SEA4_YEAST
ID SEA4_YEAST Reviewed; 1038 AA.
AC P38164; D6VPP9; Q86ZS4;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=SEH-associated protein 4;
GN Name=SEA4; OrderedLocusNames=YBL104C; ORFNames=YBL0808, YBL103C-A;
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 204508 / S288c;
RX PubMed=7502586; DOI=10.1002/yea.320111112;
RA Obermaier B., Gassenhuber J., Piravandi E., Domdey H.;
RT "Sequence analysis of a 78.6 kb segment of the left end of Saccharomyces
RT cerevisiae chromosome II.";
RL Yeast 11:1103-1112(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 942-1001, AND IDENTIFICATION OF
RP FRAMESHIFT.
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=12844361; DOI=10.1186/gb-2003-4-7-r45;
RA Brachat S., Dietrich F.S., Voegeli S., Zhang Z., Stuart L., Lerch A.,
RA Gates K., Gaffney T.D., Philippsen P.;
RT "Reinvestigation of the Saccharomyces cerevisiae genome annotation by
RT comparison to the genome of a related fungus: Ashbya gossypii.";
RL Genome Biol. 4:R45.1-R45.13(2003).
RN [5]
RP IDENTIFICATION OF FRAMESHIFTS.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
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 IDENTIFICATION OF FRAMESHIFT.
RX PubMed=12775844; DOI=10.1126/science.1084337;
RA Cliften P.F., Sudarsanam P., Desikan A., Fulton L., Fulton B., Majors J.,
RA Waterston R., Cohen B.A., Johnston M.;
RT "Finding functional features in Saccharomyces genomes by phylogenetic
RT footprinting.";
RL Science 301:71-76(2003).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123 AND SER-136, AND
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 [10]
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 SUBCELLULAR LOCATION, IDENTIFICATION IN THE SEA COMPLEX, AND FUNCTION.
RX PubMed=21454883; DOI=10.1074/mcp.m110.006478;
RA Dokudovskaya S., Waharte F., Schlessinger A., Pieper U., Devos D.P.,
RA Cristea I.M., Williams R., Salamero J., Chait B.T., Sali A., Field M.C.,
RA Rout M.P., Dargemont C.;
RT "A conserved coatomer-related complex containing Sec13 and Seh1 dynamically
RT associates with the vacuole in Saccharomyces cerevisiae.";
RL Mol. Cell. Proteomics 10:M110.006478.1-M110.006478.17(2011).
CC -!- FUNCTION: Component of the SEA complex which coats the vacuolar
CC membrane and is involved in intracellular trafficking, autophagy,
CC response to nitrogen starvation, and amino acid biogenesis.
CC {ECO:0000269|PubMed:21454883}.
CC -!- SUBUNIT: Component of the SEA complex composed of at least IML1/SEA1,
CC RTC1/SEA2, MTC5/SEA3, NPR2, NPR3, SEA4, SEC13 and SEH1.
CC {ECO:0000269|PubMed:21454883}.
CC -!- INTERACTION:
CC P38164; P15108: HSC82; NbExp=2; IntAct=EBI-21365, EBI-8666;
CC P38164; P53011: SEH1; NbExp=6; IntAct=EBI-21365, EBI-16940;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Vacuole membrane; Peripheral membrane
CC protein.
CC -!- MISCELLANEOUS: Present with 184 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the WD repeat mio family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA55991.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA84930.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X79489; CAA55991.1; ALT_FRAME; Genomic_DNA.
DR EMBL; Z35865; CAA84930.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AY260889; AAP21757.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07019.1; -; Genomic_DNA.
DR PIR; S45391; S45391.
DR RefSeq; NP_009446.2; NM_001178344.1.
DR AlphaFoldDB; P38164; -.
DR BioGRID; 32599; 184.
DR ComplexPortal; CPX-3231; SEA complex.
DR DIP; DIP-4369N; -.
DR IntAct; P38164; 56.
DR MINT; P38164; -.
DR STRING; 4932.YBL104C; -.
DR iPTMnet; P38164; -.
DR MaxQB; P38164; -.
DR PaxDb; P38164; -.
DR PRIDE; P38164; -.
DR EnsemblFungi; YBL104C_mRNA; YBL104C; YBL104C.
DR GeneID; 852170; -.
DR KEGG; sce:YBL104C; -.
DR SGD; S000000200; SEA4.
DR VEuPathDB; FungiDB:YBL104C; -.
DR eggNOG; KOG1008; Eukaryota.
DR GeneTree; ENSGT00390000015038; -.
DR HOGENOM; CLU_005843_0_0_1; -.
DR InParanoid; P38164; -.
DR OMA; EWFSFCL; -.
DR BioCyc; YEAST:G3O-28988-MON; -.
DR PRO; PR:P38164; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38164; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0097042; C:extrinsic component of fungal-type vacuolar membrane; IDA:SGD.
DR GO; GO:0035859; C:Seh1-associated complex; IDA:SGD.
DR GO; GO:0005774; C:vacuolar membrane; IC:ComplexPortal.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; IGI:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:1903432; P:regulation of TORC1 signaling; IDA:ComplexPortal.
DR CDD; cd16691; mRING-H2-C3H3C2_Mio; 1.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR037593; MIOS/Sea4.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR031488; Zn_ribbon_mio.
DR PANTHER; PTHR16453; PTHR16453; 1.
DR Pfam; PF17034; zinc_ribbon_16; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Membrane; Phosphoprotein; Protein transport; Reference proteome;
KW Repeat; Transport; Vacuole; WD repeat.
FT CHAIN 1..1038
FT /note="SEH-associated protein 4"
FT /id="PRO_0000051470"
FT REPEAT 50..90
FT /note="WD 1"
FT REPEAT 147..189
FT /note="WD 2"
FT REPEAT 235..276
FT /note="WD 3"
FT REPEAT 544..587
FT /note="WD 4"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 1038 AA; 117636 MW; 613630F9F41FF77C CRC64;
MGLIKKVTHW SYDNLIDYLS VNPTRDEVTH YKVDPENESD ESIIKLHTVK DFGSITCLDY
SESEIGMIGV GEKNGYLRIF NISGQNSSSP ASHAPVGLNA NNETSMTNAS GGKAAQAENI
VGSVSNLKDT QGYPVSETNY DIRVRAKKQR CINSLGINTN GLIAMGLDRN KHDSSLQIWD
MNYHDDSHET INPMFSYCTN ESIVSLKFLN DTSVLAASTK FLKEIDVRSP NPIYQHPTRL
TYDIKLNPFN DWQFSTYGDD GTLAIWDRRK LSDQASLGDL NVASPLLTFE KLVGSGAASR
KYMNSCFRWS CVRNNEFATL HRGDTIKRWR LGYYCDSNRD IAADDDNEMN IENLFVSSVH
DTNTMYDRVA TFDYIPRSNN GTSLICMRQS GTIYRMPISE VCSKAILNNR NSLLLSNFEN
TEIDEIRVNN EHEKSNLENV KTILKNLSFE DLDVSEDYFP SGHDEPNNEI EYSELSEEEN
EGSNDVLDSK RGFELFWKPE KLLEKDISVI MRTRASLGYG LDPMNTVEMI DSSKNLQNNA
YIRNTWRWIA IAKASVDDGT MVSGDLDLGY EGVIGIWNGI NGISNQDRYR QETILSDKQL
NKEMEKIIKL RRKNRDRNSP IANAAGSPKY VQRRLCLIIS GWDLSRSDYE DKYNIIMKNG
HYEKAAAWAV FFGDIPKAVE ILGSAKKERL RLIATAIAGY LAYKDLPGNN AWRQQCRKMS
SELDDPYLRV IFAFIADNDW WDILYEPAIS LRERLGVALR FLNDTDLTTF LDRTSSTVIE
NGELEGLILT GITPNGIDLL QSYVNKTSDV QSAALISIFG SPRYFRDQRV DEWIQTYRDM
LKSWELFSMR ARFDVLRSKL SRTKTGVLTA DIKPRQIYIQ CQNCKQNINT PRTSSPSSAV
STSAGNYKNG EAYRRNNADY KKFNTGSSEA QAADEKPRHK YCCPHCGSSF PRCAICLMPL
GTSNLPFVIN GTQSRDPMQT EDSQDGANRE LVSRKLKLNE WFSFCLSCNH GMHAGHAEEW
FDRHNVCPTP GCTCQCNK
