YIP1_YEAST
ID YIP1_YEAST Reviewed; 248 AA.
AC P53039; D6VUV6;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Protein transport protein YIP1;
DE AltName: Full=YPT-interacting protein 1;
GN Name=YIP1; OrderedLocusNames=YGR172C;
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, INTERACTION WITH YPT1 AND
RP YPT31, SUBCELLULAR LOCATION, TOPOLOGY, AND MUTAGENESIS OF PRO-114; GLY-129
RP AND GLY-175.
RC STRAIN=HLR3;
RX PubMed=9724632; DOI=10.1093/emboj/17.17.4954;
RA Yang X., Matern H.T., Gallwitz D.;
RT "Specific binding to a novel and essential Golgi membrane protein (Yip1p)
RT functionally links the transport GTPases Ypt1p and Ypt31p.";
RL EMBO J. 17:4954-4963(1998).
RN [2]
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 [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 YIF1, 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 INTERACTION WITH YOP1.
RX PubMed=11278413; DOI=10.1074/jbc.m008439200;
RA Calero M., Whittaker G.R., Collins R.N.;
RT "Yop1p, the yeast homolog of the polyposis locus protein 1, interacts with
RT Yip1p and negatively regulates cell growth.";
RL J. Biol. Chem. 276:12100-12112(2001).
RN [6]
RP INTERACTION WITH YIP3.
RX PubMed=11785952; DOI=10.1006/bbrc.2001.6242;
RA Calero M., Collins R.N.;
RT "Saccharomyces cerevisiae Pra1p/Yip3p interacts with Yip1p and Rab
RT proteins.";
RL Biochem. Biophys. Res. Commun. 290:676-681(2002).
RN [7]
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 [8]
RP INTERACTION WITH YIP4; YIP5 AND YPT1.
RX PubMed=12802060; DOI=10.1091/mbc.e02-11-0707;
RA Calero M., Chen C.Z., Zhu W., Winand N.J., Havas K.A., Gilbert P.M.,
RA Burd C.G., Collins R.N.;
RT "Dual prenylation is required for Rab protein localization and function.";
RL Mol. Biol. Cell 14:1852-1867(2003).
RN [9]
RP MUTAGENESIS OF GLU-70; GLU-76; PHE-81; LYS-130; 153-LEU--SER-155; CYS-177
RP AND PRO-180, AND INTERACTION WITH YIF1; YPT1 AND YPT31.
RX PubMed=15611160; DOI=10.1534/genetics.104.032888;
RA Chen C.Z., Calero M., DeRegis C.J., Heidtman M., Barlowe C., Collins R.N.;
RT "Genetic analysis of yeast Yip1p function reveals a requirement for Golgi-
RT localized rab proteins and rab-Guanine nucleotide dissociation inhibitor.";
RL Genetics 168:1827-1841(2004).
RN [10]
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).
CC -!- FUNCTION: Required for fusion of ER-derived vesicles with the Golgi
CC during ER-to-Golgi protein transport, probably by mediating correct
CC membrane localization of YPT1. {ECO:0000269|PubMed:12657649,
CC ECO:0000269|PubMed:9724632}.
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 prenylated form of the Rab GTPases YPT1
CC and YPT31. Interacts with the YIP1 family members YIP4 and YIP5.
CC Interacts with SNX3, YIP3 and YOP1. {ECO:0000269|PubMed:10970842,
CC ECO:0000269|PubMed:11278413, ECO:0000269|PubMed:11785952,
CC ECO:0000269|PubMed:12657649, ECO:0000269|PubMed:12802060,
CC ECO:0000269|PubMed:15263065, ECO:0000269|PubMed:15611160,
CC ECO:0000269|PubMed:9724632}.
CC -!- INTERACTION:
CC P53039; Q07528: ATG20; NbExp=2; IntAct=EBI-25295, EBI-36894;
CC P53039; P32913: VPS17; NbExp=2; IntAct=EBI-25295, EBI-20366;
CC P53039; P53845: YIF1; NbExp=5; IntAct=EBI-25295, EBI-28230;
CC P53039; P38815: YPT35; NbExp=3; IntAct=EBI-25295, EBI-24665;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein. Golgi apparatus membrane; Multi-pass membrane
CC protein.
CC -!- SIMILARITY: Belongs to the YIP1 family. {ECO:0000305}.
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DR EMBL; X97342; CAA66031.1; -; Genomic_DNA.
DR EMBL; Z72957; CAA97198.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08267.1; -; Genomic_DNA.
DR PIR; S64486; S64486.
DR RefSeq; NP_011688.3; NM_001181301.3.
DR AlphaFoldDB; P53039; -.
DR BioGRID; 33424; 472.
DR DIP; DIP-2080N; -.
DR IntAct; P53039; 15.
DR MINT; P53039; -.
DR STRING; 4932.YGR172C; -.
DR TCDB; 9.B.135.1.1; the membrane trafficking yip (yip) family.
DR MaxQB; P53039; -.
DR PaxDb; P53039; -.
DR PRIDE; P53039; -.
DR DNASU; 853082; -.
DR EnsemblFungi; YGR172C_mRNA; YGR172C; YGR172C.
DR GeneID; 853082; -.
DR KEGG; sce:YGR172C; -.
DR SGD; S000003404; YIP1.
DR VEuPathDB; FungiDB:YGR172C; -.
DR eggNOG; KOG3103; Eukaryota.
DR GeneTree; ENSGT00940000153168; -.
DR HOGENOM; CLU_074741_3_1_1; -.
DR InParanoid; P53039; -.
DR OMA; IGINFDH; -.
DR BioCyc; YEAST:G3O-30868-MON; -.
DR PRO; PR:P53039; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53039; protein.
DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0030173; C:integral component of Golgi membrane; IDA:SGD.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
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 GO; GO:0048280; P:vesicle fusion with Golgi apparatus; IMP:SGD.
DR GO; GO:0016192; P:vesicle-mediated transport; IMP:SGD.
DR InterPro; IPR045231; Yip1/4-like.
DR InterPro; IPR006977; Yip1_dom.
DR PANTHER; PTHR21236; PTHR21236; 1.
DR Pfam; PF04893; Yip1; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus; Membrane;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..248
FT /note="Protein transport protein YIP1"
FT /id="PRO_0000066269"
FT TOPO_DOM 1..110
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 132
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 154..172
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 194..196
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 218..227
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MUTAGEN 70
FT /note="E->G: In YIP1-41; lethal; abolishes binding to YIF1,
FT YPT1 and YPT31. In YIP1-40; temperature sensitive; reduces
FT binding to YPT31, and inhibits ER vesicle budding; when
FT associated with A-130."
FT /evidence="ECO:0000269|PubMed:15611160"
FT MUTAGEN 70
FT /note="E->K: In YIP1-4; temperature sensitive; reduces
FT binding to YIF1, YPT1 and YPT31. In YIP1-44; lethal; when
FT associated with E-130."
FT /evidence="ECO:0000269|PubMed:15611160"
FT MUTAGEN 70
FT /note="E->V: In YIP1-42; temperature sensitive; abolishes
FT binding to YPT1 and YPT31, and inhibits ER vesicle
FT budding."
FT /evidence="ECO:0000269|PubMed:15611160"
FT MUTAGEN 76
FT /note="E->K: In YIP1-6; lethal; reduces binding to YIF1."
FT /evidence="ECO:0000269|PubMed:15611160"
FT MUTAGEN 81
FT /note="F->Y: In YIP1-9; lethal."
FT /evidence="ECO:0000269|PubMed:15611160"
FT MUTAGEN 114
FT /note="P->L: In YIP1-1; blocks ER-Golgi protein transport,
FT and causes a severe growth defect at 36 degrees Celsius;
FT when associated with E-129."
FT /evidence="ECO:0000269|PubMed:9724632"
FT MUTAGEN 129
FT /note="G->E: In YIP1-1; blocks ER-Golgi protein transport,
FT and causes a severe growth defect at 36 degrees Celsius;
FT when associated with L-114."
FT /evidence="ECO:0000269|PubMed:9724632"
FT MUTAGEN 130
FT /note="K->A: In YIP1-40; temperature sensitive; reduces
FT binding to YPT31, and inhibits ER vesicle budding; when
FT associated with G-70."
FT /evidence="ECO:0000269|PubMed:15611160"
FT MUTAGEN 130
FT /note="K->E: In YIP1-44; lethal; when associated with K-
FT 70."
FT /evidence="ECO:0000269|PubMed:15611160"
FT MUTAGEN 153..155
FT /note="LMS->GGG: In YIP1-12; abolishes binding to YPT1 and
FT YPT31."
FT /evidence="ECO:0000269|PubMed:15611160"
FT MUTAGEN 175
FT /note="G->E: In YIP1-2; abolishes binding to YPT1 and
FT YPT31, reduces binding to YIF1, blocks ER-Golgi protein
FT transport, and causes a severe growth defect at 36 degrees
FT Celsius."
FT /evidence="ECO:0000269|PubMed:9724632"
FT MUTAGEN 177
FT /note="C->S: In YIP1-18; abolishes binding to YIF1, YPT1
FT and YPT31."
FT /evidence="ECO:0000269|PubMed:15611160"
FT MUTAGEN 180
FT /note="P->G: In YIP1-19; lethal; abolishes binding to YPT1
FT and YPT31, and reduces binding to YIF1."
FT /evidence="ECO:0000269|PubMed:15611160"
SQ SEQUENCE 248 AA; 27080 MW; 64372B4823A0BC5E CRC64;
MSFYNTSNNA NNGGGFYQPS AQFAVPQGSM SFQNTVGSSN TGNDNNLGVA PDPLPVGILH
ALSTKGYPHE PPLLEEIGIN FDHIITKTKM VLIPIRFGSG VPQEILNDSD LAGPLIFFLL
FGLFLLMAGK VHFGYIYGVA LFGTISLHNL SKLMSNNDTS TQTNLQFFNT ASILGYCFLP
LCFLSLLGIF HGLNNTTGYV VSVLFVIWST WTSSGFLNSL LQLQNARLLI AYPLLIFYSV
FALMVIFV
