Efemp2
entrez
58859
canonical
uniprot
Q9WVJ9
canonical
ensembl
ENSMUSG00000024909
resolver
ensp
ENSMUSP00000064719
resolver
ensp
ENSMUSP00000128827
resolver
ensp
ENSMUSP00000133016
resolver
ensp
ENSMUSP00000158440
resolver
ensp
ENSMUSP00000317278
resolver
enst
ENSMUST00000070118
resolver
enst
ENSMUST00000165485
resolver
enst
ENSMUST00000166303
resolver
enst
ENSMUST00000235523
resolver
genesymbol
Efemp2
resolver
genesymbol_syn
Fbln4
resolver
genesymbol_syn
Mbp1
resolver
uniprot
A0A494BBF0
resolver
uniprot
G5E8D6
resolver
uniprot
Q542X5
resolver
uniprot_entry
A0A494BBF0_MOUSE
resolver
uniprot_entry
FBLN4_MOUSE
resolver
uniprot_entry
G5E8D6_MOUSE
resolver
uniprot_entry
Q542X5_MOUSE
resolver
amino_acid_sequence
MLPFASCLPGSLLLWAFLLLLLGAASPQDPEEPDSYTECTDGYEWDADSQHCRDVNECLTIPEACKGEMKCINHYGGYLCLPRSAAVISDLHGEGPPPPAAHAQQPNPCPQGYEPDEQESCVDVDECTQALHDCRPSQDCHNLPGSYQCTCPDGYRKIGPECVDIDECRYRYCQHRCVNLPGSFRCQCEPGFQLGPNNRSCVDVNECDMGAPCEQRCFNSYGTFLCRCNQGYELHRDGFSCSDIDECGYSSYLCQYRCVNEPGRFSCHCPQGYQLLATRLCQDIDECETGAHQCSEAQTCVNFHGGYRCVDTNRCVEPYVQVSDNRCLCPASNPLCREQPSSIVHRYMSITSERSVPADVFQIQATSVYPGAYNAFQIRSGNTQGDFYIRQINNVSAMLVLARPVTGPREYVLDLEMVTMNSLMSYRASSVLRLTVFVGAYTF
uniprot
proteins
function
FUNCTION: Plays a crucial role in elastic fiber formation in tissue, and in the formation of ultrastructural connections between elastic laminae and smooth muscle cells in the aorta, therefore participates in terminal differentiation and maturation of smooth muscle cell (SMC) and in the mechanical properties and wall integrity maintenance of the aorta (PubMed:16478991, PubMed:19855011, PubMed:20019329, PubMed:26486174, PubMed:26711913, PubMed:28508064). In addition, is involved in the control of collagen fibril assembly in tissue throught proteolytic activation of LOX leading to cross- linking of collagen and elastin (PubMed:26178373, PubMed:26220971, PubMed:26690653, PubMed:26711913). Also promotes ELN coacervation and participates in the deposition of ELN coacervates on to microfibrils but also regulates ELN cross- linking through LOX interaction (PubMed:17324935). Moreover adheres to the cells through heparin binding in a calcium-dependent manner and regulates vascularlar smooth muscle cells proliferation through angiotensin signaling (PubMed:23636094). {ECO:0000269|PubMed:16478991, ECO:0000269|PubMed:17324935, ECO:0000269|PubMed:19855011, ECO:0000269|PubMed:20019329, ECO:0000269|PubMed:23636094, ECO:0000269|PubMed:26178373, ECO:0000269|PubMed:26220971, ECO:0000269|PubMed:26486174, ECO:0000269|PubMed:26690653, ECO:0000269|PubMed:26711913, ECO:0000269|PubMed:28508064}.
uniprot
proteins
mass_dalton
49425
uniprot
proteins
mutagenesis
MUTAGEN 57; /note="E->K: Knockin mutant mice are viable and survive into adulthood. Mice display abnormalities in multiple organ systems, including loose skin, bent forelimb, aortic aneurysm, tortuous artery, and pulmonary emphysema. In addition to elastic fiber abnormalities in the skin and large arteries, collagen fibrils are irregularly shaped, with many large fibrils in the dermis. Mice have large artery stiffness and systolic hypertension. Reduces protein secretion."; /evidence="ECO:0000269|PubMed:26178373, ECO:0000269|PubMed:28508064
uniprot
proteins
post_translational_modification
PTM: N-glycosylated; contains mostly complex-type glycans. Not O-glycosylated. {ECO:0000250|UniProtKB:O95967}.; PTM: Cleaved by ELANE; produces a 50-55 kDa fragment. Cleaved by MMP2 and MMP9; produces several fragments. {ECO:0000250|UniProtKB:O95967}.
uniprot
proteins
protein_family
Fibulin family
uniprot
proteins
pubmed
10380882
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16478991
uniprot
proteins
pubmed
17324935
uniprot
proteins
pubmed
19855011
uniprot
proteins
pubmed
20019329
uniprot
proteins
pubmed
23636094
uniprot
proteins
pubmed
25713297
uniprot
proteins
pubmed
26178373
uniprot
proteins
pubmed
26220971
uniprot
proteins
pubmed
26486174
uniprot
proteins
pubmed
26690653
uniprot
proteins
pubmed
26711913
uniprot
proteins
pubmed
28508064
uniprot
proteins
pubmed
28717224
uniprot
proteins
sequence_length
443
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:17324935, ECO:0000269|PubMed:26178373, ECO:0000269|PubMed:26690653}. Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000269|PubMed:17324935}. Note=Localizes on the microfibrils surrounding ELN cores. {ECO:0000269|PubMed:17324935}.
uniprot
proteins