GMH1_YEAST
ID GMH1_YEAST Reviewed; 273 AA.
AC P36125; D6VX95;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Protein GMH1;
DE AltName: Full=GEA1-6 membrane-associated high-copy suppressor protein 1;
GN Name=GMH1; Synonyms=MSG1; OrderedLocusNames=YKR030W;
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=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
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 IDENTIFICATION, SUBCELLULAR LOCATION, TOPOLOGY, AND INTERACTION WITH GEA1
RP AND GEA2.
RX PubMed=12808035; DOI=10.1091/mbc.e02-10-0693;
RA Chantalat S., Courbeyrette R., Senic-Matuglia F., Jackson C.L., Goud B.,
RA Peyroche A.;
RT "A novel Golgi membrane protein is a partner of the ARF exchange factors
RT Gea1p and Gea2p.";
RL Mol. Biol. Cell 14:2357-2371(2003).
RN [4]
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 [5]
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 -!- SUBUNIT: Interacts with GEA1 and GEA2. {ECO:0000269|PubMed:12808035}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:12808035}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:12808035}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:12808035}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:12808035}. Note=Recycles between Golgi apparatus
CC and endoplasmic reticulum.
CC -!- SIMILARITY: Belongs to the unc-50 family. {ECO:0000305}.
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DR EMBL; Z28255; CAA82102.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09185.1; -; Genomic_DNA.
DR PIR; S38102; S38102.
DR RefSeq; NP_012955.1; NM_001179820.1.
DR AlphaFoldDB; P36125; -.
DR BioGRID; 34163; 102.
DR DIP; DIP-2023N; -.
DR IntAct; P36125; 9.
DR MINT; P36125; -.
DR STRING; 4932.YKR030W; -.
DR iPTMnet; P36125; -.
DR PaxDb; P36125; -.
DR PRIDE; P36125; -.
DR EnsemblFungi; YKR030W_mRNA; YKR030W; YKR030W.
DR GeneID; 853901; -.
DR KEGG; sce:YKR030W; -.
DR SGD; S000001738; GMH1.
DR VEuPathDB; FungiDB:YKR030W; -.
DR eggNOG; KOG3012; Eukaryota.
DR GeneTree; ENSGT00390000018553; -.
DR HOGENOM; CLU_066239_1_2_1; -.
DR InParanoid; P36125; -.
DR OMA; ISTLMWV; -.
DR BioCyc; YEAST:G3O-32006-MON; -.
DR PRO; PR:P36125; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36125; protein.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030173; C:integral component of Golgi membrane; IDA:SGD.
DR GO; GO:0016192; P:vesicle-mediated transport; IPI:SGD.
DR InterPro; IPR007881; UNC-50.
DR PANTHER; PTHR12841; PTHR12841; 1.
DR Pfam; PF05216; UNC-50; 1.
PE 1: Evidence at protein level;
KW Acetylation; Endoplasmic reticulum; Golgi apparatus; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..273
FT /note="Protein GMH1"
FT /id="PRO_0000203205"
FT TOPO_DOM 2..89
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111..134
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 156..175
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 197..216
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..242
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 264..273
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..33
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 273 AA; 31993 MW; 94E991416D7630F2 CRC64;
MSYLPTYSND LPAGPQGQRR RNNGNENDAR QGYGQQSVPM VIRRLFKTPK NLDLETASWE
MFHLIFHPRK AYRSIYYQRQ TKNQWARDDP SFFIFQIALI SLSSIIWSIY NSGFNNDSDM
GALSIIGHFF KSLVMMVILD FFIFGFIMAT IFYLLLNRSH FKFKSSQNSV VEWAYCFDVH
CNSFLIILLC LYFIQFLLLP IINLQNWISL LIGNSLYCFA IGHYFILTFY GYNQLPFLKN
LNFILLPTLG LSIIYLISLF GIDLSKKLSF YNY
