ID A0A2K5YST9_MANLE Unreviewed; 1103 AA.
AC A0A2K5YST9;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=ADAM metallopeptidase with thrombospondin type 1 motif 10 {ECO:0000313|Ensembl:ENSMLEP00000018637.1};
GN Name=ADAMTS10 {ECO:0000313|Ensembl:ENSMLEP00000018637.1};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000018637.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000018637.1}
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 -!- 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_011821660.1; XM_011966270.1.
DR RefSeq; XP_011821661.1; XM_011966271.1.
DR AlphaFoldDB; A0A2K5YST9; -.
DR STRING; 9568.ENSMLEP00000018637; -.
DR Ensembl; ENSMLET00000042124.1; ENSMLEP00000018637.1; ENSMLEG00000033505.1.
DR GeneID; 105529182; -.
DR KEGG; mleu:105529182; -.
DR CTD; 81794; -.
DR GeneTree; ENSGT00940000158404; -.
DR OMA; TQQCETK; -.
DR OrthoDB; 2910701at2759; -.
DR Proteomes; UP000233140; Unplaced.
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:SF26; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 10; 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; 5.
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 Reference proteome {ECO:0000313|Proteomes:UP000233140};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR613273-2};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1103
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014328620"
FT DOMAIN 239..457
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1065..1103
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT REGION 213..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 393
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /note="in inhibited form"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 242
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 242
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 340
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 392
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 396
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 402
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 452
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 315..376
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 351..358
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 370..452
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 409..436
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 479..501
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 490..508
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 496..531
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 521..536
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 559..596
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 563..601
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 574..586
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1103 AA; 120888 MW; 30597D7C7FEF2898 CRC64;
MAPACQILRW ALALGLGLMF EVTHAFRSQD EFLSSLESYE IAFPTRVDHN GALLAFSPPP
PRRQRRGTGA TAESRLFYKV ASPSTHFLLN LTRSSRLLAG HVSVEYWTRE GLAWQRAARP
HCLYAGHLQG QASSSHVAIS TCGGLHGLIV ADKEEYLIEP LHGGPKGSRG PEESGPHVVY
KRSSLRHPHL DTACGVRDEK PWKGRPWWLR TLKPPPARPL GNETERGQPG LKRSVSRERY
VETLVVADKM MVAYHGRRDV EQYVLAIMNI VAKLFQDSSL GSTVNILVTR LILLTEDQPT
LEITHHAGKS LDSFCKWQKS IVNHSGHGNA IPENGVANHD TAVLITRYDI CIYKNKPCGT
LGLAPVGGMC ERERSCSVNE DIGLATAFTI AHEIGHTFGM NHDGVGNSCG ARGQDPAKLM
AAHITMKTNP FVWSSCSRDY ITSFLDSGLG LCLNNRPPRQ DFVYPTVAPG QAYDADEQCR
FQHGVKSRQC KYGEVCSELW CLSKSNRCIT NSIPAAEGTL CQTHTIDKGW CYKRVCVPFG
SRPEGVDGAW GPWTPWGDCS RTCGGGVSSS SRHCDSPRPT IGGKYCLGER RRHRSCNTDD
CPPGSQDFRE MQCSEFDSIP FRGKFYTWKT YRGGGVKACS LTCLAEGFNF YTERAAAVVD
GTPCRPDTVD ICVSGECKHV GCDRVLGSDV REDKCRVCGG DGSACETIEG VFSPASPGAG
YEDVVWIPKG SVHIFIQDLN LSLSHLALKG DQESLLLEGL PGTPQPHRLP LAGTTFQLRQ
GPDQFQSLEA LGPINASLIV MVLARTELPA LRYRFNAPIA RDSLPPYSWH YAPWTKCSAQ
CAGGSQVQAV ECRNQLDSSA VAPHYCSAHS KLPKRQRACN TEPCPPDWVV GNWSRCSRSC
DAGVRSRSVV CQRRVSAAEE KALDDSACPQ PRPPVLEACH GPTCPPEWAA LDWSECTPSC
GPGLRHRVVL CKSADHRATL PPAHCSPAAK PPATMRCNLR RCPPARWVAG EWGECSAQCG
LGQQQRSVRC TSHTGQASHE CTEALRPPTT QQCEAKCDSP TPGDGPEECK DVNKVAYCPL
VLKFQFCSRA YFRQMCCKTC QGH
//
