ID A0A5N4DQ20_CAMDR Unreviewed; 661 AA. AC A0A5N4DQ20; DT 26-FEB-2020, integrated into UniProtKB/TrEMBL. DT 26-FEB-2020, sequence version 1. DT 22-FEB-2023, entry version 13. DE SubName: Full=72 kDa type IV collagenase {ECO:0000313|EMBL:KAB1273157.1}; GN ORFNames=Cadr_000011373 {ECO:0000313|EMBL:KAB1273157.1}; OS Camelus dromedarius (Dromedary) (Arabian camel). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Tylopoda; Camelidae; Camelus. OX NCBI_TaxID=9838 {ECO:0000313|EMBL:KAB1273157.1, ECO:0000313|Proteomes:UP000299084}; RN [1] {ECO:0000313|EMBL:KAB1273157.1, ECO:0000313|Proteomes:UP000299084} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Drom800 {ECO:0000313|EMBL:KAB1273157.1}; RC TISSUE=Blood {ECO:0000313|EMBL:KAB1273157.1}; RX PubMed=30972949; DOI=.1111/1755-0998.13020; RA Elbers J.P., Rogers M.F., Perelman P.L., Proskuryakova A.A., RA Serdyukova N.A., Johnson W.E., Horin P., Corander J., Murphy D., RA Burger P.A.; RT "Improving Illumina assemblies with Hi-C and long reads: an example with RT the North African dromedary."; RL Mol. Ecol. Resour. 19:1015-1026(2019). 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:KAB1273157.1}. 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; JWIN03000009; KAB1273157.1; -; Genomic_DNA. DR AlphaFoldDB; A0A5N4DQ20; -. DR STRING; 9838.ENSCDRP00005002295; -. DR OrthoDB; 5340816at2759; -. DR Proteomes; UP000299084; 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:UniProtKB-EC. 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; IPR018486; Hemopexin_CS. 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; 4. 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; 4. 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; PS00024; HEMOPEXIN; 1. DR PROSITE; PS51642; HEMOPEXIN_2; 4. 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, KW ECO:0000256|PIRSR:PIRSR621190-3}; KW 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:UP000299084}; 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..30 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 31..661 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5024278471" FT DOMAIN 229..277 FT /note="Fibronectin type-II" FT /evidence="ECO:0000259|PROSITE:PS51092" FT DOMAIN 287..335 FT /note="Fibronectin type-II" FT /evidence="ECO:0000259|PROSITE:PS51092" FT DOMAIN 345..393 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..614 FT /note="Hemopexin" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01011" FT REPEAT 615..661 FT /note="Hemopexin" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01011" FT MOTIF 101..108 FT /note="Cysteine switch" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-5" FT ACT_SITE 232 FT /evidence="ECO:0000256|PIRSR:PIRSR621190-1" FT ACT_SITE 405 FT /evidence="ECO:0000256|PIRSR:PIRSR001191-1" FT BINDING 103 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 135 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 169 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 179 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 181 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 186 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 191 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 194 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 203 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 205 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 207 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 209 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 210 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 212 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 212 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" 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 479 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" 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 BINDING 619 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 621 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 234..260 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479" FT DISULFID 248..275 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479" FT DISULFID 292..318 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479" FT DISULFID 306..333 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479" FT DISULFID 350..376 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479" FT DISULFID 364..391 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479" FT DISULFID 470..661 FT /evidence="ECO:0000256|PIRSR:PIRSR621190-3" SQ SEQUENCE 661 AA; 73834 MW; 9F7507B4371E1846 CRC64; MTKARVARGA LASPLRALCV LGCLLGRAAA APSPIIKFPG DVAPKTDKEL AVQYLNTFYG CPKESCNLFV LKDTLKKMQK FFGLPQTGEL DQNTIETMRK PRCGNPDVAN YNFFPRKPKW DKNQVTYRII GYTPDLDPET VDDAFARAFQ VWSDVTPLRF SRIHDGEADI MINFGRWEHG DGYPFDGKDG LLAHAFAPGP GVGGDSHFDD DELWTLGEGQ VVRVKYGNAD GEYCKFPFLF NGKEYTSCTD TGRSDGFLWC STTYNFDKDG KYGFCPHEAL FTMGGNADGQ PCKFPFRFQG TSYDSCTTEG RTDGYRWCGT TEDYDRDKKY GFCPETAMST VGGNSEGAPC VFPFTFLGNK HESCTSAGRS DGKLWCATTA NYDDDRKWGF CPDQGYSLFL VAAHEFGHAM GLEHSQDPGA LMAPIYTYTK NFRLSHDDIK GIQDLYGASP DIDVGTGPTP TLGPITPEIC KQDIVFDGIS QIRGEIFFFK DRFIWRTVTP RDKPMGPLLV ATFWPELPEK IDAVYEAPQE EKAVFFAGNE YWVYSASTLE RGYPKPLTSL GLPPDVQKVD AAFNWSKNKK TYIFAGDKFW RYNEVKKKMD PGFPKLIADA WNAIPDNLDA VVDLQGGGHS YFFKGAYYLK LENQSLKSVK FGSVKSDWLG C //