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MMP14_PONAB
ID   MMP14_PONAB             Reviewed;         582 AA.
AC   Q5RES1;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Matrix metalloproteinase-14;
DE            Short=MMP-14;
DE            EC=3.4.24.80;
DE   Flags: Precursor;
GN   Name=MMP14;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Endopeptidase that degrades various components of the
CC       extracellular matrix, such as collagen. Activates progelatinase A.
CC       Essential for pericellular collagenolysis and modeling of skeletal and
CC       extraskeletal connective tissues during development. May be involved in
CC       actin cytoskeleton reorganization by cleaving PTK7. Acts as a positive
CC       regulator of cell growth and migration via activation of MMP15 in
CC       association with pro-MMP2. Involved in the formation of the
CC       fibrovascular tissues in association with pro-MMP2. Cleaves ADGRB1 to
CC       release vasculostatin-40 which inhibits angiogenesis.
CC       {ECO:0000250|UniProtKB:P50281, ECO:0000250|UniProtKB:P53690}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endopeptidase activity. Activates progelatinase A by cleavage
CC         of the propeptide at 37-Asn-|-Leu-38. Other bonds hydrolyzed include
CC         35-Gly-|-Ile-36 in the propeptide of collagenase 3, and 341-Asn-|-
CC         Phe-342, 441-Asp-|-Leu-442 and 354-Gln-|-Thr-355 in the aggrecan
CC         interglobular domain.; EC=3.4.24.80;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Interacts (via C-terminal cytoplasmic tail) with BST2.
CC       Interacts with DLL1; inhibits DLL1-induced Notch signaling.
CC       {ECO:0000250|UniProtKB:P50281}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}. Melanosome {ECO:0000250}. Cytoplasm
CC       {ECO:0000250}. Note=Forms a complex with BST2 and localizes to the
CC       cytoplasm. {ECO:0000250}.
CC   -!- DOMAIN: The conserved cysteine present in the cysteine-switch motif
CC       binds the catalytic zinc ion, thus inhibiting the enzyme. The
CC       dissociation of the cysteine from the zinc ion upon the activation-
CC       peptide release activates the enzyme.
CC   -!- PTM: Tyrosine phosphorylated by PKDCC/VLK.
CC       {ECO:0000250|UniProtKB:P50281}.
CC   -!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
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DR   EMBL; CR857445; CAH89736.1; -; mRNA.
DR   RefSeq; NP_001124793.1; NM_001131321.2.
DR   AlphaFoldDB; Q5RES1; -.
DR   BMRB; Q5RES1; -.
DR   SMR; Q5RES1; -.
DR   STRING; 9601.ENSPPYP00000006416; -.
DR   MEROPS; M10.014; -.
DR   GeneID; 100171646; -.
DR   KEGG; pon:100171646; -.
DR   CTD; 4323; -.
DR   eggNOG; KOG1565; Eukaryota.
DR   InParanoid; Q5RES1; -.
DR   OrthoDB; 1075463at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0004222; F:metalloendopeptidase activity; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0045746; P:negative regulation of Notch signaling pathway; ISS:UniProtKB.
DR   GO; GO:0045579; P:positive regulation of B cell differentiation; ISS:UniProtKB.
DR   GO; GO:0010831; P:positive regulation of myotube differentiation; ISS:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00094; HX; 1.
DR   CDD; cd04278; ZnMc_MMP; 1.
DR   Gene3D; 1.10.101.10; -; 1.
DR   Gene3D; 2.110.10.10; -; 1.
DR   Gene3D; 3.40.390.10; -; 1.
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; IPR033739; M10A_MMP.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001818; Pept_M10_metallopeptidase.
DR   InterPro; IPR021190; Pept_M10A.
DR   InterPro; IPR021805; Pept_M10A_metallopeptidase_C.
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   Pfam; PF11857; DUF3377; 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; SSF47090; SSF47090; 1.
DR   SUPFAM; SSF50923; SSF50923; 1.
DR   PROSITE; PS00546; CYSTEINE_SWITCH; 1.
DR   PROSITE; PS00024; HEMOPEXIN; 1.
DR   PROSITE; PS51642; HEMOPEXIN_2; 4.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Cleavage on pair of basic residues; Cytoplasm; Disulfide bond;
KW   Hydrolase; Membrane; Metal-binding; Metalloprotease; Phosphoprotein;
KW   Protease; Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix; Zinc; Zymogen.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..111
FT                   /note="Activation peptide"
FT                   /id="PRO_0000330604"
FT   CHAIN           112..582
FT                   /note="Matrix metalloproteinase-14"
FT                   /id="PRO_0000330605"
FT   TOPO_DOM        112..541
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        542..562
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        563..582
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          316..364
FT                   /note="Hemopexin 1"
FT   REPEAT          365..410
FT                   /note="Hemopexin 2"
FT   REPEAT          412..460
FT                   /note="Hemopexin 3"
FT   REPEAT          461..508
FT                   /note="Hemopexin 4"
FT   REGION          284..317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           91..98
FT                   /note="Cysteine switch"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        240
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         93
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /note="in inhibited form"
FT                   /evidence="ECO:0000250"
FT   BINDING         239
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT   BINDING         243
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT   BINDING         249
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT   MOD_RES         399
FT                   /note="Phosphotyrosine; by PKDCC"
FT                   /evidence="ECO:0000250|UniProtKB:P50281"
FT   DISULFID        319..508
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   582 AA;  65832 MW;  9CC4480F6DEE9003 CRC64;
     MSPAPRPSRC LLLPLLTLGT ALASLGSAQS SSFSPEAWLQ QYGYLPPGDL RTHTQRSPQS
     LSAAIAAMQK FYGLRVTGKA DADTMKAMRR PRCGVPDKFG AEIKANVRRK RYAIQGLKWQ
     HNEITFCIQN YTPKVGEYAT YEAIRKAFRV WESATPLRFR EVPYAYIREG HEKQADVMIF
     FAEGFHGDST PFDGEGGFLA HAYFPGPNIG GDTHFDSAEP WTVGNEDLNG NDIFLVAVHE
     LGHALGLEHS SDPSAIMAPF YQWMDTENFV LPEDDRRGIQ QLYGSESGFP TKMPPQPRTT
     SRPSVPDKPK NPTYGPNTCD GNFDTVAMLR GEMFVFKERW FWRVRNNQVM DGYPMPIGQF
     WRGLPASINT AYERKDGKFV FFKGDKHWVF DEASLEPGYP KHIKELGRGL PTDKIDAALF
     WMPNGKTYFF RGNKYYRFNE ELRAVDSEYP KNIKVWEGIP ESPRGSFMGS DEVFTYFYKG
     NKYWKFDNQK LKVEPGYPKS ALRDWMGCPS GGRPDEGTEE ETEVIIIEVD EEGGGAVSAA
     AVVLPVLLLL LVLAVGLAVF FFRRHGTPRR LLYCQRSLLD KV
 
 
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