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Protein

Meprin A subunit alpha

Gene

Mep1a

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Hydrolysis of protein and peptide substrates preferentially on carboxyl side of hydrophobic residues.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Enzyme regulationi

Inhibited by actinonin.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi59Zinc; catalyticPROSITE-ProRule annotation1
Metal bindingi156Zinc; via tele nitrogen; catalyticBy similarity1
Active sitei157PROSITE-ProRule annotation1
Metal bindingi160Zinc; via tele nitrogen; catalyticBy similarity1
Metal bindingi166Zinc; via tele nitrogen; catalyticBy similarity1

GO - Molecular functioni

GO - Biological processi

  • proteolysis Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.24.18. 5301.

Protein family/group databases

MEROPSiM12.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Meprin A subunit alpha (EC:3.4.24.18)
Alternative name(s):
Endopeptidase-2
Endopeptidase-24.18 subunit alpha
Short name:
E-24.18
MEP-1
Gene namesi
Name:Mep1a
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 9

Organism-specific databases

RGDi3080. Mep1a.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini67 – 719ExtracellularSequence analysisAdd BLAST653
Transmembranei720 – 739HelicalSequence analysisAdd BLAST20
Topological domaini740 – 748CytoplasmicSequence analysis9

GO - Cellular componenti

  • extracellular exosome Source: Ensembl
  • meprin A complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20By similarityAdd BLAST20
PropeptideiPRO_000002888121 – 66By similarityAdd BLAST46
ChainiPRO_000002888267 – 748Meprin A subunit alphaAdd BLAST682

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi108 ↔ 260PROSITE-ProRule annotation
Disulfide bondi129 ↔ 148PROSITE-ProRule annotation
Glycosylationi141N-linked (GlcNAc...)Sequence analysis1
Glycosylationi223N-linked (GlcNAc...)Sequence analysis1
Glycosylationi259N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi270 ↔ 432PROSITE-ProRule annotation
Disulfide bondi278InterchainPROSITE-ProRule annotation
Disulfide bondi309Interchain
Glycosylationi319N-linked (GlcNAc...)Sequence analysis1
Glycosylationi441N-linked (GlcNAc...)Sequence analysis1
Glycosylationi542N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi676 ↔ 687PROSITE-ProRule annotation
Disulfide bondi681 ↔ 696PROSITE-ProRule annotation
Disulfide bondi698 ↔ 711PROSITE-ProRule annotation

Post-translational modificationi

N-glycosylated; contains GlcNAc, galactose, mannose and a small amount of fucose.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiQ64230.
PRIDEiQ64230.

PTM databases

iPTMnetiQ64230.
PhosphoSitePlusiQ64230.

Expressioni

Tissue specificityi

Colocalized with E-24.11 in proximal tubules of juxtamedullary nephrons.

Gene expression databases

BgeeiENSRNOG00000011022.
GenevisibleiQ64230. RN.

Interactioni

Subunit structurei

Homotetramer consisting of disulfide-linked alpha subunits, homooligomer consisting of disulfide-linked alpha subunit homodimers, or heterotetramer of two alpha and two beta subunits formed by non-covalent association of two disulfide-linked heterodimers (By similarity). Interacts with MBL2 through its carbohydrate moiety. This interaction may inhibit its catalytic activity (By similarity).By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000014791.

Structurei

3D structure databases

ProteinModelPortaliQ64230.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini265 – 434MAMPROSITE-ProRule annotationAdd BLAST170
Domaini435 – 596MATHPROSITE-ProRule annotationAdd BLAST162
Domaini672 – 712EGF-likePROSITE-ProRule annotationAdd BLAST41

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni67 – 264MetalloproteaseAdd BLAST198

Sequence similaritiesi

Belongs to the peptidase M12A family.Curated
Contains 1 EGF-like domain.PROSITE-ProRule annotation
Contains 1 MAM domain.PROSITE-ProRule annotation
Contains 1 MATH domain.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3714. Eukaryota.
ENOG410ZPX7. LUCA.
GeneTreeiENSGT00760000119227.
HOGENOMiHOG000043106.
HOVERGENiHBG052457.
InParanoidiQ64230.
KOiK01395.
OMAiPKRKQQC.
OrthoDBiEOG091G009U.
PhylomeDBiQ64230.

