSR
     SNKVTNTRRP DDDLFRFSDW KRKHVSLKSH YVAYLLTFDK YPESIGATFP ENICNEEYAS
     GIAVYPAGLS LESFAVIIVQ LLSLSAGVMY DTSDSCYCST DVCTMTQEAV FASGLKDFST
     CSMDNFKYFA SQYGLTCLRN TSYDMPIYKQ FPPRRRRICG NSIREEGEEC DCGTLRNCTH
     KKCCDPMQCR MKKGAKCGTG PCCTVDCQFQ KANVLCRKSV DKDCDFDEYC NGRSGDCVHD
     TYAQNGHFCD SGGAFCFNGR CRTHDRQCQA LIGGDSRGAP FACYDEVNSR GDVYGNCGRH
     QCYIQHALCG KLVCTWPHKQ LVSRVNLSVV YAHVRDDICV ATTKTVRKII RDLSLTTVLL
     PEDRDETFVE DGTICGPGQY CDKWFCKEVQ FINNGSCNAE IHCQGRGICN NLDNCHCHKG
     FVPPECAPKK GQFGSLDDGH LVETTKTSGF RKINMRRGYV VLSTKRFQLI FYIGIPVIII
     VAAILIKQNQ LGKLFCRGEK EHMSSVSEDG SRSVTLSATE SKFPADTEHS NKEEDAQ
//
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