LRC59_HUMAN
ID LRC59_HUMAN Reviewed; 307 AA.
AC Q96AG4; B2RE83; D3DTX8; Q9P189;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Leucine-rich repeat-containing protein 59;
DE AltName: Full=Ribosome-binding protein p34;
DE Short=p34;
DE Contains:
DE RecName: Full=Leucine-rich repeat-containing protein 59, N-terminally processed;
GN Name=LRRC59; ORFNames=PRO1855;
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 [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Uterus;
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 PROTEIN SEQUENCE OF 72-83, HOMODIMERIZATION, INTERACTION WITH FGF1,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11964394; DOI=10.1074/jbc.m112193200;
RA Skjerpen C.S., Wesche J., Olsnes S.;
RT "Identification of ribosome-binding protein p34 as an intracellular protein
RT that binds acidic fibroblast growth factor.";
RL J. Biol. Chem. 277:23864-23871(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 89-307.
RC TISSUE=Mammary tumor;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 137-307.
RC TISSUE=Fetal liver;
RA Zhang C., Yu Y., Zhang S., Wei H., Zhang Y., Zhou G., Bi J., Liu M., He F.;
RT "Functional prediction of the coding sequences of 79 new genes deduced by
RT analysis of cDNA clones from human fetal liver.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INTERACTION WITH SGO1.
RX PubMed=16541025; DOI=10.1038/nature04663;
RA Kitajima T.S., Sakuno T., Ishiguro K., Iemura S., Natsume T.,
RA Kawashima S.A., Watanabe Y.;
RT "Shugoshin collaborates with protein phosphatase 2A to protect cohesin.";
RL Nature 441:46-52(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23 AND SER-25, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=22321063; DOI=10.1111/j.1600-0854.2012.01341.x;
RA Zhen Y., Sorensen V., Skjerpen C.S., Haugsten E.M., Jin Y., Walchli S.,
RA Olsnes S., Wiedlocha A.;
RT "Nuclear import of exogenous FGF1 requires the ER-protein LRRC59 and the
RT importins Kpnalpha1 and Kpnbeta1.";
RL Traffic 13:650-664(2012).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP ACETYLATION AT THR-2, AND CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=25489052; DOI=10.1093/hmg/ddu611;
RA Myklebust L.M., Van Damme P., Stoeve S.I., Doerfel M.J., Abboud A.,
RA Kalvik T.V., Grauffel C., Jonckheere V., Wu Y., Swensen J., Kaasa H.,
RA Liszczak G., Marmorstein R., Reuter N., Lyon G.J., Gevaert K., Arnesen T.;
RT "Biochemical and cellular analysis of Ogden syndrome reveals downstream Nt-
RT acetylation defects.";
RL Hum. Mol. Genet. 24:1956-1976(2015).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
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.
CC {ECO:0000269|PubMed:22321063}.
CC -!- SUBUNIT: Can form homodimers. Interacts with SGO1. Interacts with FGF1.
CC {ECO:0000269|PubMed:11964394, ECO:0000269|PubMed:16541025}.
CC -!- INTERACTION:
CC Q96AG4; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-358888, EBI-11522760;
CC Q96AG4; P29972: AQP1; NbExp=3; IntAct=EBI-358888, EBI-745213;
CC Q96AG4; Q96MX0: CMTM3; NbExp=3; IntAct=EBI-358888, EBI-7247651;
CC Q96AG4; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-358888, EBI-11522780;
CC Q96AG4; O95406: CNIH1; NbExp=3; IntAct=EBI-358888, EBI-12172273;
CC Q96AG4; Q15125: EBP; NbExp=3; IntAct=EBI-358888, EBI-3915253;
CC Q96AG4; P56851: EDDM3B; NbExp=3; IntAct=EBI-358888, EBI-10215665;
CC Q96AG4; Q9ULP0-2: NDRG4; NbExp=3; IntAct=EBI-358888, EBI-11978907;
CC Q96AG4; Q5VZY2: PLPP4; NbExp=3; IntAct=EBI-358888, EBI-10485931;
CC Q96AG4; Q6UX34: SNORC; NbExp=3; IntAct=EBI-358888, EBI-11957067;
CC Q96AG4; P55061: TMBIM6; NbExp=3; IntAct=EBI-358888, EBI-1045825;
CC Q96AG4; Q9H0R3: TMEM222; NbExp=3; IntAct=EBI-358888, EBI-347385;
CC Q96AG4; Q9H2L4: TMEM60; NbExp=3; IntAct=EBI-358888, EBI-2852148;
CC Q96AG4; Q5BJF2: TMEM97; NbExp=3; IntAct=EBI-358888, EBI-12111910;
CC Q96AG4; Q8N609: TRAM1L1; NbExp=3; IntAct=EBI-358888, EBI-11996766;
CC Q96AG4; Q5TGU0: TSPO2; NbExp=3; IntAct=EBI-358888, EBI-12195249;
CC -!- SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250}; Single-pass
CC type II membrane protein {ECO:0000250}. Endoplasmic reticulum membrane;
CC Single-pass type II membrane protein. Nucleus envelope.
CC Note=Localization in the nuclear envelope depends upon the nuclear
CC import machinery, including KPNB1.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11964394}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF69611.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG38180.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CH471109; EAW94615.1; -; Genomic_DNA.
DR EMBL; CH471109; EAW94616.1; -; Genomic_DNA.
