ID   A0A5N4DQ20_CAMDR        Unreviewed;       661 AA.
AC   A0A5N4DQ20;
DT   26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2020, sequence version 1.
DT   07-OCT-2020, entry version 5.
DE   RecName: Full=72 kDa gelatinase {ECO:0000256|ARBA:ARBA00015893};
DE            EC=3.4.24.24 {ECO:0000256|ARBA:ARBA00012372};
DE   AltName: Full=72 kDa type IV collagenase {ECO:0000256|ARBA:ARBA00021167};
DE   AltName: Full=Matrix metalloproteinase-2 {ECO:0000256|ARBA:ARBA00013702};
DE   AltName: Full=PEX {ECO:0000256|ARBA:ARBA00013285};
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cleavage of gelatin type I and collagen types IV, V, VII, X.
CC         Cleaves the collagen-like sequence Pro-Gln-Gly-|-Ile-Ala-Gly-Gln.;
CC         EC=3.4.24.24; Evidence={ECO:0000256|ARBA:ARBA00000178};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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}.
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DR   EMBL; JWIN03000009; KAB1273157.1; -; Genomic_DNA.
DR   Proteomes; UP000299084; Chromosome 9.
DR   GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
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   CDD; cd00062; FN2; 3.
DR   CDD; cd00094; HX; 1.
DR   CDD; cd04278; ZnMc_MMP; 1.
DR   Gene3D; 1.10.101.10; -; 1.
DR   Gene3D; 2.10.10.10; -; 3.
DR   Gene3D; 2.110.10.10; -; 1.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR028708; 72kDa_collagenase.
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   InterPro; IPR036366; PGBDSf.
DR   PANTHER; PTHR10201:SF29; PTHR10201:SF29; 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; PR00138; MATRIXIN.
DR   SMART; SM00059; FN2; 3.
DR   SMART; SM00120; HX; 4.
DR   SMART; SM00235; ZnMc; 1.
DR   SUPFAM; SSF47090; SSF47090; 1.
DR   SUPFAM; SSF50923; SSF50923; 1.
DR   SUPFAM; SSF57440; SSF57440; 3.
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};
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   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};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..661
FT                   /note="72 kDa gelatinase"
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   ACT_SITE        405
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001191-1"
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"
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
//