LRC38_HUMAN
ID LRC38_HUMAN Reviewed; 294 AA.
AC Q5VT99; Q96B32;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Leucine-rich repeat-containing protein 38;
DE AltName: Full=BK channel auxiliary gamma subunit LRRC38;
DE Flags: Precursor;
GN Name=LRRC38;
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 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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).
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 type I
CC membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in adrenal gland, thymus and
CC skeletal muscle. {ECO:0000269|PubMed:22547800}.
CC -!- DOMAIN: The transmembrane domain is necessary for interaction with
CC KCNMA1. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH16048.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AL354712; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL603749; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471167; EAW51689.1; -; Genomic_DNA.
DR EMBL; BC016048; AAH16048.1; ALT_FRAME; mRNA.
DR CCDS; CCDS53269.1; -.
DR RefSeq; NP_001010847.1; NM_001010847.1.
DR AlphaFoldDB; Q5VT99; -.
DR SMR; Q5VT99; -.
DR STRING; 9606.ENSP00000365253; -.
DR BioMuta; LRRC38; -.
DR DMDM; 74756785; -.
DR MassIVE; Q5VT99; -.
DR PaxDb; Q5VT99; -.
DR PeptideAtlas; Q5VT99; -.
DR PRIDE; Q5VT99; -.
DR ProteomicsDB; 65317; -.
DR Antibodypedia; 48140; 73 antibodies from 14 providers.
DR DNASU; 126755; -.
DR Ensembl; ENST00000376085.4; ENSP00000365253.3; ENSG00000162494.6.
DR GeneID; 126755; -.
DR KEGG; hsa:126755; -.
DR MANE-Select; ENST00000376085.4; ENSP00000365253.3; NM_001010847.2; NP_001010847.1.
DR UCSC; uc001avb.4; human.
DR CTD; 126755; -.
DR GeneCards; LRRC38; -.
DR HGNC; HGNC:27005; LRRC38.
DR HPA; ENSG00000162494; Group enriched (adrenal gland, skeletal muscle, tongue).
DR MIM; 615212; gene.
DR neXtProt; NX_Q5VT99; -.
DR OpenTargets; ENSG00000162494; -.
DR VEuPathDB; HostDB:ENSG00000162494; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000162571; -.
DR HOGENOM; CLU_000288_18_10_1; -.
DR InParanoid; Q5VT99; -.
DR OMA; CAPSKDD; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; Q5VT99; -.
DR TreeFam; TF334689; -.
DR PathwayCommons; Q5VT99; -.
DR BioGRID-ORCS; 126755; 11 hits in 1065 CRISPR screens.
DR ChiTaRS; LRRC38; human.
DR GenomeRNAi; 126755; -.
DR Pharos; Q5VT99; Tbio.
DR PRO; PR:Q5VT99; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q5VT99; protein.
DR Bgee; ENSG00000162494; Expressed in gastrocnemius and 71 other tissues.
DR Genevisible; Q5VT99; 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; IBA:GO_Central.
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; -; 1.
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; 2.
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; Disulfide bond; Ion channel; Ion transport;
KW Leucine-rich repeat; Membrane; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..294
FT /note="Leucine-rich repeat-containing protein 38"
FT /id="PRO_0000312418"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 28..56
FT /note="LRRNT"
FT REPEAT 57..78
FT /note="LRR 1"
FT REPEAT 81..102
FT /note="LRR 2"
FT REPEAT 105..126
FT /note="LRR 3"
FT REPEAT 129..150
FT /note="LRR 4"
FT REPEAT 153..174
FT /note="LRR 5"
FT DOMAIN 186..241
FT /note="LRRCT"
FT DISULFID 28..34
FT /evidence="ECO:0000255"
FT DISULFID 32..42
FT /evidence="ECO:0000255"
FT DISULFID 190..217
FT /evidence="ECO:0000255"
FT DISULFID 192..239
FT /evidence="ECO:0000255"
FT VARIANT 276
FT /note="L -> F (in dbSNP:rs2940315)"
FT /id="VAR_037504"
FT VARIANT 292
FT /note="K -> E (in dbSNP:rs3013105)"
FT /id="VAR_037505"
SQ SEQUENCE 294 AA; 32082 MW; 74A7A2E2C4E17629 CRC64;
MRPRAPACAA AALGLCSLLL LLAPGHACPA GCACTDPHTV DCRDRGLPSV PDPFPLDVRK
LLVAGNRIQR IPEDFFIFYG DLVYLDFRNN SLRSLEEGTF SGSAKLVFLD LSYNNLTQLG
AGAFRSAGRL VKLSLANNNL VGVHEDAFET LESLQVLELN DNNLRSLSVA ALAALPALRS
LRLDGNPWLC DCDFAHLFSW IQENASKLPK GLDEIQCSLP MESRRISLRE LSEASFSECR
FSLSLTDLCI IIFSGVAVSI AAIISSFFLA TVVQCLQRCA PNKDAEDEDE DKDD
