ID A0A093QQ49_PYGAD Unreviewed; 519 AA.
AC A0A093QQ49;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 08-OCT-2025, entry version 47.
DE RecName: Full=Matrix metalloproteinase-17 {ECO:0000256|ARBA:ARBA00074057};
DE AltName: Full=Membrane-type matrix metalloproteinase 4 {ECO:0000256|ARBA:ARBA00075831};
DE AltName: Full=Membrane-type-4 matrix metalloproteinase {ECO:0000256|ARBA:ARBA00076283};
DE Flags: Fragment;
GN ORFNames=AS28_10104 {ECO:0000313|EMBL:KFW60849.1};
OS Pygoscelis adeliae (Adelie penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Aequornithes; Sphenisciformes;
OC Spheniscidae; Pygoscelis.
OX NCBI_TaxID=9238 {ECO:0000313|EMBL:KFW60849.1, ECO:0000313|Proteomes:UP000054081};
RN [1] {ECO:0000313|EMBL:KFW60849.1, ECO:0000313|Proteomes:UP000054081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS28 {ECO:0000313|EMBL:KFW60849.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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: Cell membrane {ECO:0000256|ARBA:ARBA00004471};
CC Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004471}; Extracellular
CC side {ECO:0000256|ARBA:ARBA00004471}. Secreted, extracellular space,
CC extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- SIMILARITY: Belongs to the peptidase M10A family.
CC {ECO:0000256|ARBA:ARBA00010370}.
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DR EMBL; KL224529; KFW60849.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093QQ49; -.
DR STRING; 9238.A0A093QQ49; -.
DR MEROPS; M10.017; -.
DR Proteomes; UP000054081; Unassembled WGS sequence.
DR GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098552; C:side of membrane; 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:TreeGrafter.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00094; HX; 1.
DR CDD; cd04278; ZnMc_MMP; 1.
DR FunFam; 2.110.10.10:FF:000003; Matrix metallopeptidase 17; 1.
DR FunFam; 3.40.390.10:FF:000016; Matrix metallopeptidase 17; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.110.10.10; Hemopexin-like domain; 1.
DR InterPro; IPR000585; Hemopexin-like_dom.
DR InterPro; IPR036375; Hemopexin-like_dom_sf.
DR InterPro; IPR018487; Hemopexin-like_repeat.
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; IPR006026; Peptidase_Metallo.
DR InterPro; IPR002477; Peptidoglycan-bd-like.
DR InterPro; IPR036365; PGBD-like_sf.
DR PANTHER; PTHR10201; MATRIX METALLOPROTEINASE; 1.
DR PANTHER; PTHR10201:SF21; MATRIX METALLOPROTEINASE-17; 1.
DR Pfam; PF00045; Hemopexin; 4.
DR Pfam; PF00413; Peptidase_M10; 1.
DR Pfam; PF01471; PG_binding_1; 1.
DR PIRSF; PIRSF001191; Peptidase_M10A_matrix; 1.
DR PRINTS; PR00138; MATRIXIN.
DR SMART; SM00120; HX; 4.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF50923; Hemopexin-like domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF47090; PGBD-like; 1.
DR PROSITE; PS51642; HEMOPEXIN_2; 4.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRSR:PIRSR621190-2};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
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:UP000054081};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR001191-2};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 75..242
FT /note="Peptidase metallopeptidase"
FT /evidence="ECO:0000259|SMART:SM00235"
FT REPEAT 284..329
FT /note="Hemopexin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01011"
FT REPEAT 333..379
FT /note="Hemopexin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01011"
FT REPEAT 380..426
FT /note="Hemopexin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01011"
FT REPEAT 427..474
FT /note="Hemopexin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01011"
FT REGION 478..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..506
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 195
FT /evidence="ECO:0000256|PIRSR:PIRSR001191-1"
FT BINDING 57
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 130
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 147
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 148
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
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 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 171
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 172
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 174
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 174
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="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001191-2"
FT BINDING 198
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001191-2"
FT BINDING 204
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001191-2"
FT BINDING 212
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 288
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 337
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 385
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT BINDING 431
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2"
FT MOD_RES 368
FT /note="Phosphotyrosine; by PKDCC"
FT /evidence="ECO:0000256|PIRSR:PIRSR621190-4"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFW60849.1"
FT NON_TER 519
FT /evidence="ECO:0000313|EMBL:KFW60849.1"
SQ SEQUENCE 519 AA; 59189 MW; A6AA5B79037E919D CRC64;
DWLTKFGYLP PPDPVTGQLQ TQEELTKAIT AMQRFGGLEA TGVLDEATLE LMKTPRCSLP
DLAAAEARRK RFTQAVTKWS KRNLSWRVRT FPKETHLGHD TVRALMYYAL KVWSDITPLN
FHEVAGNNAD IQIDFSKADH NDGYPFDGPG GTVAHAFFPG DHHTAGDTHF DDDEYWTFRS
SDAHGMDLFA VAVHEFGHAI GLTHISAIES IMRPYYQGPV GDPLKYDLPY EDKVRIWQLY
GVRESVSPTA KPEISKTDDH PILPELPENR STVPLRRDVP NRCNTHFDAV AQIRGEAFFF
KGKYFWRLTR NKHLVSLQPA QIHRFWRGLP LNLDSLDAVY ERTSDHKIVF FKGDRYWVFK
DNNVEEGYPR PISDFGLPPG GIDAAFSWAH NDKTYFFKDN LYWRYDDHER RMDPGYPSET
ILWKGIPSPL DDAMRWSDGA SYFFRGKEYW KVLDSDLEAQ PGYPQSIARD WLVCSDMQSD
SPEAAGSSRT GARSKPGQHD ESRSENGYEV CSCTSASPS
//
