ID   RIPL1_BOVIN             Reviewed;         403 AA.
AC   Q17QG3;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=RILP-like protein 1;
DE   AltName: Full=Rab-interacting lysosomal-like protein 1;
GN   Name=RILPL1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal pons;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays a role in the regulation of cell shape and polarity (By
CC       similarity). Plays a role in cellular protein transport, including
CC       protein transport away from primary cilia (By similarity).
CC       Neuroprotective protein, which acts by sequestring GAPDH in the cytosol
CC       and prevent the apoptotic function of GAPDH in the nucleus (By
CC       similarity). Competes with SIAH1 for binding GAPDH (By similarity).
CC       Does not regulate lysosomal morphology and distribution (By
CC       similarity). Binds to RAB10 following LRRK2-mediated RAB10
CC       phosphorylation which leads to inhibition of ciliogenesis (By
CC       similarity). {ECO:0000250|UniProtKB:D3ZUQ0,
CC       ECO:0000250|UniProtKB:Q5EBL4, ECO:0000250|UniProtKB:Q9JJC6}.
CC   -!- SUBUNIT: Interacts (when S-nitrosylated) with GAPDH (By similarity).
CC       Interacts with RAB8A; interaction is dependent on the phosphorylation
CC       of 'Thr-72' of RAB8A (By similarity). Interacts with RAB10 and RAB12;
CC       the interaction is dependent on the phosphorylation of 'Thr-73' of
CC       RAB10, and 'Ser-105' of RAB12 (By similarity).
CC       {ECO:0000250|UniProtKB:D3ZUQ0, ECO:0000250|UniProtKB:Q5EBL4}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q5EBL4}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome, centriole
CC       {ECO:0000250|UniProtKB:Q5EBL4}. Cytoplasm, cytoskeleton, cilium basal
CC       body {ECO:0000250|UniProtKB:Q5EBL4}.
CC   -!- PTM: S-nitrosylation is required for the interaction with GAPDH.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RILPL family. {ECO:0000305}.
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DR   EMBL; BC118379; AAI18380.1; -; mRNA.
DR   RefSeq; NP_001068694.1; NM_001075226.1.
DR   AlphaFoldDB; Q17QG3; -.
DR   SMR; Q17QG3; -.
DR   STRING; 9913.ENSBTAP00000029666; -.
DR   PaxDb; Q17QG3; -.
DR   PRIDE; Q17QG3; -.
DR   GeneID; 505840; -.
DR   KEGG; bta:505840; -.
DR   CTD; 353116; -.
DR   eggNOG; ENOG502QR9G; Eukaryota.
DR   InParanoid; Q17QG3; -.
DR   OrthoDB; 890179at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
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; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; IEA:GOC.
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   GO; GO:1901214; P:regulation of neuron death; ISS:UniProtKB.
DR   InterPro; IPR019143; JNK/Rab-associated_protein-1_N.
DR   InterPro; IPR034743; RH1.
DR   InterPro; IPR034744; RH2.
DR   InterPro; IPR021563; RILP_dimer.
DR   Pfam; PF09744; Jnk-SapK_ap_N; 1.
DR   Pfam; PF11461; RILP; 1.
DR   PROSITE; PS51776; RH1; 1.
DR   PROSITE; PS51777; RH2; 1.
PE   2: Evidence at transcript level;
KW   Cell projection; Cilium; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Phosphoprotein; Protein transport; Reference proteome; S-nitrosylation;
KW   Transport.
FT   CHAIN           1..403
FT                   /note="RILP-like protein 1"
FT                   /id="PRO_0000299309"
FT   DOMAIN          10..97
FT                   /note="RH1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01112"
FT   DOMAIN          291..356
FT                   /note="RH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01113"
FT   REGION          329..348
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          76..265
FT                   /evidence="ECO:0000255"
FT   MOD_RES         7
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:D3ZUQ0"
FT   MOD_RES         47
FT                   /note="S-nitrosocysteine"
FT                   /evidence="ECO:0000250|UniProtKB:D3ZUQ0"
SQ   SEQUENCE   403 AA;  47010 MW;  B036657BFF238FBC CRC64;
     MEEDRGSALA AESALEKNVA ELTVMDVYDI ASLVGHEFER VIDQHGCEAI ARLIPKVVRV
     LEILEVLVSR HHVAPELDEL RLELDRLRLE RMDRIEKERK HQKELELVED VWRGEAQDLL
     SQIAQLQEEN KQLMTNLSHK DVSFSEEEFQ KHEGMSERER QVMKKLKEVV DKQRDEIRAK
     DRELGLKNED VEALQQQQTR LMKINHDLRH RVTVVEAQGK ALIEQKVELE ADLQTKEQEM
     GSLRAELGKL RERLQGELNQ NGEEEPVAEL GGEECVSEAE KVAMDLKDPN RPRFTLQELR
     DVLHERNELK SKVFLLQEEL AYYKSEEIEE ENQIPQPPPI AHPRMSPQPE SGIKRLFSFF
     SRDKKRLANT QRNVRIHETF GQWANCHRDD GYTEQGQEAL QHL