U119A_RAT
ID U119A_RAT Reviewed; 240 AA.
AC Q62885;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Protein unc-119 homolog A;
DE AltName: Full=Retinal protein 4;
DE Short=rRG4;
GN Name=Unc119; Synonyms=Rg4;
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 [MRNA].
RC STRAIN=Long Evans; TISSUE=Retina;
RX PubMed=8576185; DOI=10.1074/jbc.271.3.1797;
RA Higashide T., Murakami A., McLaren M.J., Inana G.;
RT "Cloning of the cDNA for a novel photoreceptor protein.";
RL J. Biol. Chem. 271:1797-1804(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 INTERACTION WITH ARL2, AND TISSUE SPECIFICITY.
RX PubMed=12527357; DOI=10.1016/s0014-5793(02)03766-3;
RA Kobayashi A., Kubota S., Mori N., McLaren M.J., Inana G.;
RT "Photoreceptor synaptic protein HRG4 (UNC119) interacts with ARL2 via a
RT putative conserved domain.";
RL FEBS Lett. 534:26-32(2003).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37; SER-39 AND SER-41, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Involved in synaptic functions in photoreceptor cells, the
CC signal transduction in immune cells as a Src family kinase activator,
CC endosome recycling, the uptake of bacteria and endocytosis, protein
CC trafficking in sensory neurons and as lipid-binding chaperone with
CC specificity for a diverse subset of myristoylated proteins.
CC Specifically binds the myristoyl moiety of a subset of N-terminally
CC myristoylated proteins and is required for their localization. Binds
CC myristoylated GNAT1 and is required for G-protein localization and
CC trafficking in sensory neurons. Probably plays a role in trafficking
CC proteins in photoreceptor cells. Plays important roles in mediating Src
CC family kinase signals for the completion of cytokinesis via RAB11A.
CC {ECO:0000250|UniProtKB:Q13432, ECO:0000250|UniProtKB:Q9Z2R6}.
CC -!- SUBUNIT: Interacts with CABP4; in the absence of calcium. May interact
CC with GTP-bound ARL1. Interacts with ARL2 and ARL3 (GTP-bound forms);
CC this promotes the release of myristoylated cargo proteins (By
CC similarity). Found in a complex with ARL3, RP2 and UNC119; RP2 induces
CC hydrolysis of GTP ARL3 in the complex, leading to the release of
CC UNC119. Interacts with NPHP3 (when myristoylated). Interacts with CYS1
CC (when myristoylated). Interacts with MACIR; interaction only takes
CC place when UNC119 is not liganded with myristoylated proteins (By
CC similarity). Interacts with ARL1 and ARL3 GTP-bound forms (By
CC similarity). Interacts with ARL2. Interacts with ARL2.Interacts with
CC LCK; this interaction plays a crucial role in activation of LCK (By
CC similarity). Interacts with FYN (By similarity). Interacts with RAB11A;
CC in a cell cycle-dependent manner (By similarity). Interacts with LYN
CC (via SH2 and SH3 domains); leading to LYN activation (By similarity).
CC Interacts with DNM1; leading to a decrease of DNM1 GTPase activity (By
CC similarity). Found in a complex with ABL1, ABL2, CRK and UNC119;
CC leading to the inhibition of CRK phosphorylation by ABL kinases (By
CC similarity). Interacts with CD44 (By similarity). Interacts with KLHL18
CC (via kelch repeats) (By similarity). Interacts with PPP3CA, PPP3CB and
CC PPP3CC (By similarity). {ECO:0000250|UniProtKB:Q13432,
CC ECO:0000250|UniProtKB:Q9Z2R6, ECO:0000269|PubMed:12527357}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250|UniProtKB:Q13432}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000250|UniProtKB:Q13432}. Cytoplasm,
CC cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q13432}.
CC Note=ocalizes to the centrosome in interphase cells and begins to
CC translocate from the spindle pole to the spindle midzone after the
CC onset of mitosis; it then localizes to the intercellular bridge in
CC telophase cells and to the midbody in cytokinetic cells.
CC {ECO:0000250|UniProtKB:Q13432}.
CC -!- DEVELOPMENTAL STAGE: Begins to be highly expressed around postnatal day
CC 5 in the outer retina when the photoreceptors begin to differentiate
CC and rapidly increases in expression to reach the mature adult level by
CC postnatal day 23.
CC -!- DOMAIN: Adopts an immunoglobulin-like beta-sandwich fold forming a
CC hydrophobic cavity that captures N-terminally myristoylated target
CC peptides. Phe residues within the hydrophobic beta sandwich are
CC required for myristate binding (By similarity).
CC {ECO:0000250|UniProtKB:Q13432}.
CC -!- PTM: Phosphorylation suppresses its interaction with KLHL18 and down-
CC regulates its KLHL18-mediated degradation. Phosphorylated more under
CC light conditions than dark conditions. Dephosphorylated by calcineurin.
CC {ECO:0000250|UniProtKB:Q9Z2R6}.
CC -!- SIMILARITY: Belongs to the PDE6D/unc-119 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U40999; AAC52389.1; -; mRNA.
DR EMBL; BC062057; AAH62057.1; -; mRNA.
DR RefSeq; NP_058884.1; NM_017188.1.
DR AlphaFoldDB; Q62885; -.
DR SMR; Q62885; -.
DR STRING; 10116.ENSRNOP00000015091; -.
DR iPTMnet; Q62885; -.
DR PhosphoSitePlus; Q62885; -.
DR PaxDb; Q62885; -.
DR Ensembl; ENSRNOT00000015091; ENSRNOP00000015091; ENSRNOG00000011060.
DR GeneID; 29402; -.
DR KEGG; rno:29402; -.
DR CTD; 9094; -.
DR RGD; 3942; Unc119.
DR eggNOG; KOG4037; Eukaryota.
DR GeneTree; ENSGT00390000014595; -.
DR HOGENOM; CLU_088825_1_1_1; -.
DR InParanoid; Q62885; -.
DR OMA; CNSADMG; -.
DR OrthoDB; 1270912at2759; -.
DR PhylomeDB; Q62885; -.
DR TreeFam; TF314474; -.
DR PRO; PR:Q62885; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000011060; Expressed in heart and 20 other tissues.
DR Genevisible; Q62885; RN.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0045171; C:intercellular bridge; ISS:UniProtKB.
DR GO; GO:0051233; C:spindle midzone; ISS:UniProtKB.
DR GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
DR GO; GO:0008289; F:lipid binding; ISS:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0042953; P:lipoprotein transport; ISS:UniProtKB.
DR GO; GO:0000281; P:mitotic cytokinesis; ISS:UniProtKB.
DR GO; GO:2001287; P:negative regulation of caveolin-mediated endocytosis; ISS:UniProtKB.
DR GO; GO:1900186; P:negative regulation of clathrin-dependent endocytosis; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; ISO:RGD.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0007601; P:visual perception; IBA:GO_Central.
DR Gene3D; 2.70.50.40; -; 1.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR008015; PDED_dom.
DR InterPro; IPR037036; PDED_dom_sf.
DR InterPro; IPR032977; UNC119_homologue_A.
DR PANTHER; PTHR12951:SF5; PTHR12951:SF5; 1.
DR Pfam; PF05351; GMP_PDE_delta; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; Endocytosis; Lipid-binding; Phosphoprotein;
KW Protein transport; Reference proteome; Sensory transduction; Transport;
KW Vision.
FT CHAIN 1..240
FT /note="Protein unc-119 homolog A"
FT /id="PRO_0000221214"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 131
FT /ligand="tetradecanoate"
FT /ligand_id="ChEBI:CHEBI:30807"
FT /evidence="ECO:0000250"
FT MOD_RES 37
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 39
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 41
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 240 AA; 27048 MW; D062DCAF3B2410B1 CRC64;
MKVKKGGGGT GPGAEPVPGA SNRSVEPTRE PGAEAESGSE SEPEPGPGPR LGPLQGKQPI
GPEDVLGLQR ITGDYLCSPE ENIYKIDFVR FKIRDMDSGT VLFEIKKPPV SERLPINRRD
LDPNAGRFVR YQFTPAFLRL RQVGATVEFT VGDKPVNNFR MIERHYFRNQ LLKSFDFHFG
FCIPSSKNTC EHIYDFPPLS EELISEMIRH PYETQSDSFY FVDDRLVMHN KADYSYSGTP
