GRH1_YEAST
ID GRH1_YEAST Reviewed; 372 AA.
AC Q04410; D6VTD8;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=GRASP65 homolog protein 1;
GN Name=GRH1; OrderedLocusNames=YDR517W;
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] {ECO:0000312|EMBL:AAB64958.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c {ECO:0000269|PubMed:9169867};
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
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 [3] {ECO:0000305}
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10417390; DOI=10.1126/science.285.5427.591;
RA Norman T.C., Smith D.L., Sorger P.K., Drees B.L., O'Rourke S.M.,
RA Hughes T.R., Roberts C.J., Friend S.H., Fields S., Murray A.W.;
RT "Genetic selection of peptide inhibitors of biological pathways.";
RL Science 285:591-595(1999).
RN [4] {ECO:0000305}
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5] {ECO:0000305}
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] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH BUG1; SEC23; SEC24 AND SFB2.
RX PubMed=16269340; DOI=10.1016/j.cell.2005.08.031;
RA Schuldiner M., Collins S.R., Thompson N.J., Denic V., Bhamidipati A.,
RA Punna T., Ihmels J., Andrews B., Boone C., Greenblatt J.F., Weissman J.S.,
RA Krogan N.J.;
RT "Exploration of the function and organization of the yeast early secretory
RT pathway through an epistatic miniarray profile.";
RL Cell 123:507-519(2005).
RN [7]
RP FUNCTION, INTERACTION WITH BUG1; SEC23; SEC24; SFB2 AND SBF3, SUBCELLULAR
RP LOCATION, ACETYLATION AT MET-1, AND MUTAGENESIS OF PHE-2.
RX PubMed=17261844; DOI=10.1083/jcb.200607151;
RA Behnia R., Barr F.A., Flanagan J.J., Barlowe C., Munro S.;
RT "The yeast orthologue of GRASP65 forms a complex with a coiled-coil protein
RT that contributes to ER to Golgi traffic.";
RL J. Cell Biol. 176:255-261(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Involved in the spindle assembly checkpoint. Involved in ER
CC to Golgi vesicle-mediated transport by either facilitating USO1-
CC dependent and -independent tethering or increasing target accuracy of
CC fusion events of COPII-coated vesicles. {ECO:0000269|PubMed:10417390,
CC ECO:0000269|PubMed:16269340, ECO:0000269|PubMed:17261844}.
CC -!- SUBUNIT: Homodimer. Interacts with BUG1 (via C-terminus), probably
CC forming a heterooligomer consisting of a GRH1 dimer and a BUG1 dimer.
CC Interacts with COPII coat components SEC23, SEC24, SFB2 and SFB3.
CC {ECO:0000269|PubMed:16269340, ECO:0000269|PubMed:17261844}.
CC -!- INTERACTION:
CC Q04410; Q12191: BUG1; NbExp=4; IntAct=EBI-32083, EBI-32271;
CC Q04410; P15303: SEC23; NbExp=4; IntAct=EBI-32083, EBI-16584;
CC Q04410; P40482: SEC24; NbExp=4; IntAct=EBI-32083, EBI-16592;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus, cis-Golgi network
CC membrane; Peripheral membrane protein. Note=Localizes to cytoplasm in a
CC punctate pattern. Association with the cis-Golgi requires N-terminal
CC acetylation and is probably mediated via an N-terminal amphipathic
CC helix. The localization to the Golgi is MAK3-dependent and SYS1-
CC independent. Localizes to the Golgi together with BUG1.
CC -!- PTM: N-terminal acetylation; by N-terminal acetyltransferase NatC.
CC {ECO:0000269|PubMed:17261844}.
CC -!- MISCELLANEOUS: Present with 2730 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U33057; AAB64958.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12348.1; -; Genomic_DNA.
DR PIR; S69574; S69574.
DR RefSeq; NP_010805.1; NM_001180825.1.
DR PDB; 6G8Y; X-ray; 1.40 A; A=67-144.
DR PDBsum; 6G8Y; -.
DR AlphaFoldDB; Q04410; -.
DR SMR; Q04410; -.
DR BioGRID; 32568; 90.
DR ComplexPortal; CPX-1125; BUG1-GRH1 complex.
DR DIP; DIP-6613N; -.
