SACM1L
entrez
22908
canonical
uniprot
Q9NTJ5
canonical
ensembl
ENSG00000211456
resolver
ensp
ENSP00000373713
resolver
ensp
ENSP00000396387
resolver
ensp
ENSP00000411966
resolver
ensp
ENSP00000500542
resolver
ensp
ENSP00000516562
resolver
ensp
ENSP00000516565
resolver
enst
ENST00000418611
resolver
enst
ENST00000478586
resolver
enst
ENST00000672858
resolver
enst
ENST00000706810
resolver
genesymbol
SACM1L
resolver
genesymbol_syn
KIAA0851
resolver
genesymbol_syn
SAC1
resolver
hgnc
HGNC:17059
resolver
uniprot
A0A5F9ZHN7
resolver
uniprot
A0A9L9PXJ6
resolver
uniprot
A8K527
resolver
uniprot
B4DK71
resolver
uniprot
B4DVV3
resolver
uniprot
E9PGZ4
resolver
uniprot
O94935
resolver
uniprot
Q7LA14
resolver
uniprot
Q7LA22
resolver
uniprot
Q96AX7
resolver
uniprot
Q9NQ46
resolver
uniprot
Q9NQ57
resolver
uniprot_entry
A0A5F9ZHN7_HUMAN
resolver
uniprot_entry
A0A9L9PXJ6_HUMAN
resolver
uniprot_entry
B4DVV3_HUMAN
resolver
uniprot_entry
E9PGZ4_HUMAN
resolver
uniprot_entry
SAC1_HUMAN
resolver
uniprot_sec
A8K527
resolver
uniprot_sec
B4DK71
resolver
uniprot_sec
O94935
resolver
uniprot_sec
Q7LA14
resolver
uniprot_sec
Q7LA22
resolver
uniprot_sec
Q96AX7
resolver
uniprot_sec
Q9NQ46
resolver
uniprot_sec
Q9NQ57
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by bis-peroxovanadates and hydrogen peroxide. {ECO:0000269|PubMed:29461204}.
uniprot
proteins
amino_acid_sequence
MATAAYEQLKLHITPEKFYVEACDDGADDVLTIDRVSTEVTLAVKKDVPPSAVTRPIFGILGTIHLVAGNYLIVITKKIKVGEFFSHVVWKATDFDVLSYKKTMLHLTDIQLQDNKTFLAMLNHVLNVDGFYFSTTYDLTHTLQRLSNTSPEFQEMSLLERADQRFVWNGHLLRELSAQPEVHRFALPVLHGFITMHSCSINGKYFDWILISRRSCFRAGVRYYVRGIDSEGHAANFVETEQIVHYNGSKASFVQTRGSIPVFWSQRPNLKYKPLPQISKVANHMDGFQRHFDSQVIIYGKQVIINLINQKGSEKPLEQTFATMVSSLGSGMMRYIAFDFHKECKNMRWDRLSILLDQVAEMQDELSYFLVDSAGQVVANQEGVFRSNCMDCLDRTNVIQSLLARRSLQAQLQRLGVLHVGQKLEEQDEFEKIYKNAWADNANACAKQYAGTGALKTDFTRTGKRTHLGLIMDGWNSMIRYYKNNFSDGFRQDSIDLFLGNYSVDELESHSPLSVPRDWKFLALPIIMVVAFSMCIICLLMAGDTWTETLAYVLFWGVASIGTFFIILYNGKDFVDAPRLVQKEKID
uniprot
proteins
ec_number
3.1.3.64
uniprot
proteins
function
FUNCTION: Phosphoinositide phosphatase which catalyzes the hydrolysis of phosphatidylinositol 4-phosphate (PtdIns(4)P) (PubMed:24209621, PubMed:27044890, PubMed:29461204, PubMed:30659099). Can also catalyze the hydrolysis of phosphatidylinositol 3-phosphate (PtdIns(3)P) and has low activity towards phosphatidylinositol-3,5-bisphosphate (PtdIns(3,5)P2) (By similarity). Shows a very robust PtdIns(4)P phosphatase activity when it binds PtdIns(4)P in a 'cis' configuration in the cellular environment, with much less activity seen when it binds PtdIns(4)P in 'trans' configuration (PubMed:24209621, PubMed:29461204, PubMed:30659099). PtdIns(4)P phosphatase activity (when it binds PtdIns(4)P in 'trans' configuration) is enhanced in the presence of PLEKHA3 (PubMed:30659099). {ECO:0000250|UniProtKB:Q9ES21, ECO:0000269|PubMed:24209621, ECO:0000269|PubMed:27044890, ECO:0000269|PubMed:29461204, ECO:0000269|PubMed:30659099}.
uniprot
proteins
mass_dalton
66967
uniprot
proteins
mutagenesis
MUTAGEN 389; /note="C->S: Loss of phosphatidylinositol-4-phosphate phosphatase activity."; /evidence="ECO:0000269|PubMed:29461204
uniprot
proteins
pubmed
10048485
uniprot
proteins
pubmed
11230166
uniprot
proteins
pubmed
11352561
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16641997
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
24209621
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
27044890
uniprot
proteins
pubmed
29461204
uniprot
proteins
pubmed
30659099
uniprot
proteins
pubmed
31806350
uniprot
proteins
sequence_length
587
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:27044890, ECO:0000269|PubMed:29461204, ECO:0000269|PubMed:31806350}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:29461204, ECO:0000269|PubMed:31806350}. Note=Trafficking between the ER and Golgi is regulated by nutrient status and by TMEM39A (PubMed:31806350). Localizes to endoplasmic reticulum-plasma membrane contact sites (EPCS) in the presence of phosphatidylinositol-4,5-bisphosphate (PubMed:27044890). {ECO:0000269|PubMed:27044890, ECO:0000269|PubMed:31806350}.
uniprot
proteins
transmembrane_region
TRANSMEM 521..541; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 549..569; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins