ID A0A7L4BHB4_9CHAR Unreviewed; 1084 AA. AC A0A7L4BHB4; DT 07-APR-2021, integrated into UniProtKB/TrEMBL. DT 07-APR-2021, sequence version 1. DT 29-MAY-2024, entry version 10. DE SubName: Full=ATS10 metalloproteinase {ECO:0000313|EMBL:NXW37222.1}; DE Flags: Fragment; GN Name=Adamts10 {ECO:0000313|EMBL:NXW37222.1}; GN ORFNames=PHASIM_R09655 {ECO:0000313|EMBL:NXW37222.1}; OS Phaetusa simplex (large-billed tern). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Charadriiformes; Laridae; Phaetusa. OX NCBI_TaxID=297813 {ECO:0000313|EMBL:NXW37222.1, ECO:0000313|Proteomes:UP000556165}; RN [1] {ECO:0000313|EMBL:NXW37222.1, ECO:0000313|Proteomes:UP000556165} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B10K-DU-009-16 {ECO:0000313|EMBL:NXW37222.1}; RC TISSUE=Muscle {ECO:0000313|EMBL:NXW37222.1}; RA Zhang G.; RT "Bird 10,000 Genomes (B10K) Project - Family phase."; RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases. 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:NXW37222.1}. 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 EMBL; VZZW01002203; NXW37222.1; -; Genomic_DNA. DR AlphaFoldDB; A0A7L4BHB4; -. DR Proteomes; UP000556165; Unassembled WGS sequence. DR GO; GO:0031012; C:extracellular matrix; IEA:TreeGrafter. 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:UP000556165}; 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 DOMAIN 221..439 FT /note="Peptidase M12B" FT /evidence="ECO:0000259|PROSITE:PS50215" FT DOMAIN 1046..1084 FT /note="PLAC" FT /evidence="ECO:0000259|PROSITE:PS50900" FT ACT_SITE 375 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1, FT ECO:0000256|PROSITE-ProRule:PRU00276" FT BINDING 176 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 224 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2" FT BINDING 224 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2" FT BINDING 322 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2" FT BINDING 374 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 378 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 384 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 434 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2" FT DISULFID 297..358 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3" FT DISULFID 333..340 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3" FT DISULFID 352..434 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3" FT DISULFID 391..418 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3" FT DISULFID 461..483 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3" FT DISULFID 472..490 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3" FT DISULFID 478..513 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3" FT DISULFID 503..518 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3" FT DISULFID 541..578 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3" FT DISULFID 545..583 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3" FT DISULFID 556..568 FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:NXW37222.1" FT NON_TER 1084 FT /evidence="ECO:0000313|EMBL:NXW37222.1" SQ SEQUENCE 1084 AA; 120908 MW; 2DBF89A3EC6EBF1F CRC64; FPSPEEFLSS LDHYEIAFPI QVDQNGDFLT FDVRSQLKQR PRRSLGSLPY EPSEQQVFYK VSAHRTQFLL NLTLHSNLLA EHFTVEYWKR DGVDWQHDFH EDCHYAGHLQ DQYLNSKVAI SNCNGLHGVI VADEEEYFIE PLSPGANVST GSEGKGSPHV VYKRSSLQYP HMDAACGVLD EKPWKGRHWW LRTLKPSPLK PSGNHSQRGQ LPLKRSVSTE RYVETLVVAD KMMVGYHGRR DIEQYILAIM NIVAKLFQDS SLGNIVNILV TRLILLTEDQ PTLEINHHAG KSLDSFCKWQ KSIVNRNGNG NAIPENGIAN HDTAVLITRY DICIYKNKPC GTLGLAPVGG MCERERSCSI NEDIGLATAF TIAHEIGHTF GMNHDGVGNS CGSRGQETAK LMAAHITMKT NPFVWSTCSR DYITSFLDSG MGLCLNNAPP KQDFIYPTVA PGQAYDADEQ CRFQYGVKSR QCKYGEVCSE LWCLSKSNRC ITNSIPAAEG TICQTNTIEK GWCYKRECVP FGTRPEGVDG AWGAWSSWGE CSRTCGGGVS SSIRHCDSPR PTIGGKYCLG ERKRYRSCNT DDCPPGSQDF RELQCAEFDN VPFRGKYYTW KTYRGGGVKA CSLNCLAEGF NFYTERAAAV VDGTPCRQDS NDICVNGECK HVGCDRVLGS DSKEDKCRVC GGDGSSCETI EGVFNQSLPE GGYEEVIQIP KGSVHIDIRE LNLSINYLAL RGESGEYYIN GKLSIDPPRR FDIAGTTFHY RRSPEEPESL EALGPTNITL FVMVLVRTEL QGIRYKFNAP IGRDASNQYS WHYTPWTKCS VLCAGGNQIQ SVVCKKLADG STVFNHFCSP ETKMPERQRP CNTEPCPPAW VIGNWSECSR SCNEGVRTRS VFCKRKISAT EEKTLDDASC THPRPKMLEP CNNQTCPPEW VALDWSECTP SCGPGFRHRI VLCKSGDHSA TLPTSQCSEG SKPPTSMRCN LRRCPPPRWV TGEWGECSAQ CGLGQQRRSV QCLAHTGQPS SDCVESLQPP GMQQCETKCE SGPTDNPEEC KDVNKVAYCP LVLKFKFCSR TYFRQMCCKT CQGH //