O75900 (MMP23_HUMAN) 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):
Femalysin
MIFR-1
Matrix metalloproteinase-21
Short name=MMP-21
Matrix metalloproteinase-22
Short name=MMP-22

Cleaved into the following chain:

1. Matrix metalloproteinase-23, soluble form

Gene names

Name:	MMP23A
Synonyms:	MMP21
AND
Name:	MMP23B
Synonyms:	MMP21, MMP22

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	390 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein 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 By similarity.
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 Probable. Ref.3
Tissue specificity	Predominantly expressed in ovary, testis and prostate. Ref.2
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. Ref.3 Proteolytic cleavage might yield an active form By similarity.
Sequence similarities	Belongs to the peptidase M10A family. Contains 1 Ig-like C2-type (immunoglobulin-like) domain. Contains 1 ShKT domain.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Immunoglobulin domain Signal-anchor Transmembrane Transmembrane helix
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease 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 direct assay Ref.2. Source: UniProtKB reproduction Inferred from expression pattern Ref.2. Source: UniProtKB
Cellular_component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW intracellular Non-traceable author statement Ref.2. Source: UniProtKB proteinaceous extracellular matrix Non-traceable author statement Ref.1. Source: UniProtKB
Molecular_function	metalloendopeptidase activity Inferred from direct assay Ref.2. Source: UniProtKB zinc ion binding Non-traceable author statement Ref.2. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O75900-1)

Also known as: MMP21/22A;

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: O75900-2)

Also known as: MMP21/22B;

The sequence of this isoform differs from the canonical sequence as follows:
     199-199: G → GDRPGSSWRPLLCSTVGCRGRALGQTAGGTFRGGGCHWSLAG

Isoform 3 (identifier: O75900-3)

Also known as: MMP21/22C;

The sequence of this isoform differs from the canonical sequence as follows:
     254-254: G → GESLCRAGGRGPGGPEPGVLPTLPIG

