LRC59_BOVIN
ID LRC59_BOVIN Reviewed; 306 AA.
AC Q5E9X4; Q17QQ7;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hippocampus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BT020796; AAX08813.1; -; mRNA.
DR EMBL; BC118231; AAI18232.1; -; mRNA.
DR RefSeq; NP_001029750.1; NM_001034578.1.
DR AlphaFoldDB; Q5E9X4; -.
DR SMR; Q5E9X4; -.
DR IntAct; Q5E9X4; 1.
DR STRING; 9913.ENSBTAP00000007978; -.
DR PaxDb; Q5E9X4; -.
DR PeptideAtlas; Q5E9X4; -.
DR PRIDE; Q5E9X4; -.
DR Ensembl; ENSBTAT00000007978; ENSBTAP00000007978; ENSBTAG00000006072.
DR GeneID; 532659; -.
DR KEGG; bta:532659; -.
DR CTD; 55379; -.
DR VEuPathDB; HostDB:ENSBTAG00000006072; -.
DR VGNC; VGNC:55843; LRRC59.
DR eggNOG; KOG0473; Eukaryota.
DR GeneTree; ENSGT00390000017385; -.
DR HOGENOM; CLU_062247_1_0_1; -.
DR InParanoid; Q5E9X4; -.
DR OMA; PRKQARS; -.
DR OrthoDB; 1388480at2759; -.
DR TreeFam; TF316929; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000006072; Expressed in saliva-secreting gland and 108 other tissues.
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; IEA:Ensembl.
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 2: Evidence at transcript 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..306
FT /note="Leucine-rich repeat-containing protein 59"
FT /id="PRO_0000235158"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96AG4"
FT CHAIN 2..306
FT /note="Leucine-rich repeat-containing protein 59, N-
FT terminally processed"
FT /id="PRO_0000441738"
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..306
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 175..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 152..216
FT /evidence="ECO:0000255"
FT COMPBIAS 175..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 306 AA; 34879 MW; 86859BEE2D1312EE CRC64;
MTKAGSKGGN LRDKLDGNEL DLSLSDLNEV PVKELAALPK ATVLDLSCNK LTTLPSDFCG
LTHLVKLDLS KNKLRQLPAD FGRLVNLQHL DLLNNRLVTL PVSFAQLKSL KWLDLKDNPL
DPVLAKVAGD CLDEKQCKQC ANKVLQHMKA VQADQERERQ RRLEIDREAE KKWEAKQRAK
EAQERELRKR EKAEEKERRR KEYDALKAAK REQEKKPKKE TNQAPKSKSS SRPRKPPPRK
HTRSWAVLKL LLLLLLCVAG GLVACRVTEL QQQPLCTSVN TIYDNAVRGL RSHDILQWVL
QTDSQQ
