SAM37_YEAST
ID SAM37_YEAST Reviewed; 327 AA.
AC P50110; D6VZN4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Sorting assembly machinery 37 kDa subunit;
DE AltName: Full=MAS37 protein;
DE AltName: Full=Mitochondrial 37 kDa outer membrane protein;
GN Name=SAM37; Synonyms=MAS37, PET3027, TOM37; OrderedLocusNames=YMR060C;
GN ORFNames=YM9796.13C;
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].
RX PubMed=7698990; DOI=10.1083/jcb.129.1.25;
RA Gratzer S., Lithgow T., Bauer R.E., Lamping E., Paltauf F., Kohlwein S.D.,
RA Haucke V., Junne T., Schatz G., Horst M.;
RT "Mas37p, a novel receptor subunit for protein import into mitochondria.";
RL J. Cell Biol. 129:25-34(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP IDENTIFICATION IN THE SAM COMPLEX.
RX PubMed=14570913; DOI=10.1074/jbc.c300442200;
RA Kozjak V., Wiedemann N., Milenkovic D., Lohaus C., Meyer H.E., Guiard B.,
RA Meisinger C., Pfanner N.;
RT "An essential role of Sam50 in the protein sorting and assembly machinery
RT of the mitochondrial outer membrane.";
RL J. Biol. Chem. 278:48520-48523(2003).
RN [6]
RP IDENTIFICATION IN THE SAM COMPLEX, AND FUNCTION OF THE SAM COMPLEX.
RX PubMed=12891361; DOI=10.1038/nature01753;
RA Wiedemann N., Kozjak V., Chacinska A., Schoenfisch B., Rospert S.,
RA Ryan M.T., Pfanner N., Meisinger C.;
RT "Machinery for protein sorting and assembly in the mitochondrial outer
RT membrane.";
RL Nature 424:565-571(2003).
RN [7]
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 [8]
RP IDENTIFICATION IN THE SAM COMPLEX.
RX PubMed=15590639; DOI=10.1074/jbc.m411510200;
RA Habib S.J., Waizenegger T., Lech M., Neupert W., Rapaport D.;
RT "Assembly of the TOB complex of mitochondria.";
RL J. Biol. Chem. 280:6434-6440(2005).
RN [9]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16823961; DOI=10.1021/pr050477f;
RA Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT "Toward the complete yeast mitochondrial proteome: multidimensional
RT separation techniques for mitochondrial proteomics.";
RL J. Proteome Res. 5:1543-1554(2006).
CC -!- FUNCTION: Component of the mitochondrial outer membrane sorting
CC assembly machinery (SAM or TOB) complex, which is required for the
CC sorting of proteins with complicated topology, such as beta-barrel
CC proteins, to the mitochondrial outer membrane after import by the TOM
CC complex. {ECO:0000269|PubMed:12891361}.
CC -!- SUBUNIT: Component of the mitochondrial outer membrane sorting assembly
CC machinery (SAM or TOB) complex, which at least consists of SAM35, SAM37
CC and SAM50. SAM37 interacts with TOM70. {ECO:0000269|PubMed:12891361,
CC ECO:0000269|PubMed:14570913, ECO:0000269|PubMed:15590639}.
CC -!- INTERACTION:
CC P50110; P14693: SAM35; NbExp=7; IntAct=EBI-2347180, EBI-24602;
CC P50110; P53969: SAM50; NbExp=5; IntAct=EBI-2347180, EBI-28646;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:16823961}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16823961}.
CC -!- MISCELLANEOUS: Present with 1580 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X62565; CAA44438.1; -; Genomic_DNA.
DR EMBL; Z49703; CAA89770.1; -; Genomic_DNA.
DR EMBL; AY557989; AAS56315.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09958.1; -; Genomic_DNA.
DR PIR; S54560; S54560.
DR RefSeq; NP_013776.1; NM_001182558.1.
DR PDB; 7BTX; EM; 2.80 A; C=1-327.
DR PDB; 7BTY; EM; 3.20 A; C=1-327.
DR PDB; 7E4H; EM; 3.01 A; C=1-327.
DR PDB; 7E4I; EM; 3.05 A; C=1-327.
DR PDBsum; 7BTX; -.
DR PDBsum; 7BTY; -.
DR PDBsum; 7E4H; -.
DR PDBsum; 7E4I; -.
DR AlphaFoldDB; P50110; -.
DR SMR; P50110; -.
DR BioGRID; 35235; 325.
DR ComplexPortal; CPX-1744; Mitochondrial sorting and assembly machinery complex.
DR IntAct; P50110; 9.
DR MINT; P50110; -.
DR STRING; 4932.YMR060C; -.
DR TCDB; 1.B.33.3.1; the outer membrane protein insertion porin (bam complex) (ompip) family.
DR MaxQB; P50110; -.
DR PaxDb; P50110; -.
DR PRIDE; P50110; -.
DR EnsemblFungi; YMR060C_mRNA; YMR060C; YMR060C.
DR GeneID; 855082; -.
DR KEGG; sce:YMR060C; -.
DR SGD; S000004664; SAM37.
DR VEuPathDB; FungiDB:YMR060C; -.
DR eggNOG; KOG3028; Eukaryota.
DR HOGENOM; CLU_069449_0_0_1; -.
DR InParanoid; P50110; -.
DR OMA; PMWYNTP; -.
DR BioCyc; YEAST:G3O-32763-MON; -.
DR PRO; PR:P50110; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P50110; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:ComplexPortal.
DR GO; GO:0001401; C:SAM complex; IDA:SGD.
DR GO; GO:0070096; P:mitochondrial outer membrane translocase complex assembly; IMP:SGD.
DR GO; GO:0007005; P:mitochondrion organization; IBA:GO_Central.
DR GO; GO:0015914; P:phospholipid transport; IMP:SGD.
DR GO; GO:0030150; P:protein import into mitochondrial matrix; IDA:ComplexPortal.
DR GO; GO:0045040; P:protein insertion into mitochondrial outer membrane; IMP:SGD.
DR InterPro; IPR019564; Sam37/metaxin_N.
DR InterPro; IPR031317; Tom37_C.
DR Pfam; PF10568; Tom37; 1.
DR Pfam; PF11801; Tom37_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..327
FT /note="Sorting assembly machinery 37 kDa subunit"
FT /id="PRO_0000072630"
FT TRANSMEM 17..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:7BTX"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:7E4H"
FT HELIX 20..30
FT /evidence="ECO:0007829|PDB:7BTX"
FT HELIX 35..38
FT /evidence="ECO:0007829|PDB:7BTX"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:7BTX"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:7BTX"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:7BTX"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:7BTX"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:7BTX"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:7BTX"
FT HELIX 74..83
FT /evidence="ECO:0007829|PDB:7BTX"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:7BTX"
FT HELIX 108..120
FT /evidence="ECO:0007829|PDB:7BTX"
FT HELIX 122..131
FT /evidence="ECO:0007829|PDB:7BTX"
FT HELIX 134..139
FT /evidence="ECO:0007829|PDB:7BTX"
FT TURN 140..148
FT /evidence="ECO:0007829|PDB:7BTX"
FT TURN 151..154
FT /evidence="ECO:0007829|PDB:7BTX"
FT HELIX 157..168
FT /evidence="ECO:0007829|PDB:7BTX"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:7BTX"
FT HELIX 187..193
FT /evidence="ECO:0007829|PDB:7BTX"
FT TURN 194..199
FT /evidence="ECO:0007829|PDB:7BTX"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:7BTX"
FT HELIX 205..240
FT /evidence="ECO:0007829|PDB:7BTX"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:7BTX"
FT HELIX 250..262
FT /evidence="ECO:0007829|PDB:7BTX"
FT HELIX 268..278
FT /evidence="ECO:0007829|PDB:7BTX"
FT HELIX 281..295
FT /evidence="ECO:0007829|PDB:7BTX"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:7BTX"
FT HELIX 309..311
FT /evidence="ECO:0007829|PDB:7E4H"
FT HELIX 316..318
FT /evidence="ECO:0007829|PDB:7BTX"
FT HELIX 320..325
FT /evidence="ECO:0007829|PDB:7BTX"
SQ SEQUENCE 327 AA; 37493 MW; D4ABA929CE5CAD16 CRC64;
MVKGSVHLWG KDGKASLISV DSIALVWFIK LCTSEEAKSM VAGLQIVFSN NTDLSSDGKL
PVLILDNGTK VSGYVNIVQF LHKNICTSKY EKGTDYEEDL AIVRKKDRLL EYSLLNYVDV
EISRLTDYQL FLNTKNYNEY TKKLFSKLLY FPMWYNTPLQ LRSQARENCE EIIGSLTLED
DEEFVESKAM ESASQLAQSK TFKIAHKNKI KGKQELQQVK YNLQFDNRLQ SCVSNWLAAR
KKLDDSVILS SDLLFLANLY VQLGLPDGNR IRSKLEQTFG SELLNSMSNK IDDFVHRPSN
NLEQRDPQFR EQGNVVMSLY NLACKYI