U119B_MOUSE
ID U119B_MOUSE Reviewed; 251 AA.
AC Q8C4B4; Q14BY8; Q8BRC4; Q922B4;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Protein unc-119 homolog B;
GN Name=Unc119b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-24, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Myristoyl-binding protein that acts as a cargo adapter:
CC specifically binds the myristoyl moiety of a subset of N-terminally
CC myristoylated proteins and is required for their localization. Binds
CC myristoylated NPHP3 and plays a key role in localization of NPHP3 to
CC the primary cilium membrane. Does not bind all myristoylated proteins.
CC Probably plays a role in trafficking proteins in photoreceptor cells
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Found in a complex with ARL3, RP2 and UNC119B; RP2 induces
CC hydrolysis of GTP ARL3 in the complex, leading to the release of
CC UNC119B. Interacts with NPHP3 (when myristoylated). Interacts with CYS1
CC (when myristoylated). Interacts with MACIR; interaction only takes
CC place when UNC119B is not liganded with myristoylated proteins (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000250}.
CC Note=Enriched at the transition zone and extended into the proximal end
CC of the cilium. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8C4B4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C4B4-2; Sequence=VSP_033985;
CC -!- DOMAIN: Adopts an immunoglobulin-like beta-sandwich fold forming a
CC hydrophobic cavity that capture N-terminally myristoylated target
CC peptides. Phe residues within the hydrophobic beta sandwich are
CC required for myristate binding (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PDE6D/unc-119 family. {ECO:0000305}.
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DR EMBL; AK045128; BAC32235.1; -; mRNA.
DR EMBL; AK082614; BAC38549.1; -; mRNA.
DR EMBL; BC008617; AAH08617.1; -; mRNA.
DR EMBL; BC112388; AAI12389.1; -; mRNA.
DR EMBL; BC115529; AAI15530.1; -; mRNA.
DR CCDS; CCDS19580.1; -. [Q8C4B4-1]
DR RefSeq; NP_780561.1; NM_175352.4. [Q8C4B4-1]
DR AlphaFoldDB; Q8C4B4; -.
DR SMR; Q8C4B4; -.
DR IntAct; Q8C4B4; 1.
DR STRING; 10090.ENSMUSP00000055475; -.
DR iPTMnet; Q8C4B4; -.
DR PhosphoSitePlus; Q8C4B4; -.
DR EPD; Q8C4B4; -.
DR MaxQB; Q8C4B4; -.
DR PaxDb; Q8C4B4; -.
DR PeptideAtlas; Q8C4B4; -.
DR PRIDE; Q8C4B4; -.
DR ProteomicsDB; 298162; -. [Q8C4B4-1]
DR ProteomicsDB; 298163; -. [Q8C4B4-2]
DR Antibodypedia; 53998; 60 antibodies from 14 providers.
DR DNASU; 106840; -.
DR Ensembl; ENSMUST00000060798; ENSMUSP00000055475; ENSMUSG00000046562. [Q8C4B4-1]
DR GeneID; 106840; -.
DR KEGG; mmu:106840; -.
DR UCSC; uc008zdc.1; mouse. [Q8C4B4-1]
DR UCSC; uc008zdd.1; mouse. [Q8C4B4-2]
DR CTD; 84747; -.
DR MGI; MGI:2147162; Unc119b.
DR VEuPathDB; HostDB:ENSMUSG00000046562; -.
DR eggNOG; KOG4037; Eukaryota.
DR GeneTree; ENSGT00390000014595; -.
DR HOGENOM; CLU_088825_0_0_1; -.
DR InParanoid; Q8C4B4; -.
DR OMA; IAKPPHC; -.
DR OrthoDB; 1270912at2759; -.
DR PhylomeDB; Q8C4B4; -.
DR TreeFam; TF314474; -.
DR Reactome; R-MMU-5624138; Trafficking of myristoylated proteins to the cilium.
DR BioGRID-ORCS; 106840; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Unc119b; mouse.
DR PRO; PR:Q8C4B4; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8C4B4; protein.
DR Bgee; ENSMUSG00000046562; Expressed in saccule of membranous labyrinth and 257 other tissues.
DR Genevisible; Q8C4B4; MM.
DR GO; GO:0035869; C:ciliary transition zone; ISS:UniProtKB.
DR GO; GO:0005929; C:cilium; IBA:GO_Central.
DR GO; GO:0008289; F:lipid binding; ISS:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; ISO:MGI.
DR GO; GO:0042953; P:lipoprotein transport; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; 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 Pfam; PF05351; GMP_PDE_delta; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell projection; Cilium;
KW Cilium biogenesis/degradation; Lipid-binding; Protein transport;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:A6NIH7"
FT CHAIN 2..251
FT /note="Protein unc-119 homolog B"
FT /id="PRO_0000337229"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 142
FT /ligand="tetradecanoate"
FT /ligand_id="ChEBI:CHEBI:30807"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:A6NIH7"
FT MOD_RES 24
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT VAR_SEQ 120..251
FT /note="DQDQDAEEESVDVDISVGRFVRYQFTPAFLRLRTVGATVEFTVGDRPVTGFR
FT MIERHYFRERLLKTFDFDFGFCIPSSRNTCEHIYEFPQLSEDVIRLMIENPYETRSDSF
FT YFVDNKLVMHNKADYAYNGGQ -> GGPGYCGHKPGRKGPWEAQSFWDAGVCHFHDYFL
FT SACLPVAHQFRALLKGWCVCVCVFECLCVPECTRWRPGDNFVESGFCFHICGGSREYVA
FT GTSVH (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_033985"
FT CONFLICT 26
FT /note="E -> K (in Ref. 2; AAI15530)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 251 AA; 28303 MW; AC86FFAA553028A2 CRC64;
MSGSNPKAAT AGSQAGPGGL VAGKEEKKKA GGGVLNRLKA RRQGPPHTPD DGSGAAVTEQ
ELLALDTIRP EHVLRLNRVT ENYLCKPEDN VYSIDFTRFK IRDLETGTVL FEIAKPCISD
QDQDAEEESV DVDISVGRFV RYQFTPAFLR LRTVGATVEF TVGDRPVTGF RMIERHYFRE
RLLKTFDFDF GFCIPSSRNT CEHIYEFPQL SEDVIRLMIE NPYETRSDSF YFVDNKLVMH
NKADYAYNGG Q
