RILP_MOUSE
ID RILP_MOUSE Reviewed; 369 AA.
AC Q5ND29; Q80WB8; Q8CHY9;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Rab-interacting lysosomal protein;
GN Name=Rilp;
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=Aorta, and Vein;
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] OF 164-369.
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Liver, 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 INTERACTION WITH MREG, AND IDENTIFICATION IN A COMPLEX WITH MREG AND RILP.
RX PubMed=22275436; DOI=10.1242/jcs.094185;
RA Ohbayashi N., Maruta Y., Ishida M., Fukuda M.;
RT "Melanoregulin regulates retrograde melanosome transport through
RT interaction with the RILP-p150Glued complex in melanocytes.";
RL J. Cell Sci. 125:1508-1518(2012).
CC -!- FUNCTION: Rab effector playing a role in late endocytic transport to
CC degradative compartments. Involved in the regulation of lysosomal
CC morphology and distribution. Induces recruitment of dynein-dynactin
CC motor complexes to Rab7A-containing late endosome and lysosome
CC compartments. Promotes centripetal migration of phagosomes and the
CC fusion of phagosomes with the late endosomes and lysosomes.
CC {ECO:0000250|UniProtKB:Q96NA2}.
CC -!- SUBUNIT: Homodimer. Interacts with RAB7A. Interacts with RAB34 (By
CC similarity). Identified in a complex with MREG and DCTN1; interacts
CC directly with MREG (PubMed:22275436). Interacts with CLN3 (By
CC similarity). Interacts with FLCN; the interaction is direct and
CC promotes association between RILP and RAB34 (By similarity).
CC {ECO:0000250|UniProtKB:Q96NA2, ECO:0000269|PubMed:22275436}.
CC -!- SUBCELLULAR LOCATION: Late endosome membrane
CC {ECO:0000250|UniProtKB:Q96NA2}. Lysosome membrane
CC {ECO:0000250|UniProtKB:Q96NA2}. Cytoplasmic vesicle, phagosome membrane
CC {ECO:0000250|UniProtKB:Q96NA2}. Note=Associated with late endosomal,
CC lysosomal and phagosomal membranes. The interaction with RAB7A is
CC necessary for its recruitment to phagosomes.
CC {ECO:0000250|UniProtKB:Q96NA2}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH51502.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK139016; BAE23863.1; -; mRNA.
DR EMBL; AL591496; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC038146; AAH38146.1; -; mRNA.
DR EMBL; BC051502; AAH51502.1; ALT_INIT; mRNA.
DR CCDS; CCDS25049.1; -.
DR RefSeq; NP_001025109.1; NM_001029938.2.
DR AlphaFoldDB; Q5ND29; -.
DR SMR; Q5ND29; -.
DR BioGRID; 235024; 1.
DR STRING; 10090.ENSMUSP00000037238; -.
DR iPTMnet; Q5ND29; -.
DR PhosphoSitePlus; Q5ND29; -.
DR EPD; Q5ND29; -.
DR MaxQB; Q5ND29; -.
DR PaxDb; Q5ND29; -.
DR PRIDE; Q5ND29; -.
DR ProteomicsDB; 255216; -.
DR Antibodypedia; 42527; 80 antibodies from 25 providers.
DR Ensembl; ENSMUST00000042972; ENSMUSP00000037238; ENSMUSG00000038195.
DR GeneID; 280408; -.
DR KEGG; mmu:280408; -.
DR UCSC; uc007kdz.1; mouse.
DR CTD; 83547; -.
DR MGI; MGI:2144271; Rilp.
DR VEuPathDB; HostDB:ENSMUSG00000038195; -.
DR eggNOG; ENOG502QVB3; Eukaryota.
DR GeneTree; ENSGT00940000161117; -.
DR HOGENOM; CLU_044133_1_0_1; -.
DR InParanoid; Q5ND29; -.
DR OMA; KAGQCSF; -.
DR OrthoDB; 890179at2759; -.
DR PhylomeDB; Q5ND29; -.
DR TreeFam; TF313489; -.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR BioGRID-ORCS; 280408; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Rilp; mouse.
DR PRO; PR:Q5ND29; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5ND29; protein.
DR Bgee; ENSMUSG00000038195; Expressed in interventricular septum and 122 other tissues.
DR ExpressionAtlas; Q5ND29; baseline and differential.
DR Genevisible; Q5ND29; MM.
DR GO; GO:0036064; C:ciliary basal body; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005770; C:late endosome; ISO:MGI.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0051959; F:dynein light intermediate chain binding; ISO:MGI.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0060271; P:cilium assembly; IBA:GO_Central.
DR GO; GO:0045022; P:early endosome to late endosome transport; ISO:MGI.
DR GO; GO:0008333; P:endosome to lysosome transport; ISO:MGI.
DR GO; GO:0032509; P:endosome transport via multivesicular body sorting pathway; ISO:MGI.
DR GO; GO:0070676; P:intralumenal vesicle formation; ISO:MGI.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; ISO:MGI.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; ISO:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0010796; P:regulation of multivesicular body size; ISO:MGI.
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 Coiled coil; Cytoplasmic vesicle; Endosome; Lysosome; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..369
FT /note="Rab-interacting lysosomal protein"
FT /id="PRO_0000097340"
FT DOMAIN 10..100
FT /note="RH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01112"
FT DOMAIN 219..295
FT /note="RH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01113"
FT REGION 173..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..312
FT /note="Necessary for interaction with RAB7A and RAB34 and
FT lysosomal distribution and morphology"
FT /evidence="ECO:0000250"
FT REGION 332..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 74..177
FT /evidence="ECO:0000255"
FT COMPBIAS 336..357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 287
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96NA2"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96NA2"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96NA2"
SQ SEQUENCE 369 AA; 41139 MW; E419D3E6A7D9094C CRC64;
MEPRRAAPRL PSQASSSVGA GSAAELVYHL AGALGTELQG LARRFGPDAA AGLVPLVVRA
LELLEKAAVG PAPDSLQVSA QQAEVELRRL REENQRLRQE LGSGPQEERA LLRQLKEVTD
RQRDELRAHN RDLQRRSQET EALQEQLQRL LLINSELRHK LAAVQTQLRA AQDRERERQI
AQDGSSQLAK EQSLEPDAAT SDDPVDTQKQ PGNLPEAVQC GFSREELKQI LQERNELKAN
VFLLKEELAY FQRELLTDHR VPGLLLEAMK VAVKKQRRKI KAKMLGTPEE AESSEDEDGS
WLLLSNDKED VPLVPESRIQ NFFGLWYRGE TEAPEAETSN PASSSLQKGE ETPQQPHLQP
VNSPPAPNS
