LRC59_MOUSE
ID LRC59_MOUSE Reviewed; 307 AA.
AC Q922Q8; Q3TJ35; Q3TLC7; Q3TWT9; Q3TX86;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Leucine-rich repeat-containing protein 59;
DE Contains:
DE RecName: Full=Leucine-rich repeat-containing protein 59, N-terminally processed;
GN Name=Lrrc59;
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 MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye, and Heart;
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Embryo, and Mammary tumor;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and 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 [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-135, SUCCINYLATION [LARGE SCALE
RP ANALYSIS] AT LYS-73, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Required for nuclear import of FGF1, but not that of FGF2.
CC Might regulate nuclear import of exogenous FGF1 by facilitating
CC interaction with the nuclear import machinery and by transporting
CC cytosolic FGF1 to, and possibly through, the nuclear pores (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Can form homodimers. Interacts with SGO1. Interacts with FGF1.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250}; Single-pass
CC type II membrane protein {ECO:0000250}. Endoplasmic reticulum membrane
CC {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
CC Nucleus envelope {ECO:0000250}. Note=Localization in the nuclear
CC envelope depends upon the nuclear import machinery, including KPNB1.
CC {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH06877.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE35030.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE38865.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE39660.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK053450; BAC35390.1; -; mRNA.
DR EMBL; AK159374; BAE35030.1; ALT_INIT; mRNA.
DR EMBL; AK159552; BAE35177.1; -; mRNA.
DR EMBL; AK166576; BAE38865.1; ALT_INIT; mRNA.
DR EMBL; AK167604; BAE39660.1; ALT_INIT; mRNA.
DR EMBL; AK169390; BAE41137.1; -; mRNA.
DR EMBL; AL645764; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006877; AAH06877.1; ALT_INIT; mRNA.
DR EMBL; BC066172; AAH66172.1; -; mRNA.
DR CCDS; CCDS25261.1; -.
DR RefSeq; NP_598568.1; NM_133807.1.
DR AlphaFoldDB; Q922Q8; -.
DR SMR; Q922Q8; -.
DR BioGRID; 221020; 32.
DR IntAct; Q922Q8; 4.
DR STRING; 10090.ENSMUSP00000021239; -.
DR iPTMnet; Q922Q8; -.
DR PhosphoSitePlus; Q922Q8; -.
DR SwissPalm; Q922Q8; -.
DR EPD; Q922Q8; -.
DR jPOST; Q922Q8; -.
DR MaxQB; Q922Q8; -.
DR PaxDb; Q922Q8; -.
DR PeptideAtlas; Q922Q8; -.
DR PRIDE; Q922Q8; -.
DR ProteomicsDB; 292357; -.
DR Antibodypedia; 30529; 118 antibodies from 20 providers.
DR DNASU; 98238; -.
DR Ensembl; ENSMUST00000021239; ENSMUSP00000021239; ENSMUSG00000020869.
DR GeneID; 98238; -.
DR KEGG; mmu:98238; -.
DR UCSC; uc007kze.1; mouse.
DR CTD; 55379; -.
DR MGI; MGI:2138133; Lrrc59.
DR VEuPathDB; HostDB:ENSMUSG00000020869; -.
DR eggNOG; KOG0473; Eukaryota.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00390000017385; -.
DR HOGENOM; CLU_062247_1_0_1; -.
DR InParanoid; Q922Q8; -.
DR OMA; PRKQARS; -.
DR OrthoDB; 1388480at2759; -.
DR PhylomeDB; Q922Q8; -.
DR TreeFam; TF316929; -.
DR BioGRID-ORCS; 98238; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Lrrc59; mouse.
DR PRO; PR:Q922Q8; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q922Q8; protein.
DR Bgee; ENSMUSG00000020869; Expressed in lacrimal gland and 264 other tissues.
DR Genevisible; Q922Q8; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042645; C:mitochondrial nucleoid; ISO:MGI.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
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; 1.
DR SMART; SM00369; LRR_TYP; 4.
DR PROSITE; PS51450; LRR; 4.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Endoplasmic reticulum; Leucine-rich repeat;
KW Membrane; Microsome; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..307
FT /note="Leucine-rich repeat-containing protein 59"
FT /id="PRO_0000235160"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96AG4"
FT CHAIN 2..307
FT /note="Leucine-rich repeat-containing protein 59, N-
FT terminally processed"
FT /id="PRO_0000441740"
FT TOPO_DOM 2..244
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 266..307
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REPEAT 10..31
FT /note="LRR 1"
FT REPEAT 40..62
FT /note="LRR 2"
FT REPEAT 63..84
FT /note="LRR 3"
FT REPEAT 86..107
FT /note="LRR 4"
FT REPEAT 109..128
FT /note="LRR 5"
FT REGION 150..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 148..216
FT /evidence="ECO:0000255"
FT COMPBIAS 150..225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q96AG4"
FT MOD_RES 2
FT /note="N-acetylthreonine; in Leucine-rich repeat-containing
FT protein 59, N-terminally processed"
FT /evidence="ECO:0000250|UniProtKB:Q96AG4"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96AG4"
FT MOD_RES 73
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 135
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CONFLICT 189
FT /note="K -> E (in Ref. 1; BAE38865)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 307 AA; 34877 MW; 549CD3B145413A32 CRC64;
MTKAGSKGGN LRDKLDGNEL DLSLSDLNEV PVKELAALPK ATVLDLSCNK LSTLPSDFCG
LTHLVKLDLS KNKLQQLPAD FGRLVNLQHL DLLNNRLVTL PVSFAQLKNL KWLDLKDNPL
DPVLAKVAGD CLDEKQCKQC ANKVLQHMKA VQADQERERQ RRLEVEREAE KKREAKQQAK
EAKERELRKR EKAEEKERRR KEYDAQKASK REQEKKPKKE ANQAPKSKSG SRPRKPPPRK
HTRSWAVLKV LLLLLLLCVA GGLVVCRVTG LHQQPLCTSV NTIYDNAVQG LRHHEILQWV
LQTDSQQ
