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O88676 (MMP23_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Matrix metalloproteinase-23

Short name=MMP-23
EC=3.4.24.-
Alternative name(s):
CAMP metalloproteinase
Short name=CA-MMP

Cleaved into the following chain:

  1. Matrix metalloproteinase-23, soluble form
Gene names
Name:Mmp23
Synonyms:Cammp
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length391 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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

Cofactor

Binds 1 zinc ion per subunit By similarity.

Enzyme regulation

Inhibited by TIMP2.

Subcellular location

Endoplasmic reticulum membrane; Single-pass type II membrane protein By similarity. Membrane; Single-pass type II membrane protein. Note: A secreted form produced by proteolytic cleavage may also exist By similarity. Ref.1

Tissue specificity

Expressed at relatively high level in heart, lung and spleen. Not detected in brain, liver, skeletal muscle, kidney and testis. Ref.1

Developmental stage

Expressed at relatively high level at 7 days old embryo compared to those at stadges day 11, 15 and 17. Ref.1

Domain

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 By similarity.

Post-translational modification

N-glycosylated By similarity.

Proteolytic cleavage might yield an active form.

Sequence similarities

Belongs to the peptidase M10A family.

Contains 1 Ig-like C2-type (immunoglobulin-like) domain.

Contains 1 ShKT domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O88676-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O88676-2)

The sequence of this isoform differs from the canonical sequence as follows:
     144-157: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 391391Matrix metalloproteinase-23
PRO_0000259915
Propeptide1 – 7979 Potential
PRO_0000259916
Chain80 – 391312Matrix metalloproteinase-23, soluble form
PRO_0000259917

Regions

Topological domain1 – 1818Cytoplasmic Potential
Transmembrane19 – 3921Helical; Potential
Topological domain40 – 391352Lumenal Potential
Domain256 – 29035ShKT
Domain298 – 38386Ig-like C2-type
Compositional bias76 – 794Poly-Arg

Sites

Active site2131 By similarity
Metal binding2121Zinc; catalytic By similarity
Metal binding2161Zinc; catalytic By similarity
Metal binding2221Zinc; catalytic By similarity
Site79 – 802Cleavage; by furin-like protease Potential

Amino acid modifications

Glycosylation931N-linked (GlcNAc...) Potential
Glycosylation1491N-linked (GlcNAc...) Potential
Glycosylation2331N-linked (GlcNAc...) Potential
Glycosylation3171N-linked (GlcNAc...) Potential
Disulfide bond256 ↔ 290 By similarity
Disulfide bond263 ↔ 283 By similarity
Disulfide bond272 ↔ 287 By similarity
Disulfide bond322 ↔ 371 By similarity

Natural variations

Alternative sequence144 – 15714Missing in isoform 2.
VSP_021561

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 8C9675020F02F632

FASTA39144,451
        10         20         30         40         50         60 
MGCRACLRPE ASGAVQGRWL GAALSGLCLL SALALLEWLG APTETAWRAA QGNVDAPNVG 

        70         80         90        100        110        120 
SSTAQVPRLL TMSVTRRRRY TLTPARLRWD HFNLTYRVLS FPRNLLSPEE TRRGLAAAFR 

       130        140        150        160        170        180 
MWSDVSPFSF REVAPERPSD LKIGFYPVNH TDCLVSAVHH CFDGPTGELA HAFFPPHGGI 

       190        200        210        220        230        240 
HFDDSEYWVL GPTRYSWKKG VWLTNLVHVA AHEIGHALGL MHSQQDQALM HLNATLRGWK 

       250        260        270        280        290        300 
ALSQDELWGL HRLYGCLDRI FVCASWARKG FCDVRQRLMK RLCPRSCDFC YEFPFPTVAT 

       310        320        330        340        350        360 
TTSPTRTKTR LVREGRNMTF HCGQKILHKK GKVYWYKDQE PLEFSYPGYL ALGEAQLSII 

       370        380        390 
ANAVNEGTYT CVVRRHQRVL STYSWRVRVR N 

« Hide

Isoform 2 [UniParc].

Checksum: 8C30623283790A72
Show »

FASTA37742,946

References

« Hide 'large scale' references
[1]"CA-MMP: a matrix metalloproteinase with a novel cysteine array, but without the classic cysteine switch."
Pei D.
FEBS Lett. 457:262-270(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
Strain: BALB/c.
Tissue: Spleen.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Stomach.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF085742 mRNA. Translation: AAC34886.1.
AK146510 mRNA. Translation: BAE27223.1.
BC107357 mRNA. Translation: AAI07358.1.
BC107358 mRNA. Translation: AAI07359.1.
RefSeqNP_036115.1. NM_011985.2.
XP_006538945.1. XM_006538882.1.
XP_006538946.1. XM_006538883.1.
UniGeneMm.29373.

3D structure databases

ProteinModelPortalO88676.
SMRO88676. Positions 22-389.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSM10.022.

PTM databases

PhosphoSiteO88676.

Proteomic databases

PRIDEO88676.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000030937; ENSMUSP00000030937; ENSMUSG00000029061. [O88676-1]
GeneID26561.
KEGGmmu:26561.
UCSCuc008wed.1. mouse. [O88676-1]
uc012dqs.1. mouse. [O88676-2]

Organism-specific databases

CTD26561.
MGIMGI:1347361. Mmp23.

Phylogenomic databases

eggNOGNOG245056.
GeneTreeENSGT00730000110410.
HOGENOMHOG000231157.
HOVERGENHBG053177.
InParanoidO88676.
KOK08001.
OMAGFYPVNH.
OrthoDBEOG7KSX8P.
PhylomeDBO88676.
TreeFamTF315428.

Gene expression databases

BgeeO88676.
CleanExMM_MMP23.
GenevestigatorO88676.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
3.40.390.10. 1 hit.
InterProIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR024079. MetalloPept_cat_dom.
IPR028687. MMP23.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR006026. Peptidase_Metallo.
IPR003582. ShKT_dom.
[Graphical view]
PANTHERPTHR10201. PTHR10201. 1 hit.
PTHR10201:SF7. PTHR10201:SF7. 1 hit.
PfamPF00413. Peptidase_M10. 1 hit.
PF01549. ShK. 1 hit.
[Graphical view]
PRINTSPR00138. MATRIXIN.
SMARTSM00409. IG. 1 hit.
SM00254. ShKT. 1 hit.
SM00235. ZnMc. 1 hit.
[Graphical view]
PROSITEPS50835. IG_LIKE. 1 hit.
PS51670. SHKT. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio304627.
PROO88676.
SOURCESearch...

Entry information

Entry nameMMP23_MOUSE
AccessionPrimary (citable) accession number: O88676
Secondary accession number(s): Q3KNC0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 14, 2006
Last sequence update: November 1, 1998
Last modified: April 16, 2014
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot