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UV radiation resistance associated protein

 UVRAG_MOUSE             Reviewed;         698 AA.
Q8K245; Q8BVI8; Q8C0K8;
24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
24-JUN-2015, sequence version 2.
07-JUN-2017, entry version 89.
RecName: Full=UV radiation resistance associated protein;
Name=Uvrag; Synonyms=Uvrag1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090 {ECO:0000312|EMBL:AAH34176.1};
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD;
TISSUE=Dendritic cell, Medulla oblongata, and Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N;
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).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-688, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Heart, Kidney, Liver, Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[7]
INTERACTION WITH SLAMF1.
PubMed=22493499; DOI=10.1074/jbc.M112.367060;
Ma C., Wang N., Detre C., Wang G., O'Keeffe M., Terhorst C.;
"Receptor signaling lymphocyte-activation molecule family 1 (Slamf1)
regulates membrane fusion and NADPH oxidase 2 (NOX2) activity by
recruiting a Beclin-1/Vps34/ultraviolet radiation resistance-
associated gene (UVRAG) complex.";
J. Biol. Chem. 287:18359-18365(2012).
-!- FUNCTION: Versatile protein that is involved in regulation of
different cellular pathways implicated in membrane trafficking.
Involved in regulation of the COPI-dependent retrograde transport
from Golgi and the endoplasmic reticulum by associating with the
NRZ complex; the function is dependent on its binding to
phosphatidylinositol 3-phosphate (PtdIns(3)P). During autophagy
acts as regulatory subunit of the alternative PI3K complex II
(PI3KC3-C2) that mediates formation of phosphatidylinositol 3-
phosphate and is believed to be involved in maturation of
autophagosomes and endocytosis. Activates lipid kinase activity of
PIK3C3. Involved in the regulation of degradative endocytic
trafficking and cytokinesis, and in regulation of ATG9A transport
from the Golgi to the autophagosome; the functions seems to
implicate its association with PI3KC3-C2. Involved in maturation
of autophagosomes and degradative endocytic trafficking
independently of BECN1 but depending on its association with a
class C Vps complex (possibly the HOPS complex); the association
is also proposed to promote autophagosome recruitment and
activation of Rab7 and endosome-endosome fusion events. Enhances
class C Vps complex (possibly HOPS complex) association with a
SNARE complex and promotes fusogenic SNARE complex formation
during late endocytic membrane fusion. In case of negative-strand
RNA virus infection is required for efficient virus entry,
promotes endocytic transport of virions and is implicated in a
VAMP8-specific fusogenic SNARE complex assembly (By similarity).
{ECO:0000250|UniProtKB:Q9P2Y5, ECO:0000305}.
-!- FUNCTION: Involved in maintaining chromosomal stability. Promotes
DNA double-strand break (DSB) repair by association with DNA-
dependent protein kinase complex DNA-PK and activating it in non-
homologous end joining (NHEJ). Required for centrosome stability
and proper chromosome segregation (By similarity).
{ECO:0000250|UniProtKB:Q9P2Y5}.
-!- SUBUNIT: Component of the PI3K (PI3KC3/PI3K-III/class III
phosphatidylinositol 3-kinase) complex II (PI3KC3-C2) in which the
core composed of the catalytic subunit PIK3C3, the regulatory
subunit PIK3R4 and BECN1 is associated with UVRAG; in the complex
interacts directly with BECN1. PI3KC3-C2 can associate with
further regulatory subunits such as RUBCN and probably
SH3GLB1/Bif-1. Interacts with SH3GLB1; UVRAG bridges the
interaction to BECN1 indicative for an association with the PI3K
complex PI3KC3-C2. Interacts with RINT1. Associates with the NRZ
complex under basal conditions and dissociates from it under
autophagy conditions to associate with the PI3K complex; these
complex associations seem to be mutually exclusive. Interacts with
VPS16; VPS11; VPS18; VPS33 (VPS33A or VPS33B) and VPS39;
indicative for an association with a class C Vps tethering complex
(possibly the HOPS complex). Interacts with RAB7A; RAB7A competes
with UVRAG for RUBCN binding. Interacts with STX7, VTI1B, STX8.
Interacts with PRKDC, XRCC6 and XRCC5; indicative for an
association with the DNA-dependent protein kinase complex DNA-PK.
Interacts with CEP63. Directly interacts with FEZ1 and SCOC; the
interaction with SCOC is reduced by amino acid starvation, but the
complex is stabilized in the presence of FEZ1. Interacts with
BECN1P1/BECN2 (By similarity). Interacts with SLAMF1
(PubMed:22493499). {ECO:0000250|UniProtKB:Q9P2Y5,
ECO:0000269|PubMed:22493499}.
-!- SUBCELLULAR LOCATION: Late endosome
{ECO:0000250|UniProtKB:Q9P2Y5}. Lysosome
{ECO:0000250|UniProtKB:Q9P2Y5}. Early endosome
{ECO:0000250|UniProtKB:Q9P2Y5}. Endoplasmic reticulum
{ECO:0000250|UniProtKB:Q9P2Y5}. Midbody
{ECO:0000250|UniProtKB:Q9P2Y5}. Chromosome, centromere
{ECO:0000250|UniProtKB:Q9P2Y5}. Note=Colocalizes with RAB9-
positive compartments involved in retrograde transport from late
endosomes to trans-Golgi network. Colocalization with early
endosomes is only partial (By similarity).
{ECO:0000250|UniProtKB:Q9P2Y5}.
-!- PTM: Phosphorylated at Ser-497 by MTOR under basal conditions;
increases the interaction with RUBCN implicated in inhibitory
effect of RUBCN on PI3KC3 and decreases interaction with RAB7A,
and VPS16 and VPS39 (indicative for a class C Vps complex,
possibly the HOPS complex) (By similarity).
{ECO:0000250|UniProtKB:Q9P2Y5}.
-----------------------------------------------------------------------
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EMBL; AK030814; BAC27144.1; -; mRNA.
EMBL; AK078085; BAC37120.1; -; mRNA.
EMBL; AK154903; BAE32914.1; -; mRNA.
EMBL; AC093351; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC115850; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC034176; AAH34176.1; -; mRNA.
CCDS; CCDS21476.1; -.
RefSeq; NP_848750.3; NM_178635.3.
UniGene; Mm.323072; -.
ProteinModelPortal; Q8K245; -.
SMR; Q8K245; -.
IntAct; Q8K245; 5.
STRING; 10090.ENSMUSP00000045297; -.
iPTMnet; Q8K245; -.
PhosphoSitePlus; Q8K245; -.
MaxQB; Q8K245; -.
PaxDb; Q8K245; -.
Ensembl; ENSMUST00000037968; ENSMUSP00000045297; ENSMUSG00000035354.
GeneID; 78610; -.
KEGG; mmu:78610; -.
UCSC; uc009ikz.2; mouse.
CTD; 7405; -.
MGI; MGI:1925860; Uvrag.
eggNOG; KOG2896; Eukaryota.
eggNOG; ENOG410YZ0H; LUCA.
GeneTree; ENSGT00390000012877; -.
HOGENOM; HOG000147825; -.
HOVERGEN; HBG059846; -.
KO; K21249; -.
OMA; LPGEFHP; -.
OrthoDB; EOG091G0HDH; -.
PhylomeDB; Q8K245; -.
Reactome; R-MMU-1632852; Macroautophagy.
ChiTaRS; Uvrag; mouse.
PRO; PR:Q8K245; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000035354; -.
ExpressionAtlas; Q8K245; baseline and differential.
GO; GO:0005813; C:centrosome; ISO:MGI.
GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
GO; GO:0070418; C:DNA-dependent protein kinase complex; IEA:Ensembl.
GO; GO:0005769; C:early endosome; ISO:MGI.
GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
GO; GO:0005768; C:endosome; IBA:GO_Central.
GO; GO:0005770; C:late endosome; ISO:MGI.
GO; GO:0005764; C:lysosome; ISO:MGI.
GO; GO:0000323; C:lytic vacuole; IBA:GO_Central.
GO; GO:0030496; C:midbody; ISO:MGI.
GO; GO:0045335; C:phagocytic vesicle; IPI:MGI.
GO; GO:0043234; C:protein complex; IDA:MGI.
GO; GO:0017124; F:SH3 domain binding; IPI:MGI.
GO; GO:0000149; F:SNARE binding; IDA:MGI.
GO; GO:0006914; P:autophagy; ISO:MGI.
GO; GO:0007098; P:centrosome cycle; IMP:UniProtKB.
GO; GO:0007059; P:chromosome segregation; IMP:UniProtKB.
GO; GO:0006281; P:DNA repair; IMP:UniProtKB.
GO; GO:0097680; P:double-strand break repair via classical nonhomologous end joining; ISO:MGI.
GO; GO:0051684; P:maintenance of Golgi location; ISO:MGI.
GO; GO:0010508; P:positive regulation of autophagy; IEA:InterPro.
GO; GO:0032801; P:receptor catabolic process; ISO:MGI.
GO; GO:0032465; P:regulation of cytokinesis; ISO:MGI.
GO; GO:0071900; P:regulation of protein serine/threonine kinase activity; ISO:MGI.
GO; GO:0060627; P:regulation of vesicle-mediated transport; IBA:GO_Central.
GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; ISO:MGI.
GO; GO:0035493; P:SNARE complex assembly; IMP:MGI.
GO; GO:0007051; P:spindle organization; IMP:UniProtKB.
GO; GO:0046718; P:viral entry into host cell; IMP:MGI.
Gene3D; 2.60.40.150; -; 1.
InterPro; IPR000008; C2_dom.
InterPro; IPR018791; UV_resistance/autophagy_Atg14.
Pfam; PF10186; Atg14; 1.
SUPFAM; SSF49562; SSF49562; 1.
1: Evidence at protein level;
Centromere; Chromosome; Coiled coil; Complete proteome; DNA damage;
DNA repair; Endoplasmic reticulum; Endosome; Lysosome; Phosphoprotein;
Reference proteome.
CHAIN 1 698 UV radiation resistance associated
protein.
/FTId=PRO_0000433403.
DOMAIN 44 128 C2.
REGION 199 268 Sufficient for interaction with STX7;
VTI1B AND STX8.
{ECO:0000250|UniProtKB:Q9P2Y5}.
REGION 269 441 Sufficient for interaction with VPS16,
required for interaction with CEP63.
{ECO:0000250|UniProtKB:Q9P2Y5}.
REGION 442 698 Required for interaction with PRKDC,
XRCC6 and XRCC5.
{ECO:0000250|UniProtKB:Q9P2Y5}.
COILED 200 304 {ECO:0000255}.
MOD_RES 492 492 Phosphoserine.
{ECO:0000250|UniProtKB:Q9P2Y5}.
MOD_RES 497 497 Phosphoserine; by MTOR.
{ECO:0000250|UniProtKB:Q9P2Y5}.
MOD_RES 507 507 Phosphoserine.
{ECO:0000250|UniProtKB:Q9P2Y5}.
MOD_RES 517 517 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9P2Y5}.
MOD_RES 521 521 Phosphoserine.
{ECO:0000250|UniProtKB:Q9P2Y5}.
MOD_RES 548 548 Phosphoserine.
{ECO:0000250|UniProtKB:Q9P2Y5}.
MOD_RES 549 549 Phosphoserine.
{ECO:0000250|UniProtKB:Q9P2Y5}.
MOD_RES 570 570 Phosphoserine.
{ECO:0000250|UniProtKB:Q9P2Y5}.
MOD_RES 688 688 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CONFLICT 335 335 N -> H (in Ref. 3; AAH34176).
{ECO:0000305}.
CONFLICT 355 355 D -> E (in Ref. 3; AAH34176).
{ECO:0000305}.
CONFLICT 497 497 S -> T (in Ref. 1; BAC37120).
{ECO:0000305}.
SEQUENCE 698 AA; 77525 MW; 245A411198286F33 CRC64;
MSSCASLGGP VPLPPPGPSA ALTSGAPARA LHVELPSQQR RLRHLRNIAA RNIVNRNGHQ
LLDTYFTLHL CDNEKIFKEF YRSEVIKNSL NPTWRSLDFG IMPDRLDTSV SCFVVKIWGG
KEEAFQLLIE WKVYLDGLKY LGQQIHARNQ NEIIFGLNDG YYGAPCEHKG HPNAQKNLLQ
VDQNCVRNSY DVFSLLRLHR AQCAIKQTQV TVQRLGKEIE EKLRLTSTSN ELKKESECLR
LKILVLRNEL ERQKKALGRE VAFLHKQQMA LQDKGSAFST EHGKLQLQKD SLSELRKECT
AKRELFLKTN AQLTIRCRQL LSELSYIYPI DLNENKDYFV CGVKLPNSED FQAKDDGSIA
VALGYTAHLV SMISFFLQVP LRYPIIHKGS RSTIKDNIND KLTEKEREFP LYPKGGEKLQ
FDYGVYLLNK NIAQLRYQHG LGTPDLRQTL PNLKNFMEHG LMVRCDRHHI SNAIPVPKRQ
SSTFGGADGG FSAGIPSPDK VHRKRASSEN ERLQYKTPPP SYNSALTQPG VAMPTSGDSE
RKVAPLSSSL DTSLDFSKEN KKAGVDLGSS VSGDHGNSDS GQEQGEALPG HLAAVNGTAL
PSEQAGPAGT LLPGSCHPAP SAELCCAVEQ AEEIIGLEAT GFTSGDQLEA LSCIPVDSAV
AVECDEQVLG EFEEFSRRIY ALSENVSSFR RPRRSSDK


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