USO1_RAT
ID USO1_RAT Reviewed; 959 AA.
AC P41542;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=General vesicular transport factor p115 {ECO:0000303|PubMed:7831323};
DE AltName: Full=Protein USO1 homolog;
DE AltName: Full=Transcytosis-associated protein {ECO:0000303|PubMed:7831324};
DE Short=TAP {ECO:0000303|PubMed:7831324};
DE AltName: Full=Vesicle-docking protein;
GN Name=Uso1; Synonyms=Vdp;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC TISSUE=Liver;
RX PubMed=7831323; DOI=10.1073/pnas.92.2.522;
RA Sapperstein S.K., Walter D.M., Grosvenor A.R., Heuser J.E., Waters M.G.;
RT "p115 is a general vesicular transport factor related to the yeast
RT endoplasmic reticulum to Golgi transport factor Uso1p.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:522-526(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND FUNCTION.
RC TISSUE=Liver;
RX PubMed=7831324; DOI=10.1073/pnas.92.2.527;
RA Barroso M., Nelson D.S., Sztul E.;
RT "Transcytosis-associated protein (TAP)/p115 is a general fusion factor
RT required for binding of vesicles to acceptor membranes.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:527-531(1995).
RN [3]
RP INTERACTION WITH GOLGA2.
RX PubMed=9150144; DOI=10.1016/s0092-8674(00)80225-1;
RA Nakamura N., Lowe M., Levine T.P., Rabouille C., Warren G.;
RT "The vesicle docking protein p115 binds GM130, a cis-Golgi matrix protein,
RT in a mitotically regulated manner.";
RL Cell 89:445-455(1997).
RN [4]
RP INTERACTION WITH GOLGA2.
RX PubMed=9753325; DOI=10.1016/s0092-8674(00)81737-7;
RA Lowe M., Rabouille C., Nakamura N., Watson R., Jackman M., Jamsa E.,
RA Rahman D., Pappin D.J.C., Warren G.;
RT "Cdc2 kinase directly phosphorylates the cis-Golgi matrix protein GM130 and
RT is required for Golgi fragmentation in mitosis.";
RL Cell 94:783-793(1998).
RN [5]
RP INTERACTION WITH GOLGA2.
RX PubMed=10744704; DOI=10.1074/jbc.275.14.10196;
RA Linstedt A.D., Jesch S.A., Mehta A., Lee T.H., Garcia-Mata R., Nelson D.S.,
RA Sztul E.;
RT "Binding relationships of membrane tethering components. The giantin N
RT terminus and the GM130 N terminus compete for binding to the p115 C
RT terminus.";
RL J. Biol. Chem. 275:10196-10201(2000).
RN [6]
RP INTERACTION WITH GOLGA2.
RX PubMed=10769027; DOI=10.1083/jcb.149.2.341;
RA Lowe M., Gonatas N.K., Warren G.;
RT "The mitotic phosphorylation cycle of the cis-Golgi matrix protein GM130.";
RL J. Cell Biol. 149:341-356(2000).
RN [7]
RP FUNCTION.
RX PubMed=10679020; DOI=10.1091/mbc.11.2.635;
RA Seemann J., Jokitalo E.J., Warren G.;
RT "The role of the tethering proteins p115 and GM130 in transport through the
RT Golgi apparatus in vivo.";
RL Mol. Biol. Cell 11:635-645(2000).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-940, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-940, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: General vesicular transport factor required for
CC intercisternal transport in the Golgi stack; it is required for
CC transcytotic fusion and/or subsequent binding of the vesicles to the
CC target membrane (PubMed:7831323, PubMed:7831324, PubMed:10679020). May
CC well act as a vesicular anchor by interacting with the target membrane
CC and holding the vesicular and target membranes in proximity
CC (PubMed:7831323, PubMed:7831324, PubMed:10679020).
CC {ECO:0000269|PubMed:10679020, ECO:0000269|PubMed:7831323,
CC ECO:0000269|PubMed:7831324}.
CC -!- SUBUNIT: Homodimer. Dimerizes by parallel association of the tails,
CC resulting in an elongated structure with two globular head domains side
CC by side, and a long rod-like tail structure (PubMed:7831323). Interacts
CC with MIF (By similarity). Interacts with GM130/GOLGA2; interaction is
CC disrupted upon phosphorylation of GM130/GOLGA2 by CDK1 at the onset of
CC mitosis (PubMed:9150144, PubMed:9753325, PubMed:10744704,
CC PubMed:10769027). {ECO:0000250|UniProtKB:O60763,
CC ECO:0000269|PubMed:10744704, ECO:0000269|PubMed:10769027,
CC ECO:0000269|PubMed:7831323, ECO:0000269|PubMed:9150144,
CC ECO:0000269|PubMed:9753325}.
CC -!- INTERACTION:
CC P41542; Q62931: Gosr1; NbExp=10; IntAct=EBI-4423297, EBI-7837133;
CC P41542; Q08851: Stx5; NbExp=8; IntAct=EBI-4423297, EBI-2028244;
CC P41542; Q6DFZ1: Gbf1; Xeno; NbExp=3; IntAct=EBI-4423297, EBI-761491;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:O60763}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:7831323}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O60763}. Note=Recycles between the cytosol and
CC the Golgi apparatus during interphase. {ECO:0000250|UniProtKB:O60763}.
CC -!- DOMAIN: Composed of a globular head, an elongated tail (coiled-coil)
CC and a highly acidic C-terminal domain. {ECO:0000269|PubMed:7831323}.
CC -!- PTM: Phosphorylated in a cell cycle-specific manner; phosphorylated in
CC interphase but not in mitotic cells. Dephosphorylated protein
CC associates with the Golgi membrane; phosphorylation promostes
CC dissociation (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the VDP/USO1/EDE1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U14192; AAA62632.1; -; mRNA.
DR EMBL; U15589; AAC52151.1; -; mRNA.
DR PIR; A55913; A55913.
DR RefSeq; NP_062252.1; NM_019379.1.
DR AlphaFoldDB; P41542; -.
DR SMR; P41542; -.
DR BioGRID; 248556; 3.
DR CORUM; P41542; -.
DR IntAct; P41542; 16.
DR STRING; 10116.ENSRNOP00000003277; -.
DR iPTMnet; P41542; -.
DR PhosphoSitePlus; P41542; -.
DR jPOST; P41542; -.
DR PaxDb; P41542; -.
DR PRIDE; P41542; -.
DR GeneID; 56042; -.
DR KEGG; rno:56042; -.
DR UCSC; RGD:621604; rat.
DR CTD; 8615; -.
DR RGD; 621604; Uso1.
DR VEuPathDB; HostDB:ENSRNOG00000002301; -.
DR eggNOG; KOG0946; Eukaryota.
DR HOGENOM; CLU_006318_2_0_1; -.
DR InParanoid; P41542; -.
DR OMA; YSRACKQ; -.
DR OrthoDB; 1273987at2759; -.
DR PhylomeDB; P41542; -.
DR TreeFam; TF106157; -.
DR Reactome; R-RNO-204005; COPII-mediated vesicle transport.
DR Reactome; R-RNO-6807878; COPI-mediated anterograde transport.
DR PRO; PR:P41542; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000002301; Expressed in jejunum and 20 other tissues.
DR Genevisible; P41542; RN.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IBA:GO_Central.
DR GO; GO:0001650; C:fibrillar center; IEA:Ensembl.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0005795; C:Golgi stack; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; ISO:RGD.
DR GO; GO:0048211; P:Golgi vesicle docking; IBA:GO_Central.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; TAS:RGD.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0061025; P:membrane fusion; IDA:RGD.
DR GO; GO:1900076; P:regulation of cellular response to insulin stimulus; ISO:RGD.
DR GO; GO:0032252; P:secretory granule localization; ISO:RGD.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; ISO:RGD.
DR GO; GO:0045056; P:transcytosis; IDA:RGD.
DR GO; GO:0048280; P:vesicle fusion with Golgi apparatus; IEA:InterPro.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR041209; P115_Arm_rpt.
DR InterPro; IPR006955; Uso1_p115_C.
DR InterPro; IPR006953; Vesicle_Uso1_P115_head.
DR Pfam; PF18770; Arm_vescicular; 1.
DR Pfam; PF04871; Uso1_p115_C; 1.
DR Pfam; PF04869; Uso1_p115_head; 1.
DR SMART; SM00185; ARM; 3.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50176; ARM_REPEAT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Cytoplasm; Direct protein sequencing;
KW ER-Golgi transport; Golgi apparatus; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Transport.
FT CHAIN 1..959
FT /note="General vesicular transport factor p115"
FT /id="PRO_0000065776"
FT REPEAT 20..60
FT /note="ARM 1"
FT REPEAT 61..121
FT /note="ARM 2"
FT REPEAT 123..163
FT /note="ARM 3"
FT REPEAT 166..207
FT /note="ARM 4"
FT REPEAT 208..253
FT /note="ARM 5"
FT REPEAT 255..310
FT /note="ARM 6"
FT REPEAT 311..354
FT /note="ARM 7"
FT REPEAT 363..408
FT /note="ARM 8"
FT REPEAT 420..459
FT /note="ARM 9"
FT REPEAT 473..513
FT /note="ARM 10"
FT REPEAT 518..571
FT /note="ARM 11"
FT REPEAT 573..630
FT /note="ARM 12"
FT REGION 1..637
FT /note="Globular head"
FT REGION 925..959
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 638..930
FT /evidence="ECO:0000255"
FT COMPBIAS 936..959
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60763"
FT MOD_RES 202
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O60763"
FT MOD_RES 940
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100,
FT ECO:0007744|PubMed:22673903"
FT CONFLICT 591
FT /note="S -> P (in Ref. 2; AAC52151)"
FT /evidence="ECO:0000305"
FT CONFLICT 658
FT /note="M -> V (in Ref. 2; AAC52151)"
FT /evidence="ECO:0000305"
FT CONFLICT 816
FT /note="S -> R (in Ref. 2; AAC52151)"
FT /evidence="ECO:0000305"
FT CONFLICT 873
FT /note="A -> S (in Ref. 2; AAC52151)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 959 AA; 107162 MW; 356394B48C7E003B CRC64;
MNFLRGVMGG QSAGPQHTEA ETIQKLCDRV ASSTLLDDRR NAVRALKSLS KKYRLEVGIQ
AMEHLIHVLQ TDRSDSEIIA YALDTLYNII SNDEEEEVEE NSTRQSEDLG SQFTEIFIKQ
PENVTLLLSL LEEFDFHVRW PGVRLLTSLL KQLGPPVQQI ILVSPMGVSK LMDLLADSRE
IIRNDGVLLL QALTRSNGAI QKIVAFENAF ERLLDIITEE GNSDGGIVVE DCLILLQNLL
KNNNSNQNFF KEGSYIQRMK AWFEVGDENP GWSAQKVTNL HLMLQLVRVL VSPTNPPGAT
SSCQKAMFQC GLLQQLCTIL MATGIPADIL TETINTVSEV IRGCQVNQDY FASVNAPSNP
PRPAIVVLLM SMVNERQPFV LRCAVLYCFQ CFLYKNEKGQ GEIVATLLPS TIDATGNSVS
AGQLLCGGLF STDSLSNWCA AVALAHALQG NATQKEQLLR VQLATSIGNP PVSLLQQCTN
ILSQGSKIQT RVGLLMLLCT WLSNCPIAVT HFLHNSANVP FLTGQIAENL GEEEQLVQGL
CALLLGISIY FNDNSLENYT KEKLKQLIEK RIGKENYIEK LGFISKHELY SRASQKPQPN
FPSPEYMIFD HEFTKLVKEL EGVITKAIYK SSEEDKKEEE VKKTLEQHDN IVTHYKNMIR
EQDLQLEELK QQVSTLKCQN EQLQTAVTQQ ASQIQQHKDQ YNLLKVQLGK DNHHQGSHSD
GAQVNGIQPE EISRLREEIE ELRSHQVLLQ SQLAEKDTVI ENLRSSQVSG MSEQALATCS
PRDAEQVAEL KQELSALKSQ LCSQSLEITR LQTENSELQQ RAETLAKSVP VEGESELVTA
AKTTDVEGRL SALLQETKEL KNEIKALSEE RTAIQKQLDS SNSTIAILQT EKDKLYLEVT
DSKKEQDDLL VLLADQDQKI LSLKSKLKDL GHPVEEEDES GDQEDDDDEL DDGDRDQDI
