LRC52_HUMAN
ID LRC52_HUMAN Reviewed; 313 AA.
AC Q8N7C0; A2RUN7; Q5T9K5;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 154.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP FUNCTION, SUBUNIT, DISULFIDE BONDS, AND TISSUE SPECIFICITY.
RX PubMed=22547800; DOI=10.1073/pnas.1205435109;
RA Yan J., Aldrich R.W.;
RT "BK potassium channel modulation by leucine-rich repeat-containing
RT proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:7917-7922(2012).
RN [5]
RP FUNCTION.
RX PubMed=23129643; DOI=10.1073/pnas.1215078109;
RA Leonetti M.D., Yuan P., Hsiung Y., Mackinnon R.;
RT "Functional and structural analysis of the human SLO3 pH- and voltage-gated
RT K+ channel.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:19274-19279(2012).
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. KCNU1 channel auxiliary protein. May modulate KCNU1
CC gating properties. {ECO:0000269|PubMed:22547800,
CC ECO:0000269|PubMed:23129643}.
CC -!- SUBUNIT: May interact with KCNU1; this interaction may be required for
CC LRRC52 stability and may change the channel gating properties (By
CC similarity). Interacts with KCNMA1. {ECO:0000250,
CC ECO:0000269|PubMed:22547800}.
CC -!- INTERACTION:
CC Q8N7C0; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-12176213, EBI-16439278;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane
CC protein {ECO:0000250}. Note=Expression at the cell surface may require
CC the presence of KCNU1.
CC -!- TISSUE SPECIFICITY: Mainly expressed in testis and skeletal muscle.
CC {ECO:0000269|PubMed:22547800}.
CC -!- DOMAIN: The transmembrane domain is necessary for interaction with
CC KCNMA1. {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK098677; BAC05375.1; -; mRNA.
DR EMBL; AL157714; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC132981; AAI32982.1; -; mRNA.
DR EMBL; BC132983; AAI32984.1; -; mRNA.
DR CCDS; CCDS30930.1; -.
DR RefSeq; NP_001005214.2; NM_001005214.3.
DR AlphaFoldDB; Q8N7C0; -.
DR SMR; Q8N7C0; -.
DR BioGRID; 136818; 26.
DR IntAct; Q8N7C0; 3.
DR STRING; 9606.ENSP00000294818; -.
DR GlyGen; Q8N7C0; 4 sites.
DR PhosphoSitePlus; Q8N7C0; -.
DR BioMuta; LRRC52; -.
DR DMDM; 90185259; -.
DR MassIVE; Q8N7C0; -.
DR PaxDb; Q8N7C0; -.
DR PeptideAtlas; Q8N7C0; -.
DR PRIDE; Q8N7C0; -.
DR Antibodypedia; 47069; 86 antibodies from 18 providers.
DR DNASU; 440699; -.
DR Ensembl; ENST00000294818.2; ENSP00000294818.2; ENSG00000162763.4.
DR GeneID; 440699; -.
DR KEGG; hsa:440699; -.
DR MANE-Select; ENST00000294818.2; ENSP00000294818.2; NM_001005214.4; NP_001005214.2.
DR UCSC; uc001gde.3; human.
DR CTD; 440699; -.
DR DisGeNET; 440699; -.
DR GeneCards; LRRC52; -.
DR HGNC; HGNC:32156; LRRC52.
DR HPA; ENSG00000162763; Tissue enriched (testis).
DR MIM; 615218; gene.
DR neXtProt; NX_Q8N7C0; -.
DR OpenTargets; ENSG00000162763; -.
DR PharmGKB; PA142671512; -.
DR VEuPathDB; HostDB:ENSG00000162763; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000156906; -.
DR HOGENOM; CLU_000288_18_10_1; -.
DR InParanoid; Q8N7C0; -.
DR OMA; LVYLDCH; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; Q8N7C0; -.
DR TreeFam; TF334689; -.
DR PathwayCommons; Q8N7C0; -.
DR Reactome; R-HSA-9662360; Sensory processing of sound by inner hair cells of the cochlea.
DR SignaLink; Q8N7C0; -.
DR BioGRID-ORCS; 440699; 8 hits in 1059 CRISPR screens.
DR GenomeRNAi; 440699; -.
DR Pharos; Q8N7C0; Tbio.
DR PRO; PR:Q8N7C0; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q8N7C0; protein.
DR Bgee; ENSG00000162763; Expressed in left testis and 44 other tissues.
DR Genevisible; Q8N7C0; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:UniProtKB.
DR GO; GO:0099104; F:potassium channel activator activity; IDA:UniProtKB.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:UniProtKB.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IDA:UniProtKB.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:1903818; P:positive regulation of voltage-gated potassium channel activity; IDA:UniProtKB.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IDA:UniProtKB.
DR GO; GO:0022414; P:reproductive process; IEA:Ensembl.
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; 1.
DR SMART; SM00369; LRR_TYP; 4.
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..313
FT /note="Leucine-rich repeat-containing protein 52"
FT /id="PRO_0000226826"
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..313
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 24..53
FT /note="LRRNT"
FT REPEAT 54..75
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 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"
FT VARIANT 209
FT /note="D -> E (in dbSNP:rs17407838)"
FT /id="VAR_051122"
FT CONFLICT 309
FT /note="F -> S (in Ref. 1; BAC05375)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 313 AA; 35126 MW; BD15E62DEB9395F3 CRC64;
MSLASGPGPG WLLFSFGMGL VSGSKCPNNC LCQAQEVICT GKQLTEYPLD IPLNTRRLFL
NENRITSLPA MHLGLLSDLV YLDCQNNRIR EVMDYTFIGV FKLIYLDLSS NNLTSISPFT
FSVLSNLVQL NIANNPHLLS LHKFTFANTT SLRYLDLRNT GLQTLDSAAL YHLTTLETLF
LSGNPWKCNC SFLDFAIFLI VFHMDPSDDL NATCVEPTEL TGWPITRVGN PLRYMCITHL
DHKDYIFLLL IGFCIFAAGT VAAWLTGVCA VLYQNTRHKS SEEDEDEAGT RVEVSRRIFQ
TQTSSVQEFP QLI