DR IntAct; Q04410; 24.
DR MINT; Q04410; -.
DR STRING; 4932.YDR517W; -.
DR iPTMnet; Q04410; -.
DR MaxQB; Q04410; -.
DR PaxDb; Q04410; -.
DR PRIDE; Q04410; -.
DR EnsemblFungi; YDR517W_mRNA; YDR517W; YDR517W.
DR GeneID; 852129; -.
DR KEGG; sce:YDR517W; -.
DR SGD; S000002925; GRH1.
DR VEuPathDB; FungiDB:YDR517W; -.
DR eggNOG; KOG3834; Eukaryota.
DR GeneTree; ENSGT00390000008686; -.
DR HOGENOM; CLU_742267_0_0_1; -.
DR InParanoid; Q04410; -.
DR OMA; KGQRTHT; -.
DR BioCyc; YEAST:G3O-30036-MON; -.
DR Reactome; R-SCE-162658; Golgi Cisternae Pericentriolar Stack Reorganization.
DR Reactome; R-SCE-204005; COPII-mediated vesicle transport.
DR PRO; PR:Q04410; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q04410; protein.
DR GO; GO:0005801; C:cis-Golgi network; IDA:SGD.
DR GO; GO:0033106; C:cis-Golgi network membrane; IDA:ComplexPortal.
DR GO; GO:0106103; C:COPII vesicles tethering complex; IPI:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IDA:SGD.
DR GO; GO:0031090; C:organelle membrane; IDA:SGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:SGD.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:SGD.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR GO; GO:0009306; P:protein secretion; IMP:SGD.
DR Gene3D; 2.30.42.10; -; 2.
DR InterPro; IPR007583; GRASP55_65.
DR InterPro; IPR024958; GRASP_PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR PANTHER; PTHR12893; PTHR12893; 1.
DR Pfam; PF04495; GRASP55_65; 1.
DR PROSITE; PS51865; PDZ_GRASP; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; ER-Golgi transport; Golgi apparatus;
KW Membrane; Phosphoprotein; Reference proteome; Repeat; Transport.
FT CHAIN 1..372
FT /note="GRASP65 homolog protein 1"
FT /id="PRO_0000270975"
FT DOMAIN 66..183
FT /note="PDZ GRASP-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01212"
FT DOMAIN 188..276
FT /note="PDZ GRASP-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01212"
FT REGION 66..292
FT /note="GRASP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01214"
FT REGION 312..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:17261844"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MUTAGEN 2
FT /note="F->A: Abolishes acetylation and association with
FT cis-Golgi."
FT /evidence="ECO:0000269|PubMed:17261844"
FT TURN 75..79
FT /evidence="ECO:0007829|PDB:6G8Y"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:6G8Y"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:6G8Y"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:6G8Y"
FT HELIX 109..118
FT /evidence="ECO:0007829|PDB:6G8Y"
FT TURN 119..121
FT /evidence="ECO:0007829|PDB:6G8Y"
FT STRAND 122..130
FT /evidence="ECO:0007829|PDB:6G8Y"
FT TURN 131..134
FT /evidence="ECO:0007829|PDB:6G8Y"
FT STRAND 135..142
FT /evidence="ECO:0007829|PDB:6G8Y"
SQ SEQUENCE 372 AA; 41119 MW; A7CE62DFE4631214 CRC64;
MFRIAKNLVR TFEQSVQDTL ALSQDSSNLD AFFQSIPPNL LSAQLESPVD AVSEGVKHTN
VNETLSGLRI VWVDEMQFQL QSFFDYIVGF NDDPVPVVSN QHGFSYPDYR RITSIFNEHC
GRTLKVNIWS AKGGTFRDEY ISIISKESDD LDDVSLNHDE RRPSSGEAHQ FQALGFKVQW
TPLIASTFTY HILNVNIPDG PAQSAGLIPD EDYIIGCQDG LLATGGETLL QDIVRSRANY
DLVLYVYNKV SDCVRPITVH IGPDGRLGCN VGYGFLHRIP TVKHCPQQAQ QQGQDDNPVP
VPVPVESETA FVPSAFTAPP VPTKKKSKNK KGTQPLAMDD YFNEGRDKSS TAAKSAESDI
LAPPPQKQSS SD
