ID G7PHM4_MACFA Unreviewed; 1911 AA.
AC G7PHM4;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 20 {ECO:0000313|EMBL:EHH66200.1};
GN ORFNames=EGM_03139 {ECO:0000313|EMBL:EHH66200.1};
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:EHH66200.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CE-4 {ECO:0000313|EMBL:EHH66200.1};
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; CM001286; EHH66200.1; -; Genomic_DNA.
DR MEROPS; M12.246; -.
DR eggNOG; KOG3538; Eukaryota.
DR Proteomes; UP000009130; Chromosome 11.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:InterPro.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
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; 10.
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; IPR012314; Pept_M12B_GON-ADAMTSs.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR13723:SF165; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 20; 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; PF08685; GON; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR Pfam; PF19030; TSP1_ADAMTS; 12.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00209; TSP1; 13.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 12.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS51046; GON; 1.
DR PROSITE; PS50092; TSP1; 12.
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 Integrin {ECO:0000313|EMBL:EHH66200.1};
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}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR613273-2};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1911
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003502359"
FT DOMAIN 260..468
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1712..1911
FT /note="GON"
FT /evidence="ECO:0000259|PROSITE:PS51046"
FT ACT_SITE 405
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 263
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 263
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 346
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 346
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 353
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 404
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 408
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 414
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 463
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 466
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 466
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 335..388
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 364..370
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 382..463
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 420..447
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 490..512
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 501..522
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 507..541
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 535..546
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 569..606
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 573..611
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 584..596
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1911 AA; 215077 MW; C33FF9825B798969 CRC64;
MWVAKWLTGL LCHLSLITRS WEVHFHPRQE ALVRTLTTYE VVIPERVNEF GEVFPQSHHF
SRQKRSSEAL EPMPFRTHYR VTAYGQLFQX XXXXXXXXXX XGYTEVHLGA PGRGTWESDA
GPSDLRHCFY RGQVNSQEDY KAVVSLCGGL TGTFKGHDGD YFLEPIMKAD GNEYEDGHNK
PHLIYRQELN NSFLQTLKYC SVSESQIKET SLPFHTYRNM NEDLNVMKER VLGHPSKNVP
LKDERSQLHS RKKRLISYPR YVEIMVTADA KVVSAHGSNL QNYILTLMSI VATIYKDPSI
GSFIHIVVVK LVMIHHEEEG PVINFDGATT LNNFCSWQQT QNDVDDVHPS HHDAAILITR
EDICSSKEKC NILGLSYLGT ICDPLQSCFI NEEKGLISAF TIAHELGHTL GVQHDDTPRC
REMNVTQYHV MAPVLSFHMS PWSWSNCSRK YITEFLDTGY GECLLDKPDE EIYNLPSELP
GSRYDGNKQC ELAFGPGSQM CPHINICMHL WCTSAEKLHK GCFTQHVPPA DGTDCGPGMH
CRRGLCVNKE METRPVNGEW GPWEPYSSCS RTCGGGIESS TRHCNRPEPR NGGNYCVGRR
MKFRSCNTDS CPKGTQDFRE KQCSDFNGKH LGINGIPSNV RWLPRYSGIR TKDRCKLYCQ
VAGTNDFYLL KYMVEDGTPC ENETHDICVQ GRCMAAGCDH VLNSSAKIDK CGVCGGDNSS
CKTITGVFNS SHYGYNVVVK IPAGATNIDI RQYSYSGQPD DSYLALSDAE GNFLFNGNFV
LSRSKKEVNV QGTRTVIEYS GSNNSVERIN STNRQEKELI LQVLCVGNLY NPDVRYSFNI
PLEEWSELFT WDPYGPWEGC TKMCQGLQRR KITCIHKSDH SVVSDQKCDQ LPLPSFVTQS
CNTDCELRWH VTGKSECSTQ CGQGYRTLDI HCMKYSIHKG QTVQVDDHYC GDQLKPPTRE
LCRGNCVFTR WHFSEWSQCS RSCGGGERSR ESYCMNNFGH RLADNECEEL SRVTRENCNE
FSCPSWAASE WSECLVTCGK GIKQRQVWCQ LNEDHLSDGF CNSSTKPESL SPCELHTCAS
WQVGPWGPCT TTCGHGYQMR DVKCVNELVS AVLEDKECHE ASRPSDRQNC VLTPCPFISK
LKTTSLPTAL IEKMAQWRHG SWTPCSVSCG RGTQARYVSC RDALDRIADE SYCAHLPQPA
EIWDCFTPCG EWQAGDWSPC SASCGYGKTT RQVLCMNYHQ PIDENYCDPE VRPLMEQECS
LAACPPAHSH FPSSAVQPSY YLSTNLPLTH KLEDDENQVV LPSVRGNQWR TGPWGSCSSS
CSGGLQRRAV VCQDENGQSA SYCDATSKPP ELQHCGPGPC PQWNYGNWGE CSQTCGGGIK
SRLVICQFPN GQILEDHNCE IVNKPPSVIQ CHMHACPADV SWHQEPWTSC SASCGKGRKY
REVFCIDQFQ RKLEDTNCSQ VQKPPTHKAC RSVRCPSWKA NSWNKCSMTC GSGVQQRDIY
CRLKGVGRVV EEMCDQSTRP CSQRRCWSQD CVHHKGMERE RLNCSTSCER KDSHHRTECT
DSQIGQVNEI VYNSSTMSLT SKNCRNPPCN YIVVTADSSQ CANNCGFSYR QRITYCTGIP
STKKHKLHRL QPIVYQECPV VPSSQVYKCI NSCLHLATWK VGKWSKCSVT CGIGIMKRQV
KCVTKHGLSS DLCLNHLKPG AQKKCYANDC KSFTTCEEIQ VKNHIRKDGD YYLNIKGRII
KIHCADMHLE NPKEYLTLVQ GEENFSEVYG FRLKNPYQCP FNGSRREDCE CDNGHLAAGY
TVFSKIRIDL TSMQIKTTDL RFSKTIFGNA VPFATAGDCY SAVRCPQGQF SINLAGTGMK
ISNTAKWLAQ GSYTSVSIRR SEDGTRFFGK CGGYCGKCLP HMTTGLPIQV I
//