ID G3U6B3_LOXAF Unreviewed; 1114 AA.
AC G3U6B3;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=ADAM metallopeptidase with thrombospondin type 1 motif 10 {ECO:0000313|Ensembl:ENSLAFP00000023371.1};
GN Name=ADAMTS10 {ECO:0000313|Ensembl:ENSLAFP00000023371.1};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000023371.1, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000023371.1, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000023371.1,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000023371.1}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000023371.1};
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}.
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 AlphaFoldDB; G3U6B3; -.
DR STRING; 9785.ENSLAFP00000023371; -.
DR MEROPS; M12.235; -.
DR Ensembl; ENSLAFT00000032113.1; ENSLAFP00000023371.1; ENSLAFG00000011470.3.
DR eggNOG; KOG3538; Eukaryota.
DR GeneTree; ENSGT00940000158404; -.
DR InParanoid; G3U6B3; -.
DR OMA; TQQCETK; -.
DR TreeFam; TF313537; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
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; 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; 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:UP000007646};
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}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..1114
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003456330"
FT DOMAIN 241..459
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1076..1114
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT ACT_SITE 395
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 196
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 244
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 244
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 342
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 394
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 398
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 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 454
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 317..378
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 353..360
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 372..454
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 411..438
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 481..503
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 492..510
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 498..533
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 523..538
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 561..598
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 565..603
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 576..588
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1114 AA; 121774 MW; E4B4C6B637F648D4 CRC64;
MAPACQILRW ALALGLGLTF QATPRHAFRS QDEFLSSLES YEIAFPTRVD HNGALLAFSP
PAPRRQRRGT GATTESRLFY KVVAPSTQFL LNLTRSPRLL AGHVSVEYWT REGLAWQKAA
RPHCLYAGHL QGQAGSSHVA ISTCGGLHGL IVADEEEYLI EPLQGGAKGP RGPEESGPHV
VYKRSSLRHP HLDTACGVRD EKPWKGRPWW LRTLKPSPAR PLGNETERGQ PGLKRSVNRE
RYVETLVVAD KMMVAYHGRR DVEQYVLAVM NIVAKLFQDS SLGNNVNILV TRLILLTEDQ
PTLEITHHAG KSLDSFCKWQ KSIVNRSGHG NAIPENGVAN HDTAVLITRY DICIYKNKPC
GTLGLAPVGG MCERERSCSI NEDIGLATAF TIAHEIGHTF GMNHDGVGNS CGARGQDPAK
LMAAHITMKT NPFVWSSCSR DYITSFLDSG LGLCLNNRPP RQDFVYPTVA PGQAYDADEQ
CRFQHGVKSR QCKYGEVCSE LWCLSKSNRC ITNSIPAAEG TLCQTHTIDK GWCYKRVCVP
FGSRPEGVDG AWGPWTPWGD CSRTCGGGVS SSSRHCDSPR PTIGGKYCLG ERRRHRSCNT
DDCPPGSQDF REMQCSEFDS VPFVPRGEGR GPRTQGGGGV KACSLTCAEG FNFYTERAAA
VVDGTPCRPD TVDICVSGEC KHVGCDRVLG SDLREDKCRV CGGDGSACET IEGVFNPALL
GAGEILQLSS HTPIWARPQG VTLSHKGLRG SLSMRAGKGS PEGIFRGCGE LKQPSQPLLK
EKEPQVGEGP EDQTQSLEAL GPINASLVVM VLARTELSTL RYRFNAPIAR YALPPYSWHY
APWTKCSAQC AGGSQVQAVE CRSQLDSTTV APHHCSAHSK LPKRQRACNT EPCPPDWVVG
NWSRCSRSCD AGVRSRSVVC QRRVSAAEEK ALDDSACPQP RPPVLEACQG PTCPPEWAAL
DWSECTPSCG PGLRHRVVLC KSADHRATLP PAHCPPAAKP PVTMRCNLRR CPPARWVAGE
WGECSAHCGF GQQQRTVRCT SHMGQPSREC TEALRPPATQ QCETKCESVP AGDAPEEPEC
KDVNKVAYCP LVLKFQFCSR AYFRQMCCKT CQGR
//
