O88676 (MMP23_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	391 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 toxin-like 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.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Alternative splicing
Domain	Immunoglobulin domain Signal-anchor Transmembrane Transmembrane helix
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Protease
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Zymogen
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	proteolysis Inferred from sequence or structural similarity. Source: UniProtKB reproduction Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular matrix Inferred from electronic annotation. Source: InterPro integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	metalloendopeptidase activity Inferred from sequence or structural similarity. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 391	391	Matrix metalloproteinase-23		PRO_0000259915
	Propeptide	1 – 79	79	Potential		PRO_0000259916
	Chain	80 – 391	312	Matrix metalloproteinase-23, soluble form		PRO_0000259917
Regions
	Topological domain	1 – 18	18	Cytoplasmic Potential
	Transmembrane	19 – 39	21	Helical; Potential
	Topological domain	40 – 391	352	Lumenal Potential
	Domain	298 – 383	86	Ig-like C2-type
	Region	254 – 290	37	Toxin-like domain (TxD) By similarity
	Compositional bias	76 – 79	4	Poly-Arg
Sites
	Active site	213	1	By similarity
	Metal binding	212	1	Zinc; catalytic By similarity
	Metal binding	216	1	Zinc; catalytic By similarity
	Metal binding	222	1	Zinc; catalytic By similarity
	Site	79 – 80	2	Cleavage; by furin-like protease Potential
Amino acid modifications
	Glycosylation	93	1	N-linked (GlcNAc...) Potential
	Glycosylation	149	1	N-linked (GlcNAc...) Potential
	Glycosylation	233	1	N-linked (GlcNAc...) Potential
	Glycosylation	317	1	N-linked (GlcNAc...) Potential
	Disulfide bond	256 ↔ 290		By similarity
	Disulfide bond	263 ↔ 283		By similarity
	Disulfide bond	272 ↔ 287		By similarity
	Disulfide bond	322 ↔ 371		By similarity
Natural variations
	Alternative sequence	144 – 157	14	Missing in isoform 2.		VSP_021561

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 8C9675020F02F632	FASTA	391	44,451
	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
	Isoform 2 [UniParc]. Checksum: 8C30623283790A72	FASTA	377	42,946
	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 LKIVHHCFDG PTGELAHAFF PPHGGIHFDD SEYWVLGPTR 190 200 210 220 230 240 YSWKKGVWLT NLVHVAAHEI GHALGLMHSQ QDQALMHLNA TLRGWKALSQ DELWGLHRLY 250 260 270 280 290 300 GCLDRIFVCA SWARKGFCDV RQRLMKRLCP RSCDFCYEFP FPTVATTTSP TRTKTRLVRE 310 320 330 340 350 360 GRNMTFHCGQ KILHKKGKVY WYKDQEPLEF SYPGYLALGE AQLSIIANAV NEGTYTCVVR 370 RHQRVLSTYS WRVRVRN

References

	« Hide 'large scale' referencesShow '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. , 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.
IPI	IPI00133157. IPI00808280.
RefSeq	NP_036115.1. NM_011985.2.
UniGene	Mm.29373.
3D structure databases
HSSP	HSSP built from PDB template 1CGL based on UniProtKB P03956.
ProteinModelPortal	O88676.
SMR	O88676. Positions 88-255, 309-379.
ModBase	Search...
Protein family/group databases
MEROPS	M10.022.
TCDB	8.B.14.2.1. sea anemone peptide toxin, class 1 (BgK) family.
PTM databases
PhosphoSite	O88676.
Proteomic databases
PRIDE	O88676.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000030937; ENSMUSP00000030937; ENSMUSG00000029061.
GeneID	26561.
KEGG	mmu:26561.
UCSC	uc012dqs.1. mouse.
Organism-specific databases
CTD	26561.
MGI	MGI:1347361. Mmp23.
Phylogenomic databases
eggNOG	NOG245056.
GeneTree	ENSGT00570000079061.
HOGENOM	HOG000231157.
HOVERGEN	HBG053177.
InParanoid	O88676.
KO	K08001.
OMA	HCFDGIT.
OrthoDB	EOG4RFKSV.
Gene expression databases
ArrayExpress	O88676.
Bgee	O88676.
CleanEx	MM_MMP23.
Genevestigator	O88676.
GermOnline	ENSMUSG00000029061. Mus musculus.
Family and domain databases
Gene3D	2.60.40.10. 1 hit. 3.40.390.10. 1 hit.
InterPro	IPR007110. Ig-like_dom. IPR013783. Ig-like_fold. IPR003599. Ig_sub. IPR024079. MetalloPept_cat_dom. IPR001818. Pept_M10_metallopeptidase. IPR021190. Pept_M10A. IPR006026. Peptidase_Metallo. IPR003582. ShK_toxin. [Graphical view]
Pfam	PF00413. Peptidase_M10. 1 hit. PF01549. ShK. 1 hit. [Graphical view]
PRINTS	PR00138. MATRIXIN.
SMART	SM00409. IG. 1 hit. SM00254. ShKT. 1 hit. SM00235. ZnMc. 1 hit. [Graphical view]
PROSITE	PS50835. IG_LIKE. 1 hit. PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	304627.
SOURCE	Search...

Entry information

Entry name

MMP23_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 99 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program