ID A0A091Q4T2_HALAL Unreviewed; 663 AA.
AC A0A091Q4T2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 28-JAN-2026, entry version 54.
DE RecName: Full=72 kDa type IV collagenase {ECO:0000256|ARBA:ARBA00021167};
DE EC=3.4.24.24 {ECO:0000256|ARBA:ARBA00012372};
DE AltName: Full=72 kDa gelatinase {ECO:0000256|ARBA:ARBA00029967};
DE AltName: Full=Matrix metalloproteinase-2 {ECO:0000256|ARBA:ARBA00030021};
GN Name=Mmp2 {ECO:0000313|EMBL:NWZ52158.1};
GN ORFNames=HALALB_R01919 {ECO:0000313|EMBL:NWZ52158.1}, N329_02546
GN {ECO:0000313|EMBL:KFQ04644.1};
OS Haliaeetus albicilla (White-tailed sea-eagle) (Falco albicilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Accipitrimorphae;
OC Accipitriformes; Accipitridae; Accipitrinae; Haliaeetus.
OX NCBI_TaxID=8969 {ECO:0000313|EMBL:KFQ04644.1, ECO:0000313|Proteomes:UP000054379};
RN [1] {ECO:0000313|EMBL:KFQ04644.1, ECO:0000313|Proteomes:UP000054379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N329 {ECO:0000313|EMBL:KFQ04644.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:NWZ52158.1, ECO:0000313|Proteomes:UP000585422}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OUT-0040 {ECO:0000313|EMBL:NWZ52158.1};
RC TISSUE=Blood {ECO:0000313|EMBL:NWZ52158.1};
RA Zhang G.;
RT "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
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|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}.
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DR EMBL; KK655506; KFQ04644.1; -; Genomic_DNA.
DR EMBL; VZSQ01000079; NWZ52158.1; -; Genomic_DNA.
DR RefSeq; XP_009917990.1; XM_009919688.2.
DR AlphaFoldDB; A0A091Q4T2; -.
DR MEROPS; M10.003; -.
DR GeneID; 104318434; -.
DR KEGG; hald:104318434; -.
DR CTD; 4313; -.
DR OrthoDB; 406838at2759; -.
DR Proteomes; UP000054379; Unassembled WGS sequence.
DR Proteomes; UP000585422; Unassembled WGS sequence.
DR GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
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:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0001666; P:response to hypoxia; IEA:TreeGrafter.
DR GO; GO:0048771; P:tissue remodeling; IEA:TreeGrafter.
DR CDD; cd00062; FN2; 3.
DR CDD; cd00094; HX; 1.
DR CDD; cd04278; ZnMc_MMP; 1.
DR FunFam; 2.10.10.10:FF:000002; 72 kDa type IV collagenase; 1.
DR FunFam; 2.110.10.10:FF:000004; 72 kDa type IV collagenase; 1.
DR FunFam; 3.40.390.10:FF:000010; 72 kDa type IV collagenase; 1.
DR FunFam; 2.10.10.10:FF:000001; Fibronectin 1a isoform 1; 2.
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; 2.
DR Pfam; PF00045; Hemopexin; 4.
DR Pfam; PF00413; Peptidase_M10; 2.
DR Pfam; PF01471; PG_binding_1; 1.
DR PIRSF; PIRSF001191; Peptidase_M10A_matrix; 1.
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:UP000585422};
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..663
FT /note="72 kDa type IV collagenase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5044540374"
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 475..519
FT /note="Hemopexin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01011"
FT REPEAT 520..566
FT /note="Hemopexin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01011"
FT REPEAT 568..616
FT /note="Hemopexin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01011"
FT REPEAT 617..663
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 479
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 524
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 574
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 621
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 623
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT MOD_RES 555
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 DISULFID 472..663
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-3"
SQ SEQUENCE 663 AA; 74805 MW; ED7F94C4AEDF2E7D CRC64;
MKTHIVCGFV FKVLLIQVYL FNKTLAAPSP IIKFPGDSTP KTDKELAVQY LNKYYGCPKD
NCNLFVLKDT LKKMQKFFGL PETGDLDQNT IETMKKPRCG NPDVANYNFF PRKPKWEKNH
ITYRIIGYTP DLDPETVDDA FARAFQVWSD VTPLRFNRIN DGEADIMINF GRWEHGDGYP
FDGKDGLLAH AFAPGPGIGG DSHFDDDELW TLGEGQVVRV KYGNADGEYC KFPFWFNGKE
YNSCTDAGRN DGFLWCSTTK DFDADGKYGF CPHESLFTMG GNGDGQPCKF PFKFQGQSYD
QCTTEGRTDG YRWCGTTEDY DRDKKYGFCP ETAMSTVGGN SEGAPCVFPF IFLGNKYESC
TSAGRNDGKL WCASTGSYDD DRKWGFCPDQ GYSLFLVAAH EFGHAMGLEH SEDPGALMAP
IYTYTKNFRL SQDDIKGIQE LYEVSTDVEP GPGPGPGPGP RPTLGPVTPE LCKHDIVFDG
VAQIRGETFF FKDRFMWRTV NARGKPTGPL LVATFWPDLP EKIDAVYEAP QDEKAVFFSG
NEYWVYSASN LDRGYPKKLT NLGLPPDVQR VDAAFNWGRN KRTYIFAGDR YWKYNEEKKK
MELASPKFIA DSWNGVPDNL DAVLGLGDSG YTYFFKDQYY LQMEDKSLKI VKIGKINSDW
LGC
//
