SEC2_YEAST
ID SEC2_YEAST Reviewed; 759 AA.
AC P17065; D6W0S2;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Rab guanine nucleotide exchange factor SEC2;
DE AltName: Full=GDP-GTP exchange factor SEC2;
GN Name=SEC2; OrderedLocusNames=YNL272C; ORFNames=N0641;
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=S288c / GRF88;
RX PubMed=1693620; DOI=10.1083/jcb.110.6.1897;
RA Nair J., Mueller H., Peterson M., Novick P.J.;
RT "Sec2 protein contains a coiled-coil domain essential for vesicular
RT transport and a dispensable carboxy terminal domain.";
RL J. Cell Biol. 110:1897-1909(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(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 FUNCTION, AND INTERACTION WITH SEC4.
RX PubMed=9199166; DOI=10.1083/jcb.137.7.1495;
RA Walch-Solimena C., Collins R.N., Novick P.J.;
RT "Sec2p mediates nucleotide exchange on Sec4p and is involved in polarized
RT delivery of post-Golgi vesicles.";
RL J. Cell Biol. 137:1495-1509(1997).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-483, AND
RP PHOSPHORYLATION.
RX PubMed=10747090; DOI=10.1083/jcb.149.1.95;
RA Elkind N.B., Walch-Solimena C., Novick P.J.;
RT "The role of the COOH terminus of Sec2p in the transport of post-Golgi
RT vesicles.";
RL J. Cell Biol. 149:95-110(2000).
RN [6]
RP FUNCTION, AND INTERACTION WITH YPT32.
RX PubMed=12045183; DOI=10.1083/jcb.200201003;
RA Ortiz D., Medkova M., Walch-Solimena C., Novick P.J.;
RT "Ypt32 recruits the Sec4p guanine nucleotide exchange factor, Sec2p, to
RT secretory vesicles; evidence for a Rab cascade in yeast.";
RL J. Cell Biol. 157:1005-1015(2002).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-515, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-515, AND IDENTIFICATION BY
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-168; SER-171 AND SER-515, 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).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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 -!- FUNCTION: Guanine nucleotide exchange factor for SEC4, catalyzing the
CC dissociation of GDP from SEC4 and also potently promoting binding of
CC GTP. Activation of SEC4 by SEC2 is needed for the directed transport of
CC vesicles to sites of exocytosis. Binds the Rab GTPase YPT32, but does
CC not have exchange activity on YPT32. {ECO:0000269|PubMed:10747090,
CC ECO:0000269|PubMed:12045183, ECO:0000269|PubMed:9199166}.
CC -!- SUBUNIT: Interacts with SEC4. Interacts with YPT32, preferentially in
CC its GTP-bound form. {ECO:0000269|PubMed:12045183,
CC ECO:0000269|PubMed:9199166}.
CC -!- INTERACTION:
CC P17065; P17065: SEC2; NbExp=2; IntAct=EBI-16842, EBI-16842;
CC P17065; P07560: SEC4; NbExp=4; IntAct=EBI-16842, EBI-16858;
CC -!- SUBCELLULAR LOCATION: Bud neck {ECO:0000269|PubMed:10747090}. Bud tip
CC {ECO:0000269|PubMed:10747090}. Cytoplasmic vesicle, secretory vesicle
CC {ECO:0000269|PubMed:10747090}. Note=Localizes to sites of polarized
CC growth, namely to the bud neck and to the bud tip of growing buds, and
CC associates with membranes. Colocalizes with secretory vesicles at
CC exocytic sites. Proper localization is dependent on the actin
CC cytoskeleton, MYO2, the kinesin-related protein SMY1, the Rab GTPase
CC YPT32, and the production of post-Golgi vesicles.
CC -!- DOMAIN: The N-terminal domain (1-374) is sufficient for the exchange
CC factor activity.
CC -!- MISCELLANEOUS: Present with 13200 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SEC2 family. {ECO:0000305}.
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DR EMBL; X52147; CAA36395.1; -; Genomic_DNA.
DR EMBL; Z71548; CAA96180.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10288.1; -; Genomic_DNA.
DR PIR; A35597; A35597.
DR RefSeq; NP_014127.1; NM_001183110.1.
DR PDB; 2E7S; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=31-160.
DR PDB; 2EQB; X-ray; 2.70 A; B/C=51-142.
DR PDB; 2OCY; X-ray; 3.30 A; A/B=17-167.
DR PDB; 4ZDW; X-ray; 2.90 A; B/C=51-142.
DR PDBsum; 2E7S; -.
DR PDBsum; 2EQB; -.
DR PDBsum; 2OCY; -.
DR PDBsum; 4ZDW; -.
DR AlphaFoldDB; P17065; -.
DR SMR; P17065; -.
DR BioGRID; 35568; 378.
DR DIP; DIP-2493N; -.
DR IntAct; P17065; 25.
DR MINT; P17065; -.
DR STRING; 4932.YNL272C; -.
DR iPTMnet; P17065; -.
DR MaxQB; P17065; -.
DR PaxDb; P17065; -.
DR PRIDE; P17065; -.
DR EnsemblFungi; YNL272C_mRNA; YNL272C; YNL272C.
DR GeneID; 855449; -.
DR KEGG; sce:YNL272C; -.
DR SGD; S000005216; SEC2.
DR VEuPathDB; FungiDB:YNL272C; -.
DR eggNOG; KOG4324; Eukaryota.
DR GeneTree; ENSGT00940000175137; -.
DR HOGENOM; CLU_018015_0_0_1; -.
DR InParanoid; P17065; -.
DR OMA; WSKLGFW; -.
DR BioCyc; YEAST:G3O-33266-MON; -.
DR Reactome; R-SCE-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-SCE-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR EvolutionaryTrace; P17065; -.
DR PRO; PR:P17065; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P17065; protein.
DR GO; GO:0051286; C:cell tip; IBA:GO_Central.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; IDA:SGD.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0070319; C:Golgi to plasma membrane transport vesicle; IBA:GO_Central.
DR GO; GO:0043332; C:mating projection tip; HDA:SGD.
DR GO; GO:0030133; C:transport vesicle; IDA:SGD.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:SGD.
DR GO; GO:0006914; P:autophagy; IMP:SGD.
DR GO; GO:0006887; P:exocytosis; IMP:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR040351; RAB3IL/RAB3IP/Sec2.
DR InterPro; IPR009449; Sec2_N.
DR PANTHER; PTHR14430; PTHR14430; 1.
DR Pfam; PF06428; Sec2p; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Coiled coil; Cytoplasmic vesicle;
KW Guanine-nucleotide releasing factor; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..759
FT /note="Rab guanine nucleotide exchange factor SEC2"
FT /id="PRO_0000097661"
FT REGION 451..508
FT /note="Required for proper polarized localization of the
FT protein"
FT REGION 538..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 26..164
FT /evidence="ECO:0000255"
FT COILED 651..682
FT /evidence="ECO:0000255"
FT COILED 732..759
FT /evidence="ECO:0000255"
FT COMPBIAS 564..616
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..650
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..704
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..753
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 168
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MUTAGEN 483
FT /note="C->Y: In SEC2-78; temperature-sensitive; causes
FT mislocalization of the protein, displaying many cytoplasmic
FT punctae."
FT /evidence="ECO:0000269|PubMed:10747090"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:2E7S"
FT HELIX 52..141
FT /evidence="ECO:0007829|PDB:2EQB"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:2E7S"
SQ SEQUENCE 759 AA; 84652 MW; 7F5A9B2343CBE835 CRC64;
MDASEEAKRV SIQVTSLSTQ LIESVDKQSH LEEQLNKSLK TIASQKAAIE NYNQLKEDYN
TLKRELSDRD DEVKRLREDI AKENELRTKA EEEADKLNKE VEDLTASLFD EANNMVADAR
KEKYAIEILN KRLTEQLREK DTLLDTLTLQ LKNLKKVMHS LDNESTVTNN SNRYSTILSD
SATSSSTSLN KVPTSYSLAS QDIYSGIVYS PSISSIRYDI SLYNEFLKFV AALPRCENIK
ATSTESKLIR RLVNDEIQPI LKIDNASGIG WLVKKTLLSL IIDGLVVVEP LSGVNATYQI
GYNSSSPAKQ ATSNMPKMFK FPLDSPPVAV HAACSFCGES RDDIIEHARM YILKTLHKTD
DGKEQVTNTY PLCHWCLLKL RQTCEIFAFL RSLKVGAWHL EKLTTQNITK EDLEKFSEVT
KHTKRDGRVS SQDKKTKRLS FMAGLGINSS TKNKPKMEIF SSETNAKPGQ PTTNIQRAWL
QLCKLRCILH WTHIGIWAVD DSISSKIGPL VEDDSDEDQN DAISVRLQDK ALWKQDAKRP
FSSSSAEESQ KSDAFDFESG DMENEITGES SSDESSSDGS STDNSTADSS SEDESSLADS
TTSSADSSSP ESIDNGEGDD TVTKDDKSSI KSANNNEENS DCGDKKGRSI IKKKAPQRKI
QKKKLLQDLD DLEEQFREES AIDQTEFENA ESNVKQNISS KRASSGDENS KKDNNEKTLK
TNLTIGDKTQ EQIGENSPSS GLHASSSNDD NFDDAQEQQ
