MMP21_XENLA
ID MMP21_XENLA Reviewed; 604 AA.
AC O93470;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Matrix metalloproteinase-21;
DE Short=MMP-21;
DE Short=xMMP;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN Name=mmp21; Synonyms=mmp;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX PubMed=9153198; DOI=10.1074/jbc.272.21.13527;
RA Yang M., Murray M.T., Kurkinen M.;
RT "A novel matrix metalloproteinase gene (XMMP) encoding vitronectin-like
RT motifs is transiently expressed in Xenopus laevis early embryo
RT development.";
RL J. Biol. Chem. 272:13527-13533(1997).
CC -!- FUNCTION: Plays a specialized role in the generation of left-right
CC asymmetry during embryogenesis. May act as a negative regulator of the
CC NOTCH-signaling pathway. {ECO:0000250|UniProtKB:Q8N119}.
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: Transiently expressed during embryo development.
CC Undetected in the blastula stage embryo, induced in gastrula embryo,
CC expressed in neurula embryo, and then down-regulated in pretailbud
CC embryo. {ECO:0000269|PubMed:9153198}.
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; U82541; AAC21447.1; -; mRNA.
DR RefSeq; NP_001079285.1; NM_001085816.1.
DR AlphaFoldDB; O93470; -.
DR SMR; O93470; -.
DR MEROPS; M10.026; -.
DR GeneID; 378572; -.
DR KEGG; xla:378572; -.
DR CTD; 378572; -.
DR Xenbase; XB-GENE-960307; mmp21.L.
DR OrthoDB; 1075463at2759; -.
DR Proteomes; UP000186698; Chromosome 7L.
DR Bgee; 378572; Expressed in neurula embryo and 11 other tissues.
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; cd04278; ZnMc_MMP; 1.
DR Gene3D; 2.110.10.10; -; 2.
DR Gene3D; 3.40.390.10; -; 1.
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; Reference proteome;
KW Repeat; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..180
FT /evidence="ECO:0000250"
FT /id="PRO_0000028844"
FT CHAIN 181..604
FT /note="Matrix metalloproteinase-21"
FT /id="PRO_0000028845"
FT REPEAT 365..424
FT /note="Hemopexin 1"
FT REPEAT 426..482
FT /note="Hemopexin 2"
FT REPEAT 483..531
FT /note="Hemopexin 3"
FT REPEAT 538..594
FT /note="Hemopexin 4"
FT REGION 132..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 133..140
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT COMPBIAS 153..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 319
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 135
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 318
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 322
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 328
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 404
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 407
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 364..595
FT /evidence="ECO:0000250"
SQ SEQUENCE 604 AA; 70146 MW; 4E7BC8857F660417 CRC64;
MPSIKLLVWC CLCVISPRLC HSEKLFHSRD RSDLQPSAIE QAELVKDMLS AQQFLAKYGW
TQPVIWDPSS TNENEPLKDF SLMQEGVCNP RQEVAEPTKS PQFIDALKKF QKLNNLPVTG
TLDDATINAM NKPRCGVPDN QMAKKETEKP TAAQSLENKT KDSENVTQQN PDPPKIRRKR
FLDMLMYSNK YREEQEALQK STGKVFTKKL LKWRMIGEGY SNQLSINEQR YVFRLAFRMW
SEVMPLDFEE DNTSPLSQID IKLGFGRGRH LGCSRAFDGS GQEFAHAWFL GDIHFDDDEH
FTAPSSEHGI SLLKVAAHEI GHVLGLSHIH RVGSIMQPNY IPQDSGFELD LSDRRAIQNL
YGSCEGPFDT AFDWIYKEKN QYGELVVRYN TYFFRNSWYW MYENRSNRTR YGDPLAIANG
WHGIPVQNID AFVHVWTWTR DASYFFKGTQ YWRYDSENDK AYAEDAQGKS YPRLISEGFP
GIPSPINAAY FDRRRQYIYF FRDSQVFAFD INRNRVAPDF PKRILDFFPA VAANNHPKGN
IDVAYYSYTY SSLFLFKGKE FWKVVSDKDR RQNPSLPYNG LFPRRAISQQ WFDICNVHPS
LLKI
