SRN2_YEAST
ID SRN2_YEAST Reviewed; 213 AA.
AC Q99176; D6VYB7; Q02806;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Protein SRN2;
DE AltName: Full=ESCRT-I complex subunit VPS37;
DE AltName: Full=Vacuolar protein sorting-associated protein 37;
GN Name=SRN2; Synonyms=SRN10, VPS37; OrderedLocusNames=YLR119W;
GN ORFNames=L2958, L9233.5;
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], INTERACTION WITH RNA1, AND SUBCELLULAR
RP LOCATION.
RX PubMed=9790597; DOI=10.1007/s004380050830;
RA Hong S.J., Yi Y.S., Koh S.S., Park O.K., Kang H.S.;
RT "Isolation of an extragenic suppressor of the rna1-1 mutation in
RT Saccharomyces cerevisiae.";
RL Mol. Gen. Genet. 259:404-413(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 90840 / EAY235 / FY23;
RX PubMed=9090053;
RX DOI=10.1002/(sici)1097-0061(19970315)13:3<241::aid-yea61>3.0.co;2-#;
RA Verhasselt P., Volckaert G.;
RT "Sequence analysis of a 37.6 kbp cosmid clone from the right arm of
RT Saccharomyces cerevisiae chromosome XII, carrying YAP3, HOG1, SNR6, tRNA-
RT Arg3 and 23 new open reading frames, among which several homologies to
RT proteins involved in cell division control and to mammalian growth factors
RT and other animal proteins are found.";
RL Yeast 13:241-250(1997).
RN [3]
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 [4]
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 [5]
RP X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 130-213 IN COMPLEX WITH STP22 AND
RP VPS28.
RX PubMed=16615893; DOI=10.1016/j.cell.2006.01.047;
RA Teo H., Gill D.J., Sun J., Perisic O., Veprintsev D.B., Vallis Y.,
RA Emr S.D., Williams R.L.;
RT "ESCRT-I core and ESCRT-II GLUE domain structures reveal role for GLUE in
RT linking to ESCRT-I and membranes.";
RL Cell 125:99-111(2006).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 132-213 IN COMPLEX WITH STP22 AND
RP VPS28, AND MUTAGENESIS OF LEU-181 AND ILE-185.
RX PubMed=16615894; DOI=10.1016/j.cell.2006.01.049;
RA Kostelansky M.S., Sun J., Lee S., Kim J., Ghirlando R., Hierro A.,
RA Emr S.D., Hurley J.H.;
RT "Structural and functional organization of the ESCRT-I trafficking
RT complex.";
RL Cell 125:113-126(2006).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 22-213, COMPOSITION OF THE ESCRT-I
RP COMPLEX, INTERACTION WITH STP22 AND MVB12, AND MUTAGENESIS OF LEU-67;
RP LEU-75; VAL-79; PHE-88; ILE-92; PHE-95; PHE-99 AND LEU-102.
RX PubMed=17442384; DOI=10.1016/j.cell.2007.03.016;
RA Kostelansky M.S., Schluter C., Tam Y.Y., Lee S., Ghirlando R., Beach B.,
RA Conibear E., Hurley J.H.;
RT "Molecular architecture and functional model of the complete yeast ESCRT-I
RT heterotetramer.";
RL Cell 129:485-498(2007).
CC -!- FUNCTION: Component of the ESCRT-I complex, a regulator of vesicular
CC trafficking process. Required for normal endocytic and biosynthetic
CC traffic to the yeast vacuole.
CC -!- SUBUNIT: Component of the ESCRT-I complex (endosomal sorting complex
CC required for transport I) which consists of STP22, VPS28, SRN2 and
CC MVB12 in a 1:1:1:1 stoichiometry. Interacts with STP22 and MVB12.
CC {ECO:0000269|PubMed:16615893, ECO:0000269|PubMed:16615894,
CC ECO:0000269|PubMed:17442384, ECO:0000269|PubMed:9790597}.
CC -!- INTERACTION:
CC Q99176; P42939: MVB12; NbExp=10; IntAct=EBI-18076, EBI-23478;
CC Q99176; P25604: STP22; NbExp=9; IntAct=EBI-18076, EBI-411625;
CC Q99176; Q02767: VPS28; NbExp=5; IntAct=EBI-18076, EBI-20387;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9790597}. Endosome
CC {ECO:0000305|PubMed:9790597}. Late endosome membrane
CC {ECO:0000305|PubMed:9790597}; Peripheral membrane protein
CC {ECO:0000305|PubMed:9790597}.
CC -!- SIMILARITY: Belongs to the VPS37 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB88577.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U40562; AAB88577.1; ALT_INIT; Genomic_DNA.
DR EMBL; X89514; CAA61698.1; -; Genomic_DNA.
DR EMBL; U53877; AAB82366.1; -; Genomic_DNA.
DR EMBL; Z73291; CAA97687.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09433.1; -; Genomic_DNA.
DR PIR; S64956; S64956.
DR RefSeq; NP_013220.1; NM_001182006.1.
DR PDB; 2CAZ; X-ray; 3.60 A; C/F=130-213.
DR PDB; 2F66; X-ray; 2.80 A; C/F=132-213.
DR PDB; 2P22; X-ray; 2.70 A; C=22-213.
DR PDBsum; 2CAZ; -.
DR PDBsum; 2F66; -.
DR PDBsum; 2P22; -.
DR AlphaFoldDB; Q99176; -.
DR SMR; Q99176; -.
DR BioGRID; 31391; 599.
DR ComplexPortal; CPX-940; ESCRT-I complex.
DR DIP; DIP-2130N; -.
DR IntAct; Q99176; 4.
DR MINT; Q99176; -.
DR STRING; 4932.YLR119W; -.
DR TCDB; 3.A.31.1.1; the endosomal sorting complexes required for transport iii (escrt-iii) family.
DR MaxQB; Q99176; -.
DR PaxDb; Q99176; -.
DR PRIDE; Q99176; -.
DR EnsemblFungi; YLR119W_mRNA; YLR119W; YLR119W.
DR GeneID; 850810; -.
DR KEGG; sce:YLR119W; -.
DR SGD; S000004109; SRN2.
DR VEuPathDB; FungiDB:YLR119W; -.
DR eggNOG; ENOG502S6GM; Eukaryota.
DR HOGENOM; CLU_109465_0_0_1; -.
DR InParanoid; Q99176; -.
DR OMA; YVTKFHP; -.
DR BioCyc; YEAST:G3O-32264-MON; -.
DR Reactome; R-SCE-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR EvolutionaryTrace; Q99176; -.
DR PRO; PR:Q99176; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q99176; protein.
DR GO; GO:0005768; C:endosome; IDA:SGD.
DR GO; GO:0000813; C:ESCRT I complex; IDA:SGD.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:1904669; P:ATP export; IMP:SGD.
DR GO; GO:0032509; P:endosome transport via multivesicular body sorting pathway; IEA:InterPro.
DR GO; GO:0006612; P:protein targeting to membrane; IMP:SGD.
DR GO; GO:0006623; P:protein targeting to vacuole; IMP:SGD.
DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IDA:ComplexPortal.
DR Gene3D; 1.10.287.660; -; 1.
DR InterPro; IPR017435; ESCRT-1_cplx_Vps37_fungi.
DR InterPro; IPR037202; ESCRT_assembly_dom.
DR InterPro; IPR029012; Helix_hairpin_bin_sf.
DR InterPro; IPR009851; Mod_r.
DR Pfam; PF07200; Mod_r; 1.
DR PIRSF; PIRSF038214; ESCRT1_Vps37_fungi; 1.
DR SUPFAM; SSF140111; SSF140111; 1.
DR PROSITE; PS51314; VPS37_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Endosome; Membrane; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..213
FT /note="Protein SRN2"
FT /id="PRO_0000072191"
FT DOMAIN 128..213
FT /note="VPS37 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00646"
FT MUTAGEN 67
FT /note="L->D: Defective in ESCRT-I cargo sorting."
FT /evidence="ECO:0000269|PubMed:17442384"
FT MUTAGEN 75
FT /note="L->D: Defective in ESCRT-I cargo sorting."
FT /evidence="ECO:0000269|PubMed:17442384"
FT MUTAGEN 79
FT /note="V->D: Defective in ESCRT-I cargo sorting."
FT /evidence="ECO:0000269|PubMed:17442384"
FT MUTAGEN 88
FT /note="F->D: Defective in ESCRT-I cargo sorting; when
FT associated with D-99."
FT /evidence="ECO:0000269|PubMed:17442384"
FT MUTAGEN 92
FT /note="I->D: Defective in ESCRT-I cargo sorting; when
FT associated with D-102."
FT /evidence="ECO:0000269|PubMed:17442384"
FT MUTAGEN 95
FT /note="F->D: Defective in ESCRT-I cargo sorting; when
FT associated with D-99."
FT /evidence="ECO:0000269|PubMed:17442384"
FT MUTAGEN 99
FT /note="F->D: Defective in ESCRT-I cargo sorting; when
FT associated with D-88."
FT /evidence="ECO:0000269|PubMed:17442384"
FT MUTAGEN 99
FT /note="F->D: Defective in ESCRT-I cargo sorting; when
FT associated with D-95."
FT /evidence="ECO:0000269|PubMed:17442384"
FT MUTAGEN 102
FT /note="L->D: Defective in ESCRT-I cargo sorting; when
FT associated with D-92."
FT /evidence="ECO:0000269|PubMed:17442384"
FT MUTAGEN 181
FT /note="L->R: Abolishes ESCRT-I complex assembly; class E
FT phenotype (malformed late MVB); when associated with R-
FT 185."
FT /evidence="ECO:0000269|PubMed:16615894"
FT MUTAGEN 185
FT /note="I->R: Abolishes ESCRT-I complex assembly; class E
FT phenotype (malformed late MVB); when associated with R-
FT 181."
FT /evidence="ECO:0000269|PubMed:16615894"
FT CONFLICT 90
FT /note="G -> E (in Ref. 1; AAB88577)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="E -> D (in Ref. 1; AAB88577)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="K -> E (in Ref. 1; AAB88577)"
FT /evidence="ECO:0000305"
FT HELIX 23..33
FT /evidence="ECO:0007829|PDB:2P22"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:2P22"
FT HELIX 62..70
FT /evidence="ECO:0007829|PDB:2P22"
FT HELIX 72..78
FT /evidence="ECO:0007829|PDB:2P22"
FT HELIX 79..82
FT /evidence="ECO:0007829|PDB:2P22"
FT HELIX 86..143
FT /evidence="ECO:0007829|PDB:2P22"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:2P22"
FT HELIX 147..170
FT /evidence="ECO:0007829|PDB:2P22"
FT HELIX 178..205
FT /evidence="ECO:0007829|PDB:2P22"
SQ SEQUENCE 213 AA; 25101 MW; 4E99806CED03E345 CRC64;
MKVKATKLRI KQRRKNKGLN ISRLDIIRAE MDVVPSPGLP EKVNEKSKNI PLPEGINLLS
SKEIIDLIQT HRHQLELYVT KFNPLTDFAG KIHAFRDQFK QLEENFEDLH EQKDKVQALL
ENCRILESKY VASWQDYHSE FSKKYGDIAL KKKLEQNTKK LDEESSQLET TTRSIDSADD
LDQFIKNYLD IRTQYHLRRE KLATWDKQGN LKY
