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Protein unc-119 homolog A (Retinal protein 4) (hRG4)

 U119A_HUMAN             Reviewed;         240 AA.
Q13432; A8K8G4; F1T095; O95126;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
22-NOV-2017, entry version 144.
RecName: Full=Protein unc-119 homolog A;
AltName: Full=Retinal protein 4;
Short=hRG4;
Name=UNC119; Synonyms=RG4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
TISSUE=Retina;
PubMed=8576185; DOI=10.1074/jbc.271.3.1797;
Higashide T., Murakami A., McLaren M.J., Inana G.;
"Cloning of the cDNA for a novel photoreceptor protein.";
J. Biol. Chem. 271:1797-1804(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), AND TISSUE SPECIFICITY.
TISSUE=Retina;
PubMed=9761287;
Swanson D.A., Chang J.T., Campochiaro P.A., Zack D.J., Valle D.;
"Mammalian orthologs of C. elegans unc-119 highly expressed in
photoreceptors.";
Invest. Ophthalmol. Vis. Sci. 39:2085-2094(1998).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A).
PubMed=10329014; DOI=10.1006/geno.1999.5791;
Higashide T., Inana G.;
"Characterization of the gene for HRG4 (UNC119), a novel photoreceptor
synaptic protein homologous to unc-119.";
Genomics 57:446-450(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
TISSUE=Retinoblastoma;
PubMed=21697133; DOI=10.1167/iovs.11-7479;
Oshikawa M., Tsutsui C., Ikegami T., Fuchida Y., Matsubara M.,
Toyama S., Usami R., Ohtoko K., Kato S.;
"Full-length transcriptome analysis of human retina-derived cell lines
ARPE-19 and Y79 using the vector-capping method.";
Invest. Ophthalmol. Vis. Sci. 52:6662-6670(2011).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
TISSUE=Lymph;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
INVOLVEMENT IN CONE-ROD DYSTROPHY.
PubMed=11006213;
Kobayashi A., Higashide T., Hamasaki D., Kubota S., Sakuma H., An W.,
Fujimaki T., McLaren M.J., Weleber R.G., Inana G.;
"HRG4 (UNC119) mutation found in cone-rod dystrophy causes retinal
degeneration in a transgenic model.";
Invest. Ophthalmol. Vis. Sci. 41:3268-3277(2000).
[10]
INTERACTION WITH ARL1; ARL2 AND ARL3.
PubMed=11303027; DOI=10.1074/jbc.M102359200;
Van Valkenburgh H., Shern J.F., Sharer J.D., Zhu X., Kahn R.A.;
"ADP-ribosylation factors (ARFs) and ARF-like 1 (ARL1) have both
specific and shared effectors: characterizing ARL1-binding proteins.";
J. Biol. Chem. 276:22826-22837(2001).
[11]
INTERACTION WITH LYN, AND FUNCTION IN LYN ACTIVATION.
PubMed=12496276; DOI=10.1074/jbc.M208261200;
Cen O., Gorska M.M., Stafford S.J., Sur S., Alam R.;
"Identification of UNC119 as a novel activator of SRC-type tyrosine
kinases.";
J. Biol. Chem. 278:8837-8845(2003).
[12]
INTERACTION WITH LCK AND FYN, FUNCTION IN LCK AND FYN ACTIVATION, AND
MUTAGENESIS OF 29-PRO--PRO-32.
PubMed=14757743; DOI=10.1084/jem.20030589;
Gorska M.M., Stafford S.J., Cen O., Sur S., Alam R.;
"Unc119, a novel activator of Lck/Fyn, is essential for T cell
activation.";
J. Exp. Med. 199:369-379(2004).
[13]
IDENTIFICATION IN A COMPLEX WITH ARL3 AND RP2.
PubMed=18588884; DOI=10.1016/j.febslet.2008.05.053;
Veltel S., Kravchenko A., Ismail S., Wittinghofer A.;
"Specificity of Arl2/Arl3 signaling is mediated by a ternary Arl3-
effector-GAP complex.";
FEBS Lett. 582:2501-2507(2008).
[14]
INTERACTION WITH CD44, IDENTIFICATION IN A COMPLEX WITH ABL1; ABL2 AND
CRK, AND FUNCTION IN SHIGELLA FLEXNERI UPTAKE.
PubMed=19381274; DOI=10.1371/journal.pone.0005211;
Vepachedu R., Karim Z., Patel O., Goplen N., Alam R.;
"Unc119 protects from Shigella infection by inhibiting the Abl family
kinases.";
PLoS ONE 4:E5211-E5211(2009).
[15]
FUNCTION, LIPID-BINDING, AND INTERACTION WITH NPHP3; CYS1 AND C5ORF30.
PubMed=22085962; DOI=10.1101/gad.173443.111;
Wright K.J., Baye L.M., Olivier-Mason A., Mukhopadhyay S., Sang L.,
Kwong M., Wang W., Pretorius P.R., Sheffield V.C., Sengupta P.,
Slusarski D.C., Jackson P.K.;
"An ARL3-UNC119-RP2 GTPase cycle targets myristoylated NPHP3 to the
primary cilium.";
Genes Dev. 25:2347-2360(2011).
[16]
SUBCELLULAR LOCATION, INTERACTION WITH FYN AND RAB11A, AND FUNCTION IN
ACTIVATION OF FYN.
PubMed=23535298; DOI=10.4161/cc.24404;
Lee Y., Chung S., Baek I.K., Lee T.H., Paik S.Y., Lee J.;
"UNC119a bridges the transmission of Fyn signals to Rab11, leading to
the completion of cytokinesis.";
Cell Cycle 12:1303-1315(2013).
[17]
X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 56-240 IN COMPLEX WITH
LAURYLATED GNAT1, FUNCTION, AND INTERACTION WITH GNAT1.
PubMed=21642972; DOI=10.1038/nn.2835;
Zhang H., Constantine R., Vorobiev S., Chen Y., Seetharaman J.,
Huang Y.J., Xiao R., Montelione G.T., Gerstner C.D., Davis M.W.,
Inana G., Whitby F.G., Jorgensen E.M., Hill C.P., Tong L., Baehr W.;
"UNC119 is required for G protein trafficking in sensory neurons.";
Nat. Neurosci. 14:874-880(2011).
[18]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH ARL2 AND ARL3,
AND INTERACTION WITH ARL2 AND ARL3.
PubMed=22960633; DOI=10.1038/emboj.2012.257;
Ismail S.A., Chen Y.X., Miertzschke M., Vetter I.R., Koerner C.,
Wittinghofer A.;
"Structural basis for Arl3-specific release of myristoylated ciliary
cargo from UNC119.";
EMBO J. 31:4085-4094(2012).
[19]
VARIANT IMD13 VAL-22, AND CHARACTERIZATION OF VARIANT IMD13 VAL-22.
PubMed=22184408; DOI=10.1182/blood-2011-04-350686;
Gorska M.M., Alam R.;
"A mutation in the human Uncoordinated 119 gene impairs TCR signaling
and is associated with CD4 lymphopenia.";
Blood 119:1399-1406(2012).
-!- FUNCTION: Involved in synaptic functions in photoreceptor cells,
the signal transduction in immune cells as a Src family kinase
activator, endosome recycling, the uptake of bacteria and
endocytosis, protein trafficking in sensory neurons and as lipid-
binding chaperone with specificity for a diverse subset of
myristoylated proteins. Specifically binds the myristoyl moiety of
a subset of N-terminally myristoylated proteins and is required
for their localization. Binds myristoylated GNAT1 and is required
for G-protein localization and trafficking in sensory neurons.
Probably plays a role in trafficking proteins in photoreceptor
cells. Plays important roles in mediating Src family kinase
signals for the completion of cytokinesis via RAB11A.
{ECO:0000269|PubMed:12496276, ECO:0000269|PubMed:14757743,
ECO:0000269|PubMed:19381274, ECO:0000269|PubMed:21642972,
ECO:0000269|PubMed:22085962, ECO:0000269|PubMed:23535298,
ECO:0000305|PubMed:22960633}.
-!- SUBUNIT: Interacts with CABP4; in the absence of calcium (By
similarity). Interacts with DNM1; leading to a decrease of DNM1
GTPase activity (By similarity). May interact with GTP-bound ARL1.
