LRC26_HUMAN
ID LRC26_HUMAN Reviewed; 334 AA.
AC Q2I0M4; B9EIR7; C3RUL3; Q5VSG2;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Leucine-rich repeat-containing protein 26;
DE AltName: Full=BK channel auxiliary gamma subunit LRRC26;
DE AltName: Full=Cytokeratin-associated protein in cancer;
DE Flags: Precursor;
GN Name=LRRC26; Synonyms=CAPC;
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 [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Mammary gland, and Prostatic carcinoma;
RX PubMed=16585525; DOI=10.1073/pnas.0601296103;
RA Egland K.A., Liu X.F., Squires S., Nagata S., Man Y.-G., Bera T.K.,
RA Onda M., Vincent J.J., Strausberg R.L., Lee B., Pastan I.;
RT "High expression of a cytokeratin-associated protein in many cancers.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:5929-5934(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 291-304, USE OF
RP A NON-AUG INITIATOR START CODON, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP TISSUE SPECIFICITY.
RX PubMed=19250639; DOI=10.1016/j.bbrc.2009.01.089;
RA Anaganti S., Hansen J.K., Ha D., Hahn Y., Chertov O., Pastan I., Bera T.K.;
RT "Non-AUG translational initiation of a short CAPC transcript generating
RT protein isoform.";
RL Biochem. Biophys. Res. Commun. 380:508-513(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [5]
RP FUNCTION, INTERACTION WITH KCNMA1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20613726; DOI=10.1038/nature09162;
RA Yan J., Aldrich R.W.;
RT "LRRC26 auxiliary protein allows BK channel activation at resting voltage
RT without calcium.";
RL Nature 466:513-516(2010).
RN [6]
RP FUNCTION, SUBUNIT, SIGNAL SEQUENCE, DISULFIDE BONDS, GLYCOSYLATION AT
RP ASN-147, AND SUBCELLULAR LOCATION.
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). Required for the
CC conversion of BK alpha channels from a high-voltage to a low-voltage
CC activated channel type in non-excitable cells. These are characterized
CC by negative membrane voltages and constant low levels of calcium.
CC {ECO:0000269|PubMed:20613726, ECO:0000269|PubMed:22547800}.
CC -!- SUBUNIT: Interacts with KCNMA1. {ECO:0000269|PubMed:20613726,
CC ECO:0000269|PubMed:22547800}.
CC -!- INTERACTION:
CC Q2I0M4; Q12791: KCNMA1; NbExp=3; IntAct=EBI-15863320, EBI-1220676;
CC Q2I0M4; Q12791-5: KCNMA1; NbExp=2; IntAct=EBI-15863320, EBI-15861807;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein. Cytoplasm, cytoskeleton. Note=Localizes to the cytoplasm when
CC expressed at high levels. {ECO:0000269|PubMed:15164053}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=L-CAPC;
CC IsoId=Q2I0M4-1; Sequence=Displayed;
CC Name=2; Synonyms=S-CAPC;
CC IsoId=Q2I0M4-2; Sequence=VSP_040058, VSP_040205;
CC -!- TISSUE SPECIFICITY: Isoform 1 is expressed highly in normal prostate
CC and salivary gland, very weakly in colon, pancreas, and intestine, and
CC not at all in other tissues. Isoform 1 is expressed highly in many
CC cancer cell lines and in breast cancer, pancreatic cancer and colon
CC cancer. Isoform 2 is expressed in cancer cell lines.
CC {ECO:0000269|PubMed:16585525, ECO:0000269|PubMed:19250639}.
CC -!- DOMAIN: The transmembrane domain is necessary for interaction with
CC KCNMA1.
CC -!- MISCELLANEOUS: [Isoform 2]: Translation initiates from a UGC codon. It
CC is unsure whether the initiator amino acid is a modified cysteine or a
CC methionine. Could also be the result of a proteolytic cleavage from a
CC longer precursor. {ECO:0000305}.
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; DQ355157; ABC79623.1; -; mRNA.
DR EMBL; EU588721; ACO90295.1; -; mRNA.
DR EMBL; AL929554; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC140911; AAI40912.1; -; mRNA.
DR CCDS; CCDS35184.1; -. [Q2I0M4-1]
DR RefSeq; NP_001013675.1; NM_001013653.2. [Q2I0M4-1]
DR AlphaFoldDB; Q2I0M4; -.
DR SMR; Q2I0M4; -.
DR CORUM; Q2I0M4; -.
DR DIP; DIP-60459N; -.
DR IntAct; Q2I0M4; 1.
DR STRING; 9606.ENSP00000360597; -.
DR TCDB; 8.A.43.1.14; the neat-domain containing methaemoglobin heme sequestration (n-mhs) family.
