LRC55_HUMAN
ID LRC55_HUMAN Reviewed; 298 AA.
AC Q6ZSA7; A7E2U7; B2RN81;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2018, sequence version 3.
DT 03-AUG-2022, entry version 136.
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 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=Brain;
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 MRNA].
RC TISSUE=Brain, and 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).
RN [3]
RP PROTEIN SEQUENCE OF 35-49.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(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).
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. {ECO:0000269|PubMed:22547800}.
CC -!- SUBUNIT: Interacts with KCNMA1. {ECO:0000269|PubMed:22547800}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane
CC protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in brain.
CC {ECO:0000269|PubMed:22547800}.
CC -!- DOMAIN: The transmembrane domain is necessary for interaction with
CC KCNMA1. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI36738.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI36740.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI50573.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC87047.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK127591; BAC87047.1; ALT_INIT; mRNA.
DR EMBL; BC136737; AAI36738.1; ALT_INIT; mRNA.
DR EMBL; BC136739; AAI36740.1; ALT_INIT; mRNA.
DR EMBL; BC150572; AAI50573.1; ALT_INIT; mRNA.
DR CCDS; CCDS31539.1; -.
DR RefSeq; NP_001005210.1; NM_001005210.2.
DR AlphaFoldDB; Q6ZSA7; -.
DR SMR; Q6ZSA7; -.
DR BioGRID; 128550; 82.
DR STRING; 9606.ENSP00000419542; -.
DR TCDB; 8.A.43.1.8; the neat-domain containing methaemoglobin heme sequestration (n-mhs) family.
DR BioMuta; LRRC55; -.
DR DMDM; 124056493; -.
DR MassIVE; Q6ZSA7; -.
DR PaxDb; Q6ZSA7; -.
DR PeptideAtlas; Q6ZSA7; -.
DR PRIDE; Q6ZSA7; -.
DR ProteomicsDB; 68209; -.
DR Antibodypedia; 2684; 12 antibodies from 8 providers.
DR DNASU; 219527; -.
DR Ensembl; ENST00000497933.3; ENSP00000419542.2; ENSG00000183908.7.
DR GeneID; 219527; -.
DR KEGG; hsa:219527; -.
DR MANE-Select; ENST00000497933.3; ENSP00000419542.2; NM_001005210.4; NP_001005210.2.
DR UCSC; uc001njl.3; human.
DR CTD; 219527; -.
DR DisGeNET; 219527; -.
DR GeneCards; LRRC55; -.
DR HGNC; HGNC:32324; LRRC55.
DR HPA; ENSG00000183908; Tissue enriched (brain).
DR MIM; 615213; gene.
DR neXtProt; NX_Q6ZSA7; -.
DR OpenTargets; ENSG00000183908; -.
DR PharmGKB; PA142671514; -.
DR VEuPathDB; HostDB:ENSG00000183908; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000161412; -.
DR HOGENOM; CLU_000288_18_10_1; -.
DR InParanoid; Q6ZSA7; -.
DR OMA; WSQLPWP; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; Q6ZSA7; -.
DR TreeFam; TF334689; -.
DR PathwayCommons; Q6ZSA7; -.
DR BioGRID-ORCS; 219527; 17 hits in 1066 CRISPR screens.
DR GenomeRNAi; 219527; -.
DR Pharos; Q6ZSA7; Tbio.
DR PRO; PR:Q6ZSA7; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q6ZSA7; protein.
DR Bgee; ENSG00000183908; Expressed in ganglionic eminence and 84 other tissues.
DR ExpressionAtlas; Q6ZSA7; baseline and differential.
DR Genevisible; Q6ZSA7; 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:1903818; P:positive regulation of voltage-gated potassium channel activity; IDA:UniProtKB.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IDA:UniProtKB.
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; 5.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00013; LRRNT; 1.
DR PROSITE; PS51450; LRR; 5.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Disulfide bond; Ion channel;
KW Ion transport; Leucine-rich repeat; Membrane; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..34
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 35..298
FT /note="Leucine-rich repeat-containing protein 55"
FT /id="PRO_0000232913"
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; 33009 MW; 61C716A7CC8895E1 CRC64;
MGDTWAQLPW PGPPHPAMLL ISLLLAAGLM HSDAGTSCPV LCTCRNQVVD CSSQRLFSVP
PDLPMDTRNL SLAHNRITAV PPGYLTCYME LQVLDLHNNS LMELPRGLFL HAKRLAHLDL
SYNNFSHVPA DMFQEAHGLV HIDLSHNPWL RRVHPQAFQG LMQLRDLDLS YGGLAFLSLE
ALEGLPGLVT LQIGGNPWVC GCTMEPLLKW LRNRIQRCTA DSQLAECRGP PEVEGAPLFS
LTEESFKACH LTLTLDDYLF IAFVGFVVSI ASVATNFLLG ITANCCHRWS KASEEEEI