MMP21_CYNPY
ID MMP21_CYNPY Reviewed; 616 AA.
AC Q90YC2;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Matrix metalloproteinase-21;
DE Short=MMP-21;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN Name=MMP21;
OS Cynops pyrrhogaster (Japanese fire-bellied newt) (Molge pyrrhogaster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Caudata; Salamandroidea; Salamandridae; Pleurodelinae; Cynops.
OX NCBI_TaxID=8330;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=11606053; DOI=10.1006/bbrc.2001.5784;
RA Suzuki A.S., Tadano Y., Yamamoto T., Abe S., Tajima T.;
RT "Expression of a novel matrix metalloproteinase gene during Cynops early
RT embryogenesis.";
RL Biochem. Biophys. Res. Commun. 288:380-384(2001).
CC -!- FUNCTION: May play a role in gastrulation-related cell movement
CC (PubMed:11606053). Plays a specialized role in the generation of left-
CC right asymmetry during embryogenesis. May act as a negative regulator
CC of the NOTCH-signaling pathway (By similarity).
CC {ECO:0000250|UniProtKB:O93470, ECO:0000250|UniProtKB:Q8N119,
CC ECO:0000269|PubMed:11606053}.
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Detected during early embryogenesis, then,
CC gradually decreased, but increased again starting in late gastrula.
CC There are regional diiferences in the level of expression at late
CC gastrula: the involved archenteron roof is the predominant site, while
CC there is weak expression in the neuroectoderm and epidermal ectoderm.
CC {ECO:0000269|PubMed:11606053}.
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: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
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DR EMBL; AB054185; BAB62075.1; -; mRNA.
DR PIR; JC7776; JC7776.
DR AlphaFoldDB; Q90YC2; -.
DR SMR; Q90YC2; -.
DR MEROPS; M10.026; -.
DR GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0061371; P:determination of heart left/right asymmetry; ISS:UniProtKB.
DR GO; GO:0007368; P:determination of left/right symmetry; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00094; HX; 1.
DR CDD; cd04278; ZnMc_MMP; 1.
DR Gene3D; 2.110.10.10; -; 2.
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; 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 Pfam; PF00045; Hemopexin; 3.
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; PS51642; HEMOPEXIN_2; 4.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 2: Evidence at transcript level;
KW Calcium; Cleavage on pair of basic residues; Disulfide bond; Glycoprotein;
KW Hydrolase; Metal-binding; Metalloprotease; Protease; Repeat; Secreted;
KW Signal; Zinc; Zymogen.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..192
FT /evidence="ECO:0000250"
FT /id="PRO_0000028842"
FT CHAIN 193..616
FT /note="Matrix metalloproteinase-21"
FT /id="PRO_0000028843"
FT REPEAT 376..435
FT /note="Hemopexin 1"
FT REPEAT 437..493
FT /note="Hemopexin 2"
FT REPEAT 494..542
FT /note="Hemopexin 3"
FT REPEAT 549..605
FT /note="Hemopexin 4"
FT REGION 157..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 139..146
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT ACT_SITE 330
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 141
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 329
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 333
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 339
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 418
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 597
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 375..606
FT /evidence="ECO:0000250"
SQ SEQUENCE 616 AA; 70428 MW; ABFC72D8B13E5003 CRC64;
MPTAPALGAL LLLLGALTPG HQEKLFHSRD HSDLQPSPQH QAELVTDLQS AQQFLSKYGW
TEPVKWEGTS SKNAAELPRY GDADLMQEGA SISRYGQEFP LEPTQAPAFV EALRKFQTLN
GLPATGKLDD STIAAMNKPR CGVPDNQIGK ESAIVKSNSN NVTEKASGKS LNTTTNQNPE
NGTSTSKIRK KRFLQMLAAP VRYKDQANQG STVRGAFSKK LLKWRLIGEG YSSQLSIDEQ
RYVFKTAFRM WSEVMPLDFE EDLTSPMSLI DVKLGFGRGR HLGCTRSFDG SGQEFAHAWF
LGDIHFDDDE HFTAPSSDSG ISLLKVAVHE IGHVLGLSHI YQTGSIMQPN YIPQEAGFEL
DWTDRKAIQM LYGTCEGSFD AVFDWIWKER NQYGELVLRY NTYFFRNAWY WLYENRKNRT
RYGDPVTVSL GWHGIPAEGI DAFVHVWTWT EDATYFFKGT QYWRYDSEND QAYIKDAQGN
QYPRLISEGF PKIPSPINTA FFDRRDQFIY FFKDAHVYAF DVKRNMVANH YPKRIIDVFP
AVVRNNHPFG NIDAAYYAYT HNSIFLFKGK EYWKVVSDKD RQQNPKLPRN GLFLKKNISE
QWTDICNVHS SMLKMR
