IMH1_YEAST
ID IMH1_YEAST Reviewed; 911 AA.
AC Q06704; D6VYV3;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Golgin IMH1;
DE AltName: Full=Integrins and myosins homology protein 1;
GN Name=IMH1; Synonyms=SYS3; OrderedLocusNames=YLR309C;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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]
RP FUNCTION.
RX PubMed=8663225; DOI=10.1074/jbc.271.28.16813;
RA Li B., Warner J.R.;
RT "Mutation of the Rab6 homologue of Saccharomyces cerevisiae, YPT6, inhibits
RT both early Golgi function and ribosome biosynthesis.";
RL J. Biol. Chem. 271:16813-16819(1996).
RN [4]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=9880327; DOI=10.1091/mbc.10.1.63;
RA Tsukada M., Will E., Gallwitz D.;
RT "Structural and functional analysis of a novel coiled-coil protein involved
RT in Ypt6 GTPase-regulated protein transport in yeast.";
RL Mol. Biol. Cell 10:63-75(1999).
RN [5]
RP DOMAIN, AND SUBCELLULAR LOCATION.
RX PubMed=10209120; DOI=10.1016/s0960-9822(99)80166-3;
RA Munro S., Nichols B.J.;
RT "The GRIP domain - a novel Golgi-targeting domain found in several coiled-
RT coil proteins.";
RL Curr. Biol. 9:377-380(1999).
RN [6]
RP DOMAIN.
RX PubMed=10209125; DOI=10.1016/s0960-9822(99)80168-7;
RA Kjer-Nielsen L., Teasdale R.D., van Vliet C., Gleeson P.A.;
RT "A novel Golgi-localisation domain shared by a class of coiled-coil
RT peripheral membrane proteins.";
RL Curr. Biol. 9:385-388(1999).
RN [7]
RP INDUCTION.
RX PubMed=12039763; DOI=10.1128/aem.68.6.3024-3030.2002;
RA Rodriguez-Vargas S., Estruch F., Randez-Gil F.;
RT "Gene expression analysis of cold and freeze stress in Baker's yeast.";
RL Appl. Environ. Microbiol. 68:3024-3030(2002).
RN [8]
RP INTERACTION WITH ARL1, AND SUBCELLULAR LOCATION.
RX PubMed=12620188; DOI=10.1016/s0960-9822(03)00089-7;
RA Setty S.R.G., Shin M.E., Yoshino A., Marks M.S., Burd C.G.;
RT "Golgi recruitment of GRIP domain proteins by Arf-like GTPase 1 is
RT regulated by Arf-like GTPase 3.";
RL Curr. Biol. 13:401-404(2003).
RN [9]
RP INTERACTION WITH ARL1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TYR-870.
RX PubMed=12620189; DOI=10.1016/s0960-9822(03)00091-5;
RA Panic B., Whyte J.R.C., Munro S.;
RT "The ARF-like GTPases Arl1p and Arl3p act in a pathway that interacts with
RT vesicle-tethering factors at the Golgi apparatus.";
RL Curr. Biol. 13:405-410(2003).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
RN [11]
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 [12]
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 [13]
RP SUBCELLULAR LOCATION.
RX PubMed=15077113; DOI=10.1038/ncb1120;
RA Behnia R., Panic B., Whyte J.R.C., Munro S.;
RT "Targeting of the Arf-like GTPase Arl3p to the Golgi requires N-terminal
RT acetylation and the membrane protein Sys1p.";
RL Nat. Cell Biol. 6:405-413(2004).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-827, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308, 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308 AND SER-660, AND
RP IDENTIFICATION BY 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308; SER-827 AND THR-830, AND
RP IDENTIFICATION BY 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 vesicular transport between an endosomal
CC compartment and the Golgi apparatus. {ECO:0000269|PubMed:8663225,
CC ECO:0000269|PubMed:9880327}.
CC -!- SUBUNIT: Forms oligomers and is present in high-molecular-mass
CC complexes. Interacts with ARL1. {ECO:0000269|PubMed:12620188,
CC ECO:0000269|PubMed:12620189, ECO:0000269|PubMed:9880327}.
CC -!- INTERACTION:
CC Q06704; P38116: ARL1; NbExp=3; IntAct=EBI-33343, EBI-2869;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus membrane; Peripheral
CC membrane protein. Note=IMH1 is recruited to the Golgi apparatus by
CC ARL1.
CC -!- INDUCTION: By cold. {ECO:0000269|PubMed:12039763}.
CC -!- DOMAIN: The GRIP domain may serve as a Golgi targeting domain through
CC its interaction with the ARL1 Golgi protein.
CC {ECO:0000269|PubMed:10209120, ECO:0000269|PubMed:10209125}.
CC -!- MISCELLANEOUS: Present with 2350 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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; U17247; AAB67359.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09619.1; -; Genomic_DNA.
DR PIR; S51441; S51441.
DR RefSeq; NP_013412.1; NM_001182197.2.
DR AlphaFoldDB; Q06704; -.
DR SMR; Q06704; -.
DR BioGRID; 31574; 113.
DR DIP; DIP-5583N; -.
DR IntAct; Q06704; 9.
DR MINT; Q06704; -.
DR STRING; 4932.YLR309C; -.
DR iPTMnet; Q06704; -.
DR MaxQB; Q06704; -.
DR PaxDb; Q06704; -.
DR PRIDE; Q06704; -.
DR EnsemblFungi; YLR309C_mRNA; YLR309C; YLR309C.
DR GeneID; 851018; -.
DR KEGG; sce:YLR309C; -.
DR SGD; S000004300; IMH1.
DR VEuPathDB; FungiDB:YLR309C; -.
DR eggNOG; ENOG502S0A5; Eukaryota.
DR HOGENOM; CLU_006987_0_0_1; -.
DR InParanoid; Q06704; -.
DR OMA; QSLMNSM; -.
DR BioCyc; YEAST:G3O-32395-MON; -.
DR PRO; PR:Q06704; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q06704; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IMP:SGD.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:SGD.
DR GO; GO:0016192; P:vesicle-mediated transport; IMP:SGD.
DR InterPro; IPR000237; GRIP_dom.
DR InterPro; IPR029687; Imh1.
DR PANTHER; PTHR43939:SF30; PTHR43939:SF30; 2.
DR Pfam; PF01465; GRIP; 1.
DR SMART; SM00755; Grip; 1.
DR PROSITE; PS50913; GRIP; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Golgi apparatus; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Stress response; Transport.
FT CHAIN 1..911
FT /note="Golgin IMH1"
FT /id="PRO_0000240370"
FT DOMAIN 861..909
FT /note="GRIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00250"
FT REGION 16..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 814..850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 101..280
FT /evidence="ECO:0000255"
FT COILED 312..735
FT /evidence="ECO:0000255"
FT COILED 766..814
FT /evidence="ECO:0000255"
FT COMPBIAS 820..850
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 308
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 660
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 827
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 830
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 870
FT /note="Y->A: Impairs interaction with ARL1 and Golgi
FT localization."
FT /evidence="ECO:0000269|PubMed:12620189"
SQ SEQUENCE 911 AA; 105225 MW; 090BD9AA5702C01D CRC64;
MFKQLSQIGK NLTDELAKGL ADDMSPTPSE QQIEDDKSGL PKEIQAKLRK FEKYEQKYPL
LLSAYKNEKL KSEKLEAVEK ILAENTPISN IDDAVDTLPA FFQDLNNKNN LLNDEIKRLT
KQNSEIPESA SSETLKDKEE EFLKKEQNYK NDIDDLKKKM EALNIELDTV QKEKNDTVSG
LREKIVALEN ILKEEREAKK QKEEVSISEL KEELAIKNHS LEDSRMKITE LEQNLSSKST
IMEEKSSELA ELNITLKEKE RKLSELEKKM KELPKAISHQ NVGNNNRRKK NRNKGKKNKG
GITTGDISEE ETVDNSINTE EYDKLKENLQ ELQEKYKDCE DWKQKYEDIE AELKDAKELE
NSQLEKSAKE LETLNTELID TKKSLKEKNS ELEEVRDMLR TVGNELVDAK DEIKESSSKQ
NEEVKTVKLE LDDLRHKNAT MIEAYEAKNT ELRSKIELLS KKVEHLKNLC TEKEKEQTTS
QNKVAKLNEE ISQLTYEKSN ITKELTSLRT SYKQKEKTVS YLEEQVKQFS EQKDVAEKST
EQLRKDHAKI SNRLDLLKKE NETLHNDIAK NSNSYEEYLK ENGKLSERLN ILQEKYNTLQ
NVKSNSNEHI DSIKRQCEEL NVKLKESTKK ILSLEDELNE YANIVQDKTR EANTLRRLVS
DSQTDDSSKQ KELENKLAYL TDEKNKLEAE LDLQTSRKAT ELQEWKHTVT ELKSEIHALK
LREEGLKSEV DALKHVNNDI KRKTQATSDD SDQLEQITSN LKLSLSKADE KNFELQSANE
KLLNLNNELN KKFDRLLKNY RSLSSQLNAL KERQYSDKSG RVSRSGSIGT LANANIDSSP
ANNSNPTKLE KIRSSSSLEL DSEKNEKIAY IKNVLLGFLE HKEQRNQLLP VISMLLQLDS
TDEKRLVMSL K
