Overview
| Uniprot ID | A0A0G2JXT6 |
|---|
| Protein Name | Phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR6 |
|---|
| Gene Name | Mtmr6 |
|---|
| Organism | Rattus norvegicus |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 605 |
LKTSLCLKEQSLLPV |
| 613 |
EQSLLPVKDTLRAVE |
Function
Lipid phosphatase that specifically dephosphorylates the D-3 position of phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5-bisphosphate, generating phosphatidylinositol and phosphatidylinositol 5-phosphate. Binds with high affinity to phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) but also to phosphatidylinositol 3-phosphate (PtdIns(3)P), phosphatidylinositol 4-phosphate (PtdIns(4)P), and phosphatidylinositol 5-phosphate (PtdIns(5)P), phosphatidic acid and phosphatidylserine (By similarity). Negatively regulates ER-Golgi protein transport (PubMed:23188820). Probably in association with MTMR9, plays a role in the late stages of macropinocytosis by dephosphorylating phosphatidylinositol 3-phosphate in membrane ruffles. Acts as a negative regulator of KCNN4/KCa3.1 channel activity in CD4(+) T-cells possibly by decreasing intracellular levels of phosphatidylinositol 3-phosphate. Negatively regulates proliferation of reactivated CD4(+) T-cells. In complex with MTMR9, negatively regulates DNA damage-induced apoptosis. The formation of the MTMR6-MTMR9 complex stabilizes both MTMR6 and MTMR9 protein levels (By similarity)
Protein Sequence
10
MEHIRTTKVE
20
QVKLLDRFST
30
NNKSLTGTLY
40
LTATHLLFID
50
AHQKETWILH
60
HHIASVEKLA
70
LTTSGCPLVI
80
QCKNFRIVHF
90
IVPRERDCHD
100
IYNSLLQLSK
110
QAKYEDLYAF
120
SYNPKQNDTE
130
RLNGWQLIDL
140
AAEYERMGVP
150
NANWQLSDAN
160
REYKVCETYP
170
RELYVPRTAS
180
RPVIVGSSNF
190
RSKGRLPVLS
200
YCQQGTEAAI
210
CRCSQPLSGF
220
SARCLEDEHL
230
LQAISKANPG
240
NRYMYVVDTR
250
PKLRMQSWWD
260
TQKDIGRIIV
270
RISSKIWNDE
280
KIRESDEKKR
290
LNAMANRAAG
300
KGYENEDNYS
310
NIRFQFVGIE
320
NIHVMRSSLQ
330
KLLEVNGSKG
340
LSVNDFYSGL
350
ESSGWLRHIK
360
AVLDAAIFLA
370
KAIVVENASV
380
LVHCSDGWDR
390
TSQVCSLGSL
400
LLDSYYRTMK
410
GFMVLIEKDW
420
ISFGHKFSER
430
CGHLDGDPKE
440
VSPVFTQFLE
450
CVWHLTEQFP
460
QAFEFNEAFL
470
LQIHEHIHSC
480
QFGNFLGNCQ
490
KEREELRLKE
500
KTYSLWPFLL
510
ADKKKYLNPL
520
YSSKSQRLTV
530
LEPNTASFNF
540
KFWRNMYHQF
550
DRTLHPRQSV
560
LNIIMNMNEQ
570
NKQLEEDVKD
580
LEAKIKQCKS
590
GILTKDLLHA
600
VHPESPSLKT
610
SLCLKEQSLL
620
PVKDTLRAVE
630
GSSPADNRYC
640
DYTEEFSKSE
650
PAVVSLEYGV
ARMTC
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005737 |
cytoplasm |
| Cellular Component |
GO:0005783 |
endoplasmic reticulum |
| Cellular Component |
GO:0005793 |
endoplasmic reticulum-Golgi intermediate compartment |
| Cellular Component |
GO:0005635 |
nuclear envelope |
| Cellular Component |
GO:0048471 |
perinuclear region of cytoplasm |
| Cellular Component |
GO:0032587 |
ruffle membrane |
| Molecular Function |
GO:0052629 |
phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity |
| Molecular Function |
GO:0106018 |
phosphatidylinositol-3,5-bisphosphate phosphatase activity |
| Molecular Function |
GO:0004438 |
phosphatidylinositol-3-phosphate phosphatase activity |
| Biological Process |
GO:0006897 |
endocytosis |
| Biological Process |
GO:0046856 |
phosphatidylinositol dephosphorylation |
Reference
[1] Sheng L, Xu H, Wang Y, Ni J, Xiang T et al.. Systematic analysis of lysine lactylation in nucleus pulposus cells.. iScience 27(11):111157. 2024 Nov 15. PMID: 39524337.