ID G7P769_MACFA Unreviewed; 1211 AA.
AC G7P769;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=ADAM metallopeptidase with thrombospondin type 1 motif 16 {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=EGM_14913 {ECO:0000313|EMBL:EHH54140.1};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1] {ECO:0000313|EMBL:EHH54140.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CE-4 {ECO:0000313|EMBL:EHH54140.1};
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR613273-2};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR613273-2};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
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; CM001281; EHH54140.1; -; Genomic_DNA.
DR AlphaFoldDB; G7P769; -.
DR MEROPS; M12.026; -.
DR eggNOG; KOG3538; Eukaryota.
DR Proteomes; UP000009130; Chromosome 6.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04273; ZnMc_ADAMTS_like; 1.
DR Gene3D; 2.60.120.830; -; 1.
DR Gene3D; 3.40.1620.60; -; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 5.
DR InterPro; IPR013273; ADAMTS/ADAMTS-like.
DR InterPro; IPR041645; ADAMTS_CR_2.
DR InterPro; IPR045371; ADAMTS_CR_3.
DR InterPro; IPR010294; ADAMTS_spacer1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR010909; PLAC.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR13723:SF140; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 16; 1.
DR PANTHER; PTHR13723; ADAMTS A DISINTEGRIN AND METALLOPROTEASE WITH THROMBOSPONDIN MOTIFS PROTEASE; 1.
DR Pfam; PF17771; ADAMTS_CR_2; 1.
DR Pfam; PF19236; ADAMTS_CR_3; 1.
DR Pfam; PF05986; ADAMTS_spacer1; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF08686; PLAC; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR Pfam; PF19030; TSP1_ADAMTS; 4.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00209; TSP1; 6.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 5.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50900; PLAC; 1.
DR PROSITE; PS50092; TSP1; 5.
PE 4: Predicted;
KW Calcium {ECO:0000256|PIRSR:PIRSR613273-2};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR613273-3};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR613273-2};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR613273-2};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 275..480
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1173..1210
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT REGION 15..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 419
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 278
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 278
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 366
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 418
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 422
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 428
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 475
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 478
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 478
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 351..402
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 377..384
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 396..475
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 435..459
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 503..530
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 514..537
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 525..556
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 550..561
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 585..622
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 589..627
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 600..612
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EHH54140.1"
FT NON_TER 1211
FT /evidence="ECO:0000313|EMBL:EHH54140.1"
SQ SEQUENCE 1211 AA; 134400 MW; 65D288A54484CC36 CRC64;
LLLAQVAEQA PACAMGPAAA APGSSSVPRP PPPAERPGWM EKGEYDLVSA YEVDHRGDYV
SHEIMHHQRR RRAVTMSGVE SLHLRLKGSR HDFHMDLRTS SSLVAPGFIV QTLGKTGTKS
VQTLLPEDFC FYQGSLRSHR NSSVALSTCQ GLSGMIRTEE ADYFLKPLPS HLLWKLGSAA
QGSSPSHILY KRSTEPHAPG ASEVLVTSRT WELAHQPLHS SDLHLGLPQK QHFCGRRKKY
MPQPPKEDLF ILPDEYKSCL RHKRSLLRSH RNEELNVETL VVVDKKMMQN HGHENITTYV
LTILNMVSAL FKDGTIGGNI NIAIVGLILL EDEQPGLVIS HHADHTLSSF CQWQSGLMGK
DGTRHDHAIL LTGLDICSWK NEPCDTLGFA PISGMCSKYR SCTINEDTGL GLAFTIAHES
GHNFGMIHDG EGNMCKKSEG NIMSPTLAGR NGVFSWSPCS RQYLHKFLST AQAICLADQP
KPVKEYKYPE KLPGELYDAN TQCKWQFGEK AKLCMLDFKK AKDICKALWC HRIGRKCETK
FMPAAEGTIC GHDMWCRGGQ CVKYGDEGPK PTHGHWSDWS SWSPCSRTCG GGVSHRSRLC
TNPKPSHGGK FCEGSTRTLK LCNSQKCPRD SVDFRAAQCA EHNSRRFRGR HYKWKPYTQV
EDQDLCKLYC IAEGFDFFFS LSNKVKDGTP CSEDSRNVCI DGICERVGCD NVLGSDAVED
VCGVCNGNNS ACTIHRGLYS KHHHTNQYYH MVTIPSGARS IRIYEMNVST SYISVSNALR
RYYLNGHWTV DWPGRYKFSG TTFDYRRSYN EPENLIAAGP TNETLIVELL FQGKNPGVAW
EYSMPRLGAE KQPPAQPSYT WAIVRSECSV SCGGGQMTVR EGCYRDLKFQ VNTSFCNPKT
RPVTGLVPCK VSACPPSWSV GNWSACSRTC GGGAQSRPVQ CTRRVHYDSE PVPASLCPQP
APSSRQACNS QSCPPAWSTG PWAECSHTCG KGWRKRAVAC KSTNPSARAQ LLPDTVCTSE
PKPRMHEACL LQRCHKPKKL QWLVSAWSQC SVTCERGTQK RFLKCAEKYV SGKYRELASK
KCSHLPKPSL ELERACAPLP CPKHPPFAAA GPSRGSWFAS PWSQCTASCG GGVQTRSVQC
LVGGRPASGC LLHQKPLASL ACNTHFCPIA EKKDAFCKDY FRWCYLVPPH GMCSHKFYGK
QCCKTCSKSN L
//
