USO1_BOVIN
ID USO1_BOVIN Reviewed; 961 AA.
AC P41541; Q32PH6;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 139.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, SUBUNIT, AND DOMAIN.
RC TISSUE=Kidney;
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 [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP CHARACTERIZATION.
RX PubMed=1512287; DOI=10.1083/jcb.118.5.1015;
RA Waters M.G., Clary D.O., Rothman J.E.;
RT "A novel 115-kD peripheral membrane protein is required for intercisternal
RT transport in the Golgi stack.";
RL J. Cell Biol. 118:1015-1026(1992).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS) OF 1-651, ARM REPEATS, AND SUBUNIT.
RX PubMed=19414022; DOI=10.1016/j.jmb.2009.04.062;
RA An Y., Chen C.Y., Moyer B., Rotkiewicz P., Elsliger M.A., Godzik A.,
RA Wilson I.A., Balch W.E.;
RT "Structural and functional analysis of the globular head domain of p115
RT provides insight into membrane tethering.";
RL J. Mol. Biol. 391:26-41(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. Interacts with MIF (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Golgi apparatus membrane;
CC Peripheral membrane protein. Note=Recycles between the cytosol and the
CC Golgi apparatus during interphase.
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 promotes
CC dissociation (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the VDP/USO1/EDE1 family. {ECO:0000305}.
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DR EMBL; U14186; AAA62631.1; -; mRNA.
DR EMBL; BC108112; AAI08113.1; -; mRNA.
DR RefSeq; NP_777270.2; NM_174845.2.
DR PDB; 3GQ2; X-ray; 2.18 A; A/B=1-651.
DR PDB; 3GRL; X-ray; 2.00 A; A=1-651.
DR PDBsum; 3GQ2; -.
DR PDBsum; 3GRL; -.
DR AlphaFoldDB; P41541; -.
DR SMR; P41541; -.
DR STRING; 9913.ENSBTAP00000022642; -.
DR iPTMnet; P41541; -.
DR PaxDb; P41541; -.
DR PeptideAtlas; P41541; -.
DR PRIDE; P41541; -.
DR Ensembl; ENSBTAT00000022642; ENSBTAP00000022642; ENSBTAG00000017028.
DR GeneID; 317724; -.
DR KEGG; bta:317724; -.
DR CTD; 8615; -.
DR VEuPathDB; HostDB:ENSBTAG00000017028; -.
DR VGNC; VGNC:36708; USO1.
DR eggNOG; KOG0946; Eukaryota.
DR GeneTree; ENSGT00390000017018; -.
DR HOGENOM; CLU_006318_2_0_1; -.
DR InParanoid; P41541; -.
DR OMA; YSRACKQ; -.
DR OrthoDB; 1273987at2759; -.
DR TreeFam; TF106157; -.
DR Reactome; R-BTA-204005; COPII-mediated vesicle transport.
DR Reactome; R-BTA-6807878; COPI-mediated anterograde transport.
DR EvolutionaryTrace; P41541; -.
DR Proteomes; UP000009136; Chromosome 6.
DR Bgee; ENSBTAG00000017028; Expressed in saliva-secreting gland and 107 other tissues.
DR GO; GO:0005829; C:cytosol; IDA:AgBase.
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:0090498; C:extrinsic component of Golgi membrane; IDA:AgBase.
DR GO; GO:0001650; C:fibrillar center; IEA:Ensembl.
DR GO; GO:0005795; C:Golgi stack; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:AgBase.
DR GO; GO:0042802; F:identical protein binding; IPI:AgBase.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0048211; P:Golgi vesicle docking; IBA:GO_Central.
DR GO; GO:0048219; P:inter-Golgi cisterna vesicle-mediated transport; IMP:AgBase.
DR GO; GO:0006886; P:intracellular protein transport; ISS:AgBase.
DR GO; GO:0061025; P:membrane fusion; IBA:GO_Central.
DR GO; GO:0051260; P:protein homooligomerization; IDA:AgBase.
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; 2.
DR PROSITE; PS50176; ARM_REPEAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Coiled coil; Cytoplasm;
KW Direct protein sequencing; ER-Golgi transport; Golgi apparatus; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Repeat; Transport.
