YIF1_YEAST
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 03-AUG-2022, entry version 162.
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<505::aid-yea932>3.0.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;
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}.
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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; 62.
DR DIP; DIP-1729N; -.
DR IntAct; P53845; 29.
DR MINT; P53845; -.
DR STRING; 4932.YNL263C; -.
DR iPTMnet; P53845; -.
DR MaxQB; P53845; -.
DR PaxDb; P53845; -.
DR PRIDE; P53845; -.
DR EnsemblFungi; YNL263C_mRNA; YNL263C; YNL263C.
DR GeneID; 855458; -.
DR KEGG; sce:YNL263C; -.
DR SGD; S000005207; YIF1.
DR VEuPathDB; FungiDB:YNL263C; -.
DR eggNOG; KOG3094; Eukaryota.
DR GeneTree; ENSGT00390000009423; -.
DR HOGENOM; CLU_047877_2_1_1; -.
DR InParanoid; P53845; -.
DR OMA; SHYFQVS; -.
DR BioCyc; YEAST:G3O-33259-MON; -.
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:0030173; C:integral component of Golgi membrane; IDA:SGD.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR005578; Yif1_fam.
DR PANTHER; PTHR14083; PTHR14083; 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 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
