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1.A.50.2.1
Sarcolipin (SLN) anion pore-forming protein of 31 aas and 1 TMS, with selectivity for Cl- and H2PO4-. Oligomeric interactions of sarcolipin and the Ca-ATPase have been documented (Autry et al., 2011).  Sarcolipin, but not phospholamban, promotes uncoupling of the SERCA pump (3.A.3.2.7; Sahoo et al. 2013).  SNL forms pentameric pores that can transport water, H+, Na+, Ca2+ and Cl-.  Leu21 serves as the gate (Cao et al. 2015).   In the channel, water molecules near the Leu21 pore demonstrated a clear hydrated-dehydrated transition (Cao et al. 2016). Small ankyrin 1 (sAnk1; TC#8.A.28.1.2) and SLN interact with each other in their transmembrane domains to regulate SERCA (TC# 3.A.3.2.7) (Desmond et al. 2017). The TM voltage has a positive effect on the permeability of water molecules and ions (Cao et al. 2020). The conserved C-terminus is an essential element required for the dynamic control of SLN regulatory function (Aguayo-Ortiz et al. 2020).

Accession Number:O00631
Protein Name:SLN aka Sarcolipin
Length:31
Molecular Weight:3762.00
Species:Homo sapiens (Human) [9606]
Number of TMSs:1
Location1 / Topology2 / Orientation3: Sarcoplasmic reticulum membrane1 / Single-pass membrane protein2
Substrate Ca2+, Na+, Cl-, water

Cross database links:

RefSeq: NP_003054.1   
Entrez Gene ID: 6588   
Pfam: PF05366   
OMIM: 602203  gene
KEGG: hsa:6588   

Gene Ontology

GO:0016021 C:integral to membrane
GO:0033017 C:sarcoplasmic reticulum membrane
GO:0030234 F:enzyme regulator activity
GO:0006816 P:calcium ion transport
GO:0051924 P:regulation of calcium ion transport

References (2)

[1] “Characterization of the gene encoding human sarcolipin (SLN), a proteolipid associated with SERCA1: absence of structural mutations in five patients with Brody disease.”  Odermatt A.et.al.   9367679
[2] “Structure and orientation of sarcolipin in lipid environments.”  Mascioni A.et.al.   11781085
Structure:
1JDM     

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FASTA formatted sequence
1:	MGINTRELFL NFTIVLITVI LMWLLVRSYQ Y