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Q13432 (U119A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein unc-119 homolog A
Alternative name(s):
Retinal protein 4
Short name=hRG4
Gene names
Name:UNC119
Synonyms:RG4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length240 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Myristoyl-binding protein that acts as a cargo adapter: 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. Binds myristoylated NPHP3; however, in contrast to UNC119B, does not seem to play a major role in ciliary membrane localization of NPHP3. Does not bind all myristoylated proteins. Probably plays a role in trafficking proteins in photoreceptor cells. Ref.12 Ref.13

Subunit structure

Interacts with CABP4; in the absence of calcium. May interact with ARL1, ARL2 and ARL3 GTP-bound forms. 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. Ref.10 Ref.11 Ref.12 Ref.13

Subcellular location

Cytoplasmcytoskeletonmicrotubule organizing centercentrosome Ref.12.

Tissue specificity

Retinal-specific. Localized in photoreceptor synapses in the outer plexiform layer of the retina.

Domain

Adopts an immunoglobulin-like beta-sandwich fold forming a hydrophobic cavity that capture N-terminally myristoylated target peptides (Ref.13). Phe residues within the hydrophobic beta sandwich are required for myristate binding (Ref.12).

Involvement in disease

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.

Sequence similarities

Belongs to the PDE6D/unc-119 family.

Caution

According to some authors, acts by extracting target proteins from membranes (Ref.13). According to a another report, rather acts by targeting proteins to membranes (Ref.12).

Ontologies

Keywords
   Biological processProtein transport
Sensory transduction
Transport
Vision
   Cellular componentCytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
   DiseaseCone-rod dystrophy
   LigandLipid-binding
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcytokinesis, completion of separation

Inferred from mutant phenotype PubMed 23535298. Source: UniProtKB

lipoprotein transport

Inferred from direct assay Ref.13Ref.12. Source: UniProtKB

negative regulation of caveolin-mediated endocytosis

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of clathrin-mediated endocytosis

Inferred from sequence or structural similarity. Source: UniProtKB

phototransduction

Traceable author statement PubMed 9538874. Source: ProtInc

positive regulation of protein tyrosine kinase activity

Inferred from mutant phenotype PubMed 14757743. Source: UniProtKB

synaptic transmission

Traceable author statement PubMed 9538874. Source: ProtInc

visual perception

Traceable author statement Ref.3. Source: ProtInc

   Cellular_componentcentrosome

Inferred from direct assay Ref.12PubMed 23535298. Source: UniProtKB

cytosol

Traceable author statement PubMed 9538874. Source: ProtInc

intercellular bridge

Inferred from direct assay PubMed 23535298. Source: UniProtKB

spindle midzone

Inferred from direct assay PubMed 23535298. Source: UniProtKB

spindle pole

Inferred from direct assay PubMed 23535298. Source: UniProtKB

   Molecular_functionlipid binding

Inferred from direct assay Ref.13Ref.12. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 14757743Ref.12PubMed 23535298. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ARL2P364042EBI-711260,EBI-752365
Arl2Q9D0J42EBI-711260,EBI-1033319From a different organism.
ARL3P364055EBI-711260,EBI-712710
Arl3Q9WUL73EBI-711260,EBI-6860857From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: Q13432-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform B (identifier: Q13432-2)

The sequence of this isoform differs from the canonical sequence as follows:
     204-240: ISEMIRHPYETQSDSFYFVDDRLVMHNKADYSYSGTP → SARAGSSGSGEVGASRD

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 240240Protein unc-119 homolog A
PRO_0000221212

Sites

Binding site1311Lipid

Amino acid modifications

Modified residue371Phosphoserine By similarity

Natural variations

Alternative sequence204 – 24037ISEMI…YSGTP → SARAGSSGSGEVGASRD in isoform B.
VSP_004545

Secondary structure

............................. 240
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform A [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 22FD19C3518A4446

FASTA24026,962
        10         20         30         40         50         60 
MKVKKGGGGA GTATESAPGP SGQSVAPIPQ PPAESESGSE SEPDAGPGPR PGPLQRKQPI 

        70         80         90        100        110        120 
GPEDVLGLQR ITGDYLCSPE ENIYKIDFVR FKIRDMDSGT VLFEIKKPPV SERLPINRRD 

       130        140        150        160        170        180 
LDPNAGRFVR YQFTPAFLRL RQVGATVEFT VGDKPVNNFR MIERHYFRNQ LLKSFDFHFG 

       190        200        210        220        230        240 
FCIPSSKNTC EHIYDFPPLS EELISEMIRH PYETQSDSFY FVDDRLVMHN KADYSYSGTP 

« Hide

Isoform B [UniParc].

Checksum: 70146298DD2628C7
Show »

FASTA22024,112

References

« Hide 'large scale' references
[1]"Cloning of the cDNA for a novel photoreceptor protein."
Higashide T., Murakami A., McLaren M.J., Inana G.
J. Biol. Chem. 271:1797-1804(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
Tissue: Retina.
[2]"Mammalian orthologs of C. elegans unc-119 highly expressed in photoreceptors."
Swanson D.A., Chang J.T., Campochiaro P.A., Zack D.J., Valle D.
Invest. Ophthalmol. Vis. Sci. 39:2085-2094(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
Tissue: Retina.
[3]"Characterization of the gene for HRG4 (UNC119), a novel photoreceptor synaptic protein homologous to unc-119."
Higashide T., Inana G.
Genomics 57:446-450(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A).
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
Tissue: Testis.
[5]"Full-length transcriptome analysis of human retina-derived cell lines ARPE-19 and Y79 using the vector-capping method."
Oshikawa M., Tsutsui C., Ikegami T., Fuchida Y., Matsubara M., Toyama S., Usami R., Ohtoko K., Kato S.
Invest. Ophthalmol. Vis. Sci. 52:6662-6670(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
Tissue: Retinoblastoma.
[6]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
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. expand/collapse author list , 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.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
Tissue: Lymph.
[9]"HRG4 (UNC119) mutation found in cone-rod dystrophy causes retinal degeneration in a transgenic model."
Kobayashi A., Higashide T., Hamasaki D., Kubota S., Sakuma H., An W., Fujimaki T., McLaren M.J., Weleber R.G., Inana G.
Invest. Ophthalmol. Vis. Sci. 41:3268-3277(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN CONE-ROD DYSTROPHY.
[10]"ADP-ribosylation factors (ARFs) and ARF-like 1 (ARL1) have both specific and shared effectors: characterizing ARL1-binding proteins."
Van Valkenburgh H., Shern J.F., Sharer J.D., Zhu X., Kahn R.A.
J. Biol. Chem. 276:22826-22837(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARL1; ARL2 AND ARL3.
[11]"Specificity of Arl2/Arl3 signaling is mediated by a ternary Arl3-effector-GAP complex."
Veltel S., Kravchenko A., Ismail S., Wittinghofer A.
FEBS Lett. 582:2501-2507(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH ARL3 AND RP2.
[12]"An ARL3-UNC119-RP2 GTPase cycle targets myristoylated NPHP3 to the primary cilium."
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.
Genes Dev. 25:2347-2360(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, LIPID-BINDING, SUBCELLULAR LOCATION, INTERACTION WITH NPHP3; CYS1 AND C5ORF30.
[13]"UNC119 is required for G protein trafficking in sensory neurons."
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.
Nat. Neurosci. 14:874-880(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 56-240 IN COMPLEX WITH LAURYLATED GNAT1, FUNCTION, INTERACTION WITH GNAT1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U40998 mRNA. Translation: AAC50360.1.
AF028788 mRNA. Translation: AAD01875.1.
AF028789 mRNA. Translation: AAD01876.1.
AF125998, AF125997 Genomic DNA. Translation: AAD31422.1.
AK292329 mRNA. Translation: BAF85018.1.
AB593014 mRNA. Translation: BAJ83969.1.
AC005726 Genomic DNA. No translation available.
CH471159 Genomic DNA. Translation: EAW51095.1.
BC027176 mRNA. Translation: AAH27176.1.
CCDSCCDS11233.1. [Q13432-1]
CCDS11234.1. [Q13432-2]
RefSeqNP_005139.1. NM_005148.3. [Q13432-1]
NP_473376.1. NM_054035.2. [Q13432-2]
UniGeneHs.410455.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3GQQX-ray1.95A/B/C/D/E/F56-240[»]
3RBQX-ray2.00A/B/C/D/E/F56-240[»]
4GOJX-ray2.10C/D1-240[»]
4GOKX-ray2.60C/G1-240[»]
ProteinModelPortalQ13432.
SMRQ13432. Positions 57-239.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114548. 90 interactions.
IntActQ13432. 88 interactions.
MINTMINT-1372196.
STRING9606.ENSP00000337040.

PTM databases

PhosphoSiteQ13432.

Polymorphism databases

DMDM2498854.

Proteomic databases

MaxQBQ13432.
PaxDbQ13432.
PRIDEQ13432.

Protocols and materials databases

DNASU9094.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000301032; ENSP00000301032; ENSG00000109103. [Q13432-2]
ENST00000335765; ENSP00000337040; ENSG00000109103. [Q13432-1]
GeneID9094.
KEGGhsa:9094.
UCSCuc002hbk.2. human. [Q13432-1]
uc002hbm.2. human. [Q13432-2]

Organism-specific databases

CTD9094.
GeneCardsGC17M026873.
HGNCHGNC:12565. UNC119.
HPAHPA041912.
MIM604011. gene.
neXtProtNX_Q13432.
Orphanet1872. Cone rod dystrophy.
228000. Idiopathic CD4 lymphocytopenia.
PharmGKBPA37202.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG305476.
HOGENOMHOG000258286.
HOVERGENHBG108625.
InParanoidQ13432.
OMAIHERRPQ.
OrthoDBEOG7288SP.
PhylomeDBQ13432.
TreeFamTF314474.

Gene expression databases

ArrayExpressQ13432.
BgeeQ13432.
CleanExHS_UNC119.
GenevestigatorQ13432.

Family and domain databases

Gene3D2.70.50.40. 1 hit.
InterProIPR008015. GMP_PDE_delta.
IPR014756. Ig_E-set.
[Graphical view]
PfamPF05351. GMP_PDE_delta. 1 hit.
[Graphical view]
SUPFAMSSF81296. SSF81296. 1 hit.
ProtoNetSearch...

Other

ChiTaRSUNC119. human.
EvolutionaryTraceQ13432.
GeneWikiProtein_unc-119_homolog.
GenomeRNAi9094.
NextBio34075.
PROQ13432.
SOURCESearch...

Entry information

Entry nameU119A_HUMAN
AccessionPrimary (citable) accession number: Q13432
Secondary accession number(s): A8K8G4, F1T095, O95126
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM