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Protein

Matrix metalloproteinase-23

Gene

Mmp23

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Protease. May regulate the surface expression of some potassium channels by retaining them in the endoplasmic reticulum.1 Publication

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Enzyme regulationi

Inhibited by TIMP2.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi212 – 2121Zinc; catalyticPROSITE-ProRule annotation
Active sitei213 – 2131PROSITE-ProRule annotation
Metal bindingi216 – 2161Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi222 – 2221Zinc; catalyticPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM10.022.

Names & Taxonomyi

Protein namesi
Recommended name:
Matrix metalloproteinase-23 (EC:3.4.24.-)
Short name:
MMP-23
Alternative name(s):
metalloprotease in the female reproductive tract
Short name:
MIFR
Cleaved into the following chain:
Gene namesi
Name:Mmp23
Synonyms:Mifr
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 5

Organism-specific databases

RGDi620201. Mmp23.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1919CytoplasmicSequence analysisAdd
BLAST
Transmembranei20 – 3819Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini39 – 391353LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 391391Matrix metalloproteinase-23PRO_0000259918Add
BLAST
Propeptidei1 – 7979Sequence analysisPRO_0000259919Add
BLAST
Chaini80 – 391312Matrix metalloproteinase-23, soluble formPRO_0000259920Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi93 – 931N-linked (GlcNAc...)Sequence analysis
Glycosylationi149 – 1491N-linked (GlcNAc...)Sequence analysis
Glycosylationi233 – 2331N-linked (GlcNAc...)Sequence analysis
Disulfide bondi256 ↔ 2901 Publication
Disulfide bondi263 ↔ 2831 Publication
Disulfide bondi272 ↔ 2871 Publication
Glycosylationi317 – 3171N-linked (GlcNAc...)Sequence analysis
Disulfide bondi322 ↔ 371By similarity

Post-translational modificationi

N-glycosylated.1 Publication
Proteolytic cleavage might yield an active form.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei79 – 802Cleavage; by furin-like proteaseSequence analysis

Keywords - PTMi

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

Proteomic databases

PaxDbiO88272.

Expressioni

Tissue specificityi

Expressed at the highest levels in ovary and uterus. In ovary expression is strictly confined to granulosa cells of preantral and small antral follicles. Detected also in testis and prostate.1 Publication

Gene expression databases

BgeeiENSRNOG00000017477.
GenevisibleiO88272. RN.

Interactioni

Protein-protein interaction databases

BioGridi250194. 2 interactions.
STRINGi10116.ENSRNOP00000061528.

Structurei

Secondary structure

1
391
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi263 – 2675Combined sources
Turni268 – 2736Combined sources
Helixi276 – 2827Combined sources
Turni284 – 2885Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2K72NMR-A254-290[»]
ProteinModelPortaliO88272.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO88272.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini256 – 29035ShKTPROSITE-ProRule annotationAdd
BLAST
Domaini296 – 38186Ig-like C2-typeAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi76 – 794Poly-Arg

Domaini

The ShKT domain associates with, and blocks several potassium channels in the nanomolar to low micromolar range. The relative affinity is Kv1.6 > Kv1.3 > Kv1.1 = Kv3.2 > Kv1.4.

Sequence similaritiesi

Belongs to the peptidase M10A family.Curated
Contains 1 ShKT domain.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
GeneTreeiENSGT00830000128254.
HOGENOMiHOG000231157.
HOVERGENiHBG053177.
InParanoidiO88272.
KOiK08001.
OMAiHCFDGIT.
OrthoDBiEOG091G03DP.
PhylomeDBiO88272.

Family and domain databases

CDDicd04278. ZnMc_MMP. 1 hit.
Gene3Di2.60.40.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR033739. M10A_MMP.
IPR024079. MetalloPept_cat_dom.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR006026. Peptidase_Metallo.
IPR003582. ShKT_dom.
[Graphical view]
PfamiPF00413. Peptidase_M10. 1 hit.
PF01549. ShK. 1 hit.
[Graphical view]
PRINTSiPR00138. MATRIXIN.
SMARTiSM00254. ShKT. 1 hit.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
PS51670. SHKT. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O88272-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGWRACLRPE ASGAVQGRWL GAVLSGLCLL SALAFLEWLG SPTETAWNAA
60 70 80 90 100
QGNVDAPDVG GSTPQVPSLL SMLVTRRRRY TLTPARLRWD HFNLTYRILS
110 120 130 140 150
FPRNLLSPEE TRRGLAAAFR MWSDVSPFSF REVAPERPSD LKIGFYPVNH
160 170 180 190 200
TDCLVSALHH CFDGPTGELA HAFFPPHGGI HFDDSEYWVL GPTRYSWKKG
210 220 230 240 250
VWLTDLVHVA AHEIGHALGL MHSQQDQALM HLNATLRGWK ALSQDELWGL
260 270 280 290 300
HRLYGCLDRI FVCTSWARKG FCDVRQRLMK RLCPRSCDFC YEFPFPTVAT
310 320 330 340 350
TTSPTRTKTR FVREGRNMTF HCGQKILHKK GKVYWYKDQE PLEFSYPGYL
360 370 380 390
ALGEARLSII ANAVNEGTYT CVVRHRQRVL TTYSWRVRVR S
Length:391
Mass (Da):44,618
Last modified:November 1, 1998 - v1
Checksum:iF980FD50BDDB6A10
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB010960 mRNA. Translation: BAA24832.1.
BC086586 mRNA. Translation: AAH86586.1.
RefSeqiNP_446058.1. NM_053606.2.
UniGeneiRn.22562.

Genome annotation databases

EnsembliENSRNOT00000066880; ENSRNOP00000061528; ENSRNOG00000017477.
GeneIDi94339.
KEGGirno:94339.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB010960 mRNA. Translation: BAA24832.1.
BC086586 mRNA. Translation: AAH86586.1.
RefSeqiNP_446058.1. NM_053606.2.
UniGeneiRn.22562.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2K72NMR-A254-290[»]
ProteinModelPortaliO88272.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi250194. 2 interactions.
STRINGi10116.ENSRNOP00000061528.

Protein family/group databases

MEROPSiM10.022.

Proteomic databases

PaxDbiO88272.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000066880; ENSRNOP00000061528; ENSRNOG00000017477.
GeneIDi94339.
KEGGirno:94339.

Organism-specific databases

CTDi26561.
RGDi620201. Mmp23.

Phylogenomic databases

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
GeneTreeiENSGT00830000128254.
HOGENOMiHOG000231157.
HOVERGENiHBG053177.
InParanoidiO88272.
KOiK08001.
OMAiHCFDGIT.
OrthoDBiEOG091G03DP.
PhylomeDBiO88272.

Miscellaneous databases

EvolutionaryTraceiO88272.
PROiO88272.

Gene expression databases

BgeeiENSRNOG00000017477.
GenevisibleiO88272. RN.

Family and domain databases

CDDicd04278. ZnMc_MMP. 1 hit.
Gene3Di2.60.40.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR033739. M10A_MMP.
IPR024079. MetalloPept_cat_dom.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR006026. Peptidase_Metallo.
IPR003582. ShKT_dom.
[Graphical view]
PfamiPF00413. Peptidase_M10. 1 hit.
PF01549. ShK. 1 hit.
[Graphical view]
PRINTSiPR00138. MATRIXIN.
SMARTiSM00254. ShKT. 1 hit.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
PS51670. SHKT. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMMP23_RAT
AccessioniPrimary (citable) accession number: O88272
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 14, 2006
Last sequence update: November 1, 1998
Last modified: September 7, 2016
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. 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.