Interacts with ARL2 and ARL3 (GTP-bound forms); this promotes the
release of myyristoylated cargo proteins (PubMed:22960633). Found
in a complex with ARL3, RP2 and UNC119; RP2 induces hydrolysis of
GTP ARL3 in the complex, leading to the release of UNC119.
Interacts with NPHP3 (when myristoylated). Interacts with CYS1
(when myristoylated). Interacts with C5orf30; interaction only
takes place when UNC119 is not liganded with myristoylated
proteins. Interacts with LCK; this interaction plays a crucial
role in activation of LCK. Interacts with FYN. Interacts with
RAB11A; in a cell cycle-dependent manner. Interacts with LYN (via
SH2 and SH3 domains); leading to LYN activation. Found in a
complex with ABL1, ABL2, CRK and UNC119; leading to the inhibition
of CRK phosphorylation by ABL kinases. Interacts with CD44;
leading to Shigella invasion. {ECO:0000250|UniProtKB:Q9Z2R6,
ECO:0000269|PubMed:11303027, ECO:0000269|PubMed:12496276,
ECO:0000269|PubMed:14757743, ECO:0000269|PubMed:18588884,
ECO:0000269|PubMed:19381274, ECO:0000269|PubMed:21642972,
ECO:0000269|PubMed:22085962, ECO:0000269|PubMed:22960633,
ECO:0000269|PubMed:23535298}.
-!- INTERACTION:
Q4VCS5-2:AMOT; NbExp=5; IntAct=EBI-711260, EBI-3891843;
P36404:ARL2; NbExp=8; IntAct=EBI-711260, EBI-752365;
Q9D0J4:Arl2 (xeno); NbExp=2; IntAct=EBI-711260, EBI-1033319;
P36405:ARL3; NbExp=11; IntAct=EBI-711260, EBI-712710;
Q9WUL7:Arl3 (xeno); NbExp=3; IntAct=EBI-711260, EBI-6860857;
R4GN89:C16orf74; NbExp=3; IntAct=EBI-711260, EBI-10225238;
Q7Z494:NPHP3; NbExp=3; IntAct=EBI-711260, EBI-2804263;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome {ECO:0000269|PubMed:23535298}.
Cytoplasm, cytoskeleton, spindle pole
{ECO:0000269|PubMed:23535298}. Cytoplasm, cytoskeleton, spindle
{ECO:0000269|PubMed:23535298}. Note=Localizes to the centrosome in
interphase cells and begins to translocate from the spindle pole
to the spindle midzone after the onset of mitosis; it then
localizes to the intercellular bridge in telophase cells and to
the midbody in cytokinetic cells. {ECO:0000269|PubMed:23535298}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=A;
IsoId=Q13432-1; Sequence=Displayed;
Name=B;
IsoId=Q13432-2; Sequence=VSP_004545;
-!- TISSUE SPECIFICITY: Abundantly expressed in retina, in
photoreceptor synapses and inner segments. Expressed in a much
lesser extent in several other tissues.
{ECO:0000269|PubMed:9761287}.
-!- DOMAIN: Adopts an immunoglobulin-like beta-sandwich fold forming a
hydrophobic cavity that captures N-terminally myristoylated target
peptides (PubMed:21642972). Phe residues within the hydrophobic
beta sandwich are required for myristate binding
(PubMed:22085962). {ECO:0000269|PubMed:21642972,
ECO:0000269|PubMed:22085962}.
-!- DISEASE: Note=Defects in UNC119 may be a cause of cone-rod
dystrophy. A mutation was found in a 57-year-old woman with late-
onset cone-rod dystrophy: from 40 year old, the patient suffered
from poor night vision, defective color vision and light-
sensitivity. At 57 year old, she displayed reduced visual acuity,
myopa, macular atrophy and pericentral ring scotomas. The disease
was caused by a heterozygous mutation causing premature
termination and truncated UNC119 protein with dominant-negative
effect. {ECO:0000269|PubMed:11006213}.
