RIPL2_HUMAN
ID RIPL2_HUMAN Reviewed; 211 AA.
AC Q969X0;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=RILP-like protein 2;
DE AltName: Full=Rab-interacting lysosomal protein-like 2;
DE AltName: Full=p40phox-binding protein;
GN Name=RILPL2; Synonyms=RLP2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kuribayashi F., Ago T., Sumimoto H.;
RT "p40phox binding protein.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Salivary gland;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [5]
RP LACK OF FUNCTION, 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 its
RT regulation of lysosomal morphology and interaction with Rab7 and Rab34.";
RL Mol. Biol. Cell 15:815-826(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [7]
RP INTERACTION WITH RAB8A; RAB10 AND RAB12, AND MUTAGENESIS OF ARG-130;
RP ARG-132 AND LYS-149.
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: Involved in cell shape and neuronal morphogenesis, positively
CC regulating the establishment and maintenance of dendritic spines (By
CC similarity). Plays a role in cellular protein transport, including
CC protein transport away from primary cilia (By similarity). May function
CC via activation of RAC1 and PAK1 (By similarity).
CC {ECO:0000250|UniProtKB:Q6AYA0, ECO:0000250|UniProtKB:Q99LE1}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with RAC1 (By
CC similarity). Interacts (via N-terminus) with MYO5A, the interaction is
CC required for its role in dendrite formation (By similarity). Interacts
CC with RAB8A; interaction is dependent on the phosphorylation of RAB8A on
CC 'Thr-72' (PubMed:29125462). Interacts with RAB10 and RAB12; interaction
CC is dependent on the phosphorylation of 'Thr-73' on RAB10 and 'Ser-105'
CC on RAB12 (PubMed:29125462). {ECO:0000250|UniProtKB:Q6AYA0,
CC ECO:0000250|UniProtKB:Q99LE1, ECO:0000269|PubMed:29125462}.
CC -!- INTERACTION:
CC Q969X0; P61026: RAB10; NbExp=2; IntAct=EBI-717552, EBI-726075;
CC Q969X0; P61006: RAB8A; NbExp=8; IntAct=EBI-717552, EBI-722293;
CC Q969X0; Q969X0: RILPL2; NbExp=3; IntAct=EBI-717552, EBI-717552;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:14668488}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250}. Cell projection, cilium {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in
CC lung. {ECO:0000269|PubMed:14668488}.
CC -!- SIMILARITY: Belongs to the RILPL family. {ECO:0000305}.
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DR EMBL; AB085763; BAC76826.1; -; mRNA.
DR EMBL; AK056934; BAB71313.1; -; mRNA.
DR EMBL; CH471054; EAW98411.1; -; Genomic_DNA.
DR EMBL; BC013042; AAH13042.1; -; mRNA.
DR CCDS; CCDS9248.1; -.
DR RefSeq; NP_659495.1; NM_145058.2.
DR PDB; 6RIR; X-ray; 1.77 A; C/D=129-165.
DR PDB; 6SQ2; X-ray; 1.68 A; D/E=129-165.
DR PDB; 7LWB; X-ray; 1.90 A; D=117-165.
DR PDBsum; 6RIR; -.
DR PDBsum; 6SQ2; -.
DR PDBsum; 7LWB; -.
DR AlphaFoldDB; Q969X0; -.
DR SMR; Q969X0; -.
DR BioGRID; 128200; 9.
DR IntAct; Q969X0; 11.
DR STRING; 9606.ENSP00000280571; -.
DR iPTMnet; Q969X0; -.
DR PhosphoSitePlus; Q969X0; -.
DR BioMuta; RILPL2; -.
DR DMDM; 74731067; -.
DR EPD; Q969X0; -.
DR jPOST; Q969X0; -.
DR MassIVE; Q969X0; -.
DR MaxQB; Q969X0; -.
DR PaxDb; Q969X0; -.
DR PeptideAtlas; Q969X0; -.
DR PRIDE; Q969X0; -.
DR ProteomicsDB; 75866; -.
DR TopDownProteomics; Q969X0; -.
DR Antibodypedia; 31814; 119 antibodies from 24 providers.
DR DNASU; 196383; -.
DR Ensembl; ENST00000280571.10; ENSP00000280571.8; ENSG00000150977.11.
DR GeneID; 196383; -.
DR KEGG; hsa:196383; -.
DR MANE-Select; ENST00000280571.10; ENSP00000280571.8; NM_145058.3; NP_659495.1.
DR UCSC; uc001uey.2; human.
DR CTD; 196383; -.
DR DisGeNET; 196383; -.
DR GeneCards; RILPL2; -.
DR HGNC; HGNC:28787; RILPL2.
DR HPA; ENSG00000150977; Tissue enriched (bone).
DR MIM; 614093; gene.
DR neXtProt; NX_Q969X0; -.
DR OpenTargets; ENSG00000150977; -.
DR PharmGKB; PA162401325; -.
DR VEuPathDB; HostDB:ENSG00000150977; -.
DR eggNOG; ENOG502S08B; Eukaryota.
DR GeneTree; ENSGT00940000160182; -.
DR HOGENOM; CLU_096533_1_0_1; -.
DR InParanoid; Q969X0; -.
DR OMA; HRPAMIN; -.
DR OrthoDB; 890179at2759; -.
DR PhylomeDB; Q969X0; -.
DR TreeFam; TF313489; -.
DR PathwayCommons; Q969X0; -.
DR SignaLink; Q969X0; -.
DR BioGRID-ORCS; 196383; 29 hits in 1031 CRISPR screens.
DR ChiTaRS; RILPL2; human.
DR GenomeRNAi; 196383; -.
DR Pharos; Q969X0; Tbio.
DR PRO; PR:Q969X0; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q969X0; protein.
DR Bgee; ENSG00000150977; Expressed in parotid gland and 195 other tissues.
DR Genevisible; Q969X0; HS.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; IBA:GO_Central.
DR GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016020; C:membrane; IEA:GOC.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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; ISS:UniProtKB.
DR GO; GO:1903445; P:protein transport from ciliary membrane to plasma membrane; ISS:UniProtKB.
DR InterPro; IPR034743; RH1.
DR InterPro; IPR034744; RH2.
DR InterPro; IPR021563; RILP_dimer.
DR Pfam; PF11461; RILP; 1.
DR PROSITE; PS51776; RH1; 1.
DR PROSITE; PS51777; RH2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell projection; Cilium; Coiled coil; Cytoplasm;
KW Cytoskeleton; Phosphoprotein; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..211
FT /note="RILP-like protein 2"
FT /id="PRO_0000317005"
FT DOMAIN 24..106
FT /note="RH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01112"
FT DOMAIN 130..201
FT /note="RH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01113"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 70..164
FT /evidence="ECO:0000255"
FT COMPBIAS 1..23
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MUTAGEN 130
FT /note="R->E: Loss of interaction with RAB8A, RAB10 and
FT RAB12."
FT /evidence="ECO:0000269|PubMed:29125462"
FT MUTAGEN 132
FT /note="R->E: Loss of interaction with RAB8A, RAB10 and
FT RAB12."
FT /evidence="ECO:0000269|PubMed:29125462"
FT MUTAGEN 149
FT /note="K->E: Loss of interaction with RAB8A, RAB10 and
FT RAB12."
FT /evidence="ECO:0000269|PubMed:29125462"
FT HELIX 135..157
FT /evidence="ECO:0007829|PDB:6SQ2"
SQ SEQUENCE 211 AA; 23986 MW; 5F9C132B6E81DFDD CRC64;
MEEPPVREEE EEEGEEDEER DEVGPEGALG KSPFQLTAED VYDISYLLGR ELMALGSDPR
VTQLQFKVVR VLEMLEALVN EGSLALEELK MERDHLRKEV EGLRRQSPPA SGEVNLGPNK
MVVDLTDPNR PRFTLQELRD VLQERNKLKS QLLVVQEELQ CYKSGLIPPR EGPGGRREKD
AVVTSAKNAG RNKEEKTIIK KLFFFRSGKQ T
