ID YIF1_YEAST Reviewed; 314 AA. AC P53845; D6W0T0; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 04-NOV-2026, entry version 179. DE RecName: Full=Protein transport protein YIF1; DE AltName: Full=YIP1-interacting factor 1; GN Name=YIF1; OrderedLocusNames=YNL263C; ORFNames=N0820; 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]. RC STRAIN=ATCC 96604 / S288c / FY1679; RX PubMed=8740425; RX DOI=10.1002/(sici)1097-0061(199604)12:5%3c505::aid-yea932%3e3.0.co;2-f; RA Sen-Gupta M., Lyck R., Fleig U., Niedenthal R.K., Hegemann J.H.; RT "The sequence of a 24,152 bp segment from the left arm of chromosome XIV RT from Saccharomyces cerevisiae between the BNI1 and the POL2 genes."; RL Yeast 12:505-514(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169873; DOI=10.1038/387s093; RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F., RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its RT evolutionary implications."; RL Nature 387:93-98(1997). RN [3] 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 [4] RP INTERACTION WITH YIP1, TOPOLOGY, AND SUBCELLULAR LOCATION. RX PubMed=10970842; DOI=10.1093/emboj/19.17.4485; RA Matern H.T., Yang X., Andrulis E., Sternglanz R., Trepte H.-H., RA Gallwitz D.; RT "A novel Golgi membrane protein is part of a GTPase-binding protein complex RT involved in vesicle targeting."; RL EMBO J. 19:4485-4492(2000). RN [5] RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=11157978; DOI=10.1083/jcb.152.3.503; RA Otte S., Belden W.J., Heidtman M., Liu J., Jensen O.N., Barlowe C.; RT "Erv41p and Erv46p: new components of COPII vesicles involved in transport RT between the ER and Golgi complex."; RL J. Cell Biol. 152:503-518(2001). RN [6] RP INTERACTION WITH SEC4; YIP4; YIP5; YPT1; YPT6; YPT7; YPT10; YPT11; YPT31; RP YPT32 AND YPT52. RX PubMed=11943201; DOI=10.1016/s0014-5793(02)02442-0; RA Calero M., Winand N.J., Collins R.N.; RT "Identification of the novel proteins Yip4p and Yip5p as Rab GTPase RT interacting factors."; RL FEBS Lett. 515:89-98(2002). RN [7] RP INTERACTION WITH BTN2. RX PubMed=12615067; DOI=10.1016/s0006-291x(03)00209-2; RA Chattopadhyay S., Roberts P.M., Pearce D.A.; RT "The yeast model for Batten disease: a role for Btn2p in the trafficking of RT the Golgi-associated vesicular targeting protein, Yif1p."; RL Biochem. Biophys. Res. Commun. 302:534-538(2003). RN [8] RP FUNCTION, AND INTERACTION WITH BOS1; SEC22 AND YPT1. RX PubMed=12657649; DOI=10.1074/jbc.m302406200; RA Barrowman J., Wang W., Zhang Y., Ferro-Novick S.; RT "The Yip1p.Yif1p complex is required for the fusion competence of RT endoplasmic reticulum-derived vesicles."; RL J. Biol. Chem. 278:19878-19884(2003). RN [9] RP INTERACTION WITH SNX3. RX PubMed=15263065; DOI=10.1074/mcp.m400081-mcp200; RA Vollert C.S., Uetz P.; RT "The phox homology (PX) domain protein interaction network in yeast."; RL Mol. Cell. Proteomics 3:1053-1064(2004). RN [10] RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=16107716; DOI=10.1128/mcb.25.17.7696-7710.2005; RA Inadome H., Noda Y., Adachi H., Yoda K.; RT "Immunoisolation of the yeast Golgi subcompartments and characterization of RT a novel membrane protein, Svp26, discovered in the Sed5-containing RT compartments."; RL Mol. Cell. Biol. 25:7696-7710(2005). RN [11] RP TOPOLOGY [LARGE SCALE ANALYSIS]. RC STRAIN=ATCC 208353 / W303-1A; RX PubMed=16847258; DOI=10.1073/pnas.0604075103; RA Kim H., Melen K., Oesterberg M., von Heijne G.; RT "A global topology map of the Saccharomyces cerevisiae membrane proteome."; RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006). RN [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 fusion of ER-derived vesicles with the Golgi CC during ER-to-Golgi protein transport. May be involved in proper CC membrane localization of Rab GTPases. {ECO:0000269|PubMed:12657649}. CC -!- SUBUNIT: Component of the YIP1-YIF1 complex, composed of at least YIF1, CC YIP1 and YOS1. The complex interacts with the ER to Golgi SNAREs BOS1 CC and SEC22. Interacts with the YIP1 family members YIP4 and YIP5, and CC with the Rab GTPases SEC4, YPT1, YPT6, YPT7, YPT10, YPT11, YPT31, YPT32 CC and YPT52. Interacts with BTN2 and SNX3. {ECO:0000269|PubMed:10970842, CC ECO:0000269|PubMed:11943201, ECO:0000269|PubMed:12615067, CC ECO:0000269|PubMed:12657649, ECO:0000269|PubMed:15263065}. CC -!