ID G7MLY3_MACMU Unreviewed; 958 AA.
AC G7MLY3;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=ADAM metallopeptidase domain 22 {ECO:0008006|Google:ProtNLM};
GN ORFNames=EGK_13962 {ECO:0000313|EMBL:EHH17537.1};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544 {ECO:0000313|EMBL:EHH17537.1};
RN [1] {ECO:0000313|EMBL:EHH17537.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR-5 {ECO:0000313|EMBL:EHH17537.1};
RX PubMed=22002653; DOI=10.1038/nbt.1992;
RA Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., Li Q.,
RA Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., Huang Z.,
RA Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., Huang Y.,
RA Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., Li B., Liu X.,
RA Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., Li Y., Wang W.,
RA Katze M.G., Su B., Nielsen R., Yang H., Wang J., Wang X., Wang J.;
RT "Genome sequencing and comparison of two nonhuman primate animal models,
RT the cynomolgus and Chinese rhesus macaques.";
RL Nat. Biotechnol. 29:1019-1023(2011).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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DR EMBL; CM001255; EHH17537.1; -; Genomic_DNA.
DR AlphaFoldDB; G7MLY3; -.
DR MEROPS; M12.978; -.
DR Proteomes; UP000013456; Chromosome 3.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; Collagenase (Catalytic Domain); 1.
DR Gene3D; 4.10.70.10; Disintegrin domain; 1.
DR Gene3D; 2.10.25.10; Laminin; 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; IPR013111; EGF_extracell.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR034027; Reprolysin_adamalysin.
DR PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR PANTHER; PTHR11905:SF14; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 22; 1.
DR Pfam; PF08516; ADAM_CR; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF07974; EGF_2; 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; Blood coagulation inhibitor (disintegrin); 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS00427; DISINTEGRIN_1; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
DR PROSITE; PS00022; EGF_1; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00068}; EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 789..812
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 291..490
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 496..583
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT REGION 837..958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..864
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 907..929
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 555..575
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
SQ SEQUENCE 958 AA; 105888 MW; 1BA13F8331DA4D25 CRC64;
MGRMGKGCLA SGPRSWMLSD ELVQGSPAVV SASFPDGFRE GGGGGDFRSG DVGPQDGGVR
VRVIIFAFSL HSLLSPFLPG GDASLMELEK RKENRFLERQ SIVPLRLIYR SGGEDETRHD
ALDTRVRGDP GGRQLTHVDQ ASFQVDAFGT SFILDVVLNH DLLSSEYVER HIEHGGKTVE
VKGGEHCYYQ GHIRGNPASF VALSTCHGLH GMFYDGNHTY LIEPEENDTT QEDFHFHSVY
KSRLFEFPLD DLPSEFQQVN ITPPKFILKP RPKRSKRQLR RYPRNVEEET KYIELMIVND
HLMFKKHRLS VVHTNTYAKS VVNMADIIYK DQLKTRIVLV AMETWATDNK FAISENPLIT
LREFMKYRRD FIKEKSDAVH LFSGSQFESS RSGAAYIGGI CSLLKGGGVN EFGKTDLMAV
TLAQSLAHNI GIISDKRKLA SGECKCEDTW SGCIMGDTGY YLPKKFTQCN VEEYHDFLNS
GGGACLFNKP SKLLDPPECG NGFIETGEEC DCGTPAECVL EGAECCKKCT LTQDSQCSDG
LCCKKCKFQP MGTVCREAVN DCDIRETCSG NSSQCAPNIH KMDGYSCDGV QGICFGGRCK
TRDRQCKYIW GQKVTASDKY CYEKLNIEGT EKGNCGKNKD TWIQCNKRDV LCGYLLCTNI
GNIPRLGELD GEITSTLVVQ QGRTLNCSGG HVKLEEDVDL GYVEDGTPCG PQMMCLEHRC
LPVASFNFST CLSSKEGTIC SGNGVCSNEL KCVCNRHWIG SDCNTYFPHN DDAKTGITLS
GNGVAGTNII IGIIAGTILV LALILGITAW GYKNYREQRQ LPQGDYVKKP GDGDSFYSDI
PPGVSTNSAS SSKKRSNGLS HSWSERIPDT KHISDICENG RPRSNSWQGN LGGNKKKIRG
KRFRPRSNST ETLSPAKSPS SSTGSIASSR KYPYPMPPLP DEEKKVNRQS ARLWETSI
//