DR EMBL; BC017168; AAH17168.1; -; mRNA.
DR EMBL; BC052279; AAH52279.1; -; mRNA.
DR EMBL; AK316593; BAG38180.1; ALT_INIT; mRNA.
DR EMBL; AF119857; AAF69611.1; ALT_INIT; mRNA.
DR CCDS; CCDS11566.1; -.
DR RefSeq; NP_060979.2; NM_018509.3.
DR AlphaFoldDB; Q96AG4; -.
DR SMR; Q96AG4; -.
DR BioGRID; 120649; 754.
DR IntAct; Q96AG4; 115.
DR MINT; Q96AG4; -.
DR STRING; 9606.ENSP00000225972; -.
DR ChEMBL; CHEMBL2216743; -.
DR TCDB; 1.A.25.3.7; the gap junction-forming innexin (innexin) family.
DR CarbonylDB; Q96AG4; -.
DR GlyGen; Q96AG4; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96AG4; -.
DR PhosphoSitePlus; Q96AG4; -.
DR SwissPalm; Q96AG4; -.
DR BioMuta; LRRC59; -.
DR DMDM; 74760704; -.
DR CPTAC; CPTAC-401; -.
DR CPTAC; CPTAC-402; -.
DR EPD; Q96AG4; -.
DR jPOST; Q96AG4; -.
DR MassIVE; Q96AG4; -.
DR MaxQB; Q96AG4; -.
DR PaxDb; Q96AG4; -.
DR PeptideAtlas; Q96AG4; -.
DR PRIDE; Q96AG4; -.
DR ProteomicsDB; 75962; -.
DR TopDownProteomics; Q96AG4; -.
DR Antibodypedia; 30529; 118 antibodies from 20 providers.
DR DNASU; 55379; -.
DR Ensembl; ENST00000225972.8; ENSP00000225972.7; ENSG00000108829.10.
DR GeneID; 55379; -.
DR KEGG; hsa:55379; -.
DR MANE-Select; ENST00000225972.8; ENSP00000225972.7; NM_018509.4; NP_060979.2.
DR UCSC; uc002iqt.4; human.
DR CTD; 55379; -.
DR DisGeNET; 55379; -.
DR GeneCards; LRRC59; -.
DR HGNC; HGNC:28817; LRRC59.
DR HPA; ENSG00000108829; Low tissue specificity.
DR MIM; 614854; gene.
DR neXtProt; NX_Q96AG4; -.
DR OpenTargets; ENSG00000108829; -.
DR PharmGKB; PA142671518; -.
DR VEuPathDB; HostDB:ENSG00000108829; -.
DR eggNOG; KOG0473; Eukaryota.
DR GeneTree; ENSGT00390000017385; -.
DR HOGENOM; CLU_062247_1_0_1; -.
DR InParanoid; Q96AG4; -.
DR OMA; PRKQARS; -.
DR OrthoDB; 1388480at2759; -.
DR PhylomeDB; Q96AG4; -.
DR TreeFam; TF316929; -.
DR PathwayCommons; Q96AG4; -.
DR SignaLink; Q96AG4; -.
DR BioGRID-ORCS; 55379; 24 hits in 1081 CRISPR screens.
DR ChiTaRS; LRRC59; human.
DR GenomeRNAi; 55379; -.
DR Pharos; Q96AG4; Tbio.
DR PRO; PR:Q96AG4; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q96AG4; protein.
DR Bgee; ENSG00000108829; Expressed in stromal cell of endometrium and 193 other tissues.
DR ExpressionAtlas; Q96AG4; baseline and differential.
DR Genevisible; Q96AG4; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
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:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0042645; C:mitochondrial nucleoid; IDA:BHF-UCL.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0046579; P:positive regulation of Ras protein signal transduction; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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; Direct protein sequencing; Endoplasmic reticulum;
KW Leucine-rich repeat; Membrane; Microsome; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..307
FT /note="Leucine-rich repeat-containing protein 59"
FT /id="PRO_0000235159"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000269|PubMed:25489052"
FT CHAIN 2..307
FT /note="Leucine-rich repeat-containing protein 59, N-
FT terminally processed"
FT /id="PRO_0000441739"
FT TOPO_DOM 1..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:0007744|PubMed:22814378,
FT ECO:0007744|PubMed:25944712"
FT MOD_RES 2
FT /note="N-acetylthreonine; in Leucine-rich repeat-containing
FT protein 59, N-terminally processed"
FT /evidence="ECO:0000269|PubMed:25489052"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 73
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q922Q8"
FT MOD_RES 135
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q922Q8"
SQ SEQUENCE 307 AA; 34930 MW; E39C33C72C60448D CRC64;
MTKAGSKGGN LRDKLDGNEL DLSLSDLNEV PVKELAALPK ATILDLSCNK LTTLPSDFCG
LTHLVKLDLS KNKLQQLPAD FGRLVNLQHL DLLNNKLVTL PVSFAQLKNL KWLDLKDNPL
DPVLAKVAGD CLDEKQCKQC ANKVLQHMKA VQADQERERQ RRLEVEREAE KKREAKQRAK
EAQERELRKR EKAEEKERRR KEYDALKAAK REQEKKPKKE ANQAPKSKSG SRPRKPPPRK
HTRSWAVLKL LLLLLLFGVA GGLVACRVTE LQQQPLCTSV NTIYDNAVQG LRRHEILQWV
LQTDSQQ
