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Protein transport protein TIP20

 TIP20_YEAST             Reviewed;         701 AA.
P33891; D6VU04;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 1.
25-OCT-2017, entry version 140.
RecName: Full=Protein transport protein TIP20;
Name=TIP20; Synonyms=TIP1; OrderedLocusNames=YGL145W;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
INTERACTION WITH SEC20.
PubMed=8334998;
Sweet D.J., Pelham H.R.B.;
"The TIP1 gene of Saccharomyces cerevisiae encodes an 80 kDa
cytoplasmic protein that interacts with the cytoplasmic domain of
Sec20p.";
EMBO J. 12:2831-2840(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=9046099;
DOI=10.1002/(SICI)1097-0061(199702)13:2<177::AID-YEA62>3.0.CO;2-2;
Voet M., Defoor E., Verhasselt P., Riles L., Robben J., Volckaert G.;
"The sequence of a nearly unclonable 22.8 kb segment on the left arm
chromosome VII from Saccharomyces cerevisiae reveals ARO2, RPL9A,
TIP1, MRF1 genes and six new open reading frames.";
Yeast 13:177-182(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169869;
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M.,
Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J.,
Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E.,
Clemente M.L., Coblenz A., Coglievina M., Coissac E., Defoor E.,
Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B.,
Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L.,
Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M.,
Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M.,
Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B.,
Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W.,
Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A.,
Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S.,
Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L.,
Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S.,
Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J.,
Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M.,
Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B.,
Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J.,
Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M.,
van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M.,
Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H.,
Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M.,
Zollner A., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
Nature 387:81-84(1997).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[6]
INTERACTION WITH SEC39.
PubMed=15942868; DOI=10.2323/jgam.51.73;
Ishikawa T., Unno K., Nonaka G., Nakajima H., Kitamoto K.;
"Isolation of Saccharomyces cerevisiae RNase T1 hypersensitive (rns)
mutants and genetic analysis of the RNS1/DSL1 gene.";
J. Gen. Appl. Microbiol. 51:73-82(2005).
[7]
FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH DSL1; SEC39; SEC20;
USE1 AND UFE1.
PubMed=15958492; DOI=10.1091/mbc.E05-01-0056;
Kraynack B.A., Chan A., Rosenthal E., Essid M., Umansky B.,
Waters M.G., Schmitt H.D.;
"Dsl1p, Tip20p, and the novel Dsl3(Sec39) protein are required for the
stability of the Q/t-SNARE complex at the endoplasmic reticulum in
yeast.";
Mol. Biol. Cell 16:3963-3977(2005).
[8]
IDENTIFICATION IN A COMPLEX WITH DSL1; SEC39; SEC20; UFE1; USE1 AND
SEC22.
PubMed=16429126; DOI=10.1038/nature04532;
Gavin A.-C., Aloy P., Grandi P., Krause R., Boesche M., Marzioch M.,
Rau C., Jensen L.J., Bastuck S., Duempelfeld B., Edelmann A.,
Heurtier M.-A., Hoffman V., Hoefert C., Klein K., Hudak M.,
Michon A.-M., Schelder M., Schirle M., Remor M., Rudi T., Hooper S.,
Bauer A., Bouwmeester T., Casari G., Drewes G., Neubauer G.,
Rick J.M., Kuster B., Bork P., Russell R.B., Superti-Furga G.;
"Proteome survey reveals modularity of the yeast cell machinery.";
Nature 440:631-636(2006).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
-!- FUNCTION: Required for protein transport between the Golgi and the
endoplasmic reticulum. May contribute to tethering of coatomer-
coated retrograde transport vesicles to the ER membrane through
interaction with and stabilization of the SNARE complex.
{ECO:0000269|PubMed:15958492, ECO:0000269|PubMed:8334998}.
-!- SUBUNIT: Component of a peripheral membrane protein complex
consisting of DSL1, SEC39/DSL3 and TIP20. Bound to a SNARE complex
consisting of UFE1, USE1, SEC20 and SEC22 or YKT6 through direct
interaction of TIP20 with SEC20. Interacts with DSL1, SEC39/DSL3
and the cytoplasmic domain of SEC20. {ECO:0000269|PubMed:15942868,
ECO:0000269|PubMed:15958492, ECO:0000269|PubMed:16429126,
ECO:0000269|PubMed:8334998}.
-!- INTERACTION:
P53847:DSL1; NbExp=14; IntAct=EBI-19396, EBI-29249;
P28791:SEC20; NbExp=8; IntAct=EBI-19396, EBI-16572;
Q12745:SEC39; NbExp=4; IntAct=EBI-19396, EBI-31898;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:8334998}; Peripheral membrane protein
{ECO:0000269|PubMed:8334998}.
-!- MISCELLANEOUS: Present with 6020 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-----------------------------------------------------------------------
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EMBL; X72699; CAA51249.1; -; Genomic_DNA.
EMBL; X99960; CAA68217.1; -; Genomic_DNA.
EMBL; Z72667; CAA96857.1; -; Genomic_DNA.
EMBL; BK006941; DAA07965.1; -; Genomic_DNA.
PIR; S35313; S35313.
RefSeq; NP_116577.1; NM_001181010.2.
PDB; 3ETV; X-ray; 1.94 A; A=1-40.
PDB; 3FHN; X-ray; 3.00 A; A/B/C/D=2-701.
PDBsum; 3ETV; -.
PDBsum; 3FHN; -.
ProteinModelPortal; P33891; -.
SMR; P33891; -.
BioGrid; 33107; 195.
DIP; DIP-2004N; -.
IntAct; P33891; 11.
MINT; MINT-403248; -.
STRING; 4932.YGL145W; -.
iPTMnet; P33891; -.
MaxQB; P33891; -.
PRIDE; P33891; -.
EnsemblFungi; YGL145W; YGL145W; YGL145W.
GeneID; 852732; -.
KEGG; sce:YGL145W; -.
EuPathDB; FungiDB:YGL145W; -.
SGD; S000003113; TIP20.
HOGENOM; HOG000000922; -.
InParanoid; P33891; -.
KO; K20474; -.
OMA; RFNYHFN; -.
OrthoDB; EOG092C0T80; -.
BioCyc; YEAST:G3O-30639-MONOMER; -.
EvolutionaryTrace; P33891; -.
PRO; PR:P33891; -.
Proteomes; UP000002311; Chromosome VII.
GO; GO:0070939; C:Dsl1/NZR complex; IDA:SGD.
GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; IGI:SGD.
InterPro; IPR007528; RINT1_Tip20.
PANTHER; PTHR13520; PTHR13520; 1.
Pfam; PF04437; RINT1_TIP1; 1.
PROSITE; PS51386; RINT1_TIP20; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Endoplasmic reticulum;
ER-Golgi transport; Membrane; Protein transport; Reference proteome;
Transport.
CHAIN 1 701 Protein transport protein TIP20.
/FTId=PRO_0000072543.
DOMAIN 147 701 RINT1/TIP20. {ECO:0000255|PROSITE-
ProRule:PRU00717}.
HELIX 10 31 {ECO:0000244|PDB:3ETV}.
HELIX 46 54 {ECO:0000244|PDB:3FHN}.
HELIX 59 67 {ECO:0000244|PDB:3FHN}.
HELIX 73 105 {ECO:0000244|PDB:3FHN}.
HELIX 110 112 {ECO:0000244|PDB:3FHN}.
HELIX 115 129 {ECO:0000244|PDB:3FHN}.
HELIX 142 159 {ECO:0000244|PDB:3FHN}.
HELIX 161 178 {ECO:0000244|PDB:3FHN}.
TURN 179 182 {ECO:0000244|PDB:3FHN}.
HELIX 188 190 {ECO:0000244|PDB:3FHN}.
HELIX 192 208 {ECO:0000244|PDB:3FHN}.
HELIX 239 255 {ECO:0000244|PDB:3FHN}.
HELIX 262 287 {ECO:0000244|PDB:3FHN}.
HELIX 290 292 {ECO:0000244|PDB:3FHN}.