DR GlyConnect; 1452; 1 N-Linked glycan (1 site).
DR GlyGen; Q2I0M4; 1 site, 1 N-linked glycan (1 site).
DR iPTMnet; Q2I0M4; -.
DR PhosphoSitePlus; Q2I0M4; -.
DR BioMuta; LRRC26; -.
DR DMDM; 160410009; -.
DR jPOST; Q2I0M4; -.
DR MassIVE; Q2I0M4; -.
DR MaxQB; Q2I0M4; -.
DR PaxDb; Q2I0M4; -.
DR PeptideAtlas; Q2I0M4; -.
DR PRIDE; Q2I0M4; -.
DR ProteomicsDB; 61296; -. [Q2I0M4-1]
DR Antibodypedia; 18941; 97 antibodies from 22 providers.
DR DNASU; 389816; -.
DR Ensembl; ENST00000371542.3; ENSP00000360597.3; ENSG00000184709.7. [Q2I0M4-1]
DR GeneID; 389816; -.
DR KEGG; hsa:389816; -.
DR MANE-Select; ENST00000371542.3; ENSP00000360597.3; NM_001013653.3; NP_001013675.1.
DR UCSC; uc004clp.4; human. [Q2I0M4-1]
DR CTD; 389816; -.
DR DisGeNET; 389816; -.
DR GeneCards; LRRC26; -.
DR HGNC; HGNC:31409; LRRC26.
DR HPA; ENSG00000184709; Tissue enriched (salivary).
DR MIM; 613505; gene.
DR neXtProt; NX_Q2I0M4; -.
DR OpenTargets; ENSG00000184709; -.
DR PharmGKB; PA134952867; -.
DR VEuPathDB; HostDB:ENSG00000184709; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000162780; -.
DR HOGENOM; CLU_000288_18_10_1; -.
DR InParanoid; Q2I0M4; -.
DR OMA; AAFSHCA; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; Q2I0M4; -.
DR TreeFam; TF334689; -.
DR PathwayCommons; Q2I0M4; -.
DR SignaLink; Q2I0M4; -.
DR BioGRID-ORCS; 389816; 14 hits in 1062 CRISPR screens.
DR ChiTaRS; LRRC26; human.
DR GenomeRNAi; 389816; -.
DR Pharos; Q2I0M4; Tbio.
DR PRO; PR:Q2I0M4; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q2I0M4; protein.
DR Bgee; ENSG00000184709; Expressed in olfactory segment of nasal mucosa and 62 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA: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:0015459; F:potassium channel regulator 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; -; 1.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF13855; LRR_8; 2.
DR SMART; SM00369; LRR_TYP; 5.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Ion channel;
KW Ion transport; Leucine-rich repeat; Membrane; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..26
FT CHAIN 27..334
FT /note="Leucine-rich repeat-containing protein 26"
FT /id="PRO_0000309360"
FT TOPO_DOM 27..261
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..282
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 283..334
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 34..71
FT /note="LRRNT"
FT REPEAT 72..93
FT /note="LRR 1"
FT REPEAT 96..117
FT /note="LRR 2"
FT REPEAT 120..141
FT /note="LRR 3"
FT REPEAT 144..167
FT /note="LRR 4"
FT REPEAT 168..190
FT /note="LRR 5"
FT DOMAIN 201..255
FT /note="LRRCT"
FT REGION 298..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..321
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22547800"
FT DISULFID 43..49
FT /evidence="ECO:0000255"
FT DISULFID 47..57
FT /evidence="ECO:0000255"
FT DISULFID 205..231
FT /evidence="ECO:0000255"
FT DISULFID 207..253
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..289
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19250639"
FT /id="VSP_040058"
FT VAR_SEQ 290
FT /note="C -> M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19250639"
FT /id="VSP_040205"
FT CONFLICT 27
FT /note="Q -> H (in Ref. 1; ABC79623 and 3; AAI40912)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 334 AA; 34857 MW; B3E8C6C9AADEF958 CRC64;
MRGPSWSRPR PLLLLLLLLS PWPVWAQVSA TASPSGSLGA PDCPEVCTCV PGGLASCSAL
SLPAVPPGLS LRLRALLLDH NRVRALPPGA FAGAGALQRL DLRENGLHSV HVRAFWGLGA
LQLLDLSANQ LEALAPGTFA PLRALRNLSL AGNRLARLEP AALGALPLLR SLSLQDNELA
ALAPGLLGRL PALDALHLRG NPWGCGCALR PLCAWLRRHP LPASEAETVL CVWPGRLTLS
PLTAFSDAAF SHCAQPLALR DLAVVYTLGP ASFLVSLASC LALGSGLTAC RARRRRLRTA
ALRPPRPPDP NPDPDPHGCA SPADPGSPAA AAQA