- INTERACTION: CC P53845; P53286: BTN2; NbExp=2; IntAct=EBI-28230, EBI-3796; CC P53845; P07560: SEC4; NbExp=2; IntAct=EBI-28230, EBI-16858; CC P53845; P32912: VAM7; NbExp=3; IntAct=EBI-28230, EBI-20232; CC P53845; P32913: VPS17; NbExp=2; IntAct=EBI-28230, EBI-20366; CC P53845; P53039: YIP1; NbExp=5; IntAct=EBI-28230, EBI-25295; CC P53845; P53093: YIP4; NbExp=2; IntAct=EBI-28230, EBI-24124; CC P53845; P01123: YPT1; NbExp=3; IntAct=EBI-28230, EBI-29496; CC P53845; P38146: YPT10; NbExp=2; IntAct=EBI-28230, EBI-29357; CC P53845; P38555: YPT31; NbExp=3; IntAct=EBI-28230, EBI-29379; CC P53845; P51996: YPT32; NbExp=2; IntAct=EBI-28230, EBI-29384; CC P53845; P38815: YPT35; NbExp=4; IntAct=EBI-28230, EBI-24665; CC P53845; P36019: YPT53; NbExp=2; IntAct=EBI-28230, EBI-29415; CC P53845; P32939: YPT7; NbExp=2; IntAct=EBI-28230, EBI-29509; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:11157978}; Multi-pass membrane protein CC {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:10970842, CC ECO:0000269|PubMed:16107716}; Multi-pass membrane protein CC {ECO:0000255}. Cytoplasmic vesicle, COPII-coated vesicle CC {ECO:0000269|PubMed:11157978}. Note=Also found in ER-derived COPII- CC coated vesicles. {ECO:0000269|PubMed:11157978}. CC -!- SIMILARITY: Belongs to the YIF1 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X92494; CAA63234.1; -; Genomic_DNA. DR EMBL; Z71539; CAA96170.1; -; Genomic_DNA. DR EMBL; BK006947; DAA10296.1; -; Genomic_DNA. DR PIR; S60918; S60918. DR RefSeq; NP_014136.1; NM_001183101.1. DR AlphaFoldDB; P53845; -. DR BioGRID; 35576; 75. DR DIP; DIP-1729N; -. DR FunCoup; P53845; 593. DR IntAct; P53845; 36. DR STRING; 4932.YNL263C; -. DR iPTMnet; P53845; -. DR PaxDb; 4932-YNL263C; -. DR PeptideAtlas; P53845; -. DR EnsemblFungi; YNL263C_mRNA; YNL263C; YNL263C. DR GeneID; 855458; -. DR KEGG; sce:YNL263C; -. DR AGR; SGD:S000005207; -. DR SGD; S000005207; YIF1. DR VEuPathDB; FungiDB:YNL263C; -. DR eggNOG; KOG3094; Eukaryota. DR HOGENOM; CLU_047877_2_1_1; -. DR InParanoid; P53845; -. DR OMA; AAMNQES; -. DR OrthoDB; 337750at2759; -. DR BioCyc; YEAST:G3O-33259-MONOMER; -. DR BioGRID-ORCS; 855458; 5 hits in 10 CRISPR screens. DR PRO; PR:P53845; -. DR Proteomes; UP000002311; Chromosome XIV. DR RNAct; P53845; protein. DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IDA:SGD. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IPI:SGD. DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IBA:GO_Central. DR GO; GO:0000139; C:Golgi membrane; IDA:SGD. DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:SGD. DR InterPro; IPR005578; Yif1_fam. DR PANTHER; PTHR14083; YIP1 INTERACTING FACTOR HOMOLOG YIF1 PROTEIN; 1. DR PANTHER; PTHR14083:SF0; YIP1D-INTERACTING FACTOR 1, ISOFORM C; 1. DR Pfam; PF03878; YIF1; 1. PE 1: Evidence at protein level; KW Acetylation; Cytoplasmic vesicle; Endoplasmic reticulum; KW ER-Golgi transport; Golgi apparatus; Membrane; Protein transport; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22814378" FT CHAIN 2..314 FT /note="Protein transport protein YIF1" FT /id="PRO_0000203381" FT TOPO_DOM 2..153 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 154..174 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 175..188 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 189..209 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 210..217 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 218..238 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 239..243 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 244..264 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 265..293 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 294..313 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 314 FT /note="Lumenal" FT /evidence="ECO:0000255" FT REGION 9..32 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 10..32 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0007744|PubMed:22814378" SQ SEQUENCE 314 AA; 35498 MW; 3D1550C65A7D0A92 CRC64; MSYNPYAYAT SEQNGVNDRF SHTPQQQRPM QIPRNTPVNG QGNANMNANV NGSGGGFPFQ DPRGSMAFQL GQSAFSNFIG QDNFNQFQET VNKATANAAG SQQISTYFQV STRYVINKLK LILVPFLNGT KNWQRIMDSG NFLPPRDDVN SPDMYMPIMG LVTYILIWNT QQGLKGSFNP EDLYYKLSST LAFVCLDLLI LKLGLYLLID SKIPSFSLVE LLCYVGYKFV PLILAQLLTN VTMPFNLNIL IKFYLFIAFG VFLLRSVKFN LLSRSGAEDD DIHVSISKST VKKCNYFLFV YGFIWQNVLM WLMG //