LRC55_MOUSE
ID LRC55_MOUSE Reviewed; 298 AA.
AC Q3UY51;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2018, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Leucine-rich repeat-containing protein 55;
DE AltName: Full=BK channel auxiliary gamma subunit LRRC55;
DE Flags: Precursor;
GN Name=Lrrc55; Synonyms=Gm351;
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 STRAIN=C57BL/6J; TISSUE=Olfactory bulb;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
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). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with KCNMA1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane
CC protein {ECO:0000250}.
CC -!- DOMAIN: The transmembrane domain is necessary for interaction with
CC KCNMA1. {ECO:0000250}.
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DR EMBL; AK134968; BAE22362.1; -; mRNA.
DR CCDS; CCDS38167.2; -.
DR RefSeq; NP_001028518.1; NM_001033346.2.
DR RefSeq; XP_006499530.1; XM_006499467.3.
DR RefSeq; XP_006499531.1; XM_006499468.3.
DR RefSeq; XP_006499532.1; XM_006499469.2.
DR AlphaFoldDB; Q3UY51; -.
DR SMR; Q3UY51; -.
DR STRING; 10090.ENSMUSP00000107228; -.
DR GlyConnect; 2471; 4 N-Linked glycans (1 site).
DR GlyGen; Q3UY51; 1 site, 4 N-linked glycans (1 site).
DR PaxDb; Q3UY51; -.
DR PRIDE; Q3UY51; -.
DR ProteomicsDB; 252509; -.
DR Antibodypedia; 2684; 12 antibodies from 8 providers.
DR Ensembl; ENSMUST00000234267; ENSMUSP00000157165; ENSMUSG00000075224.
DR Ensembl; ENSMUST00000234905; ENSMUSP00000157170; ENSMUSG00000075224.
DR GeneID; 241528; -.
DR KEGG; mmu:241528; -.
DR UCSC; uc008kkc.1; mouse.
DR CTD; 219527; -.
DR MGI; MGI:2685197; Lrrc55.
DR VEuPathDB; HostDB:ENSMUSG00000075224; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000161412; -.
DR HOGENOM; CLU_000288_18_10_1; -.
DR InParanoid; Q3UY51; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; Q3UY51; -.
DR TreeFam; TF334689; -.
DR BioGRID-ORCS; 241528; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Lrrc55; mouse.
DR PRO; PR:Q3UY51; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q3UY51; protein.
DR Bgee; ENSMUSG00000075224; Expressed in olfactory bulb and 49 other tissues.
DR ExpressionAtlas; Q3UY51; baseline and differential.
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:0044325; F:transmembrane transporter binding; ISO:MGI.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; ISO: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 Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
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; SM00082; LRRCT; 1.
DR SMART; SM00013; LRRNT; 1.
DR PROSITE; PS51450; LRR; 5.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Ion channel; Ion transport;
KW Leucine-rich repeat; Membrane; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..34
FT /evidence="ECO:0000250"
FT CHAIN 35..298
FT /note="Leucine-rich repeat-containing protein 55"
FT /id="PRO_0000232914"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 35..65
FT /note="LRRNT"
FT REPEAT 66..87
FT /note="LRR 1"
FT REPEAT 90..111
FT /note="LRR 2"
FT REPEAT 114..135
FT /note="LRR 3"
FT REPEAT 138..160
FT /note="LRR 4"
FT REPEAT 163..186
FT /note="LRR 5"
FT DOMAIN 196..251
FT /note="LRRCT"
FT DISULFID 38..44
FT /evidence="ECO:0000255"
FT DISULFID 42..51
FT /evidence="ECO:0000255"
FT DISULFID 200..227
FT /evidence="ECO:0000255"
FT DISULFID 202..249
FT /evidence="ECO:0000255"
SQ SEQUENCE 298 AA; 33030 MW; 1594AD98028E0596 CRC64;
MGDTWAQLPW PGPPHSALLL VFFLLAAGVM HSDAGTSCPV LCTCRNQVVD CSNQRLFSVP
PDLPMDTRNL SLAHNRIAAV PPGYLTCYME LRVLDLRNNS LMELPPGLFL HAKRLAHLDL
SYNNLSHVPA DMFREAHGLV HIDLSHNPWL RRVHPQAFQG LVHLRDLDLS YGGLAFLSLE
ALEGLPGLVT LQIGGNPWVC GCTMEPLLKW LRNRIQRCTA DSQLAECRGP PEVEGAPLFS
LTEESFKACH LTLTLDDYLF IAFVGFVVSI ASVATNFLLG ITANCCHRWS KANEEEEI