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 390	390	Matrix metalloproteinase-23		PRO_0000259513
	Propeptide	1 – 78	78	Potential		PRO_0000259514
	Chain	79 – 390	312	Matrix metalloproteinase-23, soluble form		PRO_0000259515
Regions
	Topological domain	1 – 19	19	Cytoplasmic Potential
	Transmembrane	20 – 40	21	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	41 – 390	350	Lumenal Potential
	Domain	255 – 289	35	ShKT
	Domain	295 – 380	86	Ig-like C2-type
Sites
	Active site	212	1	By similarity
	Metal binding	211	1	Zinc; catalytic By similarity
	Metal binding	215	1	Zinc; catalytic By similarity
	Metal binding	221	1	Zinc; catalytic By similarity
	Site	78 – 79	2	Cleavage; by furin-like protease Potential
Amino acid modifications
	Glycosylation	92	1	N-linked (GlcNAc...) Potential
	Glycosylation	148	1	N-linked (GlcNAc...) Potential
	Glycosylation	232	1	N-linked (GlcNAc...) Potential
	Glycosylation	316	1	N-linked (GlcNAc...) Potential
	Disulfide bond	255 ↔ 289		By similarity
	Disulfide bond	262 ↔ 282		By similarity
	Disulfide bond	271 ↔ 286		By similarity
	Disulfide bond	321 ↔ 370		By similarity
Natural variations
	Alternative sequence	199	1	G → GDRPGSSWRPLLCSTVGCRG RALGQTAGGTFRGGGCHWSL AG in isoform 2.		VSP_021411
	Alternative sequence	254	1	G → GESLCRAGGRGPGGPEPGVL PTLPIG in isoform 3.		VSP_021412
	Natural variant	91	1	F → L. Ref.1 Corresponds to variant rs1139033 [ dbSNP | Ensembl ].		VAR_028948
Experimental info
	Mutagenesis	78	1	R → G: Abolishes processing of soluble form. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (MMP21/22A) [UniParc]. Last modified October 31, 2006. Version 2. Checksum: 5D78E4B4F2053D15	FASTA	390	43,935
	10 20 30 40 50 60 MGRGARVPSE APGAGVERRW LGAALVALCL LPALVLLARL GAPAVPAWSA AQGDVAALGL 70 80 90 100 110 120 SAVPPTRVPG PLAPRRRRYT LTPARLRWDH FNLTYRILSF PRNLLSPRET RRALAAAFRM 130 140 150 160 170 180 WSDVSPFSFR EVAPEQPSDL RIGFYPINHT DCLVSALHHC FDGPTGELAH AFFPPHGGIH 190 200 210 220 230 240 FDDSEYWVLG PTRYSWKKGV WLTDLVHVAA HEIGHALGLM HSQHGRALMH LNATLRGWKA 250 260 270 280 290 300 LSQDELWGLH RLYGCLDRLF VCASWARRGF CDARRRLMKR LCPSSCDFCY EFPFPTVATT 310 320 330 340 350 360 PPPPRTKTRL VPEGRNVTFR CGQKILHKKG KVYWYKDQEP LEFSYPGYLA LGEAHLSIIA 370 380 390 NAVNEGTYTC VVRRQQRVLT TYSWRVRVRG
	Isoform 2 (MMP21/22B) [UniParc]. Checksum: 807BA712BA201EF1	FASTA	431	48,107
	10 20 30 40 50 60 MGRGARVPSE APGAGVERRW LGAALVALCL LPALVLLARL GAPAVPAWSA AQGDVAALGL 70 80 90 100 110 120 SAVPPTRVPG PLAPRRRRYT LTPARLRWDH FNLTYRILSF PRNLLSPRET RRALAAAFRM 130 140 150 160 170 180 WSDVSPFSFR EVAPEQPSDL RIGFYPINHT DCLVSALHHC FDGPTGELAH AFFPPHGGIH 190 200 210 220 230 240 FDDSEYWVLG PTRYSWKKGD RPGSSWRPLL CSTVGCRGRA LGQTAGGTFR GGGCHWSLAG 250 260 270 280 290 300 VWLTDLVHVA AHEIGHALGL MHSQHGRALM HLNATLRGWK ALSQDELWGL HRLYGCLDRL 310 320 330 340 350 360 FVCASWARRG FCDARRRLMK RLCPSSCDFC YEFPFPTVAT TPPPPRTKTR LVPEGRNVTF 370 380 390 400 410 420 RCGQKILHKK GKVYWYKDQE PLEFSYPGYL ALGEAHLSII ANAVNEGTYT CVVRRQQRVL 430 TTYSWRVRVR G
	Isoform 3 (MMP21/22C) [UniParc]. Checksum: CD428F3F07F226EB	FASTA	415	46,305
	10 20 30 40 50 60 MGRGARVPSE APGAGVERRW LGAALVALCL LPALVLLARL GAPAVPAWSA AQGDVAALGL 70 80 90 100 110 120 SAVPPTRVPG PLAPRRRRYT LTPARLRWDH FNLTYRILSF PRNLLSPRET RRALAAAFRM 130 140 150 160 170 180 WSDVSPFSFR EVAPEQPSDL RIGFYPINHT DCLVSALHHC FDGPTGELAH AFFPPHGGIH 190 200 210 220 230 240 FDDSEYWVLG PTRYSWKKGV WLTDLVHVAA HEIGHALGLM HSQHGRALMH LNATLRGWKA 250 260 270 280 290 300 LSQDELWGLH RLYGESLCRA GGRGPGGPEP GVLPTLPIGC LDRLFVCASW ARRGFCDARR 310 320 330 340 350 360 RLMKRLCPSS CDFCYEFPFP TVATTPPPPR TKTRLVPEGR NVTFRCGQKI LHKKGKVYWY 370 380 390 400 410 KDQEPLEFSY PGYLALGEAH LSIIANAVNE GTYTCVVRRQ QRVLTTYSWR VRVRG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of two novel metalloproteinase genes linked to the Cdc2L locus on human chromosome 1p36.3." Gururajan R., Grenet J., Lahti J.M., Kidd V.J. Genomics 52:101-106(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2 AND 3), VARIANT LEU-91.
