[1]	NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. STRAIN=Sprague-Dawley; TISSUE=Kidney; PubMed=1377685 [NCBI, ExPASy, EBI, Israel, Japan] Johnson G.D., Hersh L.B.; "Cloning a rat meprin cDNA reveals the enzyme is a heterodimer."; J. Biol. Chem. 267:13505-13512(1992).
[2]	ERRATUM, AND RETRACTION. Johnson G.D., Hersh L.B.; J. Biol. Chem. 268:17647-17647(1993).
[3]	INTERCHAIN DISULFIDE BOND. PubMed=8760356 [NCBI, ExPASy, EBI, Israel, Japan] Chevallier S., Ahn J., Boileau G., Crine P.; "Identification of the cysteine residues implicated in the formation of alpha 2 and alpha/beta dimers of rat meprin."; Biochem. J. 317:731-738(1996).

Comments

CATALYTIC ACTIVITY: Hydrolysis of protein and peptide substrates preferentially on carboxyl side of hydrophobic residues.
COFACTOR: Binds 1 zinc ion per subunit (By similarity).
SUBUNIT: Heterotetramer of two alpha and two beta subunits which is formed by the non-covalent association of two disulfide-linked heterodimers.
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
TISSUE SPECIFICITY: Kidney, intestinal brush borders and salivary ducts.
SIMILARITY: Belongs to the peptidase M12A family [view classification].
SIMILARITY: Contains 1 EGF-like domain.
SIMILARITY: Contains 1 MAM domain.
SIMILARITY: Contains 1 MATH domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M88601; AAA41587.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

A42908; A42908.

NP_037315.1; -.

3D structure databases

HSSP

P07584; 1IAE. [HSSP ENTRY / PDB]

ModBase

P28826.

Protein family/group databases

MEROPS

M12.004; -.

Organism-specific databases

RGD

3081; Mep1b.

Ontologies

GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0004222;	Molecular function: metalloendopeptidase activity (inferred from electronic annotation from InterPro).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0006508;	Biological process: proteolysis (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR006210; EGF.
IPR000742; EGF_3.
IPR013111; EGF_extracell.
IPR013032; EGF_like_reg_CS.
IPR000998; MAM.
IPR002083; MATH.
IPR008294; Pept_M12A_Meprin.
IPR006025; Pept_M_Zn_BS.
IPR006026; Peptidase_M.
IPR001506; Peptidase_M12A.
IPR013322; TRAF-type.
Graphical view of domain structure.

Gene3D

G3DSA:2.60.210.10; TRAF-type; 1.

Pfam

PF01400; Astacin; 1.
PF07974; EGF_2; 1.
PF00629; MAM; 1.
PF00917; MATH; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF001196; Meprin; 1.

PRINTS

PR00480; ASTACIN.
PR00020; MAMDOMAIN.

SMART

SM00181; EGF; 1.
SM00137; MAM; 1.
SM00061; MATH; 1.
SM00235; ZnMc; 1.
SMART graphical view of domain structure.

PROSITE

PS00022; EGF_1; FALSE_NEG.
PS01186; EGF_2; FALSE_NEG.
PS50026; EGF_3; 1.
PS00740; MAM_1; 1.
PS50060; MAM_2; 1.
PS50144; MATH; 1.
PS00142; ZINC_PROTEASE; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

GeneID

25727; -.

KEGG

rno:25727; -.

Phylogenomic databases

HOVERGEN

P28826; -.

Other

NextBio

607841; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Direct protein sequencing; EGF-like domain; Glycoprotein; Hydrolase; Membrane; Metal-binding; Metalloprotease; Protease; Signal; Transmembrane; Zinc; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 20`	`20`	`Potential.`
`PROPEP`	`21 64`	`44`		`PRO_0000028887`
`CHAIN`	`65 704`	`640`	`Meprin A subunit beta.`	`PRO_0000028888`
`TOPO_DOM`	`21 654`	`634`	`Extracellular (Potential).`
`TRANSMEM`	`655 678`	`24`	`Potential.`
`TOPO_DOM`	`679 704`	`26`	`Cytoplasmic (Potential).`
`DOMAIN`	`261 430`	`170`	`MAM.`
`DOMAIN`	`431 585`	`155`	`MATH.`
`DOMAIN`	`607 647`	`41`	`EGF-like.`
`REGION`	`63 260`	`198`	`Metalloprotease.`
`ACT_SITE`	`154 154`		`By similarity.`
`METAL`	`153 153`		`Zinc; catalytic (By similarity).`
`METAL`	`157 157`		`Zinc; catalytic (By similarity).`
`METAL`	`163 163`		`Zinc; catalytic (By similarity).`
`CARBOHYD`	`193 193`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`219 219`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`316 316`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`422 422`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`437 437`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`528 528`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`547 547`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`592 592`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`306 306`		`Interchain (with C-309 in MEP1A).`
`DISULFID`	`611 622`		`By similarity.`
`DISULFID`	`616 631`		`By similarity.`
`DISULFID`	`633 646`		`By similarity.`

Sequence information

Length: 704 AA [This is the length of the unprocessed precursor]

Molecular weight: 79250 Da [This is the MW of the unprocessed precursor]

CRC64: 1FBC21129EC6B875 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDARHWPWFL VFATFLLVSG LPAPEKFVKD IDGGIDQDIF DINEDLGLDL FEGDIKLEAS 

        70         80         90        100        110        120 
GRNSIIGDNY RWPHTIPYVL EDSLEMNAKG VILNAFERYR LKTCIDFKPW SGEENYISVF 

       130        140        150        160        170        180 
KGSGCWSSVG NIHAGKQELS IGTNCDRIAT VQHEFLHALG FWHEQSRADR DDYITIVWDR 

       190        200        210        220        230        240 
ILSGKEHNFN IYNDSVSDSL NVPYDYTSVM HYSKTAFQNG TESTIITKIS DFEDVIGQRM 

       250        260        270        280        290        300 
DFSDYDLLKL NQLYSCTSSL SFMDSCDFEL ENICGMIQSS QDSADWQRLS QVLSGPENDH 

       310        320        330        340        350        360 
SNMGQCKDSG FFMHFNTSTG NGGITAMLES RVLYPKRGFQ CVEFYLYNSG SGNGQLNVYT 

       370        380        390        400        410        420 
REYTAGHQDG VLTLQREIRD IPTGSWQLYY VTLQVTEKFR VVFEGVGGPG ASSGGLSIDD 

       430        440        450        460        470        480 
INLSETRCPH HIWHIQNFTQ LLGGQTTVYS PPFYSSKGYA FQINLDLTSP TNVGLYFHLI 

       490        500        510        520        530        540 
SGANDDQLQW PCPWQQATMT LLDQNPDIRQ RMSNQRSITT DPKMTDDNGS YLWDRPSKVG 

       550        560        570        580        590        600 
VEAFFPNGTQ FSRGRGYGTS VFITQERLKS REFLKGDDVY ILLTVEDISH LNSTAAVPGP 

       610        620        630        640        650        660 
VPTTSTVHNA CSEVECQNGG ICTLQEGRAE CKCPAGEDWW YMGKRCEKRG STKDTIVIAV 

       670        680        690        700 
SSTVTVFAVM LIITLISVYC TRRKYRKKAS AKTAAMNLEN QHAF

P28826 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools