[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN LATE ENDOCYTOSIS, INTERACTION WITH RAB7, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. TISSUE=Cervix carcinoma; DOI=10.1093/emboj/20.4.683; PubMed=11179213 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-81. TISSUE=Kidney, and Thalamus; DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan] Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; "Complete sequencing and characterization of 21,243 full-length human cDNAs."; Nat. Genet. 36:40-45(2004).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). DOI=10.1073/pnas.0404089101; PubMed=15498874 [NCBI, ExPASy, EBI, Israel, Japan] Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.; "Large-scale cDNA transfection screening for genes related to cancer development and progression."; Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). TISSUE=Skeletal muscle; Frigimelica E., Lanfranchi G.; "Study of 100 skeletal muscle full length mRNA (Telethon project B41)."; Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). TISSUE=Brain, Lung, Testis, and Uterus; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[6]	TISSUE SPECIFICITY. DOI=10.1006/bbrc.2001.5466; PubMed=11520070 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[7]	FUNCTION IN DYNEIN-DYNACTIN COMPLEX RECRUITMENT. DOI=10.1016/S0960-9822(01)00531-0; PubMed=11696325 [NCBI, ExPASy, EBI, Israel, Japan] Jordens I., Fernandez-Borja M., Marsman M., Dusseljee S., Janssen L., Calafat J., Janssen H., Wubbolts R., Neefjes J.; "The Rab7 effector protein RILP controls lysosomal transport by inducing the recruitment of dynein-dynactin motors."; Curr. Biol. 11:1680-1685(2001).
[8]	INTERACTION WITH RAB34. DOI=10.1091/mbc.E02-05-0280; PubMed=12475955 [NCBI, ExPASy, EBI, Israel, Japan] Wang T., Hong W.; "Interorganellar regulation of lysosome positioning by the Golgi apparatus through Rab34 interaction with Rab-interacting lysosomal protein."; Mol. Biol. Cell 13:4317-4332(2002).
[9]	FUNCTION IN PHAGOSOME MIGRATION AND PHAGOLYSOSOMAL FUSION, AND SUBCELLULAR LOCATION. DOI=10.1128/MCB.23.18.6494-6506.2003; PubMed=12944476 [NCBI, ExPASy, EBI, Israel, Japan] Harrison R.E., Bucci C., Vieira O.V., Schroer T.A., Grinstein S.; "Phagosomes fuse with late endosomes and/or lysosomes by extension of membrane protrusions along microtubules: role of Rab7 and RILP."; Mol. Cell. Biol. 23:6494-6506(2003).
[10]	FUNCTION IN LYSOSOMAL MORPHOLOGY AND DISTRIBUTION, INTERACTION WITH RAB7 AND RAB34, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. DOI=10.1091/mbc.E03-06-0413; PubMed=14668488 [NCBI, ExPASy, EBI, Israel, Japan] 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."; Mol. Biol. Cell 15:815-826(2004).
[11]	SUBUNIT. DOI=10.1016/j.bbrc.2005.06.067; PubMed=15996637 [NCBI, ExPASy, EBI, Israel, Japan] Colucci A.M.R., Campana M.C., Bellopede M., Bucci C.; "The Rab-interacting lysosomal protein, a Rab7 and Rab34 effector, is capable of self-interaction."; Biochem. Biophys. Res. Commun. 334:128-133(2005).
[12]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314 AND SER-315, AND MASS SPECTROMETRY. DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan] Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.; "A quantitative atlas of mitotic phosphorylation."; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[13]	X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 244-308 IN COMPLEX WITH RAB7, SUBUNIT, AND MUTAGENESIS OF PHE-248; ILE-251; LEU-252; ARG-255; LEU-258; LYS-304; MET-305 AND LEU-306. DOI=10.1038/sj.emboj.7600643; PubMed=15933719 [NCBI, ExPASy, EBI, Israel, Japan] Wu M., Wang T., Loh E., Hong W., Song H.; "Structural basis for recruitment of RILP by small GTPase Rab7."; EMBO J. 24:1491-1501(2005).

Comments

FUNCTION: Rab effector playing a role in late endocytic transport to degradative compartments. Involved in the regulation of lysosomal morphology and distribution. Induces recruitment of dynein-dynactin motor complexes to Rab7-containing late endosome and lysosome compartments. Promotes centripetal migration of phagosomes and the fusion of phagosomes with the late endosomes and lysosomes.
SUBUNIT: Homodimer. Each subunit can interact with either RAB7 or RAB34.
SUBCELLULAR LOCATION: Endomembrane system. Late endosome membrane. Lysosome membrane. Cytoplasmic vesicle, phagosome membrane. Note=Associated with late endosomal, lysosomal and phagosomal membranes. The interaction with RAB7 is necessary for its recruitment to phagosomes.
ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name 1

Isoform ID Q96NA2-1

This is the isoform sequence displayed in this entry.

Name 2

Isoform ID Q96NA2-2

Features which should be applied to build the isoform sequence: VSP_016043, VSP_016044.
TISSUE SPECIFICITY: Ubiquitous. Strongly expressed in fetal heart, heart, stomach, spleen, adrenal gland, thyroid gland, salivary gland, fetal liver, liver and lung. Poorly expressed in brain.
SIMILARITY: Contains 1 RILP-like domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AJ404317; CAC33443.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK055755; BAB71003.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK314767; BAG37305.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF370391; AAQ15227.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ278711; CAC82174.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC004961; AAH04961.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC031621; AAH31621.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00289188; -.
IPI00654568; -.

