ID F7HYD2_CALJA Unreviewed; 893 AA.
AC F7HYD2;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 3.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=ADAM metallopeptidase with thrombospondin type 1 motif 8 {ECO:0000313|Ensembl:ENSCJAP00000017430.4};
GN Name=ADAMTS8 {ECO:0000313|Ensembl:ENSCJAP00000017430.4};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000017430.4, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000017430.4}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000017430.4}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 AlphaFoldDB; F7HYD2; -.
DR MEROPS; M12.226; -.
DR Ensembl; ENSCJAT00000018434.5; ENSCJAP00000017430.4; ENSCJAG00000009481.5.
DR eggNOG; KOG3538; Eukaryota.
DR GeneTree; ENSGT00940000159642; -.
DR OMA; EDTKPCG; -.
DR OrthoDB; 2910701at2759; -.
DR TreeFam; TF331949; -.
DR Proteomes; UP000008225; Chromosome 11.
DR Bgee; ENSCJAG00000009481; Expressed in frontal cortex and 4 other cell types or tissues.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:InterPro.
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: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; -; 2.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 2.
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; IPR013277; Pept_M12B_ADAM-TS8.
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:SF41; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 8; 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; PF01421; Reprolysin; 1.
DR Pfam; PF19030; TSP1_ADAMTS; 1.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01861; ADAMTS8.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00209; TSP1; 2.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 2.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50092; TSP1; 2.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000008225};
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..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..893
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035282431"
FT DOMAIN 223..433
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT REGION 141..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..199
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 368
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 226
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 226
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 309
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 309
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 316
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 367
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 371
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 377
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="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 431
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 431
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 298..351
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 327..333
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 345..428
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 383..412
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 456..481
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 467..490
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 476..511
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 505..516
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 542..579
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 546..584
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 557..569
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 893 AA; 96955 MW; 6AF389455A4218FD CRC64;
MLSAPAAPRW PPLLLLLLLL LLLPPQLARG APAWPAVGGQ ASELVVPTRL PGSAGELALH
LSAFGKGFVL RLAPDDSFLA PEFKIERLGG SGRAAGGERG LRGCFFSGTV NGEPESLAAV
SLCRGLSGSF LLDGEEFTIQ PQGAGGSLGQ PHRLQRWGPA GARPLQRGPE WEVDTGEGQR
QERGDDEEDG EEESREDEAE GASELPPPLG ATSRTKRFVS EARFVETLLV ADASMAAFYG
ADLQDHILTL MSVAARIYKH PSIKNSISLM VVKVLIIEDE KWGPEVSDNG GLTLRNFCNW
QRRFNQPSDR HPEHYDTAIL LTRQNFCGQE GLCDTLGVAD IGTICDPNKS CSVIEDEGLQ
AAHTLAHELG HVLSMPHDDS KPCTRLFGPL GKHHMMAPLF VHLNQSLPWS PCSAMYLTEL
LDSGHGDCLL DAPATALPLP TGLPGRKTLY QLDQQCRQIF GPDFHHCPNT SAQDVCAQLW
CHTDGAEPLC HTKNGSLPWA DGTPCGPGHL CSEGSCLPEE EVEKPKPLVD GGWAPWGPWG
ECSRTCGGGV QFSHRECKDP EPQNGGRYCL GRRAKYQSCH TEECPPDGKS FREQQCEKYN
AYNYTDMDGN ILQWVPKYAG VSPRDRCKLF CRARGRSEFK VFEAKVIDGT LCGPETLAIC
IRGQCVKAGC DHVVDSPRKL DKCGVCGGKG NSCRKVSGSL TPSSYGYNDI VTIPAGATNI
DVKQRSHPGV QNDGNYLALK TADGQYLLNG NLAISAIEQD ILVKGTILKY SGSIATLERL
QSFRPLPEPL TVQLLTVPGE VFPPKVKYTF FVPNDVDFSM QSSKERATTN IIQPLLHAQW
VLGDWSECSS TCGAGWQRRT VECRDPSGQA SATCNKALKP EDAKPCESQL CPL
//
