U119A_HUMAN
ID U119A_HUMAN Reviewed; 240 AA.
AC Q13432; A8K8G4; F1T095; O95126;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Protein unc-119 homolog A;
DE AltName: Full=Retinal protein 4;
DE Short=hRG4;
GN Name=UNC119; Synonyms=RG4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RC 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 [MRNA] (ISOFORMS A AND B), AND TISSUE SPECIFICITY.
RC TISSUE=Retina;
RX PubMed=9761287;
RA Swanson D.A., Chang J.T., Campochiaro P.A., Zack D.J., Valle D.;
RT "Mammalian orthologs of C. elegans unc-119 highly expressed in
RT photoreceptors.";
RL Invest. Ophthalmol. Vis. Sci. 39:2085-2094(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A).
RX PubMed=10329014; DOI=10.1006/geno.1999.5791;
RA Higashide T., Inana G.;
RT "Characterization of the gene for HRG4 (UNC119), a novel photoreceptor
RT synaptic protein homologous to unc-119.";
RL Genomics 57:446-450(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC TISSUE=Retinoblastoma;
RX PubMed=21697133; DOI=10.1167/iovs.11-7479;
RA Oshikawa M., Tsutsui C., Ikegami T., Fuchida Y., Matsubara M., Toyama S.,
RA Usami R., Ohtoko K., Kato S.;
RT "Full-length transcriptome analysis of human retina-derived cell lines
RT ARPE-19 and Y79 using the vector-capping method.";
RL Invest. Ophthalmol. Vis. Sci. 52:6662-6670(2011).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC TISSUE=Lymph;
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 [9]
RP INVOLVEMENT IN CONE-ROD DYSTROPHY.
RX PubMed=11006213;
RA Kobayashi A., Higashide T., Hamasaki D., Kubota S., Sakuma H., An W.,
RA Fujimaki T., McLaren M.J., Weleber R.G., Inana G.;
RT "HRG4 (UNC119) mutation found in cone-rod dystrophy causes retinal
RT degeneration in a transgenic model.";
RL Invest. Ophthalmol. Vis. Sci. 41:3268-3277(2000).
RN [10]
RP INTERACTION WITH ARL1; ARL2 AND ARL3.
RX PubMed=11303027; DOI=10.1074/jbc.m102359200;
RA Van Valkenburgh H., Shern J.F., Sharer J.D., Zhu X., Kahn R.A.;
RT "ADP-ribosylation factors (ARFs) and ARF-like 1 (ARL1) have both specific
RT and shared effectors: characterizing ARL1-binding proteins.";
RL J. Biol. Chem. 276:22826-22837(2001).
RN [11]
RP INTERACTION WITH LYN, AND FUNCTION IN LYN ACTIVATION.
RX PubMed=12496276; DOI=10.1074/jbc.m208261200;
RA Cen O., Gorska M.M., Stafford S.J., Sur S., Alam R.;
RT "Identification of UNC119 as a novel activator of SRC-type tyrosine
RT kinases.";
RL J. Biol. Chem. 278:8837-8845(2003).
RN [12]
RP INTERACTION WITH LCK AND FYN, FUNCTION IN LCK AND FYN ACTIVATION, AND
RP MUTAGENESIS OF 29-PRO--PRO-32.
RX PubMed=14757743; DOI=10.1084/jem.20030589;
RA Gorska M.M., Stafford S.J., Cen O., Sur S., Alam R.;
RT "Unc119, a novel activator of Lck/Fyn, is essential for T cell
RT activation.";
RL J. Exp. Med. 199:369-379(2004).
RN [13]
RP IDENTIFICATION IN A COMPLEX WITH ARL3 AND RP2.
RX PubMed=18588884; DOI=10.1016/j.febslet.2008.05.053;
RA Veltel S., Kravchenko A., Ismail S., Wittinghofer A.;
RT "Specificity of Arl2/Arl3 signaling is mediated by a ternary Arl3-effector-
RT GAP complex.";
RL FEBS Lett. 582:2501-2507(2008).
RN [14]
RP INTERACTION WITH CD44, IDENTIFICATION IN A COMPLEX WITH ABL1; ABL2 AND CRK,
RP AND FUNCTION IN SHIGELLA FLEXNERI UPTAKE.
RX PubMed=19381274; DOI=10.1371/journal.pone.0005211;
RA Vepachedu R., Karim Z., Patel O., Goplen N., Alam R.;
RT "Unc119 protects from Shigella infection by inhibiting the Abl family
RT kinases.";
RL PLoS ONE 4:E5211-E5211(2009).
RN [15]
RP FUNCTION, LIPID-BINDING, AND INTERACTION WITH NPHP3; CYS1 AND MACIR.
RX PubMed=22085962; DOI=10.1101/gad.173443.111;
RA Wright K.J., Baye L.M., Olivier-Mason A., Mukhopadhyay S., Sang L.,
RA Kwong M., Wang W., Pretorius P.R., Sheffield V.C., Sengupta P.,
RA Slusarski D.C., Jackson P.K.;
RT "An ARL3-UNC119-RP2 GTPase cycle targets myristoylated NPHP3 to the primary
RT cilium.";
RL Genes Dev. 25:2347-2360(2011).
RN [16]
RP SUBCELLULAR LOCATION, INTERACTION WITH FYN AND RAB11A, AND FUNCTION IN
RP ACTIVATION OF FYN.
RX PubMed=23535298; DOI=10.4161/cc.24404;
RA Lee Y., Chung S., Baek I.K., Lee T.H., Paik S.Y., Lee J.;
RT "UNC119a bridges the transmission of Fyn signals to Rab11, leading to the
RT completion of cytokinesis.";
RL Cell Cycle 12:1303-1315(2013).
RN [17]
RP PHOSPHORYLATION AT SER-37; SER-39 AND SER-41, MUTAGENESIS OF SER-37; SER-39
RP AND SER-41, AND INTERACTION WITH KLHL18.
RX PubMed=31696965; DOI=10.15252/embj.2018101409;
RA Chaya T., Tsutsumi R., Varner L.R., Maeda Y., Yoshida S., Furukawa T.;
RT "Cul3-Klhl18 ubiquitin ligase modulates rod transducin translocation during
RT light-dark adaptation.";
RL EMBO J. 2019:E101409-E101409(2019).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 56-240 IN COMPLEX WITH LAURYLATED
RP GNAT1, FUNCTION, AND INTERACTION WITH GNAT1.
RX PubMed=21642972; DOI=10.1038/nn.2835;
RA Zhang H., Constantine R., Vorobiev S., Chen Y., Seetharaman J., Huang Y.J.,
RA Xiao R., Montelione G.T., Gerstner C.D., Davis M.W., Inana G., Whitby F.G.,
RA Jorgensen E.M., Hill C.P., Tong L., Baehr W.;
RT "UNC119 is required for G protein trafficking in sensory neurons.";
RL Nat. Neurosci. 14:874-880(2011).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH ARL2 AND ARL3, AND
RP INTERACTION WITH ARL2 AND ARL3.
RX PubMed=22960633; DOI=10.1038/emboj.2012.257;
RA Ismail S.A., Chen Y.X., Miertzschke M., Vetter I.R., Koerner C.,
RA Wittinghofer A.;
RT "Structural basis for Arl3-specific release of myristoylated ciliary cargo
RT from UNC119.";
RL EMBO J. 31:4085-4094(2012).
RN [20]
RP VARIANT IMD13 VAL-22, AND CHARACTERIZATION OF VARIANT IMD13 VAL-22.
RX PubMed=22184408; DOI=10.1182/blood-2011-04-350686;
RA Gorska M.M., Alam R.;
RT "A mutation in the human Uncoordinated 119 gene impairs TCR signaling and
RT is associated with CD4 lymphopenia.";
RL Blood 119:1399-1406(2012).
RN [21]
RP INTERACTION WITH ARL2.
RX PubMed=30945270; DOI=10.1111/cge.13541;
RA Cai X.B., Wu K.C., Zhang X., Lv J.N., Jin G.H., Xiang L., Chen J.,
RA Huang X.F., Pan D., Lu B., Lu F., Qu J., Jin Z.B.;
RT "Whole-exome sequencing identified ARL2 as a novel candidate gene for MRCS
RT (microcornea, rod-cone dystrophy, cataract, and posterior staphyloma)
RT syndrome.";
RL Clin. Genet. 96:61-71(2019).
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:0000269|PubMed:12496276, ECO:0000269|PubMed:14757743,
CC ECO:0000269|PubMed:19381274, ECO:0000269|PubMed:21642972,
CC ECO:0000269|PubMed:22085962, ECO:0000269|PubMed:23535298,
CC ECO:0000305|PubMed:22960633}.
CC -!- SUBUNIT: Interacts with CABP4; in the absence of calcium (By
CC similarity). Interacts with DNM1; leading to a decrease of DNM1 GTPase
CC activity (By similarity). May interact with GTP-bound ARL1. Interacts
CC with ARL2 and ARL3 (GTP-bound forms); this promotes the release of
CC myyristoylated cargo proteins (PubMed:22960633, PubMed:30945270). Found
CC in a complex with ARL3, RP2 and UNC119; RP2 induces hydrolysis of GTP
CC ARL3 in the complex, leading to the release of UNC119. Interacts with
CC NPHP3 (when myristoylated). Interacts with CYS1 (when myristoylated).
CC Interacts with MACIR; interaction only takes place when UNC119 is not
CC liganded with myristoylated proteins. Interacts with LCK; this
CC interaction plays a crucial role in activation of LCK. Interacts with
CC FYN. Interacts with RAB11A; in a cell cycle-dependent manner. Interacts
CC with LYN (via SH2 and SH3 domains); leading to LYN activation. Found in
CC a complex with ABL1, ABL2, CRK and UNC119; leading to the inhibition of
CC CRK phosphorylation by ABL kinases. Interacts with CD44; leading to
CC Shigella invasion. Interacts with KLHL18 (via kelch repeats)
CC (PubMed:31696965). Interacts with PPP3CA, PPP3CB and PPP3CC (By
CC similarity). {ECO:0000250|UniProtKB:Q9Z2R6,
CC ECO:0000269|PubMed:11303027, ECO:0000269|PubMed:12496276,
CC ECO:0000269|PubMed:14757743, ECO:0000269|PubMed:18588884,
CC ECO:0000269|PubMed:19381274, ECO:0000269|PubMed:21642972,
CC ECO:0000269|PubMed:22085962, ECO:0000269|PubMed:22960633,
CC ECO:0000269|PubMed:23535298, ECO:0000269|PubMed:30945270,
CC ECO:0000269|PubMed:31696965}.
CC -!- INTERACTION:
CC Q13432; A2BDD9: AMOT; NbExp=3; IntAct=EBI-711260, EBI-17286414;
CC Q13432; Q4VCS5-2: AMOT; NbExp=3; IntAct=EBI-711260, EBI-3891843;
CC Q13432; Q9NXU5: ARL15; NbExp=4; IntAct=EBI-711260, EBI-711759;
CC Q13432; P36404: ARL2; NbExp=11; IntAct=EBI-711260, EBI-752365;
CC Q13432; P36405: ARL3; NbExp=15; IntAct=EBI-711260, EBI-712710;
CC Q13432; Q96GX8: C16orf74; NbExp=4; IntAct=EBI-711260, EBI-745814;
CC Q13432; R4GN89: C16orf74; NbExp=3; IntAct=EBI-711260, EBI-10225238;
CC Q13432; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-711260, EBI-11749135;
CC Q13432; Q9BYQ3: KRTAP9-3; NbExp=3; IntAct=EBI-711260, EBI-1043191;
CC Q13432; Q9BYQ0: KRTAP9-8; NbExp=3; IntAct=EBI-711260, EBI-11958364;
CC Q13432; Q5T3J3: LRIF1; NbExp=3; IntAct=EBI-711260, EBI-473196;
CC Q13432; Q7Z494: NPHP3; NbExp=3; IntAct=EBI-711260, EBI-2804263;
CC Q13432; Q08209-2: PPP3CA; NbExp=5; IntAct=EBI-711260, EBI-11959013;
CC Q13432; P48454: PPP3CC; NbExp=3; IntAct=EBI-711260, EBI-2827192;
CC Q13432; Q6ZRY4: RBPMS2; NbExp=3; IntAct=EBI-711260, EBI-11987469;
CC Q13432; Q9UKA8: RCAN3; NbExp=3; IntAct=EBI-711260, EBI-9091952;
CC Q13432; Q86VY9: TMEM200A; NbExp=3; IntAct=EBI-711260, EBI-11732844;
CC Q13432; Q96A56: TP53INP1; NbExp=3; IntAct=EBI-711260, EBI-9986117;
CC Q13432; Q9D0J4: Arl2; Xeno; NbExp=2; IntAct=EBI-711260, EBI-1033319;
CC Q13432; Q9WUL7: Arl3; Xeno; NbExp=3; IntAct=EBI-711260, EBI-6860857;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:23535298}. Cytoplasm,
CC cytoskeleton, spindle pole {ECO:0000269|PubMed:23535298}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:23535298}. Note=Localizes to
CC the centrosome in interphase cells and begins to translocate from the
CC spindle pole to the spindle midzone after the onset of mitosis; it then
CC localizes to the intercellular bridge in telophase cells and to the
CC midbody in cytokinetic cells. {ECO:0000269|PubMed:23535298}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=Q13432-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q13432-2; Sequence=VSP_004545;
CC -!- TISSUE SPECIFICITY: Abundantly expressed in retina, in photoreceptor
CC synapses and inner segments. Expressed in a much lesser extent in
CC several other tissues. {ECO:0000269|PubMed:9761287}.
CC -!- DOMAIN: Adopts an immunoglobulin-like beta-sandwich fold forming a
CC hydrophobic cavity that captures N-terminally myristoylated target
CC peptides (PubMed:21642972). Phe residues within the hydrophobic beta
CC sandwich are required for myristate binding (PubMed:22085962).
CC {ECO:0000269|PubMed:21642972, ECO:0000269|PubMed:22085962}.
CC -!- PTM: Phosphorylation suppresses its interaction with KLHL18 and down-
CC regulates its KLHL18-mediated degradation (PubMed:31696965).
CC Phosphorylated more under light conditions than dark conditions
CC (PubMed:31696965). Dephosphorylated by calcineurin (PubMed:31696965).
CC {ECO:0000269|PubMed:31696965}.
CC -!- DISEASE: Note=Defects in UNC119 may be a cause of cone-rod dystrophy. A
CC mutation was found in a 57-year-old woman with late-onset cone-rod
CC dystrophy: from 40 year old, the patient suffered from poor night
CC vision, defective color vision and light-sensitivity. At 57 year old,
CC she displayed reduced visual acuity, myopa, macular atrophy and
CC pericentral ring scotomas. The disease was caused by a heterozygous
CC mutation causing premature termination and truncated UNC119 protein
CC with dominant-negative effect. {ECO:0000269|PubMed:11006213}.
CC -!- DISEASE: Immunodeficiency 13 (IMD13) [MIM:615518]: A rare and
CC heterogeneous syndrome defined by a reproducible reduction in the CD4
CC T-lymphocyte count (less than 300 cells per microliter or less than 20%
CC of total T-cells) in the absence of HIV infection or other known causes
CC of immunodeficiency. IMD13 predisposes to infections and malignancy.
CC {ECO:0000269|PubMed:22184408}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the PDE6D/unc-119 family. {ECO:0000305}.
CC -!- CAUTION: According to some authors, acts by extracting target proteins
CC from membranes (PubMed:21642972). According to a another report, rather
CC acts by targeting proteins to membranes (PubMed:22085962).
CC {ECO:0000305|PubMed:21642972, ECO:0000305|PubMed:22085962}.
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DR EMBL; U40998; AAC50360.1; -; mRNA.
DR EMBL; AF028788; AAD01875.1; -; mRNA.
DR EMBL; AF028789; AAD01876.1; -; mRNA.
DR EMBL; AF125998; AAD31422.1; -; Genomic_DNA.
DR EMBL; AF125997; AAD31422.1; JOINED; Genomic_DNA.
DR EMBL; AK292329; BAF85018.1; -; mRNA.
DR EMBL; AB593014; BAJ83969.1; -; mRNA.
DR EMBL; AC005726; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471159; EAW51095.1; -; Genomic_DNA.
DR EMBL; BC027176; AAH27176.1; -; mRNA.
DR CCDS; CCDS11233.1; -. [Q13432-1]
DR CCDS; CCDS11234.1; -. [Q13432-2]
DR RefSeq; NP_001317095.1; NM_001330166.1.
DR RefSeq; NP_005139.1; NM_005148.3. [Q13432-1]
DR RefSeq; NP_473376.1; NM_054035.2. [Q13432-2]
DR PDB; 3GQQ; X-ray; 1.95 A; A/B/C/D/E/F=56-240.
DR PDB; 3RBQ; X-ray; 2.00 A; A/B/C/D/E/F=56-240.
DR PDB; 4GOJ; X-ray; 2.10 A; C/D=1-240.
DR PDB; 4GOK; X-ray; 2.60 A; C/G=1-240.
DR PDB; 5L7K; X-ray; 2.10 A; A/G=58-237.
DR PDB; 6H6A; X-ray; 2.00 A; D/G/J=59-240.
DR PDBsum; 3GQQ; -.
DR PDBsum; 3RBQ; -.
DR PDBsum; 4GOJ; -.
DR PDBsum; 4GOK; -.
DR PDBsum; 5L7K; -.
DR PDBsum; 6H6A; -.
DR AlphaFoldDB; Q13432; -.
DR SMR; Q13432; -.
DR BioGRID; 114548; 150.
DR DIP; DIP-42697N; -.
DR IntAct; Q13432; 124.
DR MINT; Q13432; -.
DR STRING; 9606.ENSP00000337040; -.
DR GuidetoPHARMACOLOGY; 3011; -.
DR iPTMnet; Q13432; -.
DR MetOSite; Q13432; -.
DR PhosphoSitePlus; Q13432; -.
DR BioMuta; UNC119; -.
DR DMDM; 2498854; -.
DR EPD; Q13432; -.
DR jPOST; Q13432; -.
DR MassIVE; Q13432; -.
DR MaxQB; Q13432; -.
DR PaxDb; Q13432; -.
DR PeptideAtlas; Q13432; -.
DR PRIDE; Q13432; -.
DR ProteomicsDB; 59426; -. [Q13432-1]
DR ProteomicsDB; 59427; -. [Q13432-2]
DR Antibodypedia; 26315; 58 antibodies from 22 providers.
DR DNASU; 9094; -.
DR Ensembl; ENST00000301032.8; ENSP00000301032.4; ENSG00000109103.12. [Q13432-2]
DR Ensembl; ENST00000335765.9; ENSP00000337040.3; ENSG00000109103.12. [Q13432-1]
DR GeneID; 9094; -.
DR KEGG; hsa:9094; -.
DR MANE-Select; ENST00000335765.9; ENSP00000337040.3; NM_005148.4; NP_005139.1.
DR UCSC; uc002hbk.3; human. [Q13432-1]
DR CTD; 9094; -.
DR DisGeNET; 9094; -.
DR GeneCards; UNC119; -.
DR HGNC; HGNC:12565; UNC119.
DR HPA; ENSG00000109103; Tissue enriched (retina).
DR MalaCards; UNC119; -.
DR MIM; 604011; gene.
DR MIM; 615518; phenotype.
DR neXtProt; NX_Q13432; -.
DR OpenTargets; ENSG00000109103; -.
DR Orphanet; 1872; Cone rod dystrophy.
DR Orphanet; 228000; Idiopathic CD4 lymphocytopenia.
DR PharmGKB; PA37202; -.
DR VEuPathDB; HostDB:ENSG00000109103; -.
DR eggNOG; KOG4037; Eukaryota.
DR GeneTree; ENSGT00390000014595; -.
DR InParanoid; Q13432; -.
DR OMA; CNSADMG; -.
DR OrthoDB; 1270912at2759; -.
DR PhylomeDB; Q13432; -.
DR TreeFam; TF314474; -.
DR PathwayCommons; Q13432; -.
DR SignaLink; Q13432; -.
DR BioGRID-ORCS; 9094; 57 hits in 1080 CRISPR screens.
DR ChiTaRS; UNC119; human.
DR EvolutionaryTrace; Q13432; -.
DR GeneWiki; Protein_unc-119_homolog; -.
DR GenomeRNAi; 9094; -.
DR Pharos; Q13432; Tchem.
DR PRO; PR:Q13432; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q13432; protein.
DR Bgee; ENSG00000109103; Expressed in granulocyte and 153 other tissues.
DR ExpressionAtlas; Q13432; baseline and differential.
DR Genevisible; Q13432; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:ProtInc.
DR GO; GO:0045171; C:intercellular bridge; IDA:UniProtKB.
DR GO; GO:0051233; C:spindle midzone; IDA:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0008289; F:lipid binding; IDA:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0042953; P:lipoprotein transport; IDA:UniProtKB.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP: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:0007602; P:phototransduction; TAS:ProtInc.
DR GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; IMP:UniProtKB.
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 3D-structure; Alternative splicing; Cone-rod dystrophy; Cytoplasm;
KW Cytoskeleton; Disease variant; 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_0000221212"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1..59
FT /note="Required for midbody localization"
FT REGION 121..240
FT /note="Required for centrosome localization"
FT COMPBIAS 16..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 131
FT /ligand="tetradecanoate"
FT /ligand_id="ChEBI:CHEBI:30807"
FT MOD_RES 37
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:31696965"
FT MOD_RES 39
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:31696965"
FT MOD_RES 41
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:31696965"
FT VAR_SEQ 204..240
FT /note="ISEMIRHPYETQSDSFYFVDDRLVMHNKADYSYSGTP -> SARAGSSGSGE
FT VGASRD (in isoform B)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:21697133, ECO:0000303|PubMed:9761287"
FT /id="VSP_004545"
FT VARIANT 22
FT /note="G -> V (in IMD13; impairs interaction with LCK;
FT impairs LCK activation; induces LCK mislocalization;
FT dbSNP:rs199714731)"
FT /evidence="ECO:0000269|PubMed:22184408"
FT /id="VAR_071184"
FT MUTAGEN 29..32
FT /note="PQPP->AQPA: Impairs interaction with LCK."
FT /evidence="ECO:0000269|PubMed:14757743"
FT MUTAGEN 37
FT /note="S->A: Loss of phosphorylation; when associated with
FT A-39 and A-41."
FT /evidence="ECO:0000269|PubMed:31696965"
FT MUTAGEN 39
FT /note="S->A: Loss of phosphorylation; when associated with
FT A-37 and A-41."
FT /evidence="ECO:0000269|PubMed:31696965"
FT MUTAGEN 41
FT /note="S->A: Loss of phosphorylation; when associated with
FT A-37 and A-39."
FT /evidence="ECO:0000269|PubMed:31696965"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:3GQQ"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:3GQQ"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:3GQQ"
FT STRAND 87..95
FT /evidence="ECO:0007829|PDB:3GQQ"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:3GQQ"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:3GQQ"
FT TURN 123..127
FT /evidence="ECO:0007829|PDB:6H6A"
FT STRAND 128..132
FT /evidence="ECO:0007829|PDB:3GQQ"
FT HELIX 135..139
FT /evidence="ECO:0007829|PDB:3GQQ"
FT STRAND 141..150
FT /evidence="ECO:0007829|PDB:3GQQ"
FT STRAND 158..167
FT /evidence="ECO:0007829|PDB:3GQQ"
FT STRAND 170..178
FT /evidence="ECO:0007829|PDB:3GQQ"
FT STRAND 186..195
FT /evidence="ECO:0007829|PDB:3GQQ"
FT HELIX 201..209
FT /evidence="ECO:0007829|PDB:3GQQ"
FT STRAND 214..222
FT /evidence="ECO:0007829|PDB:3GQQ"
FT STRAND 225..235
FT /evidence="ECO:0007829|PDB:3GQQ"
SQ SEQUENCE 240 AA; 26962 MW; 22FD19C3518A4446 CRC64;
MKVKKGGGGA GTATESAPGP SGQSVAPIPQ PPAESESGSE SEPDAGPGPR PGPLQRKQPI
GPEDVLGLQR ITGDYLCSPE ENIYKIDFVR FKIRDMDSGT VLFEIKKPPV SERLPINRRD
LDPNAGRFVR YQFTPAFLRL RQVGATVEFT VGDKPVNNFR MIERHYFRNQ LLKSFDFHFG
FCIPSSKNTC EHIYDFPPLS EELISEMIRH PYETQSDSFY FVDDRLVMHN KADYSYSGTP
