LRC52_MOUSE
ID LRC52_MOUSE Reviewed; 314 AA.
AC Q5M8M9;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Leucine-rich repeat-containing protein 52;
DE AltName: Full=BK channel auxiliary gamma subunit LRRC52;
DE Flags: Precursor;
GN Name=Lrrc52;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP FUNCTION, INTERACTION WITH KCNU1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND GLYCOSYLATION.
RX PubMed=22084117; DOI=10.1073/pnas.1111104108;
RA Yang C., Zeng X.H., Zhou Y., Xia X.M., Lingle C.J.;
RT "LRRC52 (leucine-rich-repeat-containing protein 52), a testis-specific
RT auxiliary subunit of the alkalization-activated Slo3 channel.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:19419-19424(2011).
CC -!- FUNCTION: Auxiliary protein of the large-conductance, voltage and
CC calcium-activated potassium channel (BK alpha). Modulates gating
CC properties by producing a marked shift in the BK channel's voltage
CC dependence of activation in the hyperpolarizing direction, and in the
CC absence of calcium (By similarity). KCNU1 channel auxiliary protein.
CC May modulate KCNU1 gating properties, shifting KCNU1 gating to more
CC negative potentials at a given pH. {ECO:0000250,
CC ECO:0000269|PubMed:22084117}.
CC -!- SUBUNIT: Interacts with KCNMA1 (By similarity). May interact with
CC KCNU1; this interaction may be required for LRRC52 stability and may
CC change the channel gating properties. {ECO:0000250,
CC ECO:0000269|PubMed:22084117}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22084117};
CC Single-pass membrane protein {ECO:0000269|PubMed:22084117}.
CC Note=Expression at the cell surface may require the presence of KCNU1.
CC -!- TISSUE SPECIFICITY: Testis-specific (at protein level). At the mRNA
CC level, also detected in kidney, ventricle, spinal cord and skeletal
CC muscle, although at lower levels compared to testis. Expression in
CC testis at the protein level requires the presence of KCNU1.
CC {ECO:0000269|PubMed:22084117}.
CC -!- DEVELOPMENTAL STAGE: Very low expression levels in testis before
CC postnatal day 25 (P25). Levels strongly increase between P25 and P30,
CC and then remain high from P30 through P150.
CC {ECO:0000269|PubMed:22084117}.
CC -!- DOMAIN: The transmembrane domain is necessary for interaction with
CC KCNMA1. {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:22084117}.
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DR EMBL; BC087947; AAH87947.1; -; mRNA.
DR CCDS; CCDS15458.1; -.
DR RefSeq; NP_001013400.1; NM_001013382.2.
DR AlphaFoldDB; Q5M8M9; -.
DR SMR; Q5M8M9; -.
DR STRING; 10090.ENSMUSP00000047213; -.
DR GlyGen; Q5M8M9; 5 sites.
DR iPTMnet; Q5M8M9; -.
DR PhosphoSitePlus; Q5M8M9; -.
DR PaxDb; Q5M8M9; -.
DR PRIDE; Q5M8M9; -.
DR Antibodypedia; 47069; 86 antibodies from 18 providers.
DR Ensembl; ENSMUST00000036643; ENSMUSP00000047213; ENSMUSG00000040485.
DR GeneID; 240899; -.
DR KEGG; mmu:240899; -.
DR UCSC; uc007dkz.1; mouse.
DR CTD; 440699; -.
DR MGI; MGI:1924118; Lrrc52.
DR VEuPathDB; HostDB:ENSMUSG00000040485; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000156906; -.
DR HOGENOM; CLU_000288_18_10_1; -.
DR InParanoid; Q5M8M9; -.
DR OMA; LVYLDCH; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; Q5M8M9; -.
DR TreeFam; TF334689; -.
DR BioGRID-ORCS; 240899; 1 hit in 73 CRISPR screens.
DR PRO; PR:Q5M8M9; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q5M8M9; protein.
DR Bgee; ENSMUSG00000040485; Expressed in spermatid and 24 other tissues.
DR Genevisible; Q5M8M9; MM.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; ISO:MGI.
DR GO; GO:0099104; F:potassium channel activator activity; ISO:MGI.
DR GO; GO:0005267; F:potassium channel activity; IMP:MGI.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; ISO:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:1903818; P:positive regulation of voltage-gated potassium channel activity; ISO:MGI.
DR GO; GO:0071805; P:potassium ion transmembrane transport; ISO:MGI.
DR GO; GO:0006813; P:potassium ion transport; IMP:MGI.
DR GO; GO:0022414; P:reproductive process; IMP:MGI.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000372; LRRNT.
DR Pfam; PF13855; LRR_8; 2.
DR SMART; SM00369; LRR_TYP; 5.
DR SMART; SM00013; LRRNT; 1.
DR PROSITE; PS51450; LRR; 6.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW Leucine-rich repeat; Membrane; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..314
FT /note="Leucine-rich repeat-containing protein 52"
FT /id="PRO_0000226827"
FT TOPO_DOM 24..244
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 266..314
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 24..53
FT /note="LRRNT"
FT REPEAT 54..73
FT /note="LRR 1"
FT REPEAT 78..99
FT /note="LRR 2"
FT REPEAT 102..123
FT /note="LRR 3"
FT REPEAT 126..148
FT /note="LRR 4"
FT REPEAT 151..172
FT /note="LRR 5"
FT DOMAIN 184..238
FT /note="LRRCT"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 26..32
FT /evidence="ECO:0000255"
FT DISULFID 30..39
FT /evidence="ECO:0000255"
FT DISULFID 188..214
FT /evidence="ECO:0000255"
FT DISULFID 190..236
FT /evidence="ECO:0000255"
SQ SEQUENCE 314 AA; 35295 MW; A173A35F90490BA7 CRC64;
MSLASGPSSK LLLFSLGMGL VSGSKCPNKC VCQDQEVACI DLHLTEYPAD IPLNTRRLYL
NNNKITSLPA LQLGFLSDLV YLDCQNNRIR EVMDYTFIGI FRLIYLDLSS NNLTSISPFS
FSVLTNLVRL NISHNPHLLY LDKYVFANTT SLRYLDLRNT GLHIIDHNGF HHLVVLQTLY
LSGNPWICNC SFLDFTIHLL VSHMDHPDAQ NATCTEPAEL KGWPITKVGN PLQYMCITHL
DQQDYIFLLL IGFCIFAAGT VAAWLTGVCA VLYQNALRTS SGDDTEDETG SRFANQIFRS
NTHLGPIRRF PELI
