EFEMP1
entrez
2202
canonical
uniprot
Q12805
canonical
ensembl
ENSG00000115380
resolver
ensp
ENSP00000347596
resolver
ensp
ENSP00000378058
resolver
ensp
ENSP00000621549
resolver
ensp
ENSP00000621559
resolver
genesymbol
EFEMP1
resolver
genesymbol_syn
FBLN3
resolver
genesymbol_syn
FBNL
resolver
hgnc
HGNC:3218
resolver
uniprot
A0A0S2Z3V1
resolver
uniprot
A0A0S2Z4F1
resolver
uniprot
A8K3I4
resolver
uniprot
B2R6M6
resolver
uniprot
B4DW75
resolver
uniprot
D6W5D2
resolver
uniprot
Q541U7
resolver
uniprot_entry
A0A0S2Z3V1_HUMAN
resolver
uniprot_entry
A0A0S2Z4F1_HUMAN
resolver
uniprot_entry
B2R6M6_HUMAN
resolver
uniprot_entry
FBLN3_HUMAN
resolver
uniprot_sec
A8K3I4
resolver
uniprot_sec
B4DW75
resolver
uniprot_sec
D6W5D2
resolver
uniprot_sec
Q541U7
resolver
amino_acid_sequence
MLKALFLTMLTLALVKSQDTEETITYTQCTDGYEWDPVRQQCKDIDECDIVPDACKGGMKCVNHYGGYLCLPKTAQIIVNNEQPQQETQPAEGTSGATTGVVAASSMATSGVLPGGGFVASAAAVAGPEMQTGRNNFVIRRNPADPQRIPSNPSHRIQCAAGYEQSEHNVCQDIDECTAGTHNCRADQVCINLRGSFACQCPPGYQKRGEQCVDIDECTIPPYCHQRCVNTPGSFYCQCSPGFQLAANNYTCVDINECDASNQCAQQCYNILGSFICQCNQGYELSSDRLNCEDIDECRTSSYLCQYQCVNEPGKFSCMCPQGYQVVRSRTCQDINECETTNECREDEMCWNYHGGFRCYPRNPCQDPYILTPENRCVCPVSNAMCRELPQSIVYKYMSIRSDRSVPSDIFQIQATTIYANTINTFRIKSGNENGEFYLRQTSPVSAMLVLVKSLSGPREHIVDLEMLTVSSIGTFRTSSVLRLTIIVGPFSF
uniprot
proteins
disease_involvement
DISEASE: Doyne honeycomb retinal dystrophy (DHRD) [MIM:126600]: An autosomal dominant, progressive, ocular disorder characterized by yellow-white deposits known as drusen that accumulate beneath the retinal pigment epithelium. With age, drusen increase in size and number, and eventually cause visual symptoms, including decreased visual acuity, metamorphopsia, photophobia, and paracentral scotoma. {ECO:0000269|PubMed:10369267, ECO:0000269|PubMed:11384588, ECO:0000269|PubMed:12242346, ECO:0000269|PubMed:17666404, ECO:0000269|PubMed:34923728}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Cutis laxa, autosomal recessive, 1D (ARCL1D) [MIM:620780]: 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. ARCL1D features include skin laxity, thin and translucent skin with easy bruising, facial dysmorphism, joint hypermobility, muscle hypotonia, and multiple severe herniations. Skin laxity may progress with age. {ECO:0000269|PubMed:31792352, ECO:0000269|PubMed:32006683, ECO:0000269|PubMed:33807164, ECO:0000269|PubMed:35998264}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Glaucoma 1, open angle, H (GLC1H) [MIM:611276]: A form of primary open angle glaucoma (POAG). POAG is characterized by a specific pattern of optic nerve and visual field defects. The angle of the anterior chamber of the eye is open, and usually the intraocular pressure is increased. However, glaucoma can occur at any intraocular pressure. The disease is generally asymptomatic until the late stages, by which time significant and irreversible optic nerve damage has already taken place. GLC1H is an autosomal dominant form manifesting at age between 3 and 40 years, in most patients. Some affected individuals present with glaucoma after age 35 or 40 years. {ECO:0000269|PubMed:26162006, ECO:0000269|PubMed:34923728}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Binds EGFR, the EGF receptor, inducing EGFR autophosphorylation and the activation of downstream signaling pathways. May play a role in cell adhesion and migration. May function as a negative regulator of chondrocyte differentiation. In the olfactory epithelium, it may regulate glial cell migration, differentiation and the ability of glial cells to support neuronal neurite outgrowth. {ECO:0000269|PubMed:19804359, ECO:0000269|PubMed:19887559, ECO:0000269|PubMed:20005202}.
uniprot
proteins
mass_dalton
54641
uniprot
proteins
mutagenesis
MUTAGEN 29; /note="C->A: Produces extracellular disulfide-linked homodimers similar as Cys55Arg mutation."; /evidence="ECO:0000269|PubMed:35998264"; MUTAGEN 42; /note="C->A: Produces extracellular disulfide-linked homodimers similar as Cys55Arg mutation."; /evidence="ECO:0000269|PubMed:35998264"; MUTAGEN 48; /note="C->A: Produces extracellular disulfide-linked homodimers similar as Cys55Arg mutation."; /evidence="ECO:0000269|PubMed:35998264"; MUTAGEN 61; /note="C->A: Produces extracellular disulfide-linked homodimers similar as Cys55Arg mutation."; /evidence="ECO:0000269|PubMed:35998264"; MUTAGEN 70; /note="C->A: Produces extracellular disulfide-linked homodimers similar as Cys55Arg mutation."; /evidence="ECO:0000269|PubMed:35998264"; MUTAGEN 159; /note="C->A: Produces extracellular disulfide-linked homodimers similar as Cys55Arg mutation."; /evidence="ECO:0000269|PubMed:35998264"; MUTAGEN 171; /note="C->A: Produces extracellular disulfide-linked homodimers similar as Cys55Arg mutation."; /evidence="ECO:0000269|PubMed:35998264
uniprot
proteins
protein_family
Fibulin family
uniprot
proteins
pubmed
10369267
uniprot
proteins
pubmed
10601734
uniprot
proteins
pubmed
11262647
uniprot
proteins
pubmed
11384588
uniprot
proteins
pubmed
12242346
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15123717
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
17666404
uniprot
proteins
pubmed
19275936
uniprot
proteins
pubmed
19804359
uniprot
proteins
pubmed
19887559
uniprot
proteins
pubmed
20005202
uniprot
proteins
pubmed
22905912
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
26162006
uniprot
proteins
pubmed
31792352
uniprot
proteins
pubmed
32006683
uniprot
proteins
pubmed
33807164
uniprot
proteins
pubmed
34923728
uniprot
proteins
pubmed
35490425
uniprot
proteins
pubmed
35998264
uniprot
proteins
pubmed
7799918
uniprot
proteins
pubmed
8812496
uniprot
proteins
sequence_length
493
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:35998264}. Note=Localizes to the lamina propria underneath the olfactory epithelium. {ECO:0000250|UniProtKB:O35568}.
uniprot
proteins