RIPL2_MOUSE
ID RIPL2_MOUSE Reviewed; 197 AA.
AC Q99LE1; Q3TB73;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=RILP-like protein 2;
DE AltName: Full=Rab-interacting lysosomal-like protein 2;
GN Name=Rilpl2;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
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 MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 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 [4]
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).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-97 IN COMPLEX WITH MYO5A AND
RP MLPH, INTERACTION WITH MYO5A, SUBUNIT, MUTAGENESIS OF PHE-56; VAL-59 AND
RP VAL-61, AND IDENTIFICATION IN A COMPLEX WITH MYO5A AND MLPH.
RX PubMed=23798443; DOI=10.1073/pnas.1306768110;
RA Wei Z., Liu X., Yu C., Zhang M.;
RT "Structural basis of cargo recognitions for class V myosins.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:11314-11319(2013).
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 (PubMed:23264467). May
CC function via activation of RAC1 and PAK1 (By similarity).
CC {ECO:0000250|UniProtKB:Q6AYA0, ECO:0000269|PubMed:23264467}.
CC -!- SUBUNIT: Homodimer (PubMed:23798443). Interacts with RAC1 (By
CC similarity). Interacts (via N-terminus) with MYO5A, the interaction is
CC required for its role in dendrite formation (PubMed:23798443).
CC Interacts with RAB8A; interaction is dependent on the phosphorylation
CC of RAB8A on 'Thr-72' (PubMed:29125462). Interacts with RAB10 and RAB12;
CC interaction is dependent on the phosphorylation of 'Thr-73' on RAB10
CC and 'Ser-105' on RAB12 (By similarity). {ECO:0000250|UniProtKB:Q6AYA0,
CC ECO:0000250|UniProtKB:Q969X0, ECO:0000269|PubMed:23798443,
CC ECO:0000269|PubMed:29125462}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:23264467}. Cell projection, cilium
CC {ECO:0000269|PubMed:23264467}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q99LE1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99LE1-2; Sequence=VSP_030853;
CC -!- SIMILARITY: Belongs to the RILPL family. {ECO:0000305}.
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DR EMBL; AK133760; BAE21826.1; -; mRNA.
DR EMBL; AK150123; BAE29324.1; -; mRNA.
DR EMBL; AK150252; BAE29414.1; -; mRNA.
DR EMBL; AK171419; BAE42441.1; -; mRNA.
DR EMBL; BC003324; AAH03324.1; -; mRNA.
DR CCDS; CCDS19676.1; -. [Q99LE1-1]
DR RefSeq; NP_084535.1; NM_030259.1. [Q99LE1-1]
DR PDB; 4KP3; X-ray; 2.40 A; C/D=1-97.
DR PDBsum; 4KP3; -.
DR AlphaFoldDB; Q99LE1; -.
DR SMR; Q99LE1; -.
DR IntAct; Q99LE1; 1.
DR STRING; 10090.ENSMUSP00000031347; -.
DR iPTMnet; Q99LE1; -.
DR PhosphoSitePlus; Q99LE1; -.
DR EPD; Q99LE1; -.
DR MaxQB; Q99LE1; -.
DR PaxDb; Q99LE1; -.
DR PeptideAtlas; Q99LE1; -.
DR PRIDE; Q99LE1; -.
DR ProteomicsDB; 253314; -. [Q99LE1-1]
DR ProteomicsDB; 253315; -. [Q99LE1-2]
DR Antibodypedia; 31814; 119 antibodies from 24 providers.
DR DNASU; 80291; -.
DR Ensembl; ENSMUST00000031347; ENSMUSP00000031347; ENSMUSG00000029401. [Q99LE1-1]
DR GeneID; 80291; -.
DR KEGG; mmu:80291; -.
DR UCSC; uc008zpx.1; mouse. [Q99LE1-1]
DR UCSC; uc057abr.1; mouse. [Q99LE1-2]
DR CTD; 196383; -.
DR MGI; MGI:1933112; Rilpl2.
DR VEuPathDB; HostDB:ENSMUSG00000029401; -.
DR eggNOG; ENOG502S08B; Eukaryota.
DR GeneTree; ENSGT00940000160182; -.
DR HOGENOM; CLU_096533_1_0_1; -.
DR InParanoid; Q99LE1; -.
DR OMA; HRPAMIN; -.
DR OrthoDB; 890179at2759; -.
DR PhylomeDB; Q99LE1; -.
DR TreeFam; TF313489; -.
DR BioGRID-ORCS; 80291; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Rilpl2; mouse.
DR PRO; PR:Q99LE1; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q99LE1; protein.
DR Bgee; ENSMUSG00000029401; Expressed in placenta labyrinth and 247 other tissues.
DR Genevisible; Q99LE1; MM.
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; ISO:MGI.
DR GO; GO:0016020; C:membrane; IEA:GOC.
DR GO; GO:0042802; F:identical protein binding; 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 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; Alternative splicing; Cell projection; Cilium; Coiled coil;
KW Cytoplasm; Cytoskeleton; Protein transport; Reference proteome; Transport.
FT CHAIN 1..197
FT /note="RILP-like protein 2"
FT /id="PRO_0000317006"
FT DOMAIN 14..96
FT /note="RH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01112"
FT DOMAIN 119..184
FT /note="RH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01113"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 69..153
FT /evidence="ECO:0000255"
FT COMPBIAS 1..16
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 104..197
FT /note="NLGPDKMVVDLTDPNRPRFTLQELREVLQERNKLKSQLLLVQEELQCYRSGL
FT LPPRETPGGRREKDAVVAMGNGEKEERTIMKKLFSFRSGKHT -> SKTQALVWKFPHS
FT SHLLNTY (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030853"
FT MUTAGEN 56
FT /note="F->P: Loss of interaction with MYO5A."
FT /evidence="ECO:0000269|PubMed:23798443"
FT MUTAGEN 59
FT /note="V->Q: Loss of interaction with MYO5A."
FT /evidence="ECO:0000269|PubMed:23798443"
FT MUTAGEN 61
FT /note="V->E: Abolishes homodimerization."
FT /evidence="ECO:0000269|PubMed:23798443"
FT HELIX 16..19
FT /evidence="ECO:0007829|PDB:4KP3"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:4KP3"
FT HELIX 28..43
FT /evidence="ECO:0007829|PDB:4KP3"
FT HELIX 49..71
FT /evidence="ECO:0007829|PDB:4KP3"
FT HELIX 74..93
FT /evidence="ECO:0007829|PDB:4KP3"
SQ SEQUENCE 197 AA; 22393 MW; 6DBC9C7C67528B5A CRC64;
MEDHPVREEE DGEEDEGALA KSPLQLTTDD VYDISYVVGR ELMALGSDPR VTRLQFKIVR
VMEMLETLVN EGSLAVEELR MERDNLKQEV EGLRKAGVSG AQVNLGPDKM VVDLTDPNRP
RFTLQELREV LQERNKLKSQ LLLVQEELQC YRSGLLPPRE TPGGRREKDA VVAMGNGEKE
ERTIMKKLFS FRSGKHT
