ID A0A850YRR2_9PASS Unreviewed; 591 AA. AC A0A850YRR2; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 22-FEB-2023, entry version 6. DE SubName: Full=MMP2 collagenase {ECO:0000313|EMBL:NWH97046.1}; DE Flags: Fragment; GN Name=Mmp2 {ECO:0000313|EMBL:NWH97046.1}; GN ORFNames=TICMUR_R09084 {ECO:0000313|EMBL:NWH97046.1}; OS Tichodroma muraria. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Passeriformes; Sittidae; Tichodroma. OX NCBI_TaxID=237442 {ECO:0000313|EMBL:NWH97046.1, ECO:0000313|Proteomes:UP000629438}; RN [1] {ECO:0000313|EMBL:NWH97046.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=B10K-DU-012-47 {ECO:0000313|EMBL:NWH97046.1}; 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=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000256|PIRSR:PIRSR621190-2}; CC Note=Can bind about 5 Ca(2+) ions per subunit. CC {ECO:0000256|PIRSR:PIRSR621190-2}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR621190-2}; CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|PIRSR:PIRSR621190- CC 2}; CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix {ECO:0000256|ARBA:ARBA00004498}. CC -!- SIMILARITY: Belongs to the peptidase M10A family. CC {ECO:0000256|ARBA:ARBA00010370}. 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:NWH97046.1}. 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; WAAG01004455; NWH97046.1; -; Genomic_DNA. DR AlphaFoldDB; A0A850YRR2; -. DR Proteomes; UP000629438; Unassembled WGS sequence. DR GO; GO:0031012; C: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:0030574; P:collagen catabolic process; IEA:UniProtKB-KW. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR GO; GO:0050896; P:response to stimulus; IEA:UniProt. DR CDD; cd00062; FN2; 3. DR CDD; cd00094; HX; 1. DR CDD; cd04278; ZnMc_MMP; 1. DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 2. DR Gene3D; 2.10.10.10; Fibronectin, type II, collagen-binding; 2. DR Gene3D; 2.110.10.10; Hemopexin-like domain; 1. DR InterPro; IPR000562; FN_type2_dom. DR InterPro; IPR036943; FN_type2_sf. DR InterPro; IPR000585; Hemopexin-like_dom. DR InterPro; IPR036375; Hemopexin-like_dom_sf. DR InterPro; IPR018487; Hemopexin-like_repeat. DR InterPro; IPR013806; Kringle-like. DR InterPro; IPR033739; M10A_MMP. DR InterPro; IPR024079; MetalloPept_cat_dom_sf. DR InterPro; IPR001818; Pept_M10_metallopeptidase. DR InterPro; IPR021190; Pept_M10A. DR InterPro; IPR021158; Pept_M10A_Zn_BS. DR InterPro; IPR006026; Peptidase_Metallo. DR InterPro; IPR002477; Peptidoglycan-bd-like. DR InterPro; IPR036365; PGBD-like_sf. DR PANTHER; PTHR10201:SF29; 72 KDA TYPE IV COLLAGENASE; 1. DR PANTHER; PTHR10201; MATRIX METALLOPROTEINASE; 1. DR Pfam; PF00040; fn2; 3. DR Pfam; PF00045; Hemopexin; 3. DR Pfam; PF00413; Peptidase_M10; 1. DR Pfam; PF01471; PG_binding_1; 1. DR PIRSF; PIRSF001191; Peptidase_M10A_matrix; 2. DR PRINTS; PR00013; FNTYPEII. DR PRINTS; PR00138; MATRIXIN. DR SMART; SM00059; FN2; 3. DR SMART; SM00120; HX; 2. DR SMART; SM00235; ZnMc; 1. DR SUPFAM; SSF50923; Hemopexin-like domain; 1. DR SUPFAM; SSF57440; Kringle-like; 3. DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1. DR SUPFAM; SSF47090; PGBD-like; 1. DR PROSITE; PS00546; CYSTEINE_SWITCH; 1. DR PROSITE; PS00023; FN2_1; 1. DR PROSITE; PS51092; FN2_2; 3. DR PROSITE; PS51642; HEMOPEXIN_2; 3. PE 3: Inferred from homology; KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRSR:PIRSR621190-2}; KW Collagen degradation {ECO:0000256|ARBA:ARBA00023105}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE- KW ProRule:PRU00479}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022530}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR621190-2}; KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049}; KW Protease {ECO:0000256|ARBA:ARBA00022670}; KW Reference proteome {ECO:0000313|Proteomes:UP000629438}; 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:PIRSR621190-2}; KW Zymogen {ECO:0000256|ARBA:ARBA00023145}. FT SIGNAL 1..26 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 27..591 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5032892717" FT DOMAIN 225..273 FT /note="Fibronectin type-II" FT /evidence="ECO:0000259|PROSITE:PS51092" FT DOMAIN 283..331 FT /note="Fibronectin type-II" FT /evidence="ECO:0000259|PROSITE:PS51092" FT DOMAIN 341..389 FT /note="Fibronectin type-II" FT /evidence="ECO:0000259|PROSITE:PS51092" FT REPEAT 473..517 FT /note="Hemopexin" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01011" FT REPEAT 518..564 FT /note="Hemopexin" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01011" FT REPEAT 566..591 FT /note="Hemopexin" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01011" FT MOTIF 97..104 FT /note="Cysteine switch" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-5" FT ACT_SITE 228 FT /evidence="ECO:0000256|PIRSR:PIRSR621190-1" FT ACT_SITE 401 FT /evidence="ECO:0000256|PIRSR:PIRSR001191-1" FT BINDING 99 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /ligand_note="catalytic" FT /note="in inhibited form" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 131 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 165 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 175 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 177 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 182 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 183 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 187 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 190 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 199 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 201 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 203 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 205 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 206 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 208 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 208 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 477 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 522 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 572 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT MOD_RES 553 FT /note="Phosphotyrosine; by PKDCC" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-4" FT DISULFID 230..256 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479" FT DISULFID 244..271 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479" FT DISULFID 288..314 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479" FT DISULFID 302..329 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479" FT DISULFID 346..372 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479" FT DISULFID 360..387 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:NWH97046.1" FT NON_TER 591 FT /evidence="ECO:0000313|EMBL:NWH97046.1" SQ SEQUENCE 591 AA; 66494 MW; B59D5D3E119CC087 CRC64; MKTHIGCGFV FKVLFIQVYL FNKTLAAPSP IIKFPGDSTP KTDKELAVQY LNKYYGCPKD SCNLFVLKDT LKKMQKFFGL PETGDLDQNT IETMKKPRCG NPDVANYNFF ARKPKWEKNH ITYRIIGYTP DLDPETVDDA FARAFQVWSD VTPLRFNRIH DGDADIMINF GRWEHGDGYP FDGKDGLLAH AFAPGPGIGG DSHFDDDELW TLGEGQVVRV KYGNADGEYC KFPFWFNGKE YNSCTDAGRS DGFLWCSTTK DFDADGKYGF CPHESLFTMG GNGDGQPCKF PFKFQGQSYD QCTTEGRTDG YRWCGTTEDY DRDKKYGFCP ETAMSTVGGN SEGAPCVFPF IFLGNKYESC TSAGRNDGKL WCASTSSYDD DRKWGFCPDQ GYSLFLVAAH EFGHAMGLEH SEDPGALMAP IYTYTKNFRL SQDDIKGIQE LYEVSPDVGP GPGPGPGPHP TLGPVTPELC KHDIVFDGVA QIRGETFFFK DRFMWRTINP RGKPTGPLLV ATFWPDLPEK IDAVYEAPQD EKAVFFSGNE YWVYSASNLD RGYPKKLSSL GLPPDVQRVD AAFNWGRNKR TYIFAGDRYW K //