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Protein

Matrix metalloproteinase-21

Gene

mmp21

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

May play a role in early embryo development.

Cofactori

Protein has several cofactor binding sites:
  • Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity
  • Ca2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi135 – 1351Zinc; in inhibited formBy similarity
Metal bindingi318 – 3181Zinc; catalyticPROSITE-ProRule annotation
Active sitei319 – 3191PROSITE-ProRule annotation
Metal bindingi322 – 3221Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi328 – 3281Zinc; catalyticPROSITE-ProRule annotation

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Protein family/group databases

MEROPSiM10.026.

Names & Taxonomyi

Protein namesi
Recommended name:
Matrix metalloproteinase-21 (EC:3.4.24.-)
Short name:
MMP-21
Short name:
xMMP
Gene namesi
Name:mmp21
Synonyms:mmp
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-960307. mmp21.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence analysisAdd
BLAST
Propeptidei23 – 180158By similarityPRO_0000028844Add
BLAST
Chaini181 – 604424Matrix metalloproteinase-21PRO_0000028845Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi158 – 1581N-linked (GlcNAc...)Sequence analysis
Glycosylationi165 – 1651N-linked (GlcNAc...)Sequence analysis
Disulfide bondi364 ↔ 595By similarity
Glycosylationi404 – 4041N-linked (GlcNAc...)Sequence analysis
Glycosylationi407 – 4071N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

The precursor is cleaved by a furin endopeptidase.By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Zymogen

Miscellaneous databases

PMAP-CutDBO93470.

Expressioni

Developmental stagei

Transiently expressed during embryo development. Undetected in the blastula stage embryo, induced in gastrula embryo, expressed in neurula embryo, and then down-regulated in pretailbud embryo.1 Publication

Structurei

3D structure databases

ProteinModelPortaliO93470.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati365 – 42460Hemopexin 1Add
BLAST
Repeati426 – 48257Hemopexin 2Add
BLAST
Repeati483 – 53149Hemopexin 3Add
BLAST
Repeati538 – 59457Hemopexin 4Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi133 – 1408Cysteine switchBy similarity

Domaini

The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.

Sequence similaritiesi

Belongs to the peptidase M10A family.Curated
Contains 4 hemopexin repeats.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

HOVERGENiHBG052483.
KOiK08000.

Family and domain databases

Gene3Di1.10.101.10. 2 hits.
2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR024079. MetalloPept_cat_dom.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR016293. Pept_M10A_stromelysin-type.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PfamiPF00045. Hemopexin. 3 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PIRSFiPIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSiPR00138. MATRIXIN.
SMARTiSM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMiSSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
PROSITEiPS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O93470-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPSIKLLVWC CLCVISPRLC HSEKLFHSRD RSDLQPSAIE QAELVKDMLS
60 70 80 90 100
AQQFLAKYGW TQPVIWDPSS TNENEPLKDF SLMQEGVCNP RQEVAEPTKS
110 120 130 140 150
PQFIDALKKF QKLNNLPVTG TLDDATINAM NKPRCGVPDN QMAKKETEKP
160 170 180 190 200
TAAQSLENKT KDSENVTQQN PDPPKIRRKR FLDMLMYSNK YREEQEALQK
210 220 230 240 250
STGKVFTKKL LKWRMIGEGY SNQLSINEQR YVFRLAFRMW SEVMPLDFEE
260 270 280 290 300
DNTSPLSQID IKLGFGRGRH LGCSRAFDGS GQEFAHAWFL GDIHFDDDEH
310 320 330 340 350
FTAPSSEHGI SLLKVAAHEI GHVLGLSHIH RVGSIMQPNY IPQDSGFELD
360 370 380 390 400
LSDRRAIQNL YGSCEGPFDT AFDWIYKEKN QYGELVVRYN TYFFRNSWYW
410 420 430 440 450
MYENRSNRTR YGDPLAIANG WHGIPVQNID AFVHVWTWTR DASYFFKGTQ
460 470 480 490 500
YWRYDSENDK AYAEDAQGKS YPRLISEGFP GIPSPINAAY FDRRRQYIYF
510 520 530 540 550
FRDSQVFAFD INRNRVAPDF PKRILDFFPA VAANNHPKGN IDVAYYSYTY
560 570 580 590 600
SSLFLFKGKE FWKVVSDKDR RQNPSLPYNG LFPRRAISQQ WFDICNVHPS

LLKI
Length:604
Mass (Da):70,146
Last modified:November 1, 1998 - v1
Checksum:i4E7BC8857F660417
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U82541 mRNA. Translation: AAC21447.1.
RefSeqiNP_001079285.1. NM_001085816.1.
UniGeneiXl.285.

Genome annotation databases

GeneIDi378572.
KEGGixla:378572.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U82541 mRNA. Translation: AAC21447.1.
RefSeqiNP_001079285.1. NM_001085816.1.
UniGeneiXl.285.

3D structure databases

ProteinModelPortaliO93470.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM10.026.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi378572.
KEGGixla:378572.

Organism-specific databases

CTDi118856.
XenbaseiXB-GENE-960307. mmp21.

Phylogenomic databases

HOVERGENiHBG052483.
KOiK08000.

Miscellaneous databases

PMAP-CutDBO93470.

Family and domain databases

Gene3Di1.10.101.10. 2 hits.
2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR024079. MetalloPept_cat_dom.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR016293. Pept_M10A_stromelysin-type.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PfamiPF00045. Hemopexin. 3 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PIRSFiPIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSiPR00138. MATRIXIN.
SMARTiSM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMiSSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
PROSITEiPS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "A novel matrix metalloproteinase gene (XMMP) encoding vitronectin-like motifs is transiently expressed in Xenopus laevis early embryo development."
    Yang M., Murray M.T., Kurkinen M.
    J. Biol. Chem. 272:13527-13533(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiMMP21_XENLA
AccessioniPrimary (citable) accession number: O93470
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: November 1, 1998
Last modified: January 7, 2015
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.