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LRRC52 Membrane Protein Introduction

Introduction of LRRC52

LRRC52, the full protein name being leucine-rich repeat-containing protein 52, is encoded by the LRRC52 gene in human. It was identified as Slo3-associated protein, since LRRC52 can shift Slo3 gating into a range of voltages, PH values. It’s enriched in testis as a homolog of the Slo-modifying LRRC26. Its expression is dependent on Slo3, and LRRC52 can modify the function of Slo3. In addition, LRRC52 can shift the voltage of BK channels.

Basic Information of LRRC52
Protein Name Leucine-rich repeat-containing protein 52
Gene Name LRRC52
Aliases BK channel auxiliary gamma subunit LRRC52
Organism Homo sapiens (Human)
UniProt ID Q8N7C0
Transmembrane Times 1
Length (aa) 313
Sequence MSLASGPGPGWLLFSFGMGLVSGSKCPNNCLCQAQEVICTGKQLTEYPLDIPLNTRRLFLNENRITSLPAMHLGLLSDLVYLDCQNNRIREVMDYTFIGVFKLIYLDLSSNNLTSISPFTFSVLSNLVQLNIANNPHLLSLHKFTFANTTSLRYLDLRNTGLQTLDSAALYHLTTLETLFLSGNPWKCNCSFLDFAIFLIVFHMDPSDDLNATCVEPTELTGWPITRVGNPLRYMCITHLDHKDYIFLLLIGFCIFAAGTVAAWLTGVCAVLYQNTRHKSSEEDEDEAGTRVEVSRRIFQTQTSSVQEFPQLI

Function of LRRC52 Membrane Protein

LRRC52 (Leucine-rich repeat-containing protein 52) is a single transmembrane protein. It was identified as Slo3-associated protein, since LRRC52 can shift Slo3 gating into a range of voltages, PH values. Also, it’s an auxiliary subunit of the large-conductance, voltage and calcium-activated potassium channel (BK alpha channel). BK channels consist of the homotetrameric pore-forming voltage and calcium-sensing α subunits (BKα), or regulatory tissue-specific auxiliary β or γ subunits. BK channel auxiliary γ (BKγ) subunits are a group of leucine-rich repeat (LRR)-containing membrane proteins, including γ1 (LRRC26), γ2 (LRRC52), γ3 (LRRC55), and γ4 (LRRC38). LRRC52 can modulate the gating characteristics by producing a marked shift in hyperpolarizing direction and in the absence of calcium. These subunits show distinct expression in different human tissues, while LRRC52 is mainly expressed in testis. In addition, LRRC52 is KCNU1 channel auxiliary protein, and may modulate the gating properties of KCNU1.

 Structural features of LRRC52 (γ2) Fig.1 Structural features of LRRC52 (γ2) (Li, 2015)

Application of LRRC52 Membrane Protein in Literature

  1. Li Q., et al. Molecular basis for differential modulation of BK channel voltage-dependent gating by auxiliary γ subunits. J Gen Physiol. 2015, 145(6):543-54. PubMed ID: 26009545

    This article shows the molecular basis for differential modulation of BK channel by gamma subunits, and LRRC52 is gamma-2 subunit.

  2. Zeng X.H., et al. SLO3 auxiliary subunit LRRC52 controls gating of sperm KSPER currents and is critical for normal fertility. Proc Natl Acad Sci U S A. 2015, 112(8):2599-604. PubMed ID: 25675513

    This article demonstrates that LRRC52 plays an important role in KSPER channels, and LRRC52 deficiency can cause severe fertility impairment.

  3. Yan J and Aldrich R.W. BK potassium channel modulation by leucine-rich repeat-containing proteins. Proc Natl Acad Sci U S A. 2012, 109(20):7917-22. PubMed ID: 22547800

    This article demonstrates that LRRC52 can produce a marked shift in the BK channel's voltage, which is dependent on the activation in the hyperpolarizing direction in the absence of calcium.

  4. Yang C., et al. LRRC52 (leucine-rich-repeat-containing protein 52), a testis-specific auxiliary subunit of the alkalization-activated Slo3 channel. Proc Natl Acad Sci U S A. 2011, 108(48):19419-24. PubMed ID: 22084117

    This article shows that LRRC52 is identified as new auxiliary subunit which can shift Slo3 gating behavior.

  5. Monies D., et al. The landscape of genetic diseases in Saudi Arabia based on the first 1000 diagnostic panels and exomes. Hum Genet. 2017, 136(8):921-939. PubMed ID: 28600779

    This article identifies the mutated genes in Saudi Arabia based on next-generation sequencing technology, and LRRC52 is identified in this article.

LRRC52 Preparation Options

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Reference

  1. Li Q, et al. (2015). Molecular basis for differential modulation of BK channel voltage-dependent gating by auxiliary γ subunits. J Gen Physiol. 145(6):543-54.

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