U119A_CANLF
ID U119A_CANLF Reviewed; 240 AA.
AC O19177;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Protein unc-119 homolog A;
DE AltName: Full=CRG4;
DE AltName: Full=Retinal protein 4;
GN Name=UNC119; Synonyms=RG4;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Boxer;
RX PubMed=16341006; DOI=10.1038/nature04338;
RA Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
RA Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E.,
RA Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F.,
RA Smith D.R., deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W.,
RA Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S.,
RA Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A.,
RA Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P.,
RA Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
RA Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
RA Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P.,
RA Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B.,
RA Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A.,
RA Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M.,
RA Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S.,
RA Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L.,
RA Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C.,
RA Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G.,
RA Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N.,
RA Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A.,
RA Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A.,
RA Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M.,
RA Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L.,
RA LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A.,
RA Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S.,
RA Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T.,
RA Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A.,
RA Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
RA Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S.,
RA Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M.,
RA Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F.,
RA Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T.,
RA Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C.,
RA Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C.,
RA Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D.,
RA Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H.,
RA Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J.,
RA Zembek L., Zimmer A., Lander E.S.;
RT "Genome sequence, comparative analysis and haplotype structure of the
RT domestic dog.";
RL Nature 438:803-819(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 145-240.
RC TISSUE=Retina;
RX PubMed=11401471; DOI=10.1006/bbrc.2001.4587;
RA Lin C.T., Sargan D.R.;
RT "Generation and analysis of canine retinal ESTs: isolation and expression
RT of retina-specific gene transcripts.";
RL Biochem. Biophys. Res. Commun. 282:394-403(2001).
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 (By
CC similarity). {ECO:0000250|UniProtKB:Q13432,
CC 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 LCK; this interaction plays a crucial role
CC in activation of LCK (By similarity). Interacts with FYN (By
CC similarity). Interacts with RAB11A; in a cell cycle-dependent manner
CC (By similarity). Interacts with LYN (via SH2 and SH3 domains); leading
CC to LYN activation (By similarity). Interacts with DNM1; leading to a
CC decrease of DNM1 GTPase activity (By similarity). Found in a complex
CC with ABL1, ABL2, CRK and UNC119; leading to the inhibition of CRK
CC phosphorylation by ABL kinases (By similarity). Interacts with CD44 (By
CC similarity). Interacts with KLHL18 (via kelch repeats) (By similarity).
CC Interacts with PPP3CA, PPP3CB and PPP3CC (By similarity).
CC {ECO:0000250|UniProtKB:Q13432, ECO:0000250|UniProtKB:Q9Z2R6}.
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 -!- 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 -!- SEQUENCE CAUTION:
CC Sequence=CAB10748.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Z97731; CAB10748.1; ALT_FRAME; mRNA.
DR AlphaFoldDB; O19177; -.
DR STRING; 9612.ENSCAFP00000027605; -.
DR PaxDb; O19177; -.
DR eggNOG; KOG4037; Eukaryota.
DR InParanoid; O19177; -.
DR Proteomes; UP000002254; Unplaced.
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; IBA:GO_Central.
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 2: Evidence at transcript 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_0000221211"
FT REGION 1..61
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:0000250|UniProtKB:Q9Z2R6"
FT MOD_RES 39
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2R6"
FT MOD_RES 41
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2R6"
FT CONFLICT 145..146
FT /note="AT -> VR (in Ref. 2; CAB10748)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 240 AA; 27062 MW; 9AF47BE2159E3ADB CRC64;
MKVKKGGGGA GTGAEPASGA PGPSVEPKPE PQAESESGSE SEPEAGPGPR PGPLQRKQRI
GPEDVLGLQR ITGDYLCSPE ENIYKIDFIR FKIRDMDSGT VLFEIKKPPA SERLPINRRD
LDPNAGRFVR YQFTPAFLRL RQVGATVEFT VGDKPVNNFR MIERHYFRNQ LLKSFDFHFG
FCIPSSKNTC EHIYDFPPLS EELINEMIRH PYETQSDSFY FVDDRLVMHN KADYSYSGTP
