GRN
entrez
2896
canonical
uniprot
P28799
canonical
ensembl
ENSG00000030582
resolver
ensp
ENSP00000053867
resolver
genesymbol
GRN
resolver
hgnc
HGNC:4601
resolver
uniprot
D3DX55
resolver
uniprot
P23781
resolver
uniprot
P23782
resolver
uniprot
P23783
resolver
uniprot
P23784
resolver
uniprot
Q53HQ8
resolver
uniprot
Q53Y88
resolver
uniprot
Q540U8
resolver
uniprot
Q9BWE7
resolver
uniprot
Q9H8S1
resolver
uniprot
Q9UCH0
resolver
uniprot_entry
GRN_HUMAN
resolver
uniprot_sec
D3DX55
resolver
uniprot_sec
P23781
resolver
uniprot_sec
P23782
resolver
uniprot_sec
P23783
resolver
uniprot_sec
P23784
resolver
uniprot_sec
Q53HQ8
resolver
uniprot_sec
Q53Y88
resolver
uniprot_sec
Q540U8
resolver
uniprot_sec
Q9BWE7
resolver
uniprot_sec
Q9H8S1
resolver
uniprot_sec
Q9UCH0
resolver
amino_acid_sequence
MWTLVSWVALTAGLVAGTRCPDGQFCPVACCLDPGGASYSCCRPLLDKWPTTLSRHLGGPCQVDAHCSAGHSCIFTVSGTSSCCPFPEAVACGDGHHCCPRGFHCSADGRSCFQRSGNNSVGAIQCPDSQFECPDFSTCCVMVDGSWGCCPMPQASCCEDRVHCCPHGAFCDLVHTRCITPTGTHPLAKKLPAQRTNRAVALSSSVMCPDARSRCPDGSTCCELPSGKYGCCPMPNATCCSDHLHCCPQDTVCDLIQSKCLSKENATTDLLTKLPAHTVGDVKCDMEVSCPDGYTCCRLQSGAWGCCPFTQAVCCEDHIHCCPAGFTCDTQKGTCEQGPHQVPWMEKAPAHLSLPDPQALKRDVPCDNVSSCPSSDTCCQLTSGEWGCCPIPEAVCCSDHQHCCPQGYTCVAEGQCQRGSEIVAGLEKMPARRASLSHPRDIGCDQHTSCPVGQTCCPSLGGSWACCQLPHAVCCEDRQHCCPAGYTCNVKARSCEKEVVSAQPATFLARSPHVGVKDVECGEGHFCHDNQTCCRDNRQGWACCPYRQGVCCADRRHCCPAGFRCAARGTKCLRREAPRWDAPLRDPALRQLL
uniprot
proteins
disease_involvement
DISEASE: Frontotemporal dementia 2 (FTD2) [MIM:607485]: A form of dementia characterized by pathologic finding of frontotemporal lobar degeneration, presenile dementia with behavioral changes, deterioration of cognitive capacities and loss of memory. Gestural apraxia, parkinsonism, visual loss, and visual hallucinations are present in 25 to 40% of patients. {ECO:0000269|PubMed:16862116, ECO:0000269|PubMed:16983685, ECO:0000269|PubMed:18183624}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Ceroid lipofuscinosis, neuronal, 11 (CLN11) [MIM:614706]: A form of neuronal ceroid lipofuscinosis characterized by rapidly progressive visual loss due to retinal dystrophy, seizures, cerebellar ataxia, and cerebellar atrophy. Cognitive decline may also occur. Neuronal ceroid lipofuscinoses are progressive neurodegenerative, lysosomal storage diseases characterized by intracellular accumulation of autofluorescent liposomal material. {ECO:0000269|PubMed:22608501}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Secreted protein that acts as a key regulator of lysosomal function and as a growth factor involved in inflammation, wound healing and cell proliferation (PubMed:12526812, PubMed:18378771, PubMed:28073925, PubMed:28453791, PubMed:28541286). Regulates protein trafficking to lysosomes, and also the activity of lysosomal enzymes (PubMed:28453791, PubMed:28541286). Also facilitates the acidification of lysosomes, causing degradation of mature CTSD by CTSB (PubMed:28073925). In addition, functions as a wound-related growth factor that acts directly on dermal fibroblasts and endothelial cells to promote division, migration and the