LRC55_RAT
ID LRC55_RAT Reviewed; 298 AA.
AC Q4KLL3;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2018, sequence version 3.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Leucine-rich repeat-containing protein 55;
DE AltName: Full=BK channel auxiliary gamma subunit LRRC55;
DE Flags: Precursor;
GN Name=Lrrc55;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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).
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; BC099134; AAH99134.2; -; mRNA.
DR RefSeq; NP_001116447.1; NM_001122975.1.
DR RefSeq; XP_006234534.1; XM_006234472.3.
DR RefSeq; XP_017447203.1; XM_017591714.1.
DR AlphaFoldDB; Q4KLL3; -.
DR SMR; Q4KLL3; -.
DR STRING; 10116.ENSRNOP00000034072; -.
DR PaxDb; Q4KLL3; -.
DR GeneID; 311171; -.
DR KEGG; rno:311171; -.
DR UCSC; RGD:1561726; rat.
DR CTD; 219527; -.
DR RGD; 1561726; Lrrc55.
DR eggNOG; KOG0619; Eukaryota.
DR HOGENOM; CLU_000288_18_10_1; -.
DR InParanoid; Q4KLL3; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; Q4KLL3; -.
DR TreeFam; TF334689; -.
DR PRO; PR:Q4KLL3; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; ISO:RGD.
DR GO; GO:0099104; F:potassium channel activator activity; ISO:RGD.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:RGD.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; ISO:RGD.
DR GO; GO:1903818; P:positive regulation of voltage-gated potassium channel activity; ISO:RGD.
DR GO; GO:0071805; P:potassium ion transmembrane transport; ISO:RGD.
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_0000232915"
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; 33000 MW; E094A698B28E02E7 CRC64;
MGDTWAQLPW PGPPHSALLL VFFLLAAGVM HSDAGASCPV 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