EFEMP2
entrez
30008
canonical
uniprot
O95967
canonical
ensembl
ENSG00000172638
resolver
ensp
ENSP00000309953
resolver
ensp
ENSP00000435295
resolver
ensp
ENSP00000577975
resolver
ensp
ENSP00000577976
resolver
ensp
ENSP00000577977
resolver
ensp
ENSP00000577978
resolver
ensp
ENSP00000577979
resolver
ensp
ENSP00000577981
resolver
ensp
ENSP00000577982
resolver
ensp
ENSP00000617474
resolver
ensp
ENSP00000617475
resolver
ensp
ENSP00000617476
resolver
ensp
ENSP00000617478
resolver
enst
ENST00000307998
resolver
enst
ENST00000531972
resolver
enst
ENST00000907916
resolver
enst
ENST00000907917
resolver
enst
ENST00000907918
resolver
enst
ENST00000907919
resolver
enst
ENST00000907920
resolver
enst
ENST00000907922
resolver
enst
ENST00000907923
resolver
enst
ENST00000947415
resolver
enst
ENST00000947416
resolver
enst
ENST00000947417
resolver
enst
ENST00000947419
resolver
genesymbol
EFEMP2
resolver
genesymbol_syn
FBLN4
resolver
hgnc
HGNC:3219
resolver
uniprot
A8K7R4
resolver
uniprot
B3KM31
resolver
uniprot
B3KQT1
resolver
uniprot
O75967
resolver
uniprot
Q9H3D5
resolver
uniprot_entry
FBLN4_HUMAN
resolver
uniprot_entry
Q9H3D5_HUMAN
resolver
uniprot_sec
A8K7R4
resolver
uniprot_sec
B3KM31
resolver
uniprot_sec
B3KQT1
resolver
uniprot_sec
O75967
resolver
amino_acid_sequence
MLPCASCLPGSLLLWALLLLLLGSASPQDSEEPDSYTECTDGYEWDPDSQHCRDVNECLTIPEACKGEMKCINHYGGYLCLPRSAAVINDLHGEGPPPPVPPAQHPNPCPPGYEPDDQDSCVDVDECAQALHDCRPSQDCHNLPGSYQCTCPDGYRKIGPECVDIDECRYRYCQHRCVNLPGSFRCQCEPGFQLGPNNRSCVDVNECDMGAPCEQRCFNSYGTFLCRCHQGYELHRDGFSCSDIDECSYSSYLCQYRCINEPGRFSCHCPQGYQLLATRLCQDIDECESGAHQCSEAQTCVNFHGGYRCVDTNRCVEPYIQVSENRCLCPASNPLCREQPSSIVHRYMTITSERSVPADVFQIQATSVYPGAYNAFQIRAGNSQGDFYIRQINNVSAMLVLARPVTGPREYVLDLEMVTMNSLMSYRASSVLRLTVFVGAYTF
uniprot
proteins
disease_involvement
DISEASE: Cutis laxa, autosomal recessive, 1B (ARCL1B) [MIM:614437]: A connective tissue disorder characterized by loose, hyperextensible skin with decreased resilience and elasticity leading to a premature aged appearance. Face, hands, feet, joints, and torso may be differentially affected. The clinical spectrum of autosomal recessive cutis laxa is highly heterogeneous with respect to organ involvement and severity. ARCL1B features include emphysema, lethal pulmonary artery occlusion, aortic aneurysm, cardiopulmonary insufficiency, birth fractures, arachnodactyly, and fragility of blood vessels. {ECO:0000269|PubMed:16685658, ECO:0000269|PubMed:17937443, ECO:0000269|PubMed:19664000, ECO:0000269|PubMed:20389311, ECO:0000269|PubMed:22943132, ECO:0000269|PubMed:27339457}. Note=The disease is caused by variants affecting the gene represented in this entry.
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:27339457). 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 (By similarity). 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:18973305, PubMed:19570982). Moreover adheres to the cells through heparin binding in a calcium-dependent manner and regulates vascularlar smooth muscle cells proliferation through angiotensin signaling (PubMed:23782690). {ECO:0000250|UniProtKB:Q9WVJ9, ECO:0000269|PubMed:18973305, ECO:0000269|PubMed:19570982, ECO:0000269|PubMed:23782690, ECO:0000269|PubMed:27339457}.
uniprot
proteins
mass_dalton
49405
uniprot
proteins
post_translational_modification
PTM: N-glycosylated; contains mostly complex-type glycans (PubMed:23782690, PubMed:27339457). Not O-glycosylated (PubMed:27339457). {ECO:0000269|PubMed:23782690, ECO:0000269|PubMed:27339457}.; PTM: Cleaved by ELANE; produces a 50-55 kDa fragment (PubMed:27339457). Cleaved by MMP2 and MMP9; produces several fragments (PubMed:27339457). {ECO:0000269|PubMed:27339457}.
uniprot
proteins
protein_family
Fibulin family
uniprot
proteins
pubmed
10601734
uniprot
proteins
pubmed
10982184
uniprot
proteins
pubmed
12975309
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16303743
uniprot
proteins
pubmed
16554811
uniprot
proteins
pubmed
16685658
uniprot
proteins
pubmed
17255108
uniprot
proteins
pubmed
17937443
uniprot
proteins
pubmed
18973305
uniprot
proteins
pubmed
19349279
uniprot
proteins
pubmed
19570982
uniprot
proteins
pubmed
19664000
uniprot
proteins
pubmed
19855011
uniprot
proteins
pubmed
20389311
uniprot
proteins
pubmed
22919265
uniprot
proteins
pubmed
22943132
uniprot
proteins
pubmed
23782690
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
27339457
uniprot
proteins
sequence_length
443
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:20389311, ECO:0000269|PubMed:27339457}. Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000250|UniProtKB:Q9WVJ9}. Note=Localizes on the microfibrils surrounding ELN cores. {ECO:0000250|UniProtKB:Q9WVJ9}.
uniprot
proteins