SFB2_YEAST
ID SFB2_YEAST Reviewed; 876 AA.
AC P53953; D6W1D0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=SED5-binding protein 2;
DE AltName: Full=SEC24-related protein 2;
GN Name=SFB2; Synonyms=ISS1; OrderedLocusNames=YNL049C;
GN ORFNames=N2505, YNL2505C;
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], AND FUNCTION.
RX PubMed=10753972; DOI=10.1074/jbc.275.15.11521;
RA Peng R., De Antoni A., Gallwitz D.;
RT "Evidence for overlapping and distinct functions in protein transport of
RT coat protein Sec24p family members.";
RL J. Biol. Chem. 275:11521-11528(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S288c / FY1676;
RX PubMed=8533472; DOI=10.1002/yea.320111008;
RA Bergez P., Doignon F., Crouzet M.;
RT "The sequence of a 44 420 bp fragment located on the left arm of chromosome
RT XIV from Saccharomyces cerevisiae.";
RL Yeast 11:967-974(1995).
RN [3]
RP ERRATUM OF PUBMED:8533472.
RX PubMed=8904343;
RX DOI=10.1002/(sici)1097-0061(19960315)12:3<297::aid-yea940>3.0.co;2-d;
RA Bergez P., Doignon F., Crouzet M.;
RL Yeast 12:297-297(1996).
RN [4]
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 [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-544.
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8740423;
RX DOI=10.1002/(sici)1097-0061(199604)12:5<493::aid-yea929>3.0.co;2-w;
RA Nasr F., Becam A.-M., Herbert C.J.;
RT "The sequence of 12.8 kb from the left arm of chromosome XIV reveals a
RT sigma element, a pro-tRNA and six complete open reading frames, one of
RT which encodes a protein similar to the human leukotriene A4 hydrolase.";
RL Yeast 12:493-499(1996).
RN [8]
RP FUNCTION.
RX PubMed=10749860; DOI=10.1074/jbc.m000751200;
RA Higashio H., Kimata Y., Kiriyama T., Hirata A., Kohno K.;
RT "Sfb2p, a yeast protein related to Sec24p, can function as a constituent of
RT COPII coats required for vesicle budding from the endoplasmic reticulum.";
RL J. Biol. Chem. 275:17900-17908(2000).
RN [9]
RP FUNCTION.
RX PubMed=10712514; DOI=10.1091/mbc.11.3.983;
RA Kurihara T., Hamamoto S., Gimeno R.E., Kaiser C.A., Schekman R.W.,
RA Yoshihisa T.;
RT "Sec24p and Iss1p function interchangeably in transport vesicle formation
RT from the endoplasmic reticulum in Saccharomyces cerevisiae.";
RL Mol. Biol. Cell 11:983-998(2000).
RN [10]
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 [11]
RP FUNCTION, AND INTERACTION WITH GRH1.
RX PubMed=16269340; DOI=10.1016/j.cell.2005.08.031;
RA Schuldiner M., Collins S.R., Thompson N.J., Denic V., Bhamidipati A.,
RA Punna T., Ihmels J., Andrews B., Boone C., Greenblatt J.F., Weissman J.S.,
RA Krogan N.J.;
RT "Exploration of the function and organization of the yeast early secretory
RT pathway through an epistatic miniarray profile.";
RL Cell 123:507-519(2005).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [13]
RP INTERACTION WITH GRH1.
RX PubMed=17261844; DOI=10.1083/jcb.200607151;
RA Behnia R., Barr F.A., Flanagan J.J., Barlowe C., Munro S.;
RT "The yeast orthologue of GRASP65 forms a complex with a coiled-coil protein
RT that contributes to ER to Golgi traffic.";
RL J. Cell Biol. 176:255-261(2007).
RN [14]
RP IDENTIFICATION BY 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 [15]
RP IDENTIFICATION BY 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: Component of the COPII coat, that covers ER-derived vesicles
CC involved in transport from the endoplasmic reticulum to the Golgi
CC apparatus. COPII acts in the cytoplasm to promote the transport of
CC secretory, plasma membrane, and vacuolar proteins from the endoplasmic
CC reticulum to the Golgi complex. {ECO:0000269|PubMed:10712514,
CC ECO:0000269|PubMed:10749860, ECO:0000269|PubMed:10753972,
CC ECO:0000269|PubMed:16269340}.
CC -!- SUBUNIT: COPII is composed of at least five proteins: the SEC23/24
CC complex, the SEC13/31 complex and SAR1. Interacts with GRH1.
CC {ECO:0000269|PubMed:16269340, ECO:0000269|PubMed:17261844}.
CC -!- INTERACTION:
CC P53953; P15303: SEC23; NbExp=4; IntAct=EBI-17006, EBI-16584;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus membrane
CC {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}.
CC -!- MISCELLANEOUS: Present with 1720 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC24 subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ009783; CAA08830.1; -; Genomic_DNA.
DR EMBL; U12141; AAA99663.1; -; Genomic_DNA.
DR EMBL; Z71325; CAA95918.1; -; Genomic_DNA.
DR EMBL; Z71324; CAA95917.1; -; Genomic_DNA.
DR EMBL; AY692828; AAT92847.1; -; Genomic_DNA.
DR EMBL; X94547; CAA64233.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10496.1; -; Genomic_DNA.
DR PIR; S62152; S62152.
DR RefSeq; NP_014349.1; NM_001182888.1.
DR AlphaFoldDB; P53953; -.
DR SMR; P53953; -.
DR BioGRID; 35775; 163.
DR DIP; DIP-4370N; -.
DR IntAct; P53953; 32.
DR MINT; P53953; -.
DR STRING; 4932.YNL049C; -.
DR iPTMnet; P53953; -.
DR MaxQB; P53953; -.
DR PaxDb; P53953; -.
DR PRIDE; P53953; -.
DR EnsemblFungi; YNL049C_mRNA; YNL049C; YNL049C.
DR GeneID; 855678; -.
DR KEGG; sce:YNL049C; -.
DR SGD; S000004994; SFB2.
DR VEuPathDB; FungiDB:YNL049C; -.
DR eggNOG; KOG1985; Eukaryota.
DR GeneTree; ENSGT00950000182924; -.
DR HOGENOM; CLU_004589_2_1_1; -.
DR InParanoid; P53953; -.
DR OMA; MSAYNPN; -.
DR BioCyc; YEAST:G3O-33082-MON; -.
DR Reactome; R-SCE-204005; COPII-mediated vesicle transport.
DR Reactome; R-SCE-5694530; Cargo concentration in the ER.
DR Reactome; R-SCE-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR PRO; PR:P53953; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53953; protein.
DR GO; GO:0030127; C:COPII vesicle coat; IPI:SGD.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005048; F:signal sequence binding; ISS:SGD.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0090110; P:COPII-coated vesicle cargo loading; IDA:SGD.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR CDD; cd01479; Sec24-like; 1.
DR Gene3D; 3.40.20.10; -; 1.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR007123; Gelsolin-like_dom.
DR InterPro; IPR036180; Gelsolin-like_dom_sf.
DR InterPro; IPR006900; Sec23/24_helical_dom.
DR InterPro; IPR036175; Sec23/24_helical_dom_sf.
DR InterPro; IPR006896; Sec23/24_trunk_dom.
DR InterPro; IPR012990; Sec23_24_beta_S.
DR InterPro; IPR041742; Sec24-like_trunk_dom.
DR InterPro; IPR036465; vWFA_dom_sf.
DR InterPro; IPR006895; Znf_Sec23_Sec24.
DR InterPro; IPR036174; Znf_Sec23_Sec24_sf.
DR Pfam; PF00626; Gelsolin; 1.
DR Pfam; PF08033; Sec23_BS; 1.
DR Pfam; PF04815; Sec23_helical; 1.
DR Pfam; PF04811; Sec23_trunk; 1.
DR Pfam; PF04810; zf-Sec23_Sec24; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR SUPFAM; SSF81811; SSF81811; 1.
DR SUPFAM; SSF82754; SSF82754; 1.
DR SUPFAM; SSF82919; SSF82919; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus;
KW Membrane; Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..876
FT /note="SED5-binding protein 2"
FT /id="PRO_0000205151"
FT REGION 164..189
FT /note="Zinc finger-like"
FT REGION 300..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:19779198"
SQ SEQUENCE 876 AA; 98944 MW; 4534CE7E27514379 CRC64;
MSHHKKRVYP QAQVPYIASM PIVAEQQQSQ QQIDQTAYAM GNLQLNNRAN SFTQLAQNQQ
FPGSGKVVNQ LYPVDLFTEL PPPIRDLSLP PLPITISQDN IVTPSEYSNV PYQYVRSTLK
AVPKTNSLLK KTKLPFAIVI RPYLHLQDSD NQVPLNTDGV IVRCRRCRSY MNPFVVFINQ
GRKWQCNICR FKNDVPFGFD QNLQGAPINR YERNEIKNSV VDYLAPVEYS VREPPPSVYV
FLLDVSQNAV KNGLLATSAR TILENIEFLP NHDGRTRIAI ICVDHSLHYF YVPLDDDYEV
SDEDDEESDG EEEDEDEEEE DVDNSETIQM FDIGDLDEPF LPMPSDELVV PLKYCKNNLE
TLLKKIPEIF QDTHSSKFAL GPALKAASNL IKSTGGKVEV ISSTLPNTGI GKLKKRSEQG
ILNTPKESSQ LLSCKDSFYK TFTIECNKLQ ITVDMFLASE DYMDVATLSH LGRFSGGQTH
FYPGFNATSL NDVTKFTREL SRHLSMDISM EAVMRVRCST GLRATSFFGH FFNRSSDLCA
FSTMPRDQSY LFGISIEDSL MAEYCYLQVS TLLTLNTGER RIRVMTLALP TSESAREVFA
SADQLAITDF MTQNAVTKAL NSSMYSARDF ITKSLEDILN AYKKEISMSN INSVTSLNLC
ANLRMLPLLM NGLSKHIALR PGVVPSDYRA SALNRLETEP LHYLIKSIYP TVYSLHDMPD
EVGLPDFEGK TVLPEPINAT ISLFERYGLY LIDNSAELFL WVGGDAVPEL LIDVFNTDTI
SQIPVGKSEL PLLNDSPFNE RLRRIIGRIR ENNDTITFQS LYIIRGPSIN EPANLNSEKD
MASLRLWVLS TLVEDKVLNC ASYREYLQSM KTSINR
