LRC59_RAT
ID LRC59_RAT Reviewed; 307 AA.
AC Q5RJR8; Q63742;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Leucine-rich repeat-containing protein 59;
DE AltName: Full=Protein p34;
DE Contains:
DE RecName: Full=Leucine-rich repeat-containing protein 59, N-terminally processed;
GN Name=Lrrc59; Synonyms=Rbp34;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TOPOLOGY.
RC TISSUE=Liver;
RX PubMed=7690545; DOI=10.1042/bj2940465;
RA Ohsumi T., Ichimura T., Sugano H., Omata S., Isobe T., Kuwano R.;
RT "Ribosome-binding protein p34 is a member of the leucine-rich-repeat-
RT protein superfamily.";
RL Biochem. J. 294:465-472(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
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).
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}.
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DR EMBL; D13623; BAA02786.1; -; mRNA.
DR EMBL; BC086530; AAH86530.1; -; mRNA.
DR RefSeq; NP_001008281.1; NM_001008280.1.
DR AlphaFoldDB; Q5RJR8; -.
DR SMR; Q5RJR8; -.
DR BioGRID; 252266; 1.
DR IntAct; Q5RJR8; 1.
DR STRING; 10116.ENSRNOP00000004941; -.
DR iPTMnet; Q5RJR8; -.
DR PhosphoSitePlus; Q5RJR8; -.
DR jPOST; Q5RJR8; -.
DR PaxDb; Q5RJR8; -.
DR PRIDE; Q5RJR8; -.
DR Ensembl; ENSRNOT00000004941; ENSRNOP00000004941; ENSRNOG00000003524.
DR GeneID; 287633; -.
DR KEGG; rno:287633; -.
DR UCSC; RGD:1305092; rat.
DR CTD; 55379; -.
DR RGD; 1305092; Lrrc59.
DR eggNOG; KOG0473; Eukaryota.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00390000017385; -.
DR HOGENOM; CLU_062247_1_0_1; -.
DR InParanoid; Q5RJR8; -.
DR OMA; PRKQARS; -.
DR OrthoDB; 1388480at2759; -.
DR PhylomeDB; Q5RJR8; -.
DR TreeFam; TF316929; -.
DR PRO; PR:Q5RJR8; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000003524; Expressed in jejunum and 19 other tissues.
DR Genevisible; Q5RJR8; RN.
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:RGD.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
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; 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_0000235161"
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_0000441741"
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..242
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:0000250|UniProtKB:Q96AG4"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96AG4"
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; 34869 MW; BCAD25C593C1FE89 CRC64;
MTKTGSKGGN LRDKLDGNEL DLSLSDLNEV PVKELAALPK ATVLDLSCNK LSTLPSDFCG
LTHLVKLDLS KNKLQQLPAD FGRLVNLQHL DLLNNRLVTL PVSFAQLKNL KWLDLKDNPL
DPVLAKVAGD CLDEKQCKQC ANKVLQHMKA VQADQERERQ RRLEVEREAE KKREAKQQAK
EAKERELRKR EKAEEKERRR KEYDAQKASK REQEKKPKKE TNQAPKSKSG SRPRKPPPRK
HNRSWAVLKG LLLLLLLCVA GGLVVCRVTG LQQQPLCTSV NAIYDNAVQG LRHHEILQWV
LQTDSQQ
