RBCC

Full text data of RILP

RILP [Confidence: low (only semi-automatic identification from reviews)]
Rab-interacting lysosomal protein

UniProt Q96NA2
ID RILP_HUMAN Reviewed; 401 AA.
AC Q96NA2; B2RBQ8; Q71RE6; Q9BSL3; Q9BYS3;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-DEC-2001, sequence version 1.
DT 22-JAN-2014, entry version 101.
DE RecName: Full=Rab-interacting lysosomal protein;
GN Name=RILP; ORFNames=PP10141;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN LATE ENDOCYTOSIS,
RP INTERACTION WITH RAB7A, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Cervix carcinoma;
RX PubMed=11179213; DOI=10.1093/emboj/20.4.683;
RA Cantalupo G., Alifano P., Roberti V., Bruni C.B., Bucci C.;
RT "Rab-interacting lysosomal protein (RILP): the Rab7 effector required
RT for transport to lysosomes.";
RL EMBO J. 20:683-693(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP THR-81.
RC TISSUE=Kidney, and Thalamus;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H.,
RA Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y.,
RA Shu H., Chen X., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S.,
RA Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skeletal muscle;
RA Frigimelica E., Lanfranchi G.;
RT "Study of 100 skeletal muscle full length mRNA (Telethon project
RT B41).";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, Lung, Testis, 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=11520070; DOI=10.1006/bbrc.2001.5466;
RA Bucci C., De Gregorio L., Bruni C.B.;
RT "Expression analysis and chromosomal assignment of PRA1 and RILP
RT genes.";
RL Biochem. Biophys. Res. Commun. 286:815-819(2001).
RN [7]
RP FUNCTION IN DYNEIN-DYNACTIN COMPLEX RECRUITMENT.
RX PubMed=11696325; DOI=10.1016/S0960-9822(01)00531-0;
RA Jordens I., Fernandez-Borja M., Marsman M., Dusseljee S., Janssen L.,
RA Calafat J., Janssen H., Wubbolts R., Neefjes J.;
RT "The Rab7 effector protein RILP controls lysosomal transport by
RT inducing the recruitment of dynein-dynactin motors.";
RL Curr. Biol. 11:1680-1685(2001).
RN [8]
RP INTERACTION WITH RAB34.
RX PubMed=12475955; DOI=10.1091/mbc.E02-05-0280;
RA Wang T., Hong W.;
RT "Interorganellar regulation of lysosome positioning by the Golgi
RT apparatus through Rab34 interaction with Rab-interacting lysosomal
RT protein.";
RL Mol. Biol. Cell 13:4317-4332(2002).
RN [9]
RP FUNCTION IN PHAGOSOME MIGRATION AND PHAGOLYSOSOMAL FUSION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=12944476; DOI=10.1128/MCB.23.18.6494-6506.2003;
RA Harrison R.E., Bucci C., Vieira O.V., Schroer T.A., Grinstein S.;
RT "Phagosomes fuse with late endosomes and/or lysosomes by extension of
RT membrane protrusions along microtubules: role of Rab7 and RILP.";
RL Mol. Cell. Biol. 23:6494-6506(2003).
RN [10]
RP FUNCTION IN LYSOSOMAL MORPHOLOGY AND DISTRIBUTION, INTERACTION WITH
RP RAB7A AND RAB34, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=14668488; DOI=10.1091/mbc.E03-06-0413;
RA Wang T., Wong K.K., Hong W.;
RT "A unique region of RILP distinguishes it from its related proteins in
RT its regulation of lysosomal morphology and interaction with Rab7 and
RT Rab34.";
RL Mol. Biol. Cell 15:815-826(2004).
RN [11]
RP SUBUNIT.
RX PubMed=15996637; DOI=10.1016/j.bbrc.2005.06.067;
RA Colucci A.M.R., Campana M.C., Bellopede M., Bucci C.;
RT "The Rab-interacting lysosomal protein, a Rab7 and Rab34 effector, is
RT capable of self-interaction.";
RL Biochem. Biophys. Res. Commun. 334:128-133(2005).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314 AND SER-315, AND
RP MASS SPECTROMETRY.
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 [13]
RP INTERACTION WITH CLN3.
RX PubMed=22261744; DOI=10.1007/s00018-011-0913-1;
RA Uusi-Rauva K., Kyttala A., van der Kant R., Vesa J., Tanhuanpaa K.,
RA Neefjes J., Olkkonen V.M., Jalanko A.;
RT "Neuronal ceroid lipofuscinosis protein CLN3 interacts with motor
RT proteins and modifies location of late endosomal compartments.";
RL Cell. Mol. Life Sci. 69:2075-2089(2012).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 244-308 IN COMPLEX WITH
RP RAB7A, SUBUNIT, AND MUTAGENESIS OF PHE-248; ILE-251; LEU-252; ARG-255;
RP LEU-258; LYS-304; MET-305 AND LEU-306.
RX PubMed=15933719; DOI=10.1038/sj.emboj.7600643;
RA Wu M., Wang T., Loh E., Hong W., Song H.;
RT "Structural basis for recruitment of RILP by small GTPase Rab7.";
RL EMBO J. 24:1491-1501(2005).
CC -!- FUNCTION: Rab effector playing a role in late endocytic transport
CC to degradative compartments. Involved in the regulation of
CC lysosomal morphology and distribution. Induces recruitment of
CC dynein-dynactin motor complexes to Rab7A-containing late endosome
CC and lysosome compartments. Promotes centripetal migration of
CC phagosomes and the fusion of phagosomes with the late endosomes
CC and lysosomes.
CC -!- SUBUNIT: Homodimer. Each subunit can interact with either RAB7A or
CC RAB34. Interacts with CLN3.
CC -!- SUBCELLULAR LOCATION: Endomembrane system. Late endosome membrane.
CC Lysosome membrane. Cytoplasmic vesicle, phagosome membrane.
CC Note=Associated with late endosomal, lysosomal and phagosomal
CC membranes. The interaction with RAB7A is necessary for its
CC recruitment to phagosomes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96NA2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96NA2-2; Sequence=VSP_016043, VSP_016044;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Strongly expressed in fetal heart,
CC heart, stomach, spleen, adrenal gland, thyroid gland, salivary
CC gland, fetal liver, liver and lung. Poorly expressed in brain.
CC -!- SIMILARITY: Contains 1 RILP-like domain.
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DR EMBL; AJ404317; CAC33443.1; -; mRNA.
DR EMBL; AK055755; BAB71003.1; -; mRNA.
DR EMBL; AK314767; BAG37305.1; -; mRNA.
DR EMBL; AF370391; AAQ15227.1; -; mRNA.
DR EMBL; AJ278711; CAC82174.1; -; mRNA.
DR EMBL; BC004961; AAH04961.1; -; mRNA.
DR EMBL; BC031621; AAH31621.1; -; mRNA.
DR RefSeq; NP_113618.2; NM_031430.2.
DR UniGene; Hs.534497; -.
DR PDB; 1YHN; X-ray; 3.00 A; B=244-308.
DR PDBsum; 1YHN; -.
DR ProteinModelPortal; Q96NA2; -.
DR SMR; Q96NA2; 244-308.
DR IntAct; Q96NA2; 3.
DR STRING; 9606.ENSP00000301336; -.
DR PhosphoSite; Q96NA2; -.
DR DMDM; 74732524; -.
DR PaxDb; Q96NA2; -.
DR PRIDE; Q96NA2; -.
DR DNASU; 83547; -.
DR Ensembl; ENST00000301336; ENSP00000301336; ENSG00000167705.
DR GeneID; 83547; -.
DR KEGG; hsa:83547; -.
DR UCSC; uc002ftd.3; human.
DR CTD; 83547; -.
DR GeneCards; GC17M001549; -.
DR HGNC; HGNC:30266; RILP.
DR HPA; HPA052041; -.
DR MIM; 607848; gene.
DR neXtProt; NX_Q96NA2; -.
DR PharmGKB; PA134915969; -.
DR eggNOG; NOG28812; -.
DR HOGENOM; HOG000007529; -.
DR HOVERGEN; HBG082629; -.
DR InParanoid; Q96NA2; -.
DR KO; K13883; -.
DR OMA; FEQILQE; -.
DR PhylomeDB; Q96NA2; -.
DR Reactome; REACT_6900; Immune System.
DR EvolutionaryTrace; Q96NA2; -.
DR GeneWiki; RILP_(gene); -.
DR GenomeRNAi; 83547; -.
DR NextBio; 72481; -.
DR PRO; PR:Q96NA2; -.
DR ArrayExpress; Q96NA2; -.
DR Bgee; Q96NA2; -.
DR CleanEx; HS_RILP; -.
DR Genevestigator; Q96NA2; -.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0005770; C:late endosome; NAS:UniProtKB.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005765; C:lysosomal membrane; NAS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0017137; F:Rab GTPase binding; TAS:UniProtKB.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
DR GO; GO:0008333; P:endosome to lysosome transport; IMP:BHF-UCL.
DR GO; GO:0015031; P:protein transport; NAS:UniProtKB.
DR InterPro; IPR019143; JNK/Rab-associated_protein-1_N.
DR InterPro; IPR021563; RILP.
DR Pfam; PF09744; Jnk-SapK_ap_N; 1.
DR Pfam; PF11461; RILP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Complete proteome;
KW Cytoplasmic vesicle; Endosome; Lysosome; Membrane; Phosphoprotein;
KW Polymorphism; Protein transport; Reference proteome; Transport.
FT CHAIN 1 401 Rab-interacting lysosomal protein.
FT /FTId=PRO_0000097339.
FT DOMAIN 236 270 RILP-like.
FT REGION 272 333 Necessary for the interaction with RAB7A
FT and RAB34, lysosomal distribution and
FT morphology.
FT COILED 75 181 Potential.
FT MOD_RES 314 314 Phosphoserine.
FT MOD_RES 315 315 Phosphoserine.
FT VAR_SEQ 1 210 Missing (in isoform 2).
FT /FTId=VSP_016043.
FT VAR_SEQ 211 213 WAT -> MGA (in isoform 2).
FT /FTId=VSP_016044.
FT VARIANT 81 81 A -> T (in dbSNP:rs9909321).
FT /FTId=VAR_051321.
FT VARIANT 281 281 R -> Q (in dbSNP:rs34982553).
FT /FTId=VAR_034417.
FT MUTAGEN 248 248 F->A: Strongly reduces dimerization and
FT localization to late endosomal/lysosomal
FT compartments.
FT MUTAGEN 251 251 I->A: Abolishes dimerization, interaction
FT with RAB7A and localization to late
FT endosomal/lysosomal compartments.
FT MUTAGEN 252 252 L->A: Abolishes interaction with RAB7A
FT and localization to late
FT endosomal/lysosomal compartments.
FT MUTAGEN 255 255 R->A: Abolishes dimerization, interaction
FT with RAB7A and localization to late
FT endosomal/lysosomal compartments.
FT MUTAGEN 258 258 L->A: Reduces dimerization, interaction
FT with RAB7A and localization to late
FT endosomal/lysosomal compartments.
FT MUTAGEN 304 304 K->A: Abolishes interaction with RAB7A
FT and localization to late
FT endosomal/lysosomal compartments.
FT MUTAGEN 305 305 M->A: Abolishes interaction with RAB7A
FT and localization to late
FT endosomal/lysosomal compartments.
FT MUTAGEN 306 306 L->A: Abolishes interaction with RAB7A
FT and localization to late
FT endosomal/lysosomal compartments.
FT CONFLICT 284 284 G -> S (in Ref. 1; CAC33443).
FT HELIX 248 276
FT HELIX 284 306
SQ SEQUENCE 401 AA; 44200 MW; 1057A1DAC2FFED94 CRC64;
MEPRRAAPGV PGWGSREAAG SASAAELVYH LAGALGTELQ DLARRFGPEA AAGLVPLVVR
ALELLEQAAV GPAPDSLQVS AQPAEQELRR LREENERLRR ELRAGPQEER ALLRQLKEVT
DRQRDELRAH NRDLRQRGQE TEALQEQLQR LLLVNAELRH KLAAMQTQLR AAQDRERERQ
QPGEAATPQA KERARGQAGR PGHQHGQEPE WATAGAGAPG NPEDPAEAAQ QLGRPSEAGQ
CRFSREEFEQ ILQERNELKA KVFLLKEELA YFQRELLTDH RVPGLLLEAM KVAVRKQRKK
IKAKMLGTPE EAESSEDEAG PWILLSDDKG DHPPPPESKI QSFFGLWYRG KAESSEDETS
SPAPSKLGGE EEAQPQSPAP DPPCSALHEH LCLGASAAPE A
//

MIM 607848
*RECORD*
*FIELD* NO
607848
*FIELD* TI
*607848 RAB-INTERACTING LYSOSOMAL PROTEIN
;;RILP
*FIELD* TX

DESCRIPTION

RILP, along with the GTPase RAB7 (602298), controls late endocytic
read moretransport (Cantalupo et al., 2001).

CLONING

Using Rab7 as bait in a yeast 2-hybrid screen, followed by screening a
HeLa cell cDNA library, Cantalupo et al. (2001) cloned a full-length
RILP cDNA. The deduced 401-amino acid protein has a calculated molecular
mass of about 45 kD and contains 2 coiled-coil regions. RILP shares
significant homology with a mouse protein belonging to the ezrin
(123900)-radixin (179410)-moesin (309845) (ERM) family. Northern blot
analysis detected transcripts of about 1.2 and 1.8 kb in the 3 tissues
tested (lung, spleen, and stomach). Western blot analysis detected a
50-kD RILP protein in all cell lines examined. Immunolocalization
colocalized RILP with several late endosomal/lysosomal marker proteins.

By RNA dot blot analysis, Bucci et al. (2001) determined that RILP is
expressed at varying levels in all tissues examined. Expression was
highest in adult heart, stomach, adrenal gland, thyroid gland, salivary
gland, liver, and lung, and in fetal heart and liver. Expression was
lowest in whole fetal brain and in all adult brain regions. Northern
blot analysis confirmed ubiquitous expression of 0.9- and 1.8-kb
transcripts. Expression levels of the 2 transcripts varied between
tissues.

Using PCR, Wang et al. (2004) detected variable RILP expression in all 8
human tissues examined. Database analysis detected orthologs of RILP and
RILP-like proteins (RLPs; see 614092) in several multicellular
organisms, but not in unicellular organisms. Similarity among the RILP
and RLP orthologs was highest in 2 domains that Wang et al. (2004)
called RILP homology domain-1 (RH1) and RH2.

GENE FUNCTION

Cantalupo et al. (2001) determined that the C-terminal half of RILP
interacted with RAB7. It also interacted with a constitutively active
GTP-bound RAB7 mutant, but it did not bind an inactive GDP-bound RAB7
mutant or several other RAB proteins. Overexpression of RILP resulted in
perinuclear clustering of the late endosomal/lysosomal compartment,
which could be reversed by microtubule depolymerization. The perinuclear
clustering was similar to that observed in cells expressing wildtype or
constitutively active RAB7. Overexpression of the C-terminal half of
RILP resulted in lysosome dispersal and inhibition of lysosomal
substrate degradation, similar to that observed in cells expressing the
inactive GDP-bound RAB7 mutant. Overexpression of RILP was able to
prevent or reverse the effects of the inactive RAB7 mutant, leading
Cantalupo et al. (2001) to hypothesize that RILP lies downstream of RAB7
in the regulation of late endocytic traffic.

Wang et al. (2004) found that overexpression of human RILP in normal rat
kidney cells caused enlargement and relocalization of lysosomes.
Experiments with chimeric proteins made up of sequences from RILP and
RLP1 (RILPL1; 614092) revealed a 62-amino acid domain in RILP that was
necessary to regulate lysosome morphology. The ability to regulate
lysosomes correlated with the ability of the chimeric protein to
interact with GTP-bound RAB7 or both GTP-bound RAB7 and RAB34 (610917)
simultaneously, but not GTP-bound RAB34 alone.

MAPPING

By radiation hybrid analysis, Bucci et al. (2001) mapped the RILP gene
to chromosome 17p13.3. Cantalupo et al. (2001) mapped the mouse Rilp
gene to chromosome 11.

*FIELD* RF
1. Bucci, C.; De Gregorio, L.; Bruni, C. B.: Expression analysis
and chromosomal assignment of PRA1 and RILP genes. Biochem. Biophys.
Res. Commun. 286: 815-819, 2001.

2. Cantalupo, G.; Alifano, P.; Roberti, V.; Bruni, C. B.; Bucci, C.
: Rab-interacting lysosomal protein (RILP): the Rab7 effector required
for transport to lysosomes. EMBO J. 20: 683-693, 2001.

3. Wang, T.; Wong, K. K.; Hong, W.: A unique region of RILP distinguishes
it from its related proteins in its regulation of lysosomal morphology
and interaction with Rab7 and Rab34. Molec. Biol. Cell 15: 815-826,
2004.

*FIELD* CN
Patricia A. Hartz - updated: 7/11/2011

*FIELD* CD
Patricia A. Hartz: 6/3/2003

*FIELD* ED
mgross: 07/15/2011
terry: 7/11/2011
mgross: 6/3/2003

RBCC Red Blood Cell Collection

Full text data of RILP