formation of capillary-like tubule structures (By similarity). Also promotes epithelial cell proliferation by blocking TNF-mediated neutrophil activation preventing release of oxidants and proteases (PubMed:12526812). Moreover, modulates inflammation in neurons by preserving neurons survival, axonal outgrowth and neuronal integrity (PubMed:18378771). {ECO:0000250|UniProtKB:P28798, ECO:0000269|PubMed:12526812, ECO:0000269|PubMed:18378771, ECO:0000269|PubMed:28073925, ECO:0000269|PubMed:28453791, ECO:0000269|PubMed:28541286}.; FUNCTION: [Granulin-4]: Promotes proliferation of the epithelial cell line A431 in culture.; FUNCTION: [Granulin-3]: Inhibits epithelial cell proliferation and induces epithelial cells to secrete IL-8. {ECO:0000269|PubMed:12526812}.; FUNCTION: [Granulin-7]: Stabilizes CTSD through interaction with CTSD leading to maintain its aspartic-type peptidase activity. {ECO:0000269|PubMed:28453791}.
uniprot
proteins
mass_dalton
63544
uniprot
proteins
post_translational_modification
PTM: Cleaved by ELANE; proteolysis is blocked by SLPI and is concentration- and time-dependent and induces CXCL8/IL-8 production; granulin-3 and granulin-4 are resistant to ELANE (PubMed:12526812, PubMed:28743268). Cleaved by CTSL in lysosome thus regulating the maturation and turnover of progranulin within the lysosome (PubMed:28743268). {ECO:0000269|PubMed:12526812, ECO:0000269|PubMed:28743268}.
uniprot
proteins
protein_family
Granulin family
uniprot
proteins
pubmed
10715107
uniprot
proteins
pubmed
12526812
uniprot
proteins
pubmed
1417868
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
1542665
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1618805
uniprot
proteins
pubmed
16862116
uniprot
proteins
pubmed
16983685
uniprot
proteins
pubmed
18183624
uniprot
proteins
pubmed
18359860
uniprot
proteins
pubmed
18378771
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
20020531
uniprot
proteins
pubmed
20188224
uniprot
proteins
pubmed
21092856
uniprot
proteins
pubmed
22608501
uniprot
proteins
pubmed
2268320
uniprot
proteins
pubmed
23364791
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26370502
uniprot
proteins
pubmed
27789271
uniprot
proteins
pubmed
28073925
uniprot
proteins
pubmed
28453791
uniprot
proteins
pubmed
28541286
uniprot
proteins
pubmed
28743268
uniprot
proteins
pubmed
8471426
uniprot
proteins
sequence_length
593
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21092856, ECO:0000269|PubMed:26370502}. Lysosome {ECO:0000269|PubMed:21092856, ECO:0000269|PubMed:26370502, ECO:0000269|PubMed:28073925, ECO:0000269|PubMed:28541286, ECO:0000269|PubMed:28743268}. Note=Endocytosed by SORT1 and delivred to lysosomes (PubMed:21092856, PubMed:28073925). Targeted to lysosome by PSAP via M6PR and LRP1, in both biosynthetic and endocytic pathways (PubMed:26370502, PubMed:28073925). Co-localized with GBA1 in the intracellular trafficking compartments until to lysosome (By similarity). {ECO:0000250|UniProtKB:P28798, ECO:0000269|PubMed:21092856, ECO:0000269|PubMed:26370502, ECO:0000269|PubMed:28073925}.
uniprot
proteins