TIP20_YEAST
ID TIP20_YEAST Reviewed; 701 AA.
AC P33891; D6VU04;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Protein transport protein TIP20;
GN Name=TIP20; Synonyms=TIP1; OrderedLocusNames=YGL145W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH SEC20.
RX PubMed=8334998; DOI=10.1002/j.1460-2075.1993.tb05944.x;
RA Sweet D.J., Pelham H.R.B.;
RT "The TIP1 gene of Saccharomyces cerevisiae encodes an 80 kDa cytoplasmic
RT protein that interacts with the cytoplasmic domain of Sec20p.";
RL EMBO J. 12:2831-2840(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9046099;
RX DOI=10.1002/(sici)1097-0061(199702)13:2<177::aid-yea62>3.0.co;2-2;
RA Voet M., Defoor E., Verhasselt P., Riles L., Robben J., Volckaert G.;
RT "The sequence of a nearly unclonable 22.8 kb segment on the left arm
RT chromosome VII from Saccharomyces cerevisiae reveals ARO2, RPL9A, TIP1,
RT MRF1 genes and six new open reading frames.";
RL Yeast 13:177-182(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP INTERACTION WITH SEC39.
RX PubMed=15942868; DOI=10.2323/jgam.51.73;
RA Ishikawa T., Unno K., Nonaka G., Nakajima H., Kitamoto K.;
RT "Isolation of Saccharomyces cerevisiae RNase T1 hypersensitive (rns)
RT mutants and genetic analysis of the RNS1/DSL1 gene.";
RL J. Gen. Appl. Microbiol. 51:73-82(2005).
RN [7]
RP FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH DSL1; SEC39; SEC20; USE1 AND
RP UFE1.
RX PubMed=15958492; DOI=10.1091/mbc.e05-01-0056;
RA Kraynack B.A., Chan A., Rosenthal E., Essid M., Umansky B., Waters M.G.,
RA Schmitt H.D.;
RT "Dsl1p, Tip20p, and the novel Dsl3(Sec39) protein are required for the
RT stability of the Q/t-SNARE complex at the endoplasmic reticulum in yeast.";
RL Mol. Biol. Cell 16:3963-3977(2005).
RN [8]
RP IDENTIFICATION IN A COMPLEX WITH DSL1; SEC39; SEC20; UFE1; USE1 AND SEC22.
RX PubMed=16429126; DOI=10.1038/nature04532;
RA Gavin A.-C., Aloy P., Grandi P., Krause R., Boesche M., Marzioch M.,
RA Rau C., Jensen L.J., Bastuck S., Duempelfeld B., Edelmann A.,
RA Heurtier M.-A., Hoffman V., Hoefert C., Klein K., Hudak M., Michon A.-M.,
RA Schelder M., Schirle M., Remor M., Rudi T., Hooper S., Bauer A.,
RA Bouwmeester T., Casari G., Drewes G., Neubauer G., Rick J.M., Kuster B.,
RA Bork P., Russell R.B., Superti-Furga G.;
RT "Proteome survey reveals modularity of the yeast cell machinery.";
RL Nature 440:631-636(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Required for protein transport between the Golgi and the
CC endoplasmic reticulum. May contribute to tethering of coatomer-coated
CC retrograde transport vesicles to the ER membrane through interaction
CC with and stabilization of the SNARE complex.
CC {ECO:0000269|PubMed:15958492, ECO:0000269|PubMed:8334998}.
CC -!- SUBUNIT: Component of a peripheral membrane protein complex consisting
CC of DSL1, SEC39/DSL3 and TIP20. Bound to a SNARE complex consisting of
CC UFE1, USE1, SEC20 and SEC22 or YKT6 through direct interaction of TIP20
CC with SEC20. Interacts with DSL1, SEC39/DSL3 and the cytoplasmic domain
CC of SEC20. {ECO:0000269|PubMed:15942868, ECO:0000269|PubMed:15958492,
CC ECO:0000269|PubMed:16429126, ECO:0000269|PubMed:8334998}.
CC -!- INTERACTION:
CC P33891; P53847: DSL1; NbExp=14; IntAct=EBI-19396, EBI-29249;
CC P33891; P28791: SEC20; NbExp=8; IntAct=EBI-19396, EBI-16572;
CC P33891; Q12745: SEC39; NbExp=4; IntAct=EBI-19396, EBI-31898;
CC P33891; P41834: UFE1; NbExp=3; IntAct=EBI-19396, EBI-20016;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:8334998}; Peripheral membrane protein
CC {ECO:0000269|PubMed:8334998}.
CC -!- MISCELLANEOUS: Present with 6020 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X72699; CAA51249.1; -; Genomic_DNA.
DR EMBL; X99960; CAA68217.1; -; Genomic_DNA.
DR EMBL; Z72667; CAA96857.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07965.1; -; Genomic_DNA.
DR PIR; S35313; S35313.
DR RefSeq; NP_116577.1; NM_001181010.2.
DR PDB; 3ETV; X-ray; 1.94 A; A=1-40.
DR PDB; 3FHN; X-ray; 3.00 A; A/B/C/D=2-701.
DR PDBsum; 3ETV; -.
DR PDBsum; 3FHN; -.
DR AlphaFoldDB; P33891; -.
DR SMR; P33891; -.
DR BioGRID; 33107; 211.
DR ComplexPortal; CPX-1786; Dsl1 tethering complex.
DR DIP; DIP-2004N; -.
DR IntAct; P33891; 11.
DR MINT; P33891; -.
DR STRING; 4932.YGL145W; -.
DR iPTMnet; P33891; -.
DR MaxQB; P33891; -.
DR PaxDb; P33891; -.
DR PRIDE; P33891; -.
DR EnsemblFungi; YGL145W_mRNA; YGL145W; YGL145W.
DR GeneID; 852732; -.
DR KEGG; sce:YGL145W; -.
DR SGD; S000003113; TIP20.
DR VEuPathDB; FungiDB:YGL145W; -.
DR eggNOG; KOG2218; Eukaryota.
DR HOGENOM; CLU_410507_0_0_1; -.
DR InParanoid; P33891; -.
DR OMA; TCSQIFM; -.
DR BioCyc; YEAST:G3O-30639-MON; -.
DR Reactome; R-SCE-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR EvolutionaryTrace; P33891; -.
DR PRO; PR:P33891; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P33891; protein.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0070939; C:Dsl1/NZR complex; IDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006914; P:autophagy; IMP:SGD.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0060628; P:regulation of ER to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IDA:ComplexPortal.
DR Gene3D; 1.10.10.2270; -; 1.
DR Gene3D; 1.10.357.100; -; 1.
DR Gene3D; 1.20.58.1420; -; 1.
DR Gene3D; 1.20.58.670; -; 1.
DR Gene3D; 6.10.280.210; -; 1.
DR InterPro; IPR042044; EXOC6PINT-1/Sec15/Tip20_C_dom2.
DR InterPro; IPR007528; RINT1_Tip20.
DR InterPro; IPR042041; Tip20p_domA.
DR InterPro; IPR042042; Tip20p_domB.
DR InterPro; IPR042043; Tip20p_domC.
DR InterPro; IPR042040; Tip20p_domE.
DR PANTHER; PTHR13520; PTHR13520; 1.
DR Pfam; PF04437; RINT1_TIP1; 1.
DR PROSITE; PS51386; RINT1_TIP20; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endoplasmic reticulum; ER-Golgi transport; Membrane;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..701
FT /note="Protein transport protein TIP20"
FT /id="PRO_0000072543"
FT DOMAIN 147..701
FT /note="RINT1/TIP20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00717"
FT HELIX 10..31
FT /evidence="ECO:0007829|PDB:3ETV"
FT HELIX 46..54
FT /evidence="ECO:0007829|PDB:3FHN"
FT HELIX 59..67
FT /evidence="ECO:0007829|PDB:3FHN"
FT HELIX 73..105
FT /evidence="ECO:0007829|PDB:3FHN"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:3FHN"
FT HELIX 115..129
FT /evidence="ECO:0007829|PDB:3FHN"
FT HELIX 142..159
FT /evidence="ECO:0007829|PDB:3FHN"
FT HELIX 161..178
FT /evidence="ECO:0007829|PDB:3FHN"
FT TURN 179..182
FT /evidence="ECO:0007829|PDB:3FHN"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:3FHN"
FT HELIX 192..208
FT /evidence="ECO:0007829|PDB:3FHN"
FT HELIX 239..255
FT /evidence="ECO:0007829|PDB:3FHN"
FT HELIX 262..287
FT /evidence="ECO:0007829|PDB:3FHN"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:3FHN"
FT HELIX 296..307
FT /evidence="ECO:0007829|PDB:3FHN"
FT HELIX 309..320
FT /evidence="ECO:0007829|PDB:3FHN"
FT HELIX 324..344
FT /evidence="ECO:0007829|PDB:3FHN"
FT HELIX 352..355
FT /evidence="ECO:0007829|PDB:3FHN"
FT HELIX 358..378
FT /evidence="ECO:0007829|PDB:3FHN"
FT HELIX 383..388
FT /evidence="ECO:0007829|PDB:3FHN"
FT HELIX 389..404
FT /evidence="ECO:0007829|PDB:3FHN"
FT HELIX 406..409
FT /evidence="ECO:0007829|PDB:3FHN"
FT HELIX 413..416
FT /evidence="ECO:0007829|PDB:3FHN"
FT HELIX 417..425
FT /evidence="ECO:0007829|PDB:3FHN"
FT HELIX 427..439
FT /evidence="ECO:0007829|PDB:3FHN"
FT STRAND 446..449
FT /evidence="ECO:0007829|PDB:3FHN"
FT HELIX 450..474
FT /evidence="ECO:0007829|PDB:3FHN"
FT HELIX 478..490
FT /evidence="ECO:0007829|PDB:3FHN"
FT HELIX 500..511
FT /evidence="ECO:0007829|PDB:3FHN"
FT HELIX 513..529
FT /evidence="ECO:0007829|PDB:3FHN"
FT HELIX 531..535
FT /evidence="ECO:0007829|PDB:3FHN"
FT HELIX 538..540
FT /evidence="ECO:0007829|PDB:3FHN"
FT HELIX 558..560
FT /evidence="ECO:0007829|PDB:3FHN"
FT HELIX 561..575
FT /evidence="ECO:0007829|PDB:3FHN"
FT HELIX 581..601
FT /evidence="ECO:0007829|PDB:3FHN"
FT TURN 602..606
FT /evidence="ECO:0007829|PDB:3FHN"
FT HELIX 611..625
FT /evidence="ECO:0007829|PDB:3FHN"
FT HELIX 637..649
FT /evidence="ECO:0007829|PDB:3FHN"
FT HELIX 650..653
FT /evidence="ECO:0007829|PDB:3FHN"
FT HELIX 655..657
FT /evidence="ECO:0007829|PDB:3FHN"
FT TURN 658..661
FT /evidence="ECO:0007829|PDB:3FHN"
FT HELIX 663..668
FT /evidence="ECO:0007829|PDB:3FHN"
FT HELIX 673..678
FT /evidence="ECO:0007829|PDB:3FHN"
FT STRAND 681..683
FT /evidence="ECO:0007829|PDB:3FHN"
FT HELIX 685..696
FT /evidence="ECO:0007829|PDB:3FHN"
SQ 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
