USO1_HUMAN
ID USO1_HUMAN Reviewed; 962 AA.
AC O60763; B2RAQ0; Q6PK63; Q86TB8; Q8N592;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 186.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, MUTAGENESIS
RP OF SER-942, AND PHOSPHORYLATION AT SER-942.
RX PubMed=9478999; DOI=10.1074/jbc.273.9.5385;
RA Sohda M., Misumi Y., Yano A., Takami N., Ikehara Y.;
RT "Phosphorylation of the vesicle docking protein p115 regulates its
RT association with the Golgi membrane.";
RL J. Biol. Chem. 273:5385-5388(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Skeletal muscle;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-942, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-942, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH MIF.
RX PubMed=19454686; DOI=10.4049/jimmunol.0803710;
RA Merk M., Baugh J., Zierow S., Leng L., Pal U., Lee S.J., Ebert A.D.,
RA Mizue Y., Trent J.O., Mitchell R., Nickel W., Kavathas P.B., Bernhagen J.,
RA Bucala R.;
RT "The Golgi-associated protein p115 mediates the secretion of macrophage
RT migration inhibitory factor.";
RL J. Immunol. 182:6896-6906(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-942, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-202, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50 AND SER-942, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-942 AND SER-952, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-942 AND SER-952, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.22 ANGSTROMS) OF 53-629, DOMAIN ARM REPEATS, AND
RP SUBUNIT.
RX PubMed=19247479; DOI=10.1371/journal.pone.0004656;
RA Striegl H., Roske Y., Kuemmel D., Heinemann U.;
RT "Unusual armadillo fold in the human general vesicular transport factor
RT p115.";
RL PLoS ONE 4:E4656-E4656(2009).
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 (Probable). Interacts with
CC MIF. {ECO:0000269|PubMed:19247479, ECO:0000269|PubMed:19454686,
CC ECO:0000305}.
CC -!- INTERACTION:
CC O60763; Q99996-2: AKAP9; NbExp=3; IntAct=EBI-356164, EBI-9641546;
CC O60763; Q9UNI6: DUSP12; NbExp=3; IntAct=EBI-356164, EBI-715161;
CC O60763; Q8IUZ5: PHYKPL; NbExp=3; IntAct=EBI-356164, EBI-751947;
CC O60763; Q9UIA9: XPO7; NbExp=3; IntAct=EBI-356164, EBI-286668;
CC O60763; P0DTC9: N; Xeno; NbExp=4; IntAct=EBI-356164, EBI-25475856;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:19454686,
CC ECO:0000269|PubMed:9478999}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:19454686, ECO:0000269|PubMed:9478999}; Peripheral
CC membrane protein {ECO:0000269|PubMed:19454686,
CC ECO:0000269|PubMed:9478999}. Note=Recycles between the cytosol and the
CC Golgi apparatus during interphase. During interphase, the
CC phosphorylated form is found exclusively in cytosol; the
CC unphosphorylated form is associated with Golgi apparatus membranes.
CC {ECO:0000269|PubMed:19454686, ECO:0000269|PubMed:9478999}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O60763-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O60763-2; Sequence=VSP_039120, VSP_039121;
CC -!- DOMAIN: Composed of a globular head, an elongated tail (coiled-coil)
CC and a highly acidic C-terminal domain. {ECO:0000269|PubMed:19247479}.
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 promotes
CC dissociation. {ECO:0000269|PubMed:9478999}.
CC -!- SIMILARITY: Belongs to the VDP/USO1/EDE1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH06398.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; D86326; BAA25300.1; -; mRNA.
DR EMBL; AK314289; BAG36947.1; -; mRNA.
DR EMBL; AL832010; CAD89917.1; -; mRNA.
DR EMBL; AC110615; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC104828; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006398; AAH06398.1; ALT_SEQ; mRNA.
DR EMBL; BC032654; AAH32654.1; -; mRNA.
DR CCDS; CCDS75144.1; -. [O60763-1]
DR CCDS; CCDS77929.1; -. [O60763-2]
DR RefSeq; NP_001276978.1; NM_001290049.1. [O60763-2]
DR RefSeq; NP_003706.2; NM_003715.3. [O60763-1]
DR PDB; 2W3C; X-ray; 2.22 A; A=53-629.
DR PDBsum; 2W3C; -.
DR AlphaFoldDB; O60763; -.
DR SMR; O60763; -.
DR BioGRID; 114173; 173.
DR IntAct; O60763; 52.
DR MINT; O60763; -.
DR STRING; 9606.ENSP00000444850; -.
DR ChEMBL; CHEMBL4295669; -.
DR GlyGen; O60763; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O60763; -.
DR MetOSite; O60763; -.
DR PhosphoSitePlus; O60763; -.
DR SwissPalm; O60763; -.
DR BioMuta; USO1; -.
DR CPTAC; CPTAC-293; -.
DR CPTAC; CPTAC-294; -.
DR EPD; O60763; -.
DR jPOST; O60763; -.
DR MassIVE; O60763; -.
DR MaxQB; O60763; -.
DR PeptideAtlas; O60763; -.
DR PRIDE; O60763; -.
DR ProteomicsDB; 49590; -. [O60763-1]
DR ProteomicsDB; 49591; -. [O60763-2]
DR Antibodypedia; 4113; 383 antibodies from 39 providers.
DR DNASU; 8615; -.
DR Ensembl; ENST00000264904.8; ENSP00000264904.7; ENSG00000138768.15. [O60763-2]
DR Ensembl; ENST00000514213.7; ENSP00000444850.2; ENSG00000138768.15. [O60763-1]
DR GeneID; 8615; -.
DR KEGG; hsa:8615; -.
DR MANE-Select; ENST00000514213.7; ENSP00000444850.2; NM_003715.4; NP_003706.2.
DR UCSC; uc003hiv.5; human. [O60763-1]
DR CTD; 8615; -.
DR DisGeNET; 8615; -.
DR GeneCards; USO1; -.
DR HGNC; HGNC:30904; USO1.
DR HPA; ENSG00000138768; Tissue enhanced (skeletal).
DR MIM; 603344; gene.
DR neXtProt; NX_O60763; -.
DR OpenTargets; ENSG00000138768; -.
DR PharmGKB; PA162408713; -.
DR VEuPathDB; HostDB:ENSG00000138768; -.
DR eggNOG; KOG0946; Eukaryota.
DR GeneTree; ENSGT00390000017018; -.
DR HOGENOM; CLU_006318_2_0_1; -.
DR InParanoid; O60763; -.
DR OMA; YSRACKQ; -.
DR OrthoDB; 1273987at2759; -.
DR PhylomeDB; O60763; -.
DR PathwayCommons; O60763; -.
DR Reactome; R-HSA-162658; Golgi Cisternae Pericentriolar Stack Reorganization.
DR Reactome; R-HSA-204005; COPII-mediated vesicle transport.
DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
DR SignaLink; O60763; -.
DR SIGNOR; O60763; -.
DR BioGRID-ORCS; 8615; 63 hits in 271 CRISPR screens.
DR ChiTaRS; USO1; human.
DR EvolutionaryTrace; O60763; -.
DR GeneWiki; USO1; -.
DR GenomeRNAi; 8615; -.
DR Pharos; O60763; Tbio.
DR PRO; PR:O60763; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; O60763; protein.
DR Bgee; ENSG00000138768; Expressed in gluteal muscle and 213 other tissues.
DR Genevisible; O60763; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
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; IDA:HPA.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0005795; C:Golgi stack; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005815; C:microtubule organizing center; TAS:Reactome.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0030133; C:transport vesicle; TAS:Reactome.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISS:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:1900076; P:regulation of cellular response to insulin stimulus; IEA:Ensembl.
DR GO; GO:0032252; P:secretory granule localization; IEA:Ensembl.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:Ensembl.
DR GO; GO:0045056; P:transcytosis; IBA:GO_Central.
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 3D-structure; Acetylation; Alternative splicing; Coiled coil; Cytoplasm;
KW ER-Golgi transport; Golgi apparatus; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Transport.
FT CHAIN 1..962
FT /note="General vesicular transport factor p115"
FT /id="PRO_0000065774"
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 763..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 926..962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 638..930
FT /evidence="ECO:0000255"
FT COMPBIAS 763..782
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 936..955
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 202
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 942
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:9478999,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 952
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 98
FT /note="V -> VDDVE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_039120"
FT VAR_SEQ 484
FT /note="Q -> QGDKIDRR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_039121"
FT MUTAGEN 942
FT /note="S->A: Loss of phosphorylation. Promotes association
FT with Golgi membranes."
FT /evidence="ECO:0000269|PubMed:9478999"
FT MUTAGEN 942
FT /note="S->D: Decreased association with Golgi membranes."
FT /evidence="ECO:0000269|PubMed:9478999"
FT CONFLICT 75
FT /note="D -> G (in Ref. 3; CAD89917)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="T -> I (in Ref. 1; BAA25300)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="Missing (in Ref. 5; AAH32654)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="N -> Y (in Ref. 3; CAD89917)"
FT /evidence="ECO:0000305"
FT CONFLICT 650
FT /note="N -> D (in Ref. 3; CAD89917)"
FT /evidence="ECO:0000305"
FT CONFLICT 877
FT /note="Q -> R (in Ref. 2; BAG36947)"
FT /evidence="ECO:0000305"
FT TURN 57..62
FT /evidence="ECO:0007829|PDB:2W3C"
FT HELIX 63..71
FT /evidence="ECO:0007829|PDB:2W3C"
FT HELIX 76..91
FT /evidence="ECO:0007829|PDB:2W3C"
FT HELIX 112..119
FT /evidence="ECO:0007829|PDB:2W3C"
FT HELIX 122..130
FT /evidence="ECO:0007829|PDB:2W3C"
FT HELIX 136..152
FT /evidence="ECO:0007829|PDB:2W3C"
FT HELIX 154..163
FT /evidence="ECO:0007829|PDB:2W3C"
FT HELIX 167..172
FT /evidence="ECO:0007829|PDB:2W3C"
FT HELIX 173..176
FT /evidence="ECO:0007829|PDB:2W3C"
FT HELIX 180..194
FT /evidence="ECO:0007829|PDB:2W3C"
FT HELIX 198..206
FT /evidence="ECO:0007829|PDB:2W3C"
FT HELIX 209..219
FT /evidence="ECO:0007829|PDB:2W3C"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:2W3C"
FT HELIX 227..240
FT /evidence="ECO:0007829|PDB:2W3C"
FT HELIX 244..252
FT /evidence="ECO:0007829|PDB:2W3C"
FT HELIX 256..259
FT /evidence="ECO:0007829|PDB:2W3C"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:2W3C"
FT HELIX 274..290
FT /evidence="ECO:0007829|PDB:2W3C"
FT HELIX 297..309
FT /evidence="ECO:0007829|PDB:2W3C"
FT HELIX 312..321
FT /evidence="ECO:0007829|PDB:2W3C"
FT HELIX 327..341
FT /evidence="ECO:0007829|PDB:2W3C"
FT HELIX 345..352
FT /evidence="ECO:0007829|PDB:2W3C"
FT HELIX 364..372
FT /evidence="ECO:0007829|PDB:2W3C"
FT HELIX 379..393
FT /evidence="ECO:0007829|PDB:2W3C"
FT HELIX 397..405
FT /evidence="ECO:0007829|PDB:2W3C"
FT STRAND 414..416
FT /evidence="ECO:0007829|PDB:2W3C"
FT HELIX 421..429
FT /evidence="ECO:0007829|PDB:2W3C"
FT HELIX 434..448
FT /evidence="ECO:0007829|PDB:2W3C"
FT HELIX 452..458
FT /evidence="ECO:0007829|PDB:2W3C"
FT STRAND 466..469
FT /evidence="ECO:0007829|PDB:2W3C"
FT HELIX 474..481
FT /evidence="ECO:0007829|PDB:2W3C"
FT TURN 482..485
FT /evidence="ECO:0007829|PDB:2W3C"
FT HELIX 488..502
FT /evidence="ECO:0007829|PDB:2W3C"
FT HELIX 506..513
FT /evidence="ECO:0007829|PDB:2W3C"
FT HELIX 518..527
FT /evidence="ECO:0007829|PDB:2W3C"
FT TURN 531..534
FT /evidence="ECO:0007829|PDB:2W3C"
FT HELIX 535..550
FT /evidence="ECO:0007829|PDB:2W3C"
FT STRAND 557..559
FT /evidence="ECO:0007829|PDB:2W3C"
FT HELIX 561..571
FT /evidence="ECO:0007829|PDB:2W3C"
FT HELIX 574..582
FT /evidence="ECO:0007829|PDB:2W3C"
FT TURN 583..586
FT /evidence="ECO:0007829|PDB:2W3C"
FT HELIX 590..593
FT /evidence="ECO:0007829|PDB:2W3C"
FT HELIX 604..606
FT /evidence="ECO:0007829|PDB:2W3C"
FT HELIX 611..627
FT /evidence="ECO:0007829|PDB:2W3C"
SQ SEQUENCE 962 AA; 107895 MW; C963652209031008 CRC64;
MNFLRGVMGG QSAGPQHTEA ETIQKLCDRV ASSTLLDDRR NAVRALKSLS KKYRLEVGIQ
AMEHLIHVLQ TDRSDSEIIG YALDTLYNII SNEEEEEVEE NSTRQSEDLG SQFTEIFIKQ
QENVTLLLSL LEEFDFHVRW PGVKLLTSLL KQLGPQVQQI ILVSPMGVSR LMDLLADSRE
VIRNDGVLLL QALTRSNGAI QKIVAFENAF ERLLDIISEE GNSDGGIVVE DCLILLQNLL
KNNNSNQNFF KEGSYIQRMK PWFEVGDENS GWSAQKVTNL HLMLQLVRVL VSPTNPPGAT
SSCQKAMFQC GLLQQLCTIL MATGVPADIL TETINTVSEV IRGCQVNQDY FASVNAPSNP
PRPAIVVLLM SMVNERQPFV LRCAVLYCFQ CFLYKNQKGQ GEIVSTLLPS TIDATGNSVS
AGQLLCGGLF STDSLSNWCA AVALAHALQE NATQKEQLLR VQLATSIGNP PVSLLQQCTN
ILSQGSKIQT RVGLLMLLCT WLSNCPIAVT HFLHNSANVP FLTGQIAENL GEEEQLVQGL
CALLLGISIY FNDNSLESYM KEKLKQLIEK RIGKENFIEK LGFISKHELY SRASQKPQPN
FPSPEYMIFD HEFTKLVKEL EGVITKAIYK SSEEDKKEEE VKKTLEQHDN IVTHYKNMIR
EQDLQLEELR QQVSTLKCQN EQLQTAVTQQ VSQIQQHKDQ YNLLKIQLGK DNQHQGSYSE
GAQMNGIQPE EIGRLREEIE ELKRNQELLQ SQLTEKDSMI ENMKSSQTSG TNEQSSAIVS
ARDSEQVAEL KQELATLKSQ LNSQSVEITK LQTEKQELLQ KTEAFAKSVE VQGETETIIA
TKTTDVEGRL SALLQETKEL KNEIKALSEE RTAIKEQLDS SNSTIAILQT EKDKLELEIT
DSKKEQDDLL VLLADQDQKI LSLKNKLKDL GHPVEEEDEL ESGDQEDEDD ESEDPGKDLD
HI