FT CHAIN 1..961
FT /note="General vesicular transport factor p115"
FT /id="PRO_0000065773"
FT REPEAT 20..60
FT /note="ARM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00259,
FT ECO:0000269|PubMed:19414022"
FT REPEAT 61..121
FT /note="ARM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00259,
FT ECO:0000269|PubMed:19414022"
FT REPEAT 123..163
FT /note="ARM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00259,
FT ECO:0000269|PubMed:19414022"
FT REPEAT 166..207
FT /note="ARM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00259,
FT ECO:0000269|PubMed:19414022"
FT REPEAT 208..253
FT /note="ARM 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00259,
FT ECO:0000269|PubMed:19414022"
FT REPEAT 255..310
FT /note="ARM 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00259,
FT ECO:0000269|PubMed:19414022"
FT REPEAT 311..354
FT /note="ARM 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00259,
FT ECO:0000269|PubMed:19414022"
FT REPEAT 363..408
FT /note="ARM 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00259,
FT ECO:0000269|PubMed:19414022"
FT REPEAT 420..459
FT /note="ARM 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00259,
FT ECO:0000269|PubMed:19414022"
FT REPEAT 473..513
FT /note="ARM 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00259,
FT ECO:0000269|PubMed:19414022"
FT REPEAT 518..571
FT /note="ARM 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00259,
FT ECO:0000269|PubMed:19414022"
FT REPEAT 573..630
FT /note="ARM 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00259,
FT ECO:0000269|PubMed:19414022"
FT REGION 1..641
FT /note="Globular head"
FT REGION 764..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 929..961
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 642..929
FT /evidence="ECO:0000255"
FT COMPBIAS 935..954
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 941
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60763"
FT CONFLICT 335
FT /note="N -> K (in Ref. 2; AAI08113)"
FT /evidence="ECO:0000305"
FT HELIX 19..32
FT /evidence="ECO:0007829|PDB:3GRL"
FT HELIX 36..48
FT /evidence="ECO:0007829|PDB:3GRL"
FT TURN 49..55
FT /evidence="ECO:0007829|PDB:3GRL"
FT HELIX 56..60
FT /evidence="ECO:0007829|PDB:3GRL"
FT HELIX 62..70
FT /evidence="ECO:0007829|PDB:3GRL"
FT HELIX 76..90
FT /evidence="ECO:0007829|PDB:3GRL"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:3GQ2"
FT HELIX 109..118
FT /evidence="ECO:0007829|PDB:3GRL"
FT HELIX 122..130
FT /evidence="ECO:0007829|PDB:3GRL"
FT HELIX 136..152
FT /evidence="ECO:0007829|PDB:3GRL"
FT HELIX 154..163
FT /evidence="ECO:0007829|PDB:3GRL"
FT HELIX 167..172
FT /evidence="ECO:0007829|PDB:3GRL"
FT HELIX 173..176
FT /evidence="ECO:0007829|PDB:3GRL"
FT HELIX 180..194
FT /evidence="ECO:0007829|PDB:3GRL"
FT HELIX 198..206
FT /evidence="ECO:0007829|PDB:3GRL"
FT HELIX 209..220
FT /evidence="ECO:0007829|PDB:3GRL"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:3GRL"
FT HELIX 226..240
FT /evidence="ECO:0007829|PDB:3GRL"
FT HELIX 244..252
FT /evidence="ECO:0007829|PDB:3GRL"
FT HELIX 256..263
FT /evidence="ECO:0007829|PDB:3GRL"
FT HELIX 274..290
FT /evidence="ECO:0007829|PDB:3GRL"
FT HELIX 297..309
FT /evidence="ECO:0007829|PDB:3GRL"
FT HELIX 312..320
FT /evidence="ECO:0007829|PDB:3GRL"
FT HELIX 327..341
FT /evidence="ECO:0007829|PDB:3GRL"
FT HELIX 345..353
FT /evidence="ECO:0007829|PDB:3GRL"
FT STRAND 355..360
FT /evidence="ECO:0007829|PDB:3GRL"
FT HELIX 364..372
FT /evidence="ECO:0007829|PDB:3GRL"
FT HELIX 379..393
FT /evidence="ECO:0007829|PDB:3GRL"
FT HELIX 397..405
FT /evidence="ECO:0007829|PDB:3GRL"
FT STRAND 417..419
FT /evidence="ECO:0007829|PDB:3GRL"
FT HELIX 421..429
FT /evidence="ECO:0007829|PDB:3GRL"
FT HELIX 434..448
FT /evidence="ECO:0007829|PDB:3GRL"
FT HELIX 452..458
FT /evidence="ECO:0007829|PDB:3GRL"
FT HELIX 474..481
FT /evidence="ECO:0007829|PDB:3GRL"
FT TURN 482..485
FT /evidence="ECO:0007829|PDB:3GRL"
FT HELIX 488..502
FT /evidence="ECO:0007829|PDB:3GRL"
FT HELIX 506..514
FT /evidence="ECO:0007829|PDB:3GRL"
FT HELIX 518..527
FT /evidence="ECO:0007829|PDB:3GRL"
FT HELIX 532..550
FT /evidence="ECO:0007829|PDB:3GRL"
FT HELIX 557..559
FT /evidence="ECO:0007829|PDB:3GRL"
FT HELIX 561..571
FT /evidence="ECO:0007829|PDB:3GRL"
FT HELIX 574..586
FT /evidence="ECO:0007829|PDB:3GRL"
FT HELIX 590..595
FT /evidence="ECO:0007829|PDB:3GRL"
FT HELIX 604..606
FT /evidence="ECO:0007829|PDB:3GRL"
FT HELIX 611..629
FT /evidence="ECO:0007829|PDB:3GRL"
FT HELIX 633..638
FT /evidence="ECO:0007829|PDB:3GQ2"
SQ SEQUENCE 961 AA; 107515 MW; 993FEB7F90ABC0AC CRC64;
MNFLRGVMGG QSAGPQHTEA ETIQKLCDRV ASSTLLDDRR NAVRALKSLS KKYRLEVGIQ
AMEHLIHVLQ TDRSDSEIIG YALDTLYNII SNDEEEEVEE NSTRQSEDLG SQFTEIFIKQ
QENVTLLLSL LEEFDFHVRW PGVKLLTSLL KQLGPQVQQI ILVSPMGVSR LMDLLADSRE
VIRNDGVLLL QALTRSNGAI QKIVAFENAF ERLLDIITEE GNSDGGIVVE DCLILLQNLL
KNNNSNQNFF KEGSYIQRMK PWFEVGDENS GWSAQKVTNL HLMLQLVRVL VSPNNPPGAT
SSCQKAMFQC GLLQQLCTIL MATGVPADIL TETINTVSEV IRGCQVNQDY FASVNAPSNP
PRPAIVVLLM SMVNERQPFV LRCAVLYCFQ CFLYKNQKGQ GEIVSTLLPS TIDATGNTVS
AGQLLCGGLF STDSLSNWCA AVALAHALQE NATQKEQLLR VQLATSIGNP PVSLLQQCTN
ILSQGSKIQT RVGLLMLLCT WLSNCPIAVT HFLHNSANVP FLTGQIAENL GEEEQLVQGL
CALLLGISIY FNDNSLETYM KEKLKQLIEK RIGKENFIEK LGFISKHELY SRASQKPQPN
FPSPEYMIFD HEFTKLVKEL EGVITKAIYK SSEEDKKEEE VKKTLEQHDS IVTHYKNMIR
EQDLQLEELK QQISTLKCQN EQLQTAVTQQ VSQIQQHKDQ YNLLKVQLGK DSQHQGPYTD
GAQMNGVQPE EISRLREEIE ELKSNRELLQ SQLAEKDSLI ENLKSSQLSP GTNEQSSATA
GDSEQIAELK QELATLKSQL NSQSVEITKL QTEKQELLQK TEAFAKSAPV PGESETVIAT
KTTDVEGRLS ALLQETKELK NEIKALSEER TAIKEQLDSS NSTIAILQNE KNKLEVDITD
SKKEQDDLLV LLADQDQKIF SLKNKLKELG HPVEEEDELE SGDQDDEDDE DEDDGKEQGH
I
