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Leucine-rich repeat-containing protein 26 (BK channel auxiliary gamma subunit LRRC26) (Cytokeratin-associated protein in cancer)

 LRC26_HUMAN             Reviewed;         334 AA.
Q2I0M4; B9EIR7; C3RUL3; Q5VSG2;
13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
13-NOV-2007, sequence version 2.
10-OCT-2018, entry version 106.
RecName: Full=Leucine-rich repeat-containing protein 26;
AltName: Full=BK channel auxiliary gamma subunit LRRC26;
AltName: Full=Cytokeratin-associated protein in cancer;
Flags: Precursor;
Name=LRRC26; Synonyms=CAPC;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
SUBCELLULAR LOCATION.
TISSUE=Mammary gland, and Prostatic carcinoma;
PubMed=16585525; DOI=10.1073/pnas.0601296103;
Egland K.A., Liu X.F., Squires S., Nagata S., Man Y.-G., Bera T.K.,
Onda M., Vincent J.J., Strausberg R.L., Lee B., Pastan I.;
"High expression of a cytokeratin-associated protein in many
cancers.";
Proc. Natl. Acad. Sci. U.S.A. 103:5929-5934(2006).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 291-304,
USE OF A NON-AUG INITIATOR START CODON, IDENTIFICATION BY MASS
SPECTROMETRY, AND TISSUE SPECIFICITY.
PubMed=19250639; DOI=10.1016/j.bbrc.2009.01.089;
Anaganti S., Hansen J.K., Ha D., Hahn Y., Chertov O., Pastan I.,
Bera T.K.;
"Non-AUG translational initiation of a short CAPC transcript
generating protein isoform.";
Biochem. Biophys. Res. Commun. 380:508-513(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
FUNCTION, INTERACTION WITH KCNMA1, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=20613726; DOI=10.1038/nature09162;
Yan J., Aldrich R.W.;
"LRRC26 auxiliary protein allows BK channel activation at resting
voltage without calcium.";
Nature 466:513-516(2010).
[6]
FUNCTION, SUBUNIT, SIGNAL SEQUENCE, DISULFIDE BONDS, GLYCOSYLATION AT
ASN-147, AND SUBCELLULAR LOCATION.
PubMed=22547800; DOI=10.1073/pnas.1205435109;
Yan J., Aldrich R.W.;
"BK potassium channel modulation by leucine-rich repeat-containing
proteins.";
Proc. Natl. Acad. Sci. U.S.A. 109:7917-7922(2012).
-!- FUNCTION: Auxiliary protein of the large-conductance, voltage and
calcium-activated potassium channel (BK alpha). Required for the
conversion of BK alpha channels from a high-voltage to a low-
voltage activated channel type in non-excitable cells. These are
characterized by negative membrane voltages and constant low
levels of calcium. {ECO:0000269|PubMed:20613726,
ECO:0000269|PubMed:22547800}.
-!- SUBUNIT: Interacts with KCNMA1. {ECO:0000269|PubMed:20613726,
ECO:0000269|PubMed:22547800}.
-!- INTERACTION:
Q12791:KCNMA1; NbExp=3; IntAct=EBI-15863320, EBI-1220676;
Q12791-5:KCNMA1; NbExp=2; IntAct=EBI-15863320, EBI-15861807;
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
protein. Cytoplasm, cytoskeleton. Note=Localizes to the cytoplasm
when expressed at high levels. {ECO:0000269|PubMed:15164053}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=L-CAPC;
IsoId=Q2I0M4-1; Sequence=Displayed;
Name=2; Synonyms=S-CAPC;
IsoId=Q2I0M4-2; Sequence=VSP_040058, VSP_040205;
Note=Translation initiates from a UGC codon. It is unsure
whether the initiator amino acid is a modified cysteine or a
methionine. Could also be the result of a proteolytic cleavage
from a longer precursor.;
-!- TISSUE SPECIFICITY: Isoform 1 is expressed highly in normal
prostate and salivary gland, very weakly in colon, pancreas, and
intestine, and not at all in other tissues. Isoform 1 is expressed
highly in many cancer cell lines and in breast cancer, pancreatic
cancer and colon cancer. Isoform 2 is expressed in cancer cell
lines. {ECO:0000269|PubMed:16585525, ECO:0000269|PubMed:19250639}.
-!- DOMAIN: The transmembrane domain is necessary for interaction with
KCNMA1.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; DQ355157; ABC79623.1; -; mRNA.
EMBL; EU588721; ACO90295.1; -; mRNA.
EMBL; AL929554; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC140911; AAI40912.1; -; mRNA.
CCDS; CCDS35184.1; -. [Q2I0M4-1]
RefSeq; NP_001013675.1; NM_001013653.2. [Q2I0M4-1]
UniGene; Hs.669977; -.
ProteinModelPortal; Q2I0M4; -.
SMR; Q2I0M4; -.
CORUM; Q2I0M4; -.
DIP; DIP-60459N; -.
IntAct; Q2I0M4; 1.
STRING; 9606.ENSP00000360597; -.
GlyConnect; 1452; -.
iPTMnet; Q2I0M4; -.
PhosphoSitePlus; Q2I0M4; -.
BioMuta; LRRC26; -.
DMDM; 160410009; -.
MaxQB; Q2I0M4; -.
PaxDb; Q2I0M4; -.
PeptideAtlas; Q2I0M4; -.
PRIDE; Q2I0M4; -.
ProteomicsDB; 61296; -.
ProteomicsDB; 61297; -. [Q2I0M4-2]
Ensembl; ENST00000371542; ENSP00000360597; ENSG00000184709. [Q2I0M4-1]
GeneID; 389816; -.
KEGG; hsa:389816; -.
UCSC; uc004clp.4; human. [Q2I0M4-1]
CTD; 389816; -.
DisGeNET; 389816; -.
EuPathDB; HostDB:ENSG00000184709.7; -.
GeneCards; LRRC26; -.
H-InvDB; HIX0035220; -.
HGNC; HGNC:31409; LRRC26.
HPA; HPA056312; -.
MIM; 613505; gene.
neXtProt; NX_Q2I0M4; -.
OpenTargets; ENSG00000184709; -.
PharmGKB; PA134952867; -.
eggNOG; KOG0619; Eukaryota.
eggNOG; COG4886; LUCA.
GeneTree; ENSGT00920000148971; -.
HOGENOM; HOG000113367; -.
HOVERGEN; HBG096585; -.
InParanoid; Q2I0M4; -.
OMA; DAAFSHC; -.
OrthoDB; EOG091G0G9Q; -.
PhylomeDB; Q2I0M4; -.
TreeFam; TF334689; -.
ChiTaRS; LRRC26; human.
GenomeRNAi; 389816; -.
PRO; PR:Q2I0M4; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000184709; Expressed in 46 organ(s), highest expression level in minor salivary gland.
CleanEx; HS_LRRC26; -.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:UniProtKB.
GO; GO:0044325; F:ion channel binding; IPI:UniProtKB.
GO; GO:0099104; F:potassium channel activator activity; IDA:UniProtKB.
GO; GO:0015459; F:potassium channel regulator activity; IDA:UniProtKB.
GO; GO:0005249; F:voltage-gated potassium channel activity; IDA:UniProtKB.
GO; GO:1903818; P:positive regulation of voltage-gated potassium channel activity; IDA:UniProtKB.
GO; GO:0071805; P:potassium ion transmembrane transport; IDA:UniProtKB.
Gene3D; 3.80.10.10; -; 1.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR032675; LRR_dom_sf.
Pfam; PF13855; LRR_8; 2.
SMART; SM00369; LRR_TYP; 5.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome; Cytoplasm;
Cytoskeleton; Direct protein sequencing; Disulfide bond; Glycoprotein;
Ion channel; Ion transport; Leucine-rich repeat; Membrane;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix; Transport.
SIGNAL 1 26
CHAIN 27 334 Leucine-rich repeat-containing protein
26.
/FTId=PRO_0000309360.
TOPO_DOM 27 261 Extracellular. {ECO:0000255}.
TRANSMEM 262 282 Helical. {ECO:0000255}.
TOPO_DOM 283 334 Cytoplasmic. {ECO:0000255}.
DOMAIN 34 71 LRRNT.
REPEAT 72 93 LRR 1.
REPEAT 96 117 LRR 2.
REPEAT 120 141 LRR 3.
REPEAT 144 167 LRR 4.
REPEAT 168 190 LRR 5.
DOMAIN 201 255 LRRCT.
CARBOHYD 147 147 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:22547800}.
DISULFID 43 49 {ECO:0000255}.
DISULFID 47 57 {ECO:0000255}.
DISULFID 205 231 {ECO:0000255}.
DISULFID 207 253 {ECO:0000255}.
VAR_SEQ 1 289 Missing (in isoform 2).
{ECO:0000303|PubMed:19250639}.
/FTId=VSP_040058.
VAR_SEQ 290 290 C -> M (in isoform 2).
{ECO:0000303|PubMed:19250639}.
/FTId=VSP_040205.
CONFLICT 27 27 Q -> H (in Ref. 1; ABC79623 and 3;
AAI40912). {ECO:0000305}.
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


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