SFB3_YEAST
ID SFB3_YEAST Reviewed; 929 AA.
AC P38810; D3DL48;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=SED5-binding protein 3;
DE AltName: Full=Lethal with SEC13 protein 1;
DE AltName: Full=SEC24-related protein 3;
GN Name=SFB3; Synonyms=LST1; OrderedLocusNames=YHR098C;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
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 [4]
RP CHARACTERIZATION.
RX PubMed=10330397; DOI=10.1083/jcb.145.4.659;
RA Roberg K.J., Crotwell M., Espenshade P., Gimeno R., Kaiser C.A.;
RT "LST1 is a SEC24 homologue used for selective export of the plasma membrane
RT ATPase from the endoplasmic reticulum.";
RL J. Cell Biol. 145:659-672(1999).
RN [5]
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 [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-94; SER-101 AND
RP THR-216, AND 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-72; SER-83; SER-85; SER-101
RP AND SER-110, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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.
CC -!- SUBUNIT: COPII is composed of at least five proteins: the SEC23/24
CC complex, the SEC13/31 complex and SAR1. Binds to SED5. Interacts with
CC GHR1. {ECO:0000269|PubMed:17261844}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus membrane
CC {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}.
CC -!- MISCELLANEOUS: Present with 12200 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC24 subfamily.
CC {ECO:0000305}.
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DR EMBL; U00060; AAB68936.1; -; Genomic_DNA.
DR EMBL; AJ009784; CAA08831.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06792.1; -; Genomic_DNA.
DR PIR; S46728; S46728.
DR RefSeq; NP_011966.1; NM_001179228.1.
DR AlphaFoldDB; P38810; -.
DR SMR; P38810; -.
DR BioGRID; 36531; 393.
DR ComplexPortal; CPX-1341; SEC23-LST1 COPII cargo recruitment complex.
DR DIP; DIP-2949N; -.
DR IntAct; P38810; 12.
DR MINT; P38810; -.
DR STRING; 4932.YHR098C; -.
DR iPTMnet; P38810; -.
DR MaxQB; P38810; -.
DR PaxDb; P38810; -.
DR PRIDE; P38810; -.
DR EnsemblFungi; YHR098C_mRNA; YHR098C; YHR098C.
DR GeneID; 856498; -.
DR KEGG; sce:YHR098C; -.
DR SGD; S000001140; SFB3.
DR VEuPathDB; FungiDB:YHR098C; -.
DR eggNOG; KOG1984; Eukaryota.
DR GeneTree; ENSGT00950000182924; -.
DR HOGENOM; CLU_004589_1_0_1; -.
DR InParanoid; P38810; -.
DR OMA; DRRVHDM; -.
DR BioCyc; YEAST:G3O-31143-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:P38810; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38810; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0030127; C:COPII vesicle coat; IDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA: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:0043332; C:mating projection tip; HDA:SGD.
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; IDA:ComplexPortal.
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..929
FT /note="SED5-binding protein 3"
FT /id="PRO_0000205152"
FT REGION 18..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..244
FT /note="Zinc finger-like"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 72
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 216
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 929 AA; 103950 MW; 6A028AD6B1A2E031 CRC64;
MSQQNILAAS VSALSLDEST VHTGGASSKK SRRPHRAYHN FSSGTVPTLG NSPYTTPQLN
QQDGFQQPQA FTPKQFGGFN NGSGSVMSTP VMVSQERFGA SEASSPYGQS MLDMTAPQPT
SHIVPTQRFE DQAQYLQRSF ETCRDSVPPL PTTQFYCVDQ GSCDPHLMSL SMYNIPESEH
LRAATKLPLG LTIQPFSTLT PNDAEVPTIP LPMDGTPLRC RRCRAYANPK FQFTYDSSVI
CNICRVKMQV PGEHFAPMGP NGQRSDLNEK SELLHGTVDF LVPSIYNAIQ EKELLPLHYV
FLIDVSLLAN ENGSSLAMVE GVRSCIEYIS DFQPNCEVAI IVYDNKLRFF NLRPDLDNAQ
EYIVSELDDV FLPFYNGLFV KPGNSMKIIN DTLIKISGYI STDKYSHVPQ VCYGSALQAA
KLALDTVTGG QGGKIICSLN SLPTIGNGNL SLKRDNAHIA HVKCDNGFYK KLASDFLKSY
ISLDLYVTNA GFIDMATVGH PVEMTSGILK YYPHFQQETD AFTLVNDMVT NVSNIVGYQA
LLKVRCSTGL SVEQYYCDSS DNTDHDPIIP VLTRDTTLDV LLKYDSKIKT GTDVHFQTAL
LYTDIDGVRK VRSINTSGAV SNNIREIFKF INQNPVMRIM IKDVIKTLGD CDFVKIRRLI
DDKMVEILTQ YRGLVSSNSS TQLILPDSIK TLPAYMLAFE KSELMKPNAQ STRGNERIYD
LLKYDSLNSA QLCYKLYPQI VPFHVLLEET DLTFYDANDK LLQINSSSIN NLSVRASHSN
FINGGCYLIF QGDTIYLWFN ENTNRMLLQD LLSVDESLPV SQISLFSGTL PETGTSINQK
ASNVIKNWQQ VVNKSSLPLV LLRPNVDQYY SNVMSQLLCE DKTVNRIESY DNYLVIMHKK
IQEKLQKDDF IKVSTAATHE NIHQKFVQF
