USO1_MOUSE
ID USO1_MOUSE Reviewed; 959 AA.
AC Q9Z1Z0; Q3T9L9; Q3TH58; Q3U1C7; Q3UMW6; Q91WE7; Q99JZ5;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=General vesicular transport factor p115;
DE AltName: Full=Protein USO1 homolog;
DE AltName: Full=Transcytosis-associated protein;
DE Short=TAP;
DE AltName: Full=Vesicle-docking protein;
GN Name=Uso1; Synonyms=Vdp;
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 2; 3 AND 4).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Liver, Lung, and Spleen;
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=FVB/N; TISSUE=Eye, and 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 NUCLEOTIDE SEQUENCE [MRNA] OF 19-959 (ISOFORM 1).
RC STRAIN=129; TISSUE=Thymus;
RA Han S.J.;
RT "Identification of mouse TAP (transcytosis associated protein/p115).";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-940, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-940, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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).
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. May well act as a vesicular anchor by interacting with
CC the target membrane and holding the vesicular and target membranes in
CC proximity. {ECO:0000250|UniProtKB:P41542}.
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. Interacts with MIF (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Golgi apparatus
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC Note=Recycles between the cytosol and the Golgi apparatus during
CC interphase. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9Z1Z0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Z1Z0-2; Sequence=VSP_016981;
CC Name=3;
CC IsoId=Q9Z1Z0-3; Sequence=VSP_016979, VSP_016980;
CC Name=4;
CC IsoId=Q9Z1Z0-4; Sequence=VSP_016978;
CC -!- DOMAIN: Composed of a globular head, an elongated tail (coiled-coil)
CC and a highly acidic C-terminal domain.
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}.
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DR EMBL; AK144638; BAE25982.1; -; mRNA.
DR EMBL; AK156070; BAE33571.1; -; mRNA.
DR EMBL; AK168433; BAE40340.1; -; mRNA.
DR EMBL; AK172425; BAE43001.1; -; mRNA.
DR EMBL; BC005548; AAH05548.1; -; mRNA.
DR EMBL; BC016069; AAH16069.1; -; mRNA.
DR EMBL; AF096868; AAC72967.1; -; mRNA.
DR CCDS; CCDS39150.1; -. [Q9Z1Z0-1]
DR RefSeq; NP_062363.1; NM_019490.1. [Q9Z1Z0-1]
DR AlphaFoldDB; Q9Z1Z0; -.
DR SMR; Q9Z1Z0; -.
DR BioGRID; 207788; 122.
DR IntAct; Q9Z1Z0; 110.
DR MINT; Q9Z1Z0; -.
DR STRING; 10090.ENSMUSP00000031355; -.
DR iPTMnet; Q9Z1Z0; -.
DR PhosphoSitePlus; Q9Z1Z0; -.
DR SwissPalm; Q9Z1Z0; -.
DR EPD; Q9Z1Z0; -.
DR jPOST; Q9Z1Z0; -.
DR MaxQB; Q9Z1Z0; -.
DR PaxDb; Q9Z1Z0; -.
DR PeptideAtlas; Q9Z1Z0; -.
DR PRIDE; Q9Z1Z0; -.
DR ProteomicsDB; 299654; -. [Q9Z1Z0-1]
DR ProteomicsDB; 299655; -. [Q9Z1Z0-2]
DR ProteomicsDB; 299656; -. [Q9Z1Z0-3]
DR ProteomicsDB; 299657; -. [Q9Z1Z0-4]
DR Antibodypedia; 4113; 383 antibodies from 39 providers.
DR DNASU; 56041; -.
DR Ensembl; ENSMUST00000031355; ENSMUSP00000031355; ENSMUSG00000029407. [Q9Z1Z0-1]
DR Ensembl; ENSMUST00000202155; ENSMUSP00000144592; ENSMUSG00000029407. [Q9Z1Z0-2]
DR GeneID; 56041; -.
DR KEGG; mmu:56041; -.
DR UCSC; uc008ycl.1; mouse. [Q9Z1Z0-3]
DR UCSC; uc008ycm.1; mouse. [Q9Z1Z0-1]
DR UCSC; uc008ycn.1; mouse. [Q9Z1Z0-4]
DR UCSC; uc012dyl.1; mouse. [Q9Z1Z0-2]
DR CTD; 8615; -.
DR MGI; MGI:1929095; Uso1.
DR VEuPathDB; HostDB:ENSMUSG00000029407; -.
DR eggNOG; KOG0946; Eukaryota.
DR GeneTree; ENSGT00390000017018; -.
DR InParanoid; Q9Z1Z0; -.
DR OMA; YSRACKQ; -.
DR OrthoDB; 1273987at2759; -.
DR PhylomeDB; Q9Z1Z0; -.
DR TreeFam; TF106157; -.
DR Reactome; R-MMU-204005; COPII-mediated vesicle transport.
DR Reactome; R-MMU-6807878; COPI-mediated anterograde transport.
DR BioGRID-ORCS; 56041; 23 hits in 76 CRISPR screens.
DR ChiTaRS; Uso1; mouse.
DR PRO; PR:Q9Z1Z0; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9Z1Z0; protein.
DR Bgee; ENSMUSG00000029407; Expressed in prostate gland ventral lobe and 260 other tissues.
DR ExpressionAtlas; Q9Z1Z0; baseline and differential.
DR Genevisible; Q9Z1Z0; MM.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
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; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005795; C:Golgi stack; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISS:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; IMP:MGI.
DR GO; GO:0048211; P:Golgi vesicle docking; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0061025; P:membrane fusion; ISO:MGI.
DR GO; GO:1900076; P:regulation of cellular response to insulin stimulus; IDA:MGI.
DR GO; GO:0032252; P:secretory granule localization; IDA:MGI.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IDA:MGI.
DR GO; GO:0045056; P:transcytosis; ISO:MGI.
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; Alternative splicing; Coiled coil; Cytoplasm;
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_0000065775"
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:17242355,
FT ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..606
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016978"
FT VAR_SEQ 485..496
FT /note="GSKIQTRVGLLM -> VRATGLLRGERQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016979"
FT VAR_SEQ 497..959
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016980"
FT VAR_SEQ 764..825
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016981"
FT CONFLICT 225
FT /note="G -> R (in Ref. 3; AAC72967)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="V -> G (in Ref. 3; AAC72967)"
FT /evidence="ECO:0000305"
FT CONFLICT 377..378
FT /note="QP -> HA (in Ref. 3; AAC72967)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 959 AA; 106983 MW; 2C05DC35E899D81C CRC64;
MNFLRGVMGG QSAGPQHTEA ETIQKLCDRV ASSTLLDDRR NAVRALKSLS KKYRLEVGIQ
AMEHLIHVLQ TDRSDSEIIA YALDTLYNII SNDEEEELEE NSTRQSEDLG SQFTEIFIKQ
PENVTLLLSL LEEFDFHVRW PGVRLLTSLL KQLGPPVQQI ILVSPMGVSR LMDLLADSRE
IIRNDGVLLL QALTRSNGAI QKIVAFENAF ERLLDIITEE GNSDGGIVVE DCLILLQNLL
KTNNSNQNFF KEGSYIQRMK PWFEVGEENS 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 RIGKENFIEK LGFISKHELY SRASQKPQPN
FPSPEYMIFD HEFTKLVKEL EGVITKAIYK SSEEDKKEEE VKKTLEQHDN IVTHYKNMIR
EQDLQLEELK QQVSTLKCQN EQLQTAVTQQ ASQIQQHKDQ YNLLKVQLGK DNHHQGSHGD
GAQVNGIQPE EISRLREEIE ELKSQQALLQ GQLAEKDSLI ENLKSSQASG MSEQASATCP
PRDPEQVAEL KQELTALKSQ LCSQSLEITR LQTENCELLQ RAETLAKSVP VEGESEHVSA
AKTTDVEGRL SALLQETKEL KNEIKALSEE RTAIQKQLDS SNSTIAILQT EKDKLDLEVT
DSKKEQDDLL VLLADQDQKI LSLKSKLKDL GHPVEEEDES GDQEDDDDEI DDGDKDQDI
