ID A0A2K5WLY8_MACFA Unreviewed; 857 AA.
AC A0A2K5WLY8;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=ADAM metallopeptidase with thrombospondin type 1 motif 8 {ECO:0000313|Ensembl:ENSMFAP00000038189.2};
GN Name=ADAMTS8 {ECO:0000313|Ensembl:ENSMFAP00000038189.2};
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 {ECO:0000313|Ensembl:ENSMFAP00000038189.2, ECO:0000313|Proteomes:UP000233100};
RN [1] {ECO:0000313|Ensembl:ENSMFAP00000038189.2, ECO:0000313|Proteomes:UP000233100}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSMFAP00000038189.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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DR AlphaFoldDB; A0A2K5WLY8; -.
DR STRING; 9541.ENSMFAP00000038189; -.
DR Ensembl; ENSMFAT00000012444.2; ENSMFAP00000038189.2; ENSMFAG00000038449.2.
DR VEuPathDB; HostDB:ENSMFAG00000038449; -.
DR GeneTree; ENSGT00940000159642; -.
DR Proteomes; UP000233100; Chromosome 14.
DR Bgee; ENSMFAG00000038449; Expressed in lung 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; 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; 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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023049};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR613273-2, ECO:0000256|PROSITE-
KW ProRule:PRU00276}; Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000233100};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Zinc {ECO:0000256|PIRSR:PIRSR613273-2, ECO:0000256|PROSITE-
KW ProRule:PRU00276}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 187..397
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT REGION 117..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..164
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 332
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 190
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 190
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 273
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 273
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 280
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 331
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 335
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 341
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 392
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 395
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 395
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 262..315
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 291..297
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 309..392
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 347..376
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 420..445
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 431..454
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 440..475
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 469..480
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 506..543
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 510..548
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 521..533
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 857 AA; 93041 MW; 4F65BDE916589AAE CRC64;
MLPAPAAPRW PPAPAAAAAA AAAGPRRGPA RSWGAGLELV VPTRLPGSAG ELALHLSAFG
KGFVLRLAPD DSFLRGLRGC FFSGTVNGEP ESLAAVSLCR GLSGSFLLDG EEFTIQPQGR
WGPAGARPLP RGPEWEVETG EGQRQERGDN EEDSEEESQE EEAEGASELP PPLGATSRTK
RFVSEARFVE TLLVADASMA AFYGADLQNH ILTLMSVAAR IYKHPSIKNS INLMVVKVLI
VEDEKWGPEV SDNGGLTLRN FCNWQRRFNQ PSDRHPEHYD TAILLTRQNF CGQEGLCDTL
GVADIGTICD PNKSCSVIED EGLQAAHTLA HELGHVLSMP HDDSKPCTRL FGPMGKHHMM
APLFVHLNQT LPWSPCSAMY LTELLDGGHG DCLLDAPAAA LPLPTGLPGR MALYQLDQQC
RQIFGPDFHH CPNTSAQDVC AQLWCHTDGA EPLCHTKNGS LPWADGTPCG PGHLCSEGSC
LPEEEVERPK PVVDGGWAPW GPWGECSRTC GGGVQFSHRE CKDPEPQNGG RYCLGRRAKY
QSCHTEECPP DGKSFREQQC EKYNAYNYTD MDGNLLQWVP KYAGVSPRDR CKLFCRARGR
SEFKVFEAKV IDGTLCGPET LAICVRGQCV KAGCDHVVDS PRKLDKCGVC GGKGNSCRKV
SGSLTPTSYG YNDIVTIPAG ATNIDVKQRS HPGVQNDGNY LALKTADGQY LLNGNLAISA
IEQDILVKGT ILKYSGSIAT LERLQSFRPL PEPLTVQLLT VPGEVFPPKV KYTFFVPNDV
DFGMQSSRER ATTNIIQPLL HAQWVLGDWS ECSSTCGPGW QRRTVECRDP SGQASATCNK
ALKPEDAKPC ESQLCPL
//
