SLAC1_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SLAC1_ARATH
• UniProt AC: Q9LD83
• Protein Name: Guard cell S-type anion channel SLAC1
• Gene Name: SLAC1
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 556
• Subcellular Localization: Cell membrane ; Multi-pass membrane protein .
• Protein Description: Slow, weak voltage-dependent S-type anion efflux channel involved in maintenance of anion homeostasis. Cl(-) efflux through SLAC1 causes membrane depolarization, which activates outward-rectifying K1 channels, leading to KCl and water efflux to reduce turgor further and cause stomatal closure, that reduces water loss and promotes leaf turgor. Essential for stomatal closure in response to CO(2), abscisic acid (ABA), ozone O(3), light/dark transitions, humidity change, calcium ions, hydrogen peroxide H(2)O(2), reactive oxygen species (ROS), and nitric oxide. Binds to the highly selective inward-rectifying potassium channels KAT1 and AKT2, and inhibits their actvities. Functions as an essential negative regulator of inward potassium channels in guard cells. Essential for the efficient stomatal closure and opening in guard cells. [PubMed: 27002025]
• Protein Sequence: MERKQSNAHSTFADINEVEDEAEQELQQQENNNNKRFSGNRGPNRGKQRPFRGFSRQVSLETGFSVLNRESRERDDKKSLPRSGRSFGGFESGGIINGGDGRKTDFSMFRTKSTLSKQKSLLPSIIRERDIENSLRTEDGETKDDSINENVSAGRYFAALRGPELDEVKDNEDILLPKEEQWPFLLRFPIGCFGICLGLSSQAVLWLALAKSPATNFLHITPLINLVVWLFSLVVLVSVSFTYILKCIFYFEAVKREYFHPVRVNFFFAPWVVCMFLAISVPPMFSPNRKYLHPAIWCVFMGPYFFLELKIYGQWLSGGKRRLCKVANPSSHLSVVGNFVGAILASKVGWDEVAKFLWAVGFAHYLVVFVTLYQRLPTSEALPKELHPVYSMFIAAPSAASIAWNTIYGQFDGCSRTCFFIALFLYISLVARINFFTGFKFSVAWWSYTFPMTTASVATIKYAEAVPGYPSRALALTLSFISTAMVCVLFVSTLLHAFVWQTLFPNDLAIAITKRKLTREKKPFKRAYDLKRWTKQALAKKISAEKDFEAEEESHH

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
59	Phosphorylation	RGFSRQVSLETGFSV CCCCCEEEHHHCCHH	16.49	20128877
86	Phosphorylation	SLPRSGRSFGGFESG CCCCCCCCCCCCCCC	31.59	20128877
113	Phosphorylation	FSMFRTKSTLSKQKS HHHEECHHHHHHHHH	33.69	20128877
120	Phosphorylation	STLSKQKSLLPSIIR HHHHHHHHHHHHHHH	32.42	19880383
146	Phosphorylation	DGETKDDSINENVSA CCCCCCCCCCCCCHH	37.13	19955405

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
59	S	Phosphorylation	Kinase	SRK2E	Q940H6	Uniprot
86	S	Phosphorylation	Kinase	SRK2E	Q940H6	Uniprot
113	S	Phosphorylation	Kinase	SRK2E	Q940H6	Uniprot
120	S	Phosphorylation	Kinase	SRK2E	Q940H6	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
120	S	Phosphorylation	Phosphorylation by SRK2E, especially on Ser-120, activates the channel.	20128877

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of SLAC1_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SRK2E_ARATH	OST1	physical	22730405
SRK2E_ARATH	OST1	physical	19955427
P2C37_ARATH	PP2CA	physical	19955427
CDPKN_ARATH	CPK23	physical	20385816
CDPK6_ARATH	CPK6	physical	20385816
CDPKL_ARATH	CPK21	physical	20385816
CDPK3_ARATH	CDPK6	physical	20385816

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Ozone-triggered rapid stomatal response involves the production ofreactive oxygen species, and is controlled by SLAC1 and OST1.";
Vahisalu T., Puzorjova I., Brosche M., Valk E., Lepiku M., Moldau H.,Pechter P., Wang Y.-S., Lindgren O., Salojaervi J., Loog M.,Kangasjaervi J., Kollist H.;
Plant J. 62:442-453(2010).
Cited for: FUNCTION, DISRUPTION PHENOTYPE, PHOSPHORYLATION AT SER-59; SER-86;SER-113; SER-120 AND SER-146, PHOSPHORYLATION BY SRK2E/OST1, MASSSPECTROMETRY, AND MUTAGENESIS OF SER-120 AND SER-146.
PubMed: 20128877