HELIX 296 307 {ECO:0000244|PDB:3FHN}.
HELIX 309 320 {ECO:0000244|PDB:3FHN}.
HELIX 324 344 {ECO:0000244|PDB:3FHN}.
HELIX 352 355 {ECO:0000244|PDB:3FHN}.
HELIX 358 378 {ECO:0000244|PDB:3FHN}.
HELIX 383 388 {ECO:0000244|PDB:3FHN}.
HELIX 389 404 {ECO:0000244|PDB:3FHN}.
HELIX 406 409 {ECO:0000244|PDB:3FHN}.
HELIX 413 416 {ECO:0000244|PDB:3FHN}.
HELIX 417 425 {ECO:0000244|PDB:3FHN}.
HELIX 427 439 {ECO:0000244|PDB:3FHN}.
STRAND 446 449 {ECO:0000244|PDB:3FHN}.
HELIX 450 474 {ECO:0000244|PDB:3FHN}.
HELIX 478 490 {ECO:0000244|PDB:3FHN}.
HELIX 500 511 {ECO:0000244|PDB:3FHN}.
HELIX 513 529 {ECO:0000244|PDB:3FHN}.
HELIX 531 535 {ECO:0000244|PDB:3FHN}.
HELIX 538 540 {ECO:0000244|PDB:3FHN}.
HELIX 558 560 {ECO:0000244|PDB:3FHN}.
HELIX 561 575 {ECO:0000244|PDB:3FHN}.
HELIX 581 601 {ECO:0000244|PDB:3FHN}.
TURN 602 606 {ECO:0000244|PDB:3FHN}.
HELIX 611 625 {ECO:0000244|PDB:3FHN}.
HELIX 637 649 {ECO:0000244|PDB:3FHN}.
HELIX 650 653 {ECO:0000244|PDB:3FHN}.
HELIX 655 657 {ECO:0000244|PDB:3FHN}.
TURN 658 661 {ECO:0000244|PDB:3FHN}.
HELIX 663 668 {ECO:0000244|PDB:3FHN}.
HELIX 673 678 {ECO:0000244|PDB:3FHN}.
STRAND 681 683 {ECO:0000244|PDB:3FHN}.
HELIX 685 696 {ECO:0000244|PDB:3FHN}.
SEQUENCE 701 AA; 81167 MW; 3E561DD4C0B9C176 CRC64;
MNGIDDLLNI NDRIKQVQNE RNELASKLQN LKQSLASNDT EVALSEVIAQ DIIEVGASVE
GLEQLRAKYG DLQILNKLEK VAVQQTQMQA GVDKLDSFER QLDELAEQPP DQFTLDDVKA
LHSKLTSVFA TVPQINNIDS QYAAYNKLKS KVTGKYNDVI IQRLATNWSN TFDQKLLEAQ
WDTQKFASTS VGLVKCLREN STKLYQLSLL YLPLEEETQN GDSERPLSRS NNNQEPVLWN
FKSLANNFNV RFTYHFHATS SSSKIETYFQ FLNDYLAENL YKCINIFHDD CNGLTKPVIH
EQFINYVLQP IRDKVRSTLF QNDLKTLIVL ISQILATDKN LLNSFHYHGL GLVSLISDEV
WEKWINYEVE MANRQFINIT KNPEDFPKSS QNFVKLINKI YDYLEPFYDL DFDLLVRYKL
MTCSLIFMNL TSSYLDYILT VDSLNETRTK EQELYQTMAK LQHVNFVYRK IKSLSSNFIF
IQLTDIVNST ESKKYNSLFQ NVENDYEKAM STDMQNSIVH RIQKLLKETL RNYFKISTWS
TLEMSVDENI GPSSVPSAEL VNSINVLRRL INKLDSMDIP LAISLKVKNE LLNVIVNYFT
ESILKLNKFN QNGLNQFLHD FKSLSSILSL PSHATNYKCM SLHELVKILK LKYDPNNQQF
LNPEYIKTGN FTSLKEAYSI KYLKDTKIQD ALYRIIYGNI L


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