ADAM5_CAVPO
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 03-AUG-2022, entry version 100.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC 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., Primakoff P.,
RA 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 domain.";
RL Dev. Biol. 169:378-383(1995).
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 type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Detected in testis. {ECO:0000269|PubMed:7750654}.
CC -!- PTM: Subject to proteolytic processing during epididymal transit of
CC spermatozoa. {ECO:0000250}.
CC -!- CAUTION: Not expected to have protease activity. {ECO:0000305}.
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DR EMBL; U22060; AAA74918.1; -; mRNA.
DR PIR; I48100; I48100.
DR RefSeq; NP_001166570.1; NM_001173099.1.
DR AlphaFoldDB; Q60472; -.
DR SMR; Q60472; -.
DR MEROPS; M12.957; -.
DR GeneID; 100379225; -.
DR KEGG; cpoc:100379225; -.
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 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; Glycoprotein; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT PROPEP 17..142
FT /evidence="ECO:0000255"
FT /id="PRO_0000349298"
FT CHAIN 143..777
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein 5"
FT /id="PRO_5000144556"
FT TOPO_DOM 17..706
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 707..727
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 728..777
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 185..382
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 396..485
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DOMAIN 633..667
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 744..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..764
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 566
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 294..377
FT /evidence="ECO:0000250"
FT DISULFID 336..361
FT /evidence="ECO:0000250"
FT DISULFID 338..343
FT /evidence="ECO:0000250"
FT DISULFID 456..477
FT /evidence="ECO:0000250"
FT DISULFID 637..649
FT /evidence="ECO:0000250"
FT DISULFID 643..655
FT /evidence="ECO:0000250"
FT DISULFID 657..666
FT /evidence="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
