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Reviewed, UniProtKB/Swiss-Prot P28826 (MEP1B_RAT)

Last modified June 16, 2009. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Meprin A subunit beta
    EC=3.4.24.18
Alternative name(s):
    Endopeptidase-2
Gene names
Name: Mep1b
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length704 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (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 structure

Heterotetramer of two alpha and two beta subunits which is formed by the non-covalent association of two disulfide-linked heterodimers. Ref.3

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Kidney, intestinal brush borders and salivary ducts.

Sequence similarities

Belongs to the peptidase M12A family.

Contains 1 EGF-like domain.

Contains 1 MAM domain.

Contains 1 MATH domain.

Ontologies

Keywords
   Cellular componentMembrane
   DomainEGF-like domain
Signal
Transmembrane
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processproteolysis

Non-traceable author statement. Source: RGD

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionmetalloendopeptidase activity

Inferred from direct assay. Source: RGD

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Propeptide21 – 6444
PRO_0000028887
Chain65 – 704640Meprin A subunit beta
PRO_0000028888

Regions

Topological domain21 – 654634Extracellular Potential
Transmembrane655 – 67824 Potential
Topological domain679 – 70426Cytoplasmic Potential
Domain261 – 430170MAM
Domain431 – 585155MATH
Domain607 – 64741EGF-like
Region63 – 260198Metalloprotease

Sites

Active site1541 By similarity
Metal binding1531Zinc; catalytic By similarity
Metal binding1571Zinc; catalytic By similarity
Metal binding1631Zinc; catalytic By similarity

Amino acid modifications

Glycosylation1931N-linked (GlcNAc...) Potential
Glycosylation2191N-linked (GlcNAc...) Potential
Glycosylation3161N-linked (GlcNAc...) Potential
Glycosylation4221N-linked (GlcNAc...) Potential
Glycosylation4371N-linked (GlcNAc...) Potential
Glycosylation5281N-linked (GlcNAc...) Potential
Glycosylation5471N-linked (GlcNAc...) Potential
Glycosylation5921N-linked (GlcNAc...) Potential
Disulfide bond306Interchain (with C-309 in MEP1A) Ref.3
Disulfide bond611 ↔ 622 By similarity
Disulfide bond616 ↔ 631 By similarity
Disulfide bond633 ↔ 646 By similarity

Sequences

Sequence LengthMass (Da)Tools
P28826-1 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: 1FBC21129EC6B875

FASTA70479,250
        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 

« Hide

References

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

Cross-references

Sequence databases

M88601 mRNA. Translation: AAA41587.1.
IPIIPI00204808.
PIRA42908.
RefSeqNP_037315.1.
UniGeneRn.3520

3D structure databases

HSSPHSSP built from PDB template 1IAE based on UniProtKB P07584.
ModBaseSearch...

Protein family/group databases

MEROPSM12.004.

Genome annotation databases

GeneID25727.
KEGGrno:25727.

Organism-specific databases

RGD3081. Mep1b.

Phylogenomic databases

HOVERGENP28826.

Enzyme and pathway databases

BRENDA3.4.24.18. 248.

Family and domain databases

InterProIPR006209. EGF.
IPR006210. EGF-like.
IPR013032. EGF-like_reg_CS.
IPR000742. EGF_3.
IPR000998. MAM.
IPR002083. MATH.
IPR008294. Pept_M12A_Meprin.
IPR006025. Pept_M_Zn_BS.
IPR006026. Peptidase_M.
IPR001506. Peptidase_M12A.
IPR013322. TRAF-type.
[Graphical view]
Gene3DG3DSA:2.60.210.10. TRAF-type. 1 hit.
PfamPF01400. Astacin. 1 hit.
PF00008. EGF. 1 hit.
PF00629. MAM. 1 hit.
PF00917. MATH. 1 hit.
[Graphical view]
PIRSFPIRSF001196. Meprin. 1 hit.
PRINTSPR00480. ASTACIN.
PR00020. MAMDOMAIN.
SMARTSM00181. EGF. 1 hit.
SM00137. MAM. 1 hit.
SM00061. MATH. 1 hit.
SM00235. ZnMc. 1 hit.
[Graphical view]
PROSITEPS00022. EGF_1. False negative.
PS01186. EGF_2. False negative.
PS50026. EGF_3. 1 hit.
PS00740. MAM_1. 1 hit.
PS50060. MAM_2. 1 hit.
PS50144. MATH. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio607841.

Entry information

Entry nameMEP1B_RAT
AccessionPrimary (citable) accession number: P28826
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: February 1, 1996
Last modified: June 16, 2009
This is version 88 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents