ID A0A1D5NZ82_CHICK Unreviewed; 1109 AA.
AC A0A1D5NZ82;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 2.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=ADAM metallopeptidase with thrombospondin type 1 motif, 10 {ECO:0000313|Ensembl:ENSGALP00010042586.1};
GN Name=ADAMTS10 {ECO:0000313|Ensembl:ENSGALP00010042586.1};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031 {ECO:0000313|Ensembl:ENSGALP00010042586.1, ECO:0000313|Proteomes:UP000000539};
RN [1] {ECO:0000313|Ensembl:ENSGALP00010042586.1}
RP IDENTIFICATION.
RC STRAIN=broiler {ECO:0000313|Ensembl:ENSGALP00010042586.1};
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}.
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DR AlphaFoldDB; A0A1D5NZ82; -.
DR SMR; A0A1D5NZ82; -.
DR STRING; 9031.ENSGALP00000045697; -.
DR PaxDb; 9031-ENSGALP00000002345; -.
DR Ensembl; ENSGALT00010069144.1; ENSGALP00010042586.1; ENSGALG00010028549.1.
DR VEuPathDB; HostDB:geneid_769592; -.
DR GeneTree; ENSGT00940000158404; -.
DR InParanoid; A0A1D5NZ82; -.
DR OMA; TQQCETK; -.
DR OrthoDB; 2910701at2759; -.
DR Reactome; R-GGA-5173214; O-glycosylation of TSR domain-containing proteins.
DR Proteomes; UP000000539; Chromosome 28.
DR Bgee; ENSGALG00000033157; Expressed in lung and 9 other cell types or tissues.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
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:UP000000539};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR613273-2}.
FT ACT_SITE 400
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 201
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 249
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 249
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 347
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 399
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 403
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 409
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 459
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 322..383
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 358..365
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 377..459
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 416..443
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 486..508
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 497..515
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 503..538
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 528..543
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 566..603
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 570..608
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 581..593
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1109 AA; 123937 MW; 8C7706712BFAF049 CRC64;
MAIAWRLLIW TVTFTTTVCS FRGYMFQSQE EFLSSLDHYE IAFPIQVDQN GDFLTFDMRS
QLKQRPRRSL GSLPYEPSEQ QVFYKVSAHR TQFLLNLTLH SNLLAEHFTV EYWKRDGVDW
QHDFHEDCHY AGHLQDQYLN SKVAISNCNG LHGVIVADEE EYFIEPLSPG ANVSAGNEGK
GSPHVVYKRS SLQYPHMDAA CGVLDEKPWK GRHWWLRTLK PSPLKPSGNH SQRGQLPLKR
SVSTERYVET LVVADKMMVG YHGRRDIEQY ILAIMNIVAK LFQDSSLGNI VNILVTRLIL
LTEDQPTLEI NHHAGKSLDS FCKWQKSIVN RNGNGNAIPE NGIANHDTAV LITRYDICIY
KNKPCGTLGL APVGGMCERE RSCSINEDIG LATAFTIAHE IGHTFGMNHD GVGNSCGSRG
QETAKLMAAH ITMKTNPFVW STCSRDYITS FLDSGMGLCL NNAPPKQDFI YPTVAPGQAY
DADEQCRFQY GVKSRQCKYG EVCSELWCLS KSNRCITNSI PAAEGTICQT NTIEKGWCYK
RECVPFGTRP EGVDGAWGSW SSWGECSRTC GGGVSSSVRH CDSPRPTIGG KYCLGERKRY
RSCNTDDCPP GSQDFRELQC AEFDNVPFRG KYYTWKTYRG GGVKACSLNC LAEGFNFYTE
RAAAVVDGTP CRQDSNDICV NGECKHVGCD RVLGSDAKED KCRVCGGDGS SCETIEGIFN
QSLPEGGYEE VIQIPKGSVH IDIRELNLSI NYLALRGDAG EYYINGKLSI DPPRRFDIAG
TTFHYRRSPD EPESLEALGP TNVTLFVMVL VRTELQGIRY KFNAPISRDA SNQYSWHYTP
WTKCSVLCAG GSQIQSVVCR KLSDSSTVSN HFCSPETKML ERQRPCNTEP CAPAWVIGNW
SECSRSCNEG VRTRSVFCKR KISATEEKTL DDASCTQPRP KMLEPCNNQT CPPEWVALDW
SECTPSCGPG FRHRIVLCKS GDHSATLPTS QCPEGSKPPT SMRCNLRRCP PPRWVTGEWG
ECSAHCGLGQ QRRSVQCLAH TGQPSSDCLE TLQPPGMQQC ETKCESGPTD NPEECKDVNK
VAYCPLVLKF KFCSRTYFRQ MCCKTCQGH
//
