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LRC14_MOUSE
ID   LRC14_MOUSE             Reviewed;         493 AA.
AC   Q8VC16; Q6A0E7; Q80WK3;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 146.
DE   RecName: Full=Leucine-rich repeat-containing protein 14 {ECO:0000250|UniProtKB:Q15048};
GN   Name=Lrrc14 {ECO:0000312|MGI:MGI:2445060};
GN   Synonyms=Kiaa0014 {ECO:0000303|PubMed:15368895};
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 [MRNA].
RC   STRAIN=C57BL/6J;
RA   Uwanogho D.A., Mellodew K., Molloy G., Galloway D., Starling B.B.,
RA   Crossland N., Price J.;
RT   "A novel program of gene expression driven by Notch, is associated with
RT   commitment in neural stem cell lines.";
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Spleen;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT   The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
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).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Brain, and Liver;
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   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [7]
RP   TISSUE SPECIFICITY.
RX   PubMed=27426725; DOI=10.1016/j.yexcr.2016.07.011;
RA   Wu C., Yang Y., Ou J., Zhu L., Zhao W., Cui J.;
RT   "LRRC14 attenuates Toll-like receptor-mediated NF-kappa-B signaling through
RT   disruption of IKK complex.";
RL   Exp. Cell Res. 347:65-73(2016).
CC   -!- FUNCTION: Negatively regulates Toll-like receptor-mediated NF-kappa-B
CC       signaling by disrupting IKK core complex formation through interaction
CC       with IKBKB. {ECO:0000250|UniProtKB:Q15048}.
CC   -!- SUBUNIT: Interacts with IKBKB; disrupts IKBKB-IKBKG interaction
CC       preventing I-kappa-B-kinase (IKK) core complex formation and leading to
CC       a decrease of IKBKB phosphorylation and NF-kappaB activation. Interacts
CC       with CHUK. {ECO:0000250|UniProtKB:Q15048}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q15048}.
CC   -!- SIMILARITY: Belongs to the PRAME family. LRRC14 subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32149.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR   EMBL; AY239226; AAP23937.1; -; mRNA.
DR   EMBL; AK172871; BAD32149.1; ALT_FRAME; Transcribed_RNA.
DR   EMBL; AK036278; BAC29370.1; -; mRNA.
DR   EMBL; AK159836; BAE35414.1; -; mRNA.
DR   EMBL; CH466545; EDL29611.1; -; Genomic_DNA.
DR   EMBL; CH466545; EDL29614.1; -; Genomic_DNA.
DR   EMBL; BC022126; AAH22126.1; -; mRNA.
DR   EMBL; BC138217; AAI38218.1; -; mRNA.
DR   CCDS; CCDS27589.1; -.
DR   RefSeq; NP_663446.1; NM_145471.2.
DR   RefSeq; XP_006520848.1; XM_006520785.3.
DR   RefSeq; XP_006520849.1; XM_006520786.3.
DR   RefSeq; XP_006520850.1; XM_006520787.2.
DR   RefSeq; XP_006520852.1; XM_006520789.3.
DR   RefSeq; XP_011243881.1; XM_011245579.2.
DR   RefSeq; XP_017172047.1; XM_017316558.1.
DR   RefSeq; XP_017172048.1; XM_017316559.1.
DR   AlphaFoldDB; Q8VC16; -.
DR   STRING; 10090.ENSMUSP00000121982; -.
DR   iPTMnet; Q8VC16; -.
DR   PhosphoSitePlus; Q8VC16; -.
DR   EPD; Q8VC16; -.
DR   MaxQB; Q8VC16; -.
DR   PaxDb; Q8VC16; -.
DR   PeptideAtlas; Q8VC16; -.
DR   PRIDE; Q8VC16; -.
DR   ProteomicsDB; 290149; -.
DR   Antibodypedia; 14965; 59 antibodies from 16 providers.
DR   DNASU; 223664; -.
DR   Ensembl; ENSMUST00000036423; ENSMUSP00000049466; ENSMUSG00000033728.
DR   Ensembl; ENSMUST00000127208; ENSMUSP00000114921; ENSMUSG00000033728.
DR   Ensembl; ENSMUST00000137649; ENSMUSP00000121982; ENSMUSG00000033728.
DR   Ensembl; ENSMUST00000155735; ENSMUSP00000115446; ENSMUSG00000033728.
DR   GeneID; 223664; -.
DR   KEGG; mmu:223664; -.
DR   UCSC; uc007wlx.2; mouse.
DR   CTD; 9684; -.
DR   MGI; MGI:2445060; Lrrc14.
DR   VEuPathDB; HostDB:ENSMUSG00000033728; -.
DR   eggNOG; ENOG502QWSJ; Eukaryota.
DR   GeneTree; ENSGT01030000234531; -.
DR   HOGENOM; CLU_039635_0_1_1; -.
DR   InParanoid; Q8VC16; -.
DR   OMA; VTECELM; -.
DR   OrthoDB; 563553at2759; -.
DR   PhylomeDB; Q8VC16; -.
DR   TreeFam; TF332708; -.
DR   BioGRID-ORCS; 223664; 0 hits in 71 CRISPR screens.
DR   ChiTaRS; Lrrc14; mouse.
DR   PRO; PR:Q8VC16; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   RNAct; Q8VC16; protein.
DR   Bgee; ENSMUSG00000033728; Expressed in embryonic brain and 252 other tissues.
DR   ExpressionAtlas; Q8VC16; baseline and differential.
DR   Genevisible; Q8VC16; MM.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0019900; F:kinase binding; ISO:MGI.
DR   GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR   GO; GO:0034122; P:negative regulation of toll-like receptor signaling pathway; ISS:UniProtKB.
DR   Gene3D; 3.80.10.10; -; 1.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR026292; LRRC14.
DR   PANTHER; PTHR14224:SF9; PTHR14224:SF9; 1.
DR   Pfam; PF13516; LRR_6; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Leucine-rich repeat; Reference proteome; Repeat.
FT   CHAIN           1..493
FT                   /note="Leucine-rich repeat-containing protein 14"
FT                   /id="PRO_0000343681"
FT   REPEAT          111..146
FT                   /note="LRR 1; degenerate"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UWY1"
FT   REPEAT          194..218
FT                   /note="LRR 2; degenerate"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UWY1"
FT   REPEAT          219..246
FT                   /note="LRR 3; degenerate"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UWY1"
FT   REPEAT          247..282
FT                   /note="LRR 4; degenerate"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UWY1"
FT   REPEAT          283..307
FT                   /note="LRR 5"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UWY1"
FT   REPEAT          308..339
FT                   /note="LRR 6"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UWY1"
FT   REPEAT          340..360
FT                   /note="LRR 7"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UWY1"
FT   REPEAT          364..391
FT                   /note="LRR 8"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UWY1"
FT   REPEAT          392..416
FT                   /note="LRR 9"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UWY1"
FT   CONFLICT        49..50
FT                   /note="EL -> DV (in Ref. 1; AAP23937)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        155
FT                   /note="T -> TA (in Ref. 1; AAP23937)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        160..161
FT                   /note="LS -> CP (in Ref. 1; AAP23937)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        255
FT                   /note="L -> V (in Ref. 1; AAP23937)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        327
FT                   /note="R -> C (in Ref. 2; BAD32149)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        363..364
FT                   /note="VA -> SS (in Ref. 1; AAP23937)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   493 AA;  54969 MW;  DD516098BA9DBE89 CRC64;
     MHTLVFLSTR QVLQCQPAAC QALPLLPREL FPLLFKVAFM DKKTLVLREL VHTWPFPLLS
     FQQLLQECAH CSRALLQERL STESMQAVIL GLTARIHTQE TEAGTQPLCR KHALRVLDMT
     GLLDDGVEQD PETMSMWDCT AAVARTCIAQ QQGGTAEPGL SPVPVEIRVD LRVNRASYTF
     LREALQSSVA SPLRLCCRDL RAEDLPMRNT VALLQLLDAG CLRRIDLRFN NLGLRGLSVI
     IPHVARFQHL ASLRLHYVHG DSRQPSVDGE DNFRYFLAQM GRFMCLRELS MGSSLLSGRL
     DQLLSTLQRP LESLELAFCA LLPEDLRFLA QSSHAAHLKK LDLSGNDLSG NQLTPFQGLL
     QAVATTLLHL ELTECQLADA QLLATLPTLT RCASLRYLGL YGNPLSMAGL KELLRDSVVQ
     AELRTVVHPF PVDCYEGLPW PPPASVLLEA SINEEKFARV EAELHQLLLA SGRAHVLWTT
     DIYGRLAADY FSL
 
 
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