Mep1a
entrez
17287
canonical
uniprot
P28825
canonical
ensembl
ENSMUSG00000023914
resolver
ensp
ENSMUSP00000024707
resolver
ensp
ENSMUSP00000113838
resolver
enst
ENSMUST00000024707
resolver
enst
ENSMUST00000117137
resolver
genesymbol
Mep1a
resolver
uniprot
A0A0R4J043
resolver
uniprot
B0V2P9
resolver
uniprot
Q91WH9
resolver
uniprot_entry
A0A0R4J043_MOUSE
resolver
uniprot_entry
MEP1A_MOUSE
resolver
uniprot_sec
B0V2P9
resolver
uniprot_sec
Q91WH9
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by metal ion chelators EDTA and 1,10-phenanthroline, bradykinin analogs, cysteine, CONA65, and several hydroxamate compounds, particularly tyrosine hydroxamate. Not inhibited by 3,4-dichloroisocourmarin, soybean trypsin inhibitor, or the cysteine proteinase inhibitors iodoacetic acid and E-64. {ECO:0000269|PubMed:17976009, ECO:0000269|PubMed:1883833, ECO:0000269|PubMed:1894622}.
uniprot
proteins
amino_acid_sequence
MLWIQPACLLSLIFSAHIAAVSIKHLLNGSDHDTDVGEQKDIFEINLAAGLNLFQGDILLPRTRNAMRDPSSRWKLPIPYILADNLELNAKGAILHAFEMFRLKSCVDFKPYEGESSYIIFQKLSGCWSMIGDQQVGQNISIGEGCDFKATIEHEILHALGFFHEQSRTDRDDYVNIWWDQIITDYEHNFNTYDDNTITDLNTPYDYESLMHYGPFSFNKNESIPTITTKIPEFNTIIGQLPDFSAIDLIRLNRMYNCTATHTLLDHCDFEKTNVCGMIQGTRDDADWAHGDSSQPEQVDHTLVGQCKGAGYFMFFNTSLGARGEAALLESRILYPKRKQQCLQFFYKMTGSPADRFEVWVRRDDNAGKVRQLAKIQTFQGDSDHNWKIAHVTLNEEKKFRYVFLGTKGDPGNSSGGIYLDDITLTETPCPAGVWTIRNISQILENTVKGDKLVSPRFYNSEGYGVGVTLYPNGRITSNSGFLGLTFHLYSGDNDAILEWPVENRQAIMTILDQEADTRNRMSLTLMFTTSKNQTSSAINGSVIWDRPSKVGVYDKDCDCFRSLDWGWGQAISHQLLKRRNFLKGDSLIIFVDFKDLTHLNRTEVPASARSTMPRGLLLQGQESPALGESSRKAMLEESLPSSLGQRHPSRQKRSVENTGPMEDHNWPQYFRDPCDPNPCQNEGTCVNVKGMASCRCVSGHAFFYAGERCQAMHVHGSLLGLLIGCIAGLIFLTFVTFSTTNGKLRQ
uniprot
proteins
ec_number
3.4.24.18
uniprot
proteins
mass_dalton
84231
uniprot
proteins
mutagenesis
MUTAGEN 139; /note="N->Q: Increased susceptibility to heat-inactivation. Forms homodimers and oligomers; when associated with Q-221. Inactive, impaired ability to form homodimers or oligomers; when associated with Q-257 or Q-221 and Q-257."; /evidence="ECO:0000269|PubMed:17040911"; MUTAGEN 141; /note="S->A: Impaired ability to form homodimers or oligomers; when associated with A-259."; /evidence="ECO:0000269|PubMed:17040911"; MUTAGEN 221; /note="N->Q: Increased susceptibility to heat-inactivation. Forms homodimers and oligomers; when associated with Q-139 or Q-257. Inactive, impaired ability to form homodimers or oligomers; when associated with Q-139 and Q-257."; /evidence="ECO:0000269|PubMed:17040911"; MUTAGEN 257; /note="N->Q: Increased susceptibility to heat-inactivation. Forms homodimers and oligomers; when associated with Q-221. Inactive, impaired ability to form homodimers or oligomers; when associated with Q-139 or Q-139 and Q-221."; /evidence="ECO:0000269|PubMed:17040911"; MUTAGEN 259; /note="T->A: Impaired ability to form homodimers or oligomers; when associated with A-141."; /evidence="ECO:0000269|PubMed:17040911
uniprot
proteins
post_translational_modification
PTM: N-glycosylated; contains GlcNAc, galactose, mannose and a small amount of fucose. {ECO:0000269|PubMed:17040911, ECO:0000269|PubMed:1894622}.
uniprot
proteins
pubmed
11278902
uniprot
proteins
pubmed
1374387
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16116208
uniprot
proteins
pubmed
17040911
uniprot
proteins
pubmed
17976009
uniprot
proteins
pubmed
1883833
uniprot
proteins
pubmed
1894622
uniprot
proteins
pubmed
1929422
uniprot
proteins
pubmed
1939172
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
8508794
uniprot
proteins
pubmed
8615815
uniprot
proteins
pubmed
9161413
uniprot
proteins
sequence_length
747
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
uniprot
proteins
transmembrane_region
TRANSMEM 714..741; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins