RIPL1_MOUSE
ID RIPL1_MOUSE Reviewed; 406 AA.
AC Q9JJC6; Q80WV8;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=RILP-like protein 1;
DE AltName: Full=Rab-interacting lysosomal-like protein 1;
GN Name=Rilpl1; ORFNames=MNCb-2440;
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=Brain;
RA Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from mouse brain cDNA library made by
RT oligo-capping method.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, and Spleen;
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 [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23264467; DOI=10.1091/mbc.e12-08-0598;
RA Schaub J.R., Stearns T.;
RT "The Rilp-like proteins Rilpl1 and Rilpl2 regulate ciliary membrane
RT content.";
RL Mol. Biol. Cell 24:453-464(2013).
RN [5]
RP INTERACTION WITH RAB8A.
RX PubMed=29125462; DOI=10.7554/elife.31012;
RA Steger M., Diez F., Dhekne H.S., Lis P., Nirujogi R.S., Karayel O.,
RA Tonelli F., Martinez T.N., Lorentzen E., Pfeffer S.R., Alessi D.R.,
RA Mann M.;
RT "Systematic proteomic analysis of LRRK2-mediated Rab GTPase phosphorylation
RT establishes a connection to ciliogenesis.";
RL Elife 6:0-0(2017).
CC -!- FUNCTION: Neuroprotective protein, which acts by sequestring GAPDH in
CC the cytosol and prevent the apoptotic function of GAPDH in the nucleus
CC (By similarity). Competes with SIAH1 for binding GAPDH (By similarity).
CC Does not regulate lysosomal morphology and distribution (By
CC similarity). Plays a role in the regulation of cell shape and polarity
CC (PubMed:23264467). Plays a role in cellular protein transport,
CC including protein transport away from primary cilia (PubMed:23264467).
CC Binds to RAB10 following LRRK2-mediated RAB10 phosphorylation which
CC leads to inhibition of ciliogenesis (By similarity).
CC {ECO:0000250|UniProtKB:D3ZUQ0, ECO:0000250|UniProtKB:Q5EBL4,
CC ECO:0000269|PubMed:23264467}.
CC -!- SUBUNIT: Interacts (when S-nitrosylated) with GAPDH (By similarity).
CC Interacts with RAB8A; interaction is dependent on the phosphorylation
CC of 'Thr-72' of RAB8A (PubMed:29125462). Interacts with RAB10 and RAB12;
CC the interaction is dependent on the phosphorylation of 'Thr-73' of
CC RAB10, and 'Ser-105' of RAB12 (By similarity).
CC {ECO:0000250|UniProtKB:D3ZUQ0, ECO:0000250|UniProtKB:Q5EBL4,
CC ECO:0000269|PubMed:29125462}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q5EBL4}. Cell projection, cilium
CC {ECO:0000269|PubMed:23264467}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole {ECO:0000269|PubMed:23264467}.
CC -!- PTM: S-nitrosylation is required for the interaction with GAPDH.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RILPL family. {ECO:0000305}.
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DR EMBL; AB041584; BAA95067.1; -; mRNA.
DR EMBL; BC051945; AAH51945.1; -; mRNA.
DR EMBL; BC051946; AAH51946.2; -; mRNA.
DR EMBL; BC058384; AAH58384.1; -; mRNA.
DR CCDS; CCDS19678.1; -.
DR RefSeq; NP_067405.1; NM_021430.2.
DR AlphaFoldDB; Q9JJC6; -.
DR SMR; Q9JJC6; -.
DR BioGRID; 217678; 4.
DR IntAct; Q9JJC6; 3.
DR MINT; Q9JJC6; -.
DR STRING; 10090.ENSMUSP00000050014; -.
DR iPTMnet; Q9JJC6; -.
DR PhosphoSitePlus; Q9JJC6; -.
DR EPD; Q9JJC6; -.
DR MaxQB; Q9JJC6; -.
DR PaxDb; Q9JJC6; -.
DR PeptideAtlas; Q9JJC6; -.
DR PRIDE; Q9JJC6; -.
DR ProteomicsDB; 253313; -.
DR Antibodypedia; 31816; 106 antibodies from 25 providers.
DR DNASU; 75695; -.
DR Ensembl; ENSMUST00000062153; ENSMUSP00000050014; ENSMUSG00000029392.
DR GeneID; 75695; -.
DR KEGG; mmu:75695; -.
DR UCSC; uc008zpz.1; mouse.
DR CTD; 353116; -.
DR MGI; MGI:1922945; Rilpl1.
DR VEuPathDB; HostDB:ENSMUSG00000029392; -.
DR eggNOG; ENOG502QR9G; Eukaryota.
DR GeneTree; ENSGT00940000157897; -.
DR HOGENOM; CLU_044133_3_0_1; -.
DR InParanoid; Q9JJC6; -.
DR OMA; NHELHGA; -.
DR OrthoDB; 890179at2759; -.
DR PhylomeDB; Q9JJC6; -.
DR TreeFam; TF313489; -.
DR BioGRID-ORCS; 75695; 4 hits in 71 CRISPR screens.
DR PRO; PR:Q9JJC6; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9JJC6; protein.
DR Bgee; ENSMUSG00000029392; Expressed in interventricular septum and 249 other tissues.
DR ExpressionAtlas; Q9JJC6; baseline and differential.
DR Genevisible; Q9JJC6; MM.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; IBA:GO_Central.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0060271; P:cilium assembly; IBA:GO_Central.
DR GO; GO:0003382; P:epithelial cell morphogenesis; IMP:UniProtKB.
DR GO; GO:1903445; P:protein transport from ciliary membrane to plasma membrane; IMP:UniProtKB.
DR GO; GO:1901214; P:regulation of neuron death; IMP:UniProtKB.
DR InterPro; IPR019143; JNK/Rab-associated_protein-1_N.
DR InterPro; IPR034743; RH1.
DR InterPro; IPR034744; RH2.
DR InterPro; IPR021563; RILP_dimer.
DR Pfam; PF09744; Jnk-SapK_ap_N; 1.
DR Pfam; PF11461; RILP; 1.
DR PROSITE; PS51776; RH1; 1.
DR PROSITE; PS51777; RH2; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cilium; Coiled coil; Cytoplasm; Cytoskeleton;
KW Phosphoprotein; Protein transport; Reference proteome; S-nitrosylation;
KW Transport.
FT CHAIN 1..406
FT /note="RILP-like protein 1"
FT /id="PRO_0000299311"
FT DOMAIN 10..97
FT /note="RH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01112"
FT DOMAIN 294..359
FT /note="RH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01113"
FT REGION 255..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 76..258
FT /evidence="ECO:0000255"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3ZUQ0"
FT MOD_RES 47
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:D3ZUQ0"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 406 AA; 47323 MW; F866CA2025C71E87 CRC64;
MEEPLGSPPA ALSALEKNVA ELTVMDVYDI ASLVGHEFER VIDQHGCESI ARLMPKVVRV
LEILEVLVSR HHVAPELDEL RLELDRLRVE RMDRIEKERK HQKELELVED VWRGEAQDLL
SQIAQLQEEN KQLMTNLNHK DVGFSEEEFQ KQEGMSERER QVMKRLKEVV DKQRDELRAK
DRELGLKNED VEALQQQQTR LMKINHDLRH RVTVVEAQGK ALIEQKVELE ADLQTKEQEM
GSLRAELGKL RERLQGEHSQ NGEEEEAEIQ PQPDGEESIS DAEKAALDLK DPNRPRFTLQ
ELRDVLHERN ELKSKVFLLQ EELAYYKSEE IEEENRIPQP PPITHPRTSP QPESGIKRLF
SFFSRDKKRL ANTQRPTHIH ESFGQWAITQ RDDGYTEQGQ EALQHL