[2]	"Cloning and characterization of human MMP-23, a new matrix metalloproteinase predominantly expressed in reproductive tissues and lacking conserved domains in other family members." Velasco G., Pendas A.M., Fueyo A., Knaueper V., Murphy G., Lopez-Otin C. J. Biol. Chem. 274:4570-4576(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY. Tissue: Ovary.
[3]	"Cloning and characterization of a rat ortholog of MMP-23 (matrix metalloproteinase-23), a unique type of membrane-anchored matrix metalloproteinase and conditioned switching of its expression during the ovarian follicular development." Ohnishi J., Ohnishi E., Jin M., Hirano W., Nakane D., Matsui H., Kimura A., Sawa H., Nakayama K., Shibuya H., Nagashima K., Takahashi T. Mol. Endocrinol. 15:747-764(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), GLYCOSYLATION, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-78. Tissue: Uterus.
[4]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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] (ISOFORM 1). Tissue: Pancreas.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF055334 Genomic DNA. Translation: AAC63527.1. AF055334 Genomic DNA. Translation: AAC63528.1. AF055334 Genomic DNA. Translation: AAC63529.1. AF056200 mRNA. Translation: AAC62616.1. AF057061 mRNA. Translation: AAC62617.1. AF057062 mRNA. Translation: AAC62618.1. AJ005256 mRNA. Translation: CAB38176.1. AB031068 Genomic DNA. Translation: BAA92769.1. AB010961 mRNA. Translation: BAA24833.1. AL691432 Genomic DNA. No translation available. BC025719 mRNA. Translation: AAH25719.1.
IPI	IPI00012949. IPI00719650. IPI00783823.
RefSeq	NP_008914.1. NM_006983.1.
UniGene	Hs.192316. Hs.671760.
3D structure databases
ProteinModelPortal	O75900.
ModBase	Search...
Protein-protein interaction databases
IntAct	O75900. 1 interaction.
Protein family/group databases
MEROPS	M10.022.
PTM databases
PhosphoSite	O75900.
Proteomic databases
PaxDb	O75900.
PRIDE	O75900.
Protocols and materials databases
DNASU	8510.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000356026; ENSP00000348308; ENSG00000189409.
GeneID	8510.
KEGG	hsa:8510.
UCSC	uc001agp.3. human.
Organism-specific databases
CTD	8510.
GeneCards	GC01P001559. GC01P001619.
H-InvDB	HIX0178039.
HGNC	HGNC:7170. MMP23A. HGNC:7171. MMP23B.
HPA	CAB002768.
MIM	603320. gene. 603321. gene.
neXtProt	NX_O75900.
PharmGKB	PA30880.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG245056.
HOVERGEN	HBG053177.
InParanoid	O75900.
KO	K08001.
OrthoDB	EOG4RFKSV.
Gene expression databases
ArrayExpress	O75900.
Bgee	O75900.
CleanEx	HS_MMP21.
Genevestigator	O75900.
GermOnline	ENSG00000189409. Homo sapiens.
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. PS51670. SHKT. 1 hit. PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	8510.
NextBio	31851.
SOURCE	Search...

Entry information

Entry name

MMP23_HUMAN

Accession

Primary (citable) accession number: O75900
Secondary accession number(s): A2AGN0 , A2AGN1, O75894, O75895, Q5QPQ8, Q76P96, Q7LDM6, Q7LDM7, Q9UBR9, Q9UJK8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	October 31, 2006
Last modified:	May 29, 2013
This is version 105 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.