RefSeq

NP_113618.2; -.

UniGene

Hs.534497

3D structure databases

PDB

1YHN; X-ray; 3.00 A; B=244-308.

[ExPASy / RCSB / EBI]

1YHN; -.

PTM databases

Q96NA2; -.

Organism-specific databases

GC17M001496; -.

HIX0013403; -.

HGNC:30266; RILP.

607848; gene. [NCBI / EBI]

PharmGKB

PA134915969; -.

Gene expression databases

Q96NA2; -.

Q96NA2; -.

HS_RILP; -.

ENSG00000167705; Homo sapiens.

Ontologies

GO:0031902;	Cellular component: late endosome membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005765;	Cellular component: lysosomal membrane (non-traceable author statement from UniProtKB).
GO:0030670;	Cellular component: phagocytic vesicle membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0017137;	Molecular function: Rab GTPase binding (traceable author statement from UniProtKB).
GO:0015031;	Biological process: protein transport (non-traceable author statement from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR019143; JNK/Rab-associated_protein-1.
Graphical view of domain structure.

Pfam

PF09744; Jnk-SapK_ap_N; 1.
Pfam graphical view of domain structure.

Proteomic databases

PRIDE

Q96NA2; -.

Genome annotation databases

Ensembl

ENSG00000167705; Homo sapiens. [Contig view]

GeneID

83547; -.

KEGG

hsa:83547; -.

Phylogenomic databases

HOGENOM

Q96NA2; -.

HOVERGEN

Q96NA2; -.

OMA

Q96NA2; KVAVKKQ.

Other

72481; -.

RILP; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Alternative splicing; Coiled coil; Cytoplasmic vesicle; Endosome; Lysosome; Membrane; Phosphoprotein; Polymorphism; Protein transport; Transport.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 401`	`401`	`Rab-interacting lysosomal protein.`	`PRO_0000097339`
`DOMAIN`	`236 270`	`35`	`RILP-like.`
`REGION`	`272 333`	`62`	`Necessary for the interaction with RAB7 and RAB34, lysosomal distribution and morphology.`
`COILED`	`75 181`	`107`	`Potential.`
`MOD_RES`	`314 314`		`Phosphoserine.`
`MOD_RES`	`315 315`		`Phosphoserine.`
`VAR_SEQ`	`1 210`		`Missing (in isoform 2).`	`VSP_016043`
`VAR_SEQ`	`211 213`		`WAT -> MGA (in isoform 2).`	`VSP_016044`
`VARIANT`	`81 81`	`1`	`A -> T (in dbSNP:rs9909321 [NCBI]).`	`VAR_051321`
`VARIANT`	`281 281`	`1`	`R -> Q (in dbSNP:rs34982553 [NCBI]).`	`VAR_034417`
`MUTAGEN`	`248 248`		`F->A: Strongly reduces dimerization and localization to late endosomal/lysosomal compartments.`
`MUTAGEN`	`251 251`		`I->A: Abolishes dimerization, interaction with RAB7 and localization to late endosomal/lysosomal compartments.`
`MUTAGEN`	`252 252`		`L->A: Abolishes interaction with RAB7 and localization to late endosomal/lysosomal compartments.`
`MUTAGEN`	`255 255`		`R->A: Abolishes dimerization, interaction with RAB7 and localization to late endosomal/lysosomal compartments.`
`MUTAGEN`	`258 258`		`L->A: Reduces dimerization, interaction with RAB7 and localization to late endosomal/lysosomal compartments.`
`MUTAGEN`	`304 304`		`K->A: Abolishes interaction with RAB7 and localization to late endosomal/lysosomal compartments.`
`MUTAGEN`	`305 305`		`M->A: Abolishes interaction with RAB7 and localization to late endosomal/lysosomal compartments.`
`MUTAGEN`	`306 306`		`L->A: Abolishes interaction with RAB7 and localization to late endosomal/lysosomal compartments.`
`CONFLICT`	`284 284`		`G -> S (in Ref. 1; CAC33443).`
`HELIX`	`248 276`	`29`
`HELIX`	`284 306`	`23`

Sequence information

Length: 401 AA [This is the length of the unprocessed precursor]

Molecular weight: 44200 Da [This is the MW of the unprocessed precursor]

CRC64: 1057A1DAC2FFED94 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEPRRAAPGV PGWGSREAAG SASAAELVYH LAGALGTELQ DLARRFGPEA AAGLVPLVVR 

        70         80         90        100        110        120 
ALELLEQAAV GPAPDSLQVS AQPAEQELRR LREENERLRR ELRAGPQEER ALLRQLKEVT 

       130        140        150        160        170        180 
DRQRDELRAH NRDLRQRGQE TEALQEQLQR LLLVNAELRH KLAAMQTQLR AAQDRERERQ 

       190        200        210        220        230        240 
QPGEAATPQA KERARGQAGR PGHQHGQEPE WATAGAGAPG NPEDPAEAAQ QLGRPSEAGQ 

       250        260        270        280        290        300 
CRFSREEFEQ ILQERNELKA KVFLLKEELA YFQRELLTDH RVPGLLLEAM KVAVRKQRKK 

       310        320        330        340        350        360 
IKAKMLGTPE EAESSEDEAG PWILLSDDKG DHPPPPESKI QSFFGLWYRG KAESSEDETS 

       370        380        390        400 
SPAPSKLGGE EEAQPQSPAP DPPCSALHEH LCLGASAAPE A

Q96NA2 in FASTA format

View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools