ADAM5_RAT
ID ADAM5_RAT Reviewed; 709 AA.
AC Q5BK84;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Disintegrin and metalloproteinase domain-containing protein 5;
DE AltName: Full=Transmembrane metalloproteinase-like, disintegrin-like, and cysteine-rich protein II;
DE Short=tMDC II;
DE Flags: Precursor;
GN Name=Adam5; Synonyms=Tmdc2;
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], DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
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).
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).
CC -!- FUNCTION: This is a non catalytic metalloprotease-like protein. May
CC play a role in sperm-egg fusion (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with TEX101. {ECO:0000250|UniProtKB:Q3TTE0}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Detected in testis. {ECO:0000269|PubMed:9291465}.
CC -!- DEVELOPMENTAL STAGE: Not detectable in newborns. First detected 23 days
CC after birth. Levels increase up to 28 days after birth, and remain
CC constant in adults. {ECO:0000269|PubMed:9291465}.
CC -!- CAUTION: Not expected to have protease activity. {ECO:0000305}.
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DR EMBL; BC091169; AAH91169.1; -; mRNA.
DR RefSeq; NP_064699.1; NM_020303.1.
DR AlphaFoldDB; Q5BK84; -.
DR SMR; Q5BK84; -.
DR STRING; 10116.ENSRNOP00000055132; -.
DR MEROPS; M12.953; -.
DR PaxDb; Q5BK84; -.
DR PRIDE; Q5BK84; -.
DR Ensembl; ENSRNOT00000058330; ENSRNOP00000055132; ENSRNOG00000017518.
DR GeneID; 498654; -.
DR KEGG; rno:498654; -.
DR UCSC; RGD:621471; rat.
DR CTD; 255926; -.
DR RGD; 621471; Adam5.
DR eggNOG; KOG3607; Eukaryota.
DR GeneTree; ENSGT00940000162784; -.
DR HOGENOM; CLU_012714_4_3_1; -.
DR InParanoid; Q5BK84; -.
DR OrthoDB; 162519at2759; -.
DR PhylomeDB; Q5BK84; -.
DR PRO; PR:Q5BK84; -.
DR Proteomes; UP000002494; Chromosome 16.
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:0008584; P:male gonad development; IEP:RGD.
DR GO; GO:0006508; P:proteolysis; 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; 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 Disulfide bond; EGF-like domain; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT PROPEP 1..98
FT /evidence="ECO:0000255"
FT /id="PRO_0000349302"
FT CHAIN 99..709
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein 5"
FT /id="PRO_0000349303"
FT TOPO_DOM 1..649
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 650..670
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 671..709
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 141..334
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 346..434
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DOMAIN 581..615
FT /note="EGF-like; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 690..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 247..329
FT /evidence="ECO:0000250"
FT DISULFID 289..314
FT /evidence="ECO:0000250"
FT DISULFID 291..296
FT /evidence="ECO:0000250"
FT DISULFID 406..426
FT /evidence="ECO:0000250"
FT DISULFID 585..597
FT /evidence="ECO:0000250"
FT DISULFID 591..603
FT /evidence="ECO:0000250"
FT DISULFID 605..614
FT /evidence="ECO:0000250"
SQ SEQUENCE 709 AA; 79907 MW; 5B25B3D49E6AA039 CRC64;
MKTPISSILK SNGLGIFLYR SFITSTAVSY TYDRQDVRHS QSLSSLKNCN YNGYVAGFPN
SIVSLTVCSG LRGMIQFENV SYGIEPVETL SGFIHVIYEN TNQQAKIPDL GENQTYSWSD
ELDYQFRSNM KKSGFAVLRP RYIKTDIVVD KKLFDYMGSD TRVVLQKVIQ IIGFINTMFS
KLKLTVLINS VEIWSKENRI DFPEAPENLL VQFLHWKHKY RPQHISYLLA FVEHPASTGA
LYPGNLCKPI YGAAIALYPK GLSLESYSVI VLQLLSIGIG LTYDNADSCH CTGDVCLMTP
KAIYSGGVKD FSTCSLDDFK YLSTQDLECL QDLPMERQKK KPSRPRRICG NGILEMNEQC
DCGTLKNCTH KKCCDPMSCR LKSKAVCGSG ECCGQDCKVK PVNVLCRKSK NECDFEEYCN
GNDAYCVPDT FARNGQYCDS GQAFCYSGLC MTSNNQCMNL LGKYVRGASF ACYEEFNSRN
DRFGNCIRKF CSFENSLCGK LVCTWPFKRL LMKDNMSAAY GQIRDDLCIS LYKGGRPLKT
TLSTYSDMSE RDETFVKDGT ICGPDMFCLE TQCKETRFLV DFQQCNTSRD CNDHGVCNNF
NHCHCDKGYN PPYCESVKGQ FGSIDDGHKY YIDEGKSAKQ QNRGIHPKQQ LQLILYITLP
LIMIISAVFI KQSKLSRLCG RERSEGTSCI TEDSVSNTKM TTNEGSTLH
