ADA29_MOUSE
ID ADA29_MOUSE Reviewed; 763 AA.
AC Q811Q4;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Disintegrin and metalloproteinase domain-containing protein 29;
DE Short=ADAM 29;
DE Flags: Precursor;
GN Name=Adam29;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ICR; TISSUE=Testis;
RX PubMed=15028286; DOI=10.1016/j.ygeno.2003.10.001;
RA Choi I., Oh J., Cho B.-N., Ahnn J., Jung Y.-K., Han Kim D., Cho C.;
RT "Characterization and comparative genomic analysis of intronless Adams with
RT testicular gene expression.";
RL Genomics 83:636-646(2004).
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: May be involved in spermatogenesis and fertilization. Seems
CC to be a non catalytic metalloprotease-like protein (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
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DR EMBL; AY190759; AAO38663.1; -; mRNA.
DR EMBL; BC119089; AAI19090.1; -; mRNA.
DR EMBL; BC119091; AAI19092.1; -; mRNA.
DR CCDS; CCDS22311.1; -.
DR AlphaFoldDB; Q811Q4; -.
DR SMR; Q811Q4; -.
DR STRING; 10090.ENSMUSP00000054292; -.
DR MEROPS; M12.984; -.
DR GlyGen; Q811Q4; 8 sites.
DR iPTMnet; Q811Q4; -.
DR PhosphoSitePlus; Q811Q4; -.
DR PaxDb; Q811Q4; -.
DR PRIDE; Q811Q4; -.
DR ProteomicsDB; 285885; -.
DR MGI; MGI:2676326; Adam29.
DR eggNOG; KOG3607; Eukaryota.
DR InParanoid; Q811Q4; -.
DR PhylomeDB; Q811Q4; -.
DR PRO; PR:Q811Q4; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q811Q4; protein.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:1990913; C:sperm head plasma membrane; IDA:MGI.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008584; P:male gonad development; IBA:GO_Central.
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; 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 PRINTS; PR00289; DISINTEGRIN.
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.
PE 2: Evidence at transcript level;
KW Disulfide bond; EGF-like domain; Glycoprotein; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT PROPEP 32..200
FT /evidence="ECO:0000250"
FT /id="PRO_0000373775"
FT CHAIN 201..763
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein 29"
FT /id="PRO_0000373776"
FT TOPO_DOM 201..684
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 685..705
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 706..763
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 205..396
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 403..489
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DOMAIN 631..660
FT /note="EGF-like"
FT REGION 712..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..763
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 164
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 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 374
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 424
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 475
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 584
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 313..390
FT /evidence="ECO:0000250"
FT DISULFID 353..375
FT /evidence="ECO:0000250"
FT DISULFID 355..360
FT /evidence="ECO:0000250"
FT DISULFID 461..481
FT /evidence="ECO:0000250"
FT DISULFID 631..642
FT /evidence="ECO:0000250"
FT DISULFID 636..648
FT /evidence="ECO:0000250"
FT DISULFID 650..659
FT /evidence="ECO:0000250"
SQ SEQUENCE 763 AA; 86445 MW; F9EF082C3BFBBA80 CRC64;
MNMIEALLSM RVLFLTQVFG IFLCFPGLTK AGHLHYHSSI EVVIPMKVTE KTRGMNLPNW
ISYSLKLGGQ RYIIHMKIKN LFLTRHLPVF TYSDQDSLLE DYPFVQDDCY YQGYVEGDSE
SLVSLSSCFG GFHGLLEINN IVYEIMPKKF SRKFEHLVYK VDINKTESRG SSLMQDNITC
QVELQKSGNP ILKQSSFEDW WTHTKIVELV VVVDKTLYDH YGNYTVMLSD LYSVINIVDT
IYEVIGIKIL LVGVEVWNKK NLIVIDDVSK SLRLYCRWKA SNFLHRLKHD VSHLFIYRHL
RGLSGIGSTG GICDPKRSCA VVTFIDRTLN LRAIGVAHHL GHNLGMKHDE DICKCSYSKC
IMHMDSPPIP KFSNCSYNYF WSYTVKNTRC LMENMYTKDI FDRTRCGNGV VEDKEQCDCG
SLRNCTNDLC CMSNCTLSTG SSCAFGLCCK NCQFLPSGTL CRKRDNICDL PEWCNGTSHE
CPDDAYVEDG IPCGVSAYCY EKQCNDRNEH CRQIFGQNAK TASVHCYREI NTKGDRFGHC
GLQGPTYIKC KSNDALCGRI QCDNVVQIPN MKDHSTIHFA LVKNVSCWGT DYHTGTSLTD
IGDVKDGTEC EQNHICINRH CVHISTLDSN CTPAFCNYRG ICNNKHHCHC NFHWDPPNCM
IRGHGGSVDS GLPPKTNKKK HFFYLLLLQL IILACLLSCL LWLLFNIKGS KRKPQVQPTP
VKTKKVSKKV PSQKPSPVPS PSLPQLRMPS RSASPTSSIK STN
