CTSD
entrez
1509
canonical
uniprot
P07339
canonical
ensembl
ENSG00000117984
resolver
ensp
ENSP00000236671
resolver
enst
ENST00000236671
resolver
genesymbol
CTSD
resolver
genesymbol
HEL-S-130P
resolver
genesymbol_syn
CPSD
resolver
genesymbol_syn
CTSD
resolver
hgnc
HGNC:2529
resolver
uniprot
Q6IB57
resolver
uniprot
V9HWI3
resolver
uniprot_entry
CATD_HUMAN
resolver
uniprot_entry
V9HWI3_HUMAN
resolver
uniprot_sec
Q6IB57
resolver
amino_acid_sequence
MQPSSLLPLALCLLAAPASALVRIPLHKFTSIRRTMSEVGGSVEDLIAKGPVSKYSQAVPAVTEGPIPEVLKNYMDAQYYGEIGIGTPPQCFTVVFDTGSSNLWVPSIHCKLLDIACWIHHKYNSDKSSTYVKNGTSFDIHYGSGSLSGYLSQDTVSVPCQSASSASALGGVKVERQVFGEATKQPGITFIAAKFDGILGMAYPRISVNNVLPVFDNLMQQKLVDQNIFSFYLSRDPDAQPGGELMLGGTDSKYYKGSLSYLNVTRKAYWQVHLDQVEVASGLTLCKEGCEAIVDTGTSLMVGPVDEVRELQKAIGAVPLIQGEYMIPCEKVSTLPAITLKLGGKGYKLSPEDYTLKVSQAGKTLCLSGFMGMDIPPPSGPLWILGDVFIGRYYTVFDRDNNRVGFAEAARL
uniprot
proteins
disease_involvement
DISEASE: Ceroid lipofuscinosis, neuronal, 10 (CLN10) [MIM:610127]: A form of neuronal ceroid lipofuscinosis with onset at birth or early childhood. Neuronal ceroid lipofuscinoses are progressive neurodegenerative, lysosomal storage diseases characterized by intracellular accumulation of autofluorescent liposomal material, and clinically by seizures, dementia, visual loss, and/or cerebral atrophy. {ECO:0000269|PubMed:16670177, ECO:0000269|PubMed:16685649, ECO:0000269|PubMed:21990111}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.4.23.5
uniprot
proteins
function
FUNCTION: Acid protease active in intracellular protein breakdown. Plays a role in APP processing following cleavage and activation by ADAM30 which leads to APP degradation (PubMed:27333034). Involved in the pathogenesis of several diseases such as breast cancer and possibly Alzheimer disease. {ECO:0000269|PubMed:27333034}.
uniprot
proteins
mass_dalton
44552
uniprot
proteins
post_translational_modification
PTM: N- and O-glycosylated. {ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:23234360}.; PTM: Undergoes proteolytic cleavage and activation by ADAM30. {ECO:0000269|PubMed:27333034}.; PTM: As well as the major heavy chain which starts at Leu-169, 2 minor forms starting at Gly-170 and Gly-171 have been identified (PubMed:1426530). An additional form starting at Ala-168 has also been identified (PubMed:27333034). {ECO:0000269|PubMed:1426530, ECO:0000269|PubMed:27333034}.
uniprot
proteins
protein_family
Peptidase A1 family
uniprot
proteins
pubmed
10716266
uniprot
proteins
pubmed
12643545
uniprot
proteins
pubmed
12754519
uniprot
proteins
pubmed
1426530
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16263699
uniprot
proteins
pubmed
16335952
uniprot
proteins
pubmed
16670177
uniprot
proteins
pubmed
16685649
uniprot
proteins
pubmed
17081065
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
20551380
uniprot
proteins
pubmed
2069717
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21990111
uniprot
proteins
pubmed
23234360
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
27333034
uniprot
proteins
pubmed
3588310
uniprot
proteins
pubmed
3927292
uniprot
proteins
pubmed
7935485
uniprot
proteins
pubmed
8262386
uniprot
proteins
pubmed
8393577
uniprot
proteins
pubmed
8467789
uniprot
proteins
sequence_length
412
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Lysosome. Melanosome. Secreted, extracellular space. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. In aortic samples, detected as an extracellular protein loosely bound to the matrix (PubMed:20551380). {ECO:0000269|PubMed:20551380}.
uniprot
proteins