ID G7PR86_MACFA Unreviewed; 1378 AA.
AC G7PR86;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=ADAM cysteine-rich domain-containing protein {ECO:0000259|SMART:SM00608};
GN ORFNames=EGM_06555 {ECO:0000313|EMBL:EHH57002.1};
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:EHH57002.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CE-4 {ECO:0000313|EMBL:EHH57002.1};
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};
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DR EMBL; CM001290; EHH57002.1; -; Genomic_DNA.
DR eggNOG; KOG3538; Eukaryota.
DR Proteomes; UP000009130; Chromosome 15.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:InterPro.
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; IPR006586; ADAM_Cys-rich.
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; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR13723:SF20; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 13; 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; PF19030; TSP1_ADAMTS; 4.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00209; TSP1; 7.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 2.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 5.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS50092; TSP1; 5.
PE 4: Predicted;
KW Calcium {ECO:0000256|PIRSR:PIRSR613273-2};
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR613273-3};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR613273-2};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Zinc {ECO:0000256|PIRSR:PIRSR613273-2};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 255..328
FT /note="ADAM cysteine-rich"
FT /evidence="ECO:0000259|SMART:SM00608"
FT REGION 785..804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1124..1157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1133..1148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 224
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1"
FT BINDING 83
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 83
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 166
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 166
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 173
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 227
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 155..207
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 201..236
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 266..291
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 277..301
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 286..320
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 314..325
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 350..387
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 354..392
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 365..377
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1378 AA; 148768 MW; 32410F610C57944A CRC64;
MRQRHPWARC PSLCVAGILA CGFLLGCWGP SHFQQSFLQA LEPQAVSSYL SSGAPLKGHP
PSPGFQRQRQ RQRRAAGSIL HLELLVAVGP DVFQAHQEDT ERYVLTNLNI GAELLRDPSL
GAQFRVHLVK MVILTEPEGA PNITANLTSS LLSVCGWSRT INPEDDTDPG HADLVLYIRF
DLELPDGNRQ VRGVTQLGGA CSPTWSCLIT EDTGFDLGVT IAHEIGHLSS AGRARCVWDP
PRPQPGSAGR QPEAQPGLYY SANEQCRVAF GPKAVACTFS REHDMCQALS CHTDPLDQSS
CSRLLVPLLD GTECGVEKWC SKGRCRSLVE LTPIAAVHGH WSSWGPQSPC SRSCGGGVVT
RRRQCNNPRP AFGGRACVGA DLQAEMCNTQ ACEKTQLEFM SEQCARTDNQ PLHSSPGGAS
FYHWGAAVPH SQGDALCRHM CRAVGESFIM KRGDSFLDGT RCVPSGPQED GTLSLCVSGS
CRTFGCDGRM DSQQVRDVCQ VCGGDNSTCS PRNGSFTAGR AREYVTFLTV TPNLTSVYIA
NHRPLFTHLA VRIGGRYVVA GKTSISSNTT YPSLLEDGRV EYRVALTKDR LPHLEEIRIW
GPLQEDAEIQ VYRRYGEEYG NLTCPDITFT YFQPKPRQAW VWAAVRGPCS VSCGAGLRWV
NYSCLDQARK ELVETARCQG SQQPPAWPEA CMLEPCPWAV GDFGPCSVSC GGGLRERPVR
CVEAQGSLLK TLPPARCTAG AQQPAVAVEI CNPQPCPARW EVSEPGPCTS ASGAGPALQN
KTCVPGADGL EAPATEGPDS VDEKLPAPEP CVGMSCPAGW GHLDATSAGE EAPSPWGSIR
TGAQAAHVWT PLAGPCSVSC GRGLMELRFL CMDAALRVPV QEELCGLASK PGSRREVCQA
VPCPARWQYK LAACSVSCGG GVMRRILYCA RAHGEDEEEE ILLDTQCQGL PRPDPQEACS
LEPCPPRWKV MSLGPCSASC GLGTARRSVA CVQLDQGRDV EVDEAACAAL VRPQASVPCL
IADCTYRWYV GTWTECSVSC GDGIQRRHDT CLGPQAQAPV PADFCQHLPK PVTVRGCWAG
PCVGQGTPNL VPHEEATAPG QTTATPAGAS LEWSQAPALL FSPAPQPRRL LPGPQESSAQ
SSACGRQHLE PTGTIDMRGP GQADCAVAIG RPLGEVVTLR VLESSLNCSA GDMLLLWGRL
TWRKMCRKLL GMTFSSKTNT LVVKQRCRQP GGGVLLRYGS QLAPETFYRE CDMQLFGPWG
EIVSPSLSPA MSKAEGCRLF INVAPHARIA IHALATNMDN GTKGANASYI IRDIHSLRTT
TFHGQQVLYW ESESSQAEME FSEDFLKAQA SLRGQYWTLQ SWVPEGQDPQ SWKGKEGT
//
