MME
entrez
4311
canonical
uniprot
P08473
canonical
ensembl
ENSG00000196549
resolver
ensp
ENSP00000353679
resolver
ensp
ENSP00000372450
resolver
ensp
ENSP00000417079
resolver
ensp
ENSP00000418525
resolver
ensp
ENSP00000418791
resolver
ensp
ENSP00000419653
resolver
ensp
ENSP00000420389
resolver
ensp
ENSP00000420542
resolver
ensp
ENSP00000502021
resolver
ensp
ENSP00000505211
resolver
ensp
ENSP00000505690
resolver
ensp
ENSP00000541538
resolver
ensp
ENSP00000541540
resolver
ensp
ENSP00000541541
resolver
ensp
ENSP00000541542
resolver
ensp
ENSP00000541543
resolver
ensp
ENSP00000614292
resolver
enst
ENST00000360490
resolver
enst
ENST00000382989
resolver
enst
ENST00000460393
resolver
enst
ENST00000462745
resolver
enst
ENST00000473730
resolver
enst
ENST00000491026
resolver
enst
ENST00000492661
resolver
enst
ENST00000493237
resolver
enst
ENST00000675418
resolver
enst
ENST00000680057
resolver
enst
ENST00000680282
resolver
enst
ENST00000871479
resolver
enst
ENST00000871481
resolver
enst
ENST00000871482
resolver
enst
ENST00000871483
resolver
enst
ENST00000871484
resolver
enst
ENST00000944233
resolver
genesymbol
MME
resolver
genesymbol_syn
EPN
resolver
hgnc
HGNC:7154
resolver
uniprot
A8K6U6
resolver
uniprot
D3DNJ9
resolver
uniprot
F6RAQ6
resolver
uniprot
Q3KQS6
resolver
uniprot
Q3MIX4
resolver
uniprot_entry
F6RAQ6_HUMAN
resolver
uniprot_entry
NEP_HUMAN
resolver
uniprot_entry
Q3KQS6_HUMAN
resolver
uniprot_sec
A8K6U6
resolver
uniprot_sec
D3DNJ9
resolver
uniprot_sec
Q3MIX4
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited in a dose dependent manner by opiorphin (PubMed:17101991). Activated by K49-P1-20, a twenty-residue synthetic peptide shortened from the snake B.asper myotoxin II (PubMed:26931059). {ECO:0000269|PubMed:17101991, ECO:0000269|PubMed:26931059}.
uniprot
proteins
amino_acid_sequence
MGKSESQMDITDINTPKPKKKQRWTPLEISLSVLVLLLTIIAVTMIALYATYDDGICKSSDCIKSAARLIQNMDATTEPCTDFFKYACGGWLKRNVIPETSSRYGNFDILRDELEVVLKDVLQEPKTEDIVAVQKAKALYRSCINESAIDSRGGEPLLKLLPDIYGWPVATENWEQKYGASWTAEKAIAQLNSKYGKKVLINLFVGTDDKNSVNHVIHIDQPRLGLPSRDYYECTGIYKEACTAYVDFMISVARLIRQEERLPIDENQLALEMNKVMELEKEIANATAKPEDRNDPMLLYNKMTLAQIQNNFSLEINGKPFSWLNFTNEIMSTVNISITNEEDVVVYAPEYLTKLKPILTKYSARDLQNLMSWRFIMDLVSSLSRTYKESRNAFRKALYGTTSETATWRRCANYVNGNMENAVGRLYVEAAFAGESKHVVEDLIAQIREVFIQTLDDLTWMDAETKKRAEEKALAIKERIGYPDDIVSNDNKLNNEYLELNYKEDEYFENIIQNLKFSQSKQLKKLREKVDKDEWISGAAVVNAFYSSGRNQIVFPAGILQPPFFSAQQSNSLNYGGIGMVIGHEITHGFDDNGRNFNKDGDLVDWWTQQSASNFKEQSQCMVYQYGNFSWDLAGGQHLNGINTLGENIADNGGLGQAYRAYQNYIKKNGEEKLLPGLDLNHKQLFFLNFAQVWCGTYRPEYAVNSIKTDVHSPGNFRIIGTLQNSAEFSEAFHCRKNSYMNPEKKCRVW
uniprot
proteins
disease_involvement
DISEASE: Charcot-Marie-Tooth disease, axonal, type 2T (CMT2T) [MIM:617017]: An axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. {ECO:0000269|PubMed:26991897, ECO:0000269|PubMed:27588448}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Spinocerebellar ataxia 43 (SCA43) [MIM:617018]: A form of spinocerebellar ataxia, a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA43 is a slowly progressive, autosomal dominant form. {ECO:0000269|PubMed:27583304}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.4.24.11
uniprot
proteins
function
FUNCTION: Thermolysin-like specificity, but is almost confined on acting on polypeptides of up to 30 amino acids (PubMed:15283675, PubMed:6208535, PubMed:6349683, PubMed:8168535). Biologically important in the destruction of opioid peptides such as Met- and Leu-enkephalins by cleavage of a Gly-Phe bond (PubMed:17101991, PubMed:6349683). Catalyzes cleavage of bradykinin, substance P and neurotensin peptides (PubMed:6208535). Able to cleave angiotensin-1, angiotensin-2 and angiotensin 1-9 (PubMed:15283675, PubMed:6349683). Involved in the degradation of atrial natriuretic factor (ANF) and brain natriuretic factor (BNP(1-32)) (PubMed:16254193, PubMed:2531377, PubMed:2972276). Displays UV-inducible elastase activity toward skin preelastic and elastic fibers (PubMed:20876573). {ECO:0000269|PubMed:15283675, ECO:0000269|PubMed:17101991, ECO:0000269|PubMed:20876573, ECO:0000269|PubMed:2531377, ECO:0000269|PubMed:27588448, ECO:0000269|PubMed:2972276, ECO:0000269|PubMed:6208535, ECO:0000269|PubMed:6349683}.
uniprot
proteins
mass_dalton
85514
uniprot
proteins
post_translational_modification
PTM: Myristoylation is a determinant of membrane targeting. {ECO:0000269|PubMed:19756956}.; PTM: Glycosylation at Asn-628 is necessary both for surface expression and neutral endopeptidase activity. {ECO:0000269|PubMed:10669592, ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:14747736, ECO:0000269|PubMed:17704566, ECO:0000269|PubMed:22766194}.
uniprot
proteins
protein_family
Peptidase M13 family
uniprot
proteins
pubmed
10669592
uniprot
proteins
pubmed
12754519
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14747736
uniprot
proteins
pubmed
15283675
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16254193
uniprot
proteins
pubmed
17101991
uniprot
proteins
pubmed
17704566
uniprot
proteins
pubmed
19756956
uniprot
proteins
pubmed
20876573
uniprot
proteins
pubmed
22766194
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
2528730
uniprot
proteins
pubmed
2531377
uniprot
proteins
pubmed
26931059
uniprot
proteins
pubmed
26991897
uniprot
proteins
pubmed
27102936
uniprot
proteins
pubmed
27583304
uniprot
proteins
pubmed
27588448
uniprot
proteins
pubmed
2968607
uniprot
proteins
pubmed
2971756
uniprot
proteins
pubmed
2972276
uniprot
proteins
pubmed
3162217
uniprot
proteins
pubmed
6208535
uniprot
proteins
pubmed
6349683
uniprot
proteins
pubmed
8168535
uniprot
proteins
sequence_length
750
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20876573}; Single-pass type II membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 29..51; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255
uniprot
proteins