VAM3_YEAST
ID VAM3_YEAST Reviewed; 283 AA.
AC Q12241; D6W2G5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Syntaxin VAM3;
DE AltName: Full=Vacuolar morphogenesis protein 3;
GN Name=VAM3; Synonyms=PTH1; OrderedLocusNames=YOR106W; ORFNames=YOR3220W;
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].
RC STRAIN=ATCC 26786 / X2180-1A;
RX PubMed=9202390; DOI=10.1242/jcs.110.11.1299;
RA Wada Y., Nakamura N., Ohsumi Y., Hirata A.;
RT "Vam3p, a new member of syntaxin related protein, is required for vacuolar
RT assembly in the yeast Saccharomyces cerevisiae.";
RL J. Cell Sci. 110:1299-1306(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9200815;
RX DOI=10.1002/(sici)1097-0061(19970615)13:7<655::aid-yea120>3.0.co;2-i;
RA Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C.,
RA Schwager C., Paces V., Sander C., Ansorge W.;
RT "DNA sequencing and analysis of 130 kb from yeast chromosome XV.";
RL Yeast 13:655-672(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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 CHARACTERIZATION.
RX PubMed=9245783; DOI=10.1083/jcb.138.3.517;
RA Darsow T., Rieder S.E., Emr S.D.;
RT "A multispecificity syntaxin homologue, Vam3p, essential for autophagic and
RT biosynthetic protein transport to the vacuole.";
RL J. Cell Biol. 138:517-529(1997).
RN [6]
RP CHARACTERIZATION.
RX PubMed=9880567; DOI=10.1074/jbc.274.3.1835;
RA Stefan C.J., Blumer K.J.;
RT "A syntaxin homolog encoded by VAM3 mediates down-regulation of a yeast G
RT protein-coupled receptor.";
RL J. Biol. Chem. 274:1835-1841(1999).
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 STRUCTURE BY NMR OF 23-119.
RX PubMed=11224573; DOI=10.1038/85012;
RA Dulubova I., Yamaguchi T., Wang Y., Suedhof T.C., Rizo J.;
RT "Vam3p structure reveals conserved and divergent properties of syntaxins.";
RL Nat. Struct. Biol. 8:258-264(2001).
CC -!- FUNCTION: Required for vacuolar assembly. Provides the t-SNARE function
CC in a late step of the vacuolar assembly. Required for homotypic vacuole
CC membrane fusion, autophagy and fusion of biosynthetic transport
CC vesicles with the vacuole. Required for the delivery of alpha-factor
CC receptor-ligand complexes to the vacuole.
CC -!- SUBUNIT: Associates with VAM7.
CC -!- INTERACTION:
CC Q12241; Q12255: NYV1; NbExp=21; IntAct=EBI-20227, EBI-35465;
CC Q12241; P32912: VAM7; NbExp=11; IntAct=EBI-20227, EBI-20232;
CC Q12241; P20795: VPS33; NbExp=12; IntAct=EBI-20227, EBI-20395;
CC Q12241; Q04338: VTI1; NbExp=13; IntAct=EBI-20227, EBI-20519;
CC -!- SUBCELLULAR LOCATION: Vacuole membrane; Single-pass type IV membrane
CC protein.
CC -!- MISCELLANEOUS: Present with 414 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
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DR EMBL; U57827; AAC49737.1; -; Genomic_DNA.
DR EMBL; X94335; CAA64026.1; -; Genomic_DNA.
DR EMBL; Z75014; CAA99304.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10881.1; -; Genomic_DNA.
DR PIR; S61664; S61664.
DR RefSeq; NP_014749.1; NM_001183525.1.
DR PDB; 1HS7; NMR; -; A=23-119.
DR PDBsum; 1HS7; -.
DR AlphaFoldDB; Q12241; -.
DR BMRB; Q12241; -.
DR SMR; Q12241; -.
DR BioGRID; 34502; 517.
DR ComplexPortal; CPX-1887; Vacuolar SNARE complex VAM3-VTI1-VAM7-YKT6.
DR ComplexPortal; CPX-5401; Vacuolar SNARE complex VAM3-VTI1-VAM7-NYV1.
DR DIP; DIP-1726N; -.
DR IntAct; Q12241; 10.
DR MINT; Q12241; -.
DR STRING; 4932.YOR106W; -.
DR TCDB; 1.F.1.1.2; the synaptosomal vesicle fusion pore (svf-pore) family.
DR iPTMnet; Q12241; -.
DR SwissPalm; Q12241; -.
DR MaxQB; Q12241; -.
DR PaxDb; Q12241; -.
DR PRIDE; Q12241; -.
DR EnsemblFungi; YOR106W_mRNA; YOR106W; YOR106W.
DR GeneID; 854273; -.
DR KEGG; sce:YOR106W; -.
DR SGD; S000005632; VAM3.
DR VEuPathDB; FungiDB:YOR106W; -.
DR eggNOG; KOG0811; Eukaryota.
DR GeneTree; ENSGT01000000214440; -.
DR HOGENOM; CLU_059257_0_0_1; -.
DR InParanoid; Q12241; -.
DR OMA; ERVHNTM; -.
DR BioCyc; YEAST:G3O-33637-MON; -.
DR Reactome; R-SCE-204005; COPII-mediated vesicle transport.
DR EvolutionaryTrace; Q12241; -.
DR PRO; PR:Q12241; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12241; protein.
DR GO; GO:0000421; C:autophagosome membrane; IC:ComplexPortal.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0031201; C:SNARE complex; IDA:SGD.
DR GO; GO:0005774; C:vacuolar membrane; IDA:ComplexPortal.
DR GO; GO:0005484; F:SNAP receptor activity; IDA:SGD.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0061911; P:amphisome-lysosome fusion; IC:ComplexPortal.
DR GO; GO:0097352; P:autophagosome maturation; IMP:SGD.
DR GO; GO:0006896; P:Golgi to vacuole transport; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IMP:SGD.
DR GO; GO:0007036; P:vacuolar calcium ion homeostasis; IDA:ComplexPortal.
DR GO; GO:0042144; P:vacuole fusion, non-autophagic; IDA:SGD.
DR GO; GO:0048278; P:vesicle docking; IGI:SGD.
DR GO; GO:0006906; P:vesicle fusion; IDA:SGD.
DR GO; GO:0051469; P:vesicle fusion with vacuole; IGI:SGD.
DR InterPro; IPR010989; SNARE.
DR InterPro; IPR045242; Syntaxin.
DR InterPro; IPR006012; Syntaxin/epimorphin_CS.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR19957; PTHR19957; 1.
DR Pfam; PF05739; SNARE; 1.
DR SMART; SM00397; t_SNARE; 1.
DR SUPFAM; SSF47661; SSF47661; 1.
DR PROSITE; PS00914; SYNTAXIN; 1.
DR PROSITE; PS50192; T_SNARE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autophagy; Coiled coil; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Vacuole.
FT CHAIN 1..283
FT /note="Syntaxin VAM3"
FT /id="PRO_0000210280"
FT TOPO_DOM 1..261
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..282
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 283
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT DOMAIN 190..252
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 28..48
FT /evidence="ECO:0000255"
FT COILED 84..111
FT /evidence="ECO:0000255"
FT COILED 169..189
FT /evidence="ECO:0000255"
FT COMPBIAS 125..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 25..50
FT /evidence="ECO:0007829|PDB:1HS7"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:1HS7"
FT HELIX 58..66
FT /evidence="ECO:0007829|PDB:1HS7"
FT HELIX 68..81
FT /evidence="ECO:0007829|PDB:1HS7"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:1HS7"
FT HELIX 89..115
FT /evidence="ECO:0007829|PDB:1HS7"
SQ SEQUENCE 283 AA; 32498 MW; 6415D9D852C6C64D CRC64;
MSFFDIEAQS SKGNSQQEPQ FSTNQKTKEL SNLIETFAEQ SRVLEKECTK IGSKRDSKEL
RYKIETELIP NCTSVRDKIE SNILIHQNGK LSADFKNLKT KYQSLQQSYN QRKSLFPLKT
PISPGTSKER KDIHPRTEAV RQDPESSYIS IKVNEQSPLL HNEGQHQLQL QEEQEQQQQG
LSQEELDFQT IIHQERSQQI GRIHTAVQEV NAIFHQLGSL VKEQGEQVTT IDENISHLHD
NMQNANKQLT RADQHQRDRN KCGKVTLIII IVVCMVVLLA VLS
