ID   RIPL2_RAT               Reviewed;         197 AA.
AC   Q6AYA0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=RILP-like protein 2;
DE   AltName: Full=Rab-interacting lysosomal-like protein 2;
GN   Name=Rilpl2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
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   [2]
RP   FUNCTION, AND INTERACTION WITH MYO5A AND RAC1.
RX   PubMed=19812310; DOI=10.1242/jcs.050344;
RA   Lise M.F., Srivastava D.P., Arstikaitis P., Lett R.L., Sheta R.,
RA   Viswanathan V., Penzes P., O'Connor T.P., El-Husseini A.;
RT   "Myosin-Va-interacting protein, RILPL2, controls cell shape and neuronal
RT   morphogenesis via Rac signaling.";
RL   J. Cell Sci. 122:3810-3821(2009).
CC   -!- FUNCTION: Involved in cell shape and neuronal morphogenesis, positively
CC       regulating the establishment and maintenance of dendritic spines
CC       (PubMed:19812310). Plays a role in cellular protein transport,
CC       including protein transport away from primary cilia (By similarity).
CC       May function via activation of RAC1 and PAK1 (PubMed:19812310).
CC       {ECO:0000250|UniProtKB:Q99LE1, ECO:0000269|PubMed:19812310}.
CC   -!- SUBUNIT: Homodimer (By similarity). Interacts (via N-terminus) with
CC       MYO5A, the interaction is required for its role in dendrite formation
CC       (PubMed:19812310). Interacts with RAC1 (PubMed:19812310). Interacts
CC       with RAB8A; interaction is dependent on the phosphorylation of RAB8A on
CC       'Thr-72' (By similarity). Interacts with RAB10 and RAB12; interaction
CC       is dependent on the phosphorylation of 'Thr-73' on RAB10 and 'Ser-105'
CC       on RAB12 (By similarity). {ECO:0000250|UniProtKB:Q969X0,
CC       ECO:0000250|UniProtKB:Q99LE1, ECO:0000269|PubMed:19812310}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Cytoplasm,
CC       cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}.
CC       Cell projection, cilium {ECO:0000250}.
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DR   EMBL; BC079132; AAH79132.1; -; mRNA.
DR   RefSeq; NP_001004205.1; NM_001004205.1.
DR   AlphaFoldDB; Q6AYA0; -.
DR   SMR; Q6AYA0; -.
DR   STRING; 10116.ENSRNOP00000001403; -.
DR   PaxDb; Q6AYA0; -.
DR   Ensembl; ENSRNOT00000001403; ENSRNOP00000001403; ENSRNOG00000001061.
DR   GeneID; 288652; -.
DR   KEGG; rno:288652; -.
DR   UCSC; RGD:1303140; rat.
DR   CTD; 196383; -.
DR   RGD; 1303140; Rilpl2.
DR   eggNOG; ENOG502S08B; Eukaryota.
DR   GeneTree; ENSGT00940000160182; -.
DR   HOGENOM; CLU_096533_1_0_1; -.
DR   InParanoid; Q6AYA0; -.
DR   OMA; HRPAMIN; -.
DR   OrthoDB; 890179at2759; -.
DR   PhylomeDB; Q6AYA0; -.
DR   PRO; PR:Q6AYA0; -.
DR   Proteomes; UP000002494; Chromosome 12.
DR   Bgee; ENSRNOG00000001061; Expressed in spleen and 19 other tissues.
DR   Genevisible; Q6AYA0; RN.
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; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:GOC.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
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   Cell projection; Cilium; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Protein transport; Reference proteome; Transport.
FT   CHAIN           1..197
FT                   /note="RILP-like protein 2"
FT                   /id="PRO_0000317007"
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   COILED          65..153
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   197 AA;  22445 MW;  46CED33D2197B95F CRC64;
     MEEPPVREEE DGEEDEGALA KSPLQLTTED VYDISYVVGR ELMALGSDPR VTRLQFKIVR
     VMEMLEALVN EGSLAVEELR MERDNLKQEV EGLRRAGVSG SEVNLGPDKM VVDLTDPNRP
     RFTLQELRDV LQERNKLKSQ LLLVQEELQC YRSGLLPPRE TPGGRREKDA MVTMGNGEKE
     ERTIMKKLFS FRSGKHT