-!- DISEASE: Immunodeficiency 13 (IMD13) [MIM:615518]: A rare and
heterogeneous syndrome defined by a reproducible reduction in the
CD4 T-lymphocyte count (less than 300 cells per microliter or less
than 20% of total T-cells) in the absence of HIV infection or
other known causes of immunodeficiency. IMD13 predisposes to
infections and malignancy. {ECO:0000269|PubMed:22184408}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the PDE6D/unc-119 family. {ECO:0000305}.
-!- CAUTION: According to some authors, acts by extracting target
proteins from membranes (PubMed:21642972). According to a another
report, rather acts by targeting proteins to membranes
(PubMed:22085962). {ECO:0000305|PubMed:21642972,
ECO:0000305|PubMed:22085962}.
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EMBL; U40998; AAC50360.1; -; mRNA.
EMBL; AF028788; AAD01875.1; -; mRNA.
EMBL; AF028789; AAD01876.1; -; mRNA.
EMBL; AF125998; AAD31422.1; -; Genomic_DNA.
EMBL; AF125997; AAD31422.1; JOINED; Genomic_DNA.
EMBL; AK292329; BAF85018.1; -; mRNA.
EMBL; AB593014; BAJ83969.1; -; mRNA.
EMBL; AC005726; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471159; EAW51095.1; -; Genomic_DNA.
EMBL; BC027176; AAH27176.1; -; mRNA.
CCDS; CCDS11233.1; -. [Q13432-1]
CCDS; CCDS11234.1; -. [Q13432-2]
RefSeq; NP_001317095.1; NM_001330166.1.
RefSeq; NP_005139.1; NM_005148.3. [Q13432-1]
RefSeq; NP_473376.1; NM_054035.2. [Q13432-2]
UniGene; Hs.410455; -.
PDB; 3GQQ; X-ray; 1.95 A; A/B/C/D/E/F=56-240.
PDB; 3RBQ; X-ray; 2.00 A; A/B/C/D/E/F=56-240.
PDB; 4GOJ; X-ray; 2.10 A; C/D=1-240.
PDB; 4GOK; X-ray; 2.60 A; C/G=1-240.
PDB; 5L7K; X-ray; 2.10 A; A/G=58-237.
PDBsum; 3GQQ; -.
PDBsum; 3RBQ; -.
PDBsum; 4GOJ; -.
PDBsum; 4GOK; -.
PDBsum; 5L7K; -.
ProteinModelPortal; Q13432; -.
SMR; Q13432; -.
BioGrid; 114548; 120.
DIP; DIP-42697N; -.
IntAct; Q13432; 96.
MINT; MINT-1372196; -.
STRING; 9606.ENSP00000337040; -.
iPTMnet; Q13432; -.
PhosphoSitePlus; Q13432; -.
BioMuta; UNC119; -.
DMDM; 2498854; -.
EPD; Q13432; -.
MaxQB; Q13432; -.
PaxDb; Q13432; -.
PeptideAtlas; Q13432; -.
PRIDE; Q13432; -.
DNASU; 9094; -.
Ensembl; ENST00000301032; ENSP00000301032; ENSG00000109103. [Q13432-2]
Ensembl; ENST00000335765; ENSP00000337040; ENSG00000109103. [Q13432-1]
GeneID; 9094; -.
KEGG; hsa:9094; -.
UCSC; uc002hbk.3; human. [Q13432-1]
CTD; 9094; -.
DisGeNET; 9094; -.
EuPathDB; HostDB:ENSG00000109103.11; -.
GeneCards; UNC119; -.
HGNC; HGNC:12565; UNC119.
HPA; HPA041912; -.
MalaCards; UNC119; -.
MIM; 604011; gene.
MIM; 615518; phenotype.
neXtProt; NX_Q13432; -.
OpenTargets; ENSG00000109103; -.
Orphanet; 1872; Cone rod dystrophy.
Orphanet; 228000; Idiopathic CD4 lymphocytopenia.
PharmGKB; PA37202; -.
eggNOG; KOG4037; Eukaryota.
eggNOG; ENOG410YJ3E; LUCA.
GeneTree; ENSGT00390000014595; -.
HOGENOM; HOG000258286; -.
HOVERGEN; HBG108625; -.
InParanoid; Q13432; -.
OMA; YKIDFIR; -.
OrthoDB; EOG091G0J2K; -.
PhylomeDB; Q13432; -.
TreeFam; TF314474; -.
ChiTaRS; UNC119; human.
EvolutionaryTrace; Q13432; -.
GeneWiki; Protein_unc-119_homolog; -.
GenomeRNAi; 9094; -.
PRO; PR:Q13432; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000109103; -.
CleanEx; HS_UNC119; -.
ExpressionAtlas; Q13432; baseline and differential.
Genevisible; Q13432; HS.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:ProtInc.
GO; GO:0045171; C:intercellular bridge; IDA:UniProtKB.
GO; GO:0051233; C:spindle midzone; IDA:UniProtKB.
GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
GO; GO:0008289; F:lipid binding; IDA:UniProtKB.
GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
GO; GO:0042953; P:lipoprotein transport; IDA:UniProtKB.
GO; GO:0000281; P:mitotic cytokinesis; IMP:UniProtKB.
GO; GO:2001287; P:negative regulation of caveolin-mediated endocytosis; ISS:UniProtKB.
GO; GO:1900186; P:negative regulation of clathrin-dependent endocytosis; ISS:UniProtKB.
GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
GO; GO:0007602; P:phototransduction; TAS:ProtInc.
GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; IMP:UniProtKB.
GO; GO:0007601; P:visual perception; TAS:ProtInc.
Gene3D; 2.70.50.40; -; 1.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR008015; PDED_dom.
InterPro; IPR037036; PDED_dom_sf.
InterPro; IPR032977; UNC119_homologue_A.
PANTHER; PTHR12951:SF5; PTHR12951:SF5; 1.
Pfam; PF05351; GMP_PDE_delta; 1.
SUPFAM; SSF81296; SSF81296; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Cone-rod dystrophy; Cytoplasm; Cytoskeleton; Disease mutation;
Endocytosis; Lipid-binding; Phosphoprotein; Protein transport;
Reference proteome; Sensory transduction; Transport; Vision.
CHAIN 1 240 Protein unc-119 homolog A.
/FTId=PRO_0000221212.
REGION 1 59 Required for midbody localization.
REGION 121 240 Required for centrosome localization.
BINDING 131 131 Lipid.
MOD_RES 37 37 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Z2R6}.
MOD_RES 39 39 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Z2R6}.
MOD_RES 41 41 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Z2R6}.
VAR_SEQ 204 240 ISEMIRHPYETQSDSFYFVDDRLVMHNKADYSYSGTP ->
SARAGSSGSGEVGASRD (in isoform B).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:21697133,
ECO:0000303|PubMed:9761287}.
/FTId=VSP_004545.
VARIANT 22 22 G -> V (in IMD13; impairs interaction
with LCK; impairs LCK activation; induces
LCK mislocalization; dbSNP:rs199714731).
{ECO:0000269|PubMed:22184408}.
/FTId=VAR_071184.
MUTAGEN 29 32 PQPP->AQPA: Impairs interaction with LCK.
{ECO:0000269|PubMed:14757743}.
HELIX 62 64 {ECO:0000244|PDB:3GQQ}.
TURN 65 67 {ECO:0000244|PDB:3GQQ}.
HELIX 79 81 {ECO:0000244|PDB:3GQQ}.
STRAND 87 95 {ECO:0000244|PDB:3GQQ}.
TURN 96 98 {ECO:0000244|PDB:3GQQ}.
STRAND 101 106 {ECO:0000244|PDB:3GQQ}.
STRAND 128 132 {ECO:0000244|PDB:3GQQ}.
HELIX 135 139 {ECO:0000244|PDB:3GQQ}.
STRAND 141 150 {ECO:0000244|PDB:3GQQ}.
STRAND 158 167 {ECO:0000244|PDB:3GQQ}.
STRAND 170 178 {ECO:0000244|PDB:3GQQ}.
STRAND 186 195 {ECO:0000244|PDB:3GQQ}.
HELIX 201 209 {ECO:0000244|PDB:3GQQ}.
STRAND 214 222 {ECO:0000244|PDB:3GQQ}.
STRAND 225 235 {ECO:0000244|PDB:3GQQ}.
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


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