Family and domain databases

CDDicd06263. MAM. 1 hit.
Gene3Di2.60.210.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR000742. EGF-like_dom.
IPR000998. MAM_dom.
IPR002083. MATH/TRAF_dom.
IPR008294. Meprin.
IPR024079. MetalloPept_cat_dom.
IPR001506. Peptidase_M12A.
IPR006026. Peptidase_Metallo.
IPR008974. TRAF-like.
[Graphical view]
PfamiPF01400. Astacin. 1 hit.
PF00008. EGF. 1 hit.
PF00629. MAM. 1 hit.
[Graphical view]
PIRSFiPIRSF001196. Meprin. 1 hit.
PRINTSiPR00480. ASTACIN.
PR00020. MAMDOMAIN.
SMARTiSM00137. MAM. 1 hit.
SM00061. MATH. 1 hit.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMiSSF49599. SSF49599. 1 hit.
SSF49899. SSF49899. 1 hit.
PROSITEiPS50026. 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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q64230-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLWTLPVCLL SLSFSAHIAA VSIQHLSTGH DHDDVDVGEQ QKDISEINSA
60 70 80 90 100
AGLNLFQGDI LLPRTRNALR DPSSRWKLPI PYILADNLDL NAKGAILNAF
110 120 130 140 150
EMFRLKSCVD FKPYEGESSY IIFQQFSGCW SMVGDQHVGQ NISIGEGCDY
160 170 180 190 200
KAIIEHEILH ALGFFHEQSR TDRDDYVNIW WNEIMTDYEH NFNTYDDKTI
210 220 230 240 250
TDLNTPYDYE SLMHYGPFSF NKNETIPTIT TKIPEFNAII GQRLDFSATD
260 270 280 290 300
LTRLNRMYNC TRTHTLLDHC AFEKTNICGM IQGTRDDADW VHEDSSQPGQ
310 320 330 340 350
VDHTLVGRCK AAGYFMYFNT SSGVTGEVAL LESRILYPKR KQQCLQFFYK
360 370 380 390 400
MTGSPADRLL IWVRRDDNTG NVCQLAKIQT FQGDSDHNWK IAHVTLNEEK
410 420 430 440 450
KFRYVFQGTK GDPGNSDGGI YLDDITLTET PCPTGVWTIR NISQVLENTV
460 470 480 490 500
KGDRLVSPRF YNSEGYGFGV TLYPNGRITS NSGYLGLAFH LYSGDNDVIL
510 520 530 540 550
EWPVENRQAI MTILDQEPDA RNRMSLSLMF TTSKYQTSSA INGSVIWDRP
560 570 580 590 600
TKVGVYDKDC DCFRSIDWGW GQAISHQMLM RRNFLKDDTL IIFVDFKDLT
610 620 630 640 650
HLRQTEVPIP SRSVIPRGLL LQGQEPLALG DSRIAMMEES LPRRLDQRQP
660 670 680 690 700
SRPKRSVENT GPMEDHNWPQ YFRDPCDPNP CQNEGTCVNV KGMASCRCVS
710 720 730 740
GHAFFYTGER CQAMHVHGSL LGLLIGCITA LIFLTFITFS NTYQKLRQ
Length:748
Mass (Da):85,123
Last modified:July 13, 2010 - v2
Checksum:iBCAE2DCD53B8C6A4
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti78L → P in AAB23030 (PubMed:1505684).Curated1
Sequence conflicti356A → S in AAB23030 (PubMed:1505684).Curated1
Sequence conflicti373C → R in AAB23030 (PubMed:1505684).Curated1
Sequence conflicti507R → E in AAB23030 (PubMed:1505684).Curated1
Sequence conflicti610P → S in AAB23030 (PubMed:1505684).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S43408 mRNA. Translation: AAB23030.1.
BC081834 mRNA. Translation: AAH81834.1.
PIRiS24134.
RefSeqiNP_037275.1. NM_013143.1.
UniGeneiRn.16265.

Genome annotation databases

EnsembliENSRNOT00000014791; ENSRNOP00000014791; ENSRNOG00000011022.
GeneIDi25684.
KEGGirno:25684.
UCSCiRGD:3080. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S43408 mRNA. Translation: AAB23030.1.
BC081834 mRNA. Translation: AAH81834.1.
PIRiS24134.
RefSeqiNP_037275.1. NM_013143.1.
UniGeneiRn.16265.

3D structure databases

ProteinModelPortaliQ64230.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000014791.

Protein family/group databases

MEROPSiM12.002.

PTM databases

iPTMnetiQ64230.
PhosphoSitePlusiQ64230.

Proteomic databases

PaxDbiQ64230.
PRIDEiQ64230.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000014791; ENSRNOP00000014791; ENSRNOG00000011022.
GeneIDi25684.
KEGGirno:25684.
UCSCiRGD:3080. rat.

Organism-specific databases

CTDi4224.
RGDi3080. Mep1a.

Phylogenomic databases

eggNOGiKOG3714. Eukaryota.
ENOG410ZPX7. LUCA.
GeneTreeiENSGT00760000119227.
HOGENOMiHOG000043106.
HOVERGENiHBG052457.
InParanoidiQ64230.
KOiK01395.
OMAiPKRKQQC.
OrthoDBiEOG091G009U.
PhylomeDBiQ64230.

Enzyme and pathway databases

BRENDAi3.4.24.18. 5301.

Miscellaneous databases

PROiQ64230.

Gene expression databases

BgeeiENSRNOG00000011022.
GenevisibleiQ64230. RN.

Family and domain databases

CDDicd06263. MAM. 1 hit.
Gene3Di2.60.210.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR000742. EGF-like_dom.
IPR000998. MAM_dom.
IPR002083. MATH/TRAF_dom.
IPR008294. Meprin.
IPR024079. MetalloPept_cat_dom.
IPR001506. Peptidase_M12A.
IPR006026. Peptidase_Metallo.
IPR008974. TRAF-like.
[Graphical view]
PfamiPF01400. Astacin. 1 hit.
PF00008. EGF. 1 hit.
PF00629. MAM. 1 hit.
[Graphical view]
PIRSFiPIRSF001196. Meprin. 1 hit.
PRINTSiPR00480. ASTACIN.
PR00020. MAMDOMAIN.
SMARTiSM00137. MAM. 1 hit.
SM00061. MATH. 1 hit.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMiSSF49599. SSF49599. 1 hit.
SSF49899. SSF49899. 1 hit.
PROSITEiPS50026. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiMEP1A_RAT
AccessioniPrimary (citable) accession number: Q64230
Secondary accession number(s): Q642C9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 13, 2010
Last modified: November 2, 2016
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.