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LRC38_MOUSE
ID   LRC38_MOUSE             Reviewed;         298 AA.
AC   A2VDH3; A2A8J4; Q3TVH8; Q8BR15;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 2.
DT   03-AUG-2022, entry version 112.
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   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 11-298.
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
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 type I
CC       membrane protein {ECO:0000250}.
CC   -!- DOMAIN: The transmembrane domain is necessary for interaction with
CC       KCNMA1. {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI29964.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AL611982; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC129963; AAI29964.1; ALT_INIT; mRNA.
DR   EMBL; AK045936; BAC32537.1; -; mRNA.
DR   EMBL; AK160116; BAE35640.1; -; mRNA.
DR   CCDS; CCDS51351.1; -.
DR   RefSeq; NP_001156455.1; NM_001162983.1.
DR   AlphaFoldDB; A2VDH3; -.
DR   SMR; A2VDH3; -.
DR   STRING; 10090.ENSMUSP00000053597; -.
DR   GlyGen; A2VDH3; 1 site.
DR   PaxDb; A2VDH3; -.
DR   PRIDE; A2VDH3; -.
DR   ProteomicsDB; 290152; -.
DR   Antibodypedia; 48140; 73 antibodies from 14 providers.
DR   Ensembl; ENSMUST00000052458; ENSMUSP00000053597; ENSMUSG00000028584.
DR   GeneID; 242735; -.
DR   KEGG; mmu:242735; -.
DR   UCSC; uc008vqb.2; mouse.
DR   CTD; 126755; -.
DR   MGI; MGI:2442845; Lrrc38.
DR   VEuPathDB; HostDB:ENSMUSG00000028584; -.
DR   eggNOG; KOG0619; Eukaryota.
DR   GeneTree; ENSGT00940000162571; -.
DR   HOGENOM; CLU_000288_18_10_1; -.
DR   InParanoid; A2VDH3; -.
DR   OMA; CAPSKDD; -.
DR   OrthoDB; 826997at2759; -.
DR   PhylomeDB; A2VDH3; -.
DR   TreeFam; TF334689; -.
DR   BioGRID-ORCS; 242735; 1 hit in 71 CRISPR screens.
DR   PRO; PR:A2VDH3; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; A2VDH3; protein.
DR   Bgee; ENSMUSG00000028584; Expressed in quadriceps femoris and 22 other tissues.
DR   Genevisible; A2VDH3; MM.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; ISO:MGI.
DR   GO; GO:0099104; F:potassium channel activator activity; ISO:MGI.
DR   GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
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; ISO:MGI.
DR   GO; GO:0071805; P:potassium ion transmembrane transport; ISO:MGI.
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; 4.
DR   SMART; SM00082; LRRCT; 1.
DR   SMART; SM00013; LRRNT; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW   Leucine-rich repeat; Membrane; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..298
FT                   /note="Leucine-rich repeat-containing protein 38"
FT                   /id="PRO_0000312419"
FT   TOPO_DOM        32..251
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        252..272
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        273..298
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          32..60
FT                   /note="LRRNT"
FT   REPEAT          61..82
FT                   /note="LRR 1"
FT   REPEAT          85..106
FT                   /note="LRR 2"
FT   REPEAT          109..130
FT                   /note="LRR 3"
FT   REPEAT          133..154
FT                   /note="LRR 4"
FT   REPEAT          157..177
FT                   /note="LRR 5"
FT   DOMAIN          190..245
FT                   /note="LRRCT"
FT   CARBOHYD        119
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        32..38
FT                   /evidence="ECO:0000255"
FT   DISULFID        36..46
FT                   /evidence="ECO:0000255"
FT   DISULFID        194..221
FT                   /evidence="ECO:0000255"
FT   DISULFID        196..243
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   298 AA;  32343 MW;  7B278DB70683569E CRC64;
     MSLCVAPRHP TGAAAALGLG SLLVLLGPGR ACPAGCACTD PHTVDCRDRG LPSVPDPFPL
     DVRKLLVAGN RIQQIPEDFF IFHGDLVYLD FRNNSLRSLE EGTFSGSGKL AFLDLSYNNL
     TQLGAGAFRS AGRLVKLSLA NNHLAGVHEA AFESLESLQV LELNDNNLRS LNVAALDALP
     ALRTVRLDGN PWLCDCDFAH LFSWIQENTS KLPKGLDAIQ CSLPMEDRRV ALRELSEASF
     SECKFSLSLT DLFIIIFSGV AVSIAAIISS FFLATVVQCF QRCAPNKDTE DEDDDEDD
 
 
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