GenomeNet

Database: UniProt
Entry: A0A3Q3B4I4_KRYMA
LinkDB: A0A3Q3B4I4_KRYMA
Original site: A0A3Q3B4I4_KRYMA 
ID   A0A3Q3B4I4_KRYMA        Unreviewed;       691 AA.
AC   A0A3Q3B4I4;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Matrix metalloproteinase-9 {ECO:0000256|ARBA:ARBA00013698};
DE            EC=3.4.24.35 {ECO:0000256|ARBA:ARBA00012395};
DE   AltName: Full=92 kDa gelatinase {ECO:0000256|ARBA:ARBA00030375};
DE   AltName: Full=92 kDa type IV collagenase {ECO:0000256|ARBA:ARBA00032382};
DE   AltName: Full=Gelatinase B {ECO:0000256|ARBA:ARBA00033338};
OS   Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX   NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000023990.1, ECO:0000313|Proteomes:UP000264800};
RN   [1] {ECO:0000313|Ensembl:ENSKMAP00000023990.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cleavage of gelatin types I and V and collagen types IV and
CC         V.; EC=3.4.24.35; Evidence={ECO:0000256|ARBA:ARBA00001425};
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   ---------------------------------------------------------------------------
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   RefSeq; XP_017273077.1; XM_017417588.1.
DR   AlphaFoldDB; A0A3Q3B4I4; -.
DR   STRING; 37003.ENSKMAP00000023990; -.
DR   Ensembl; ENSKMAT00000024294.1; ENSKMAP00000023990.1; ENSKMAG00000017773.1.
DR   GeneID; 108236720; -.
DR   KEGG; kmr:108236720; -.
DR   CTD; 4318; -.
DR   GeneTree; ENSGT00940000157415; -.
DR   OMA; REKAYFC; -.
DR   OrthoDB; 5340816at2759; -.
DR   Proteomes; UP000264800; Unplaced.
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); 1.
DR   Gene3D; 2.10.10.10; Fibronectin, type II, collagen-binding; 3.
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; MATRIX METALLOPROTEINASE; 1.
DR   PANTHER; PTHR10201:SF30; MATRIX METALLOPROTEINASE-9; 1.
DR   Pfam; PF00040; fn2; 3.
DR   Pfam; PF00045; Hemopexin; 3.
DR   Pfam; PF00413; Peptidase_M10; 2.
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; PS51642; HEMOPEXIN_2; 2.
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:PIRSR001191-2};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000264800};
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:PIRSR001191-2};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..691
FT                   /note="Matrix metalloproteinase-9"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018616570"
FT   DOMAIN          227..275
FT                   /note="Fibronectin type-II"
FT                   /evidence="ECO:0000259|PROSITE:PS51092"
FT   DOMAIN          285..333
FT                   /note="Fibronectin type-II"
FT                   /evidence="ECO:0000259|PROSITE:PS51092"
FT   DOMAIN          343..391
FT                   /note="Fibronectin type-II"
FT                   /evidence="ECO:0000259|PROSITE:PS51092"
FT   REPEAT          546..590
FT                   /note="Hemopexin"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01011"
FT   REPEAT          592..639
FT                   /note="Hemopexin"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01011"
FT   REGION          443..495
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           99..106
FT                   /note="Cysteine switch"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-5"
FT   ACT_SITE        403
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001191-1"
FT   BINDING         101
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         133
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT   BINDING         167
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
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         179
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT   BINDING         184
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT   BINDING         185
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT   BINDING         189
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT   BINDING         192
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="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT   BINDING         207
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         210
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT   BINDING         210
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT   BINDING         233
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001191-2"
FT   BINDING         233
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT   BINDING         504
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT   BINDING         506
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT   BINDING         550
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT   BINDING         552
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT   BINDING         598
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT   BINDING         646
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT   DISULFID        232..258
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT   DISULFID        246..273
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT   DISULFID        290..316
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT   DISULFID        304..331
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT   DISULFID        348..374
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT   DISULFID        362..389
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
SQ   SEQUENCE   691 AA;  77553 MW;  FF52CF08329D83F0 CRC64;
     MRCCTLAVCL LLGITVQNGW SIPLKSVFVT FPGDIVKNMT DVELAESYLK KFGYINTVQR
     SGFQSMTSTD KALKRMQRQL GLEETGQLDK QTLDAMKQPR CGVPDVANYK TFDGDLKWDH
     QDVTYRILNY SPDMESSLID DAFARAFKVW RDVTPLTFTR LFEGTADIMI SFGKADHGDL
     YPFDGKDGLL AHAYPPGEGI QGDAHFDDDE FWTLGKGPAV KTLYGNADGA MCHFPFTFEG
     RSYTSCTTDG RTDNLPWCST TSDYNKDKKF GFCPSELLYT FGGNADGAKC VFPFTFLEKE
     YDSCTTEGRN DGYRWCATTS NFDTDKKYGF CPSRDTAVIG GNSEGEPCHF PFVFLGKEYN
     SCTSEGRGDG KLWCSTTGNY DEDKKWGFCP DQGYSLFLVA AHEFGHALGL DHSSIREALM
     YPMYTYAEDF SLHQDDIEGI QYLYGSGTGP KPTTPEPDTP STTSNPDPDE TDSTDEPKPT
     DVPNPTTPST VDPDKDACKT LKFDTITVIE GVLHFFKDGH VWKVPSRGDA GHKGALSISE
     RWPALPAVID SAFEDVLTKK IYFFSGTRFW VYTGKSVLGP RSIEKLGLPS SVQKVEGALQ
     RGKGKVLLFS GENFWRLDLK TQKIDRGYPK YTDVVFGGVP NDAHDVFQYK GHIYFCRDRF
     YWRMNSRRQV DRVGYVKYDL LRCPESSGLR Y
//
DBGET integrated database retrieval system