SEC7_YEAST
ID SEC7_YEAST Reviewed; 2009 AA.
AC P11075; D6VSF1; Q03960; Q04139;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Protein transport protein SEC7;
GN Name=SEC7; OrderedLocusNames=YDR170C; ORFNames=YD9395.01C, YD9489.05C;
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].
RX PubMed=3042778; DOI=10.1016/s0021-9258(18)37842-6;
RA Achstetter T., Franzusoff A., Field C., Schekman R.;
RT "SEC7 encodes an unusual, high molecular weight protein required for
RT membrane traffic from the yeast Golgi apparatus.";
RL J. Biol. Chem. 263:11711-11717(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 CHARACTERIZATION.
RX PubMed=1986005; DOI=10.1083/jcb.112.1.27;
RA Franzusoff A., Redding K., Crosby J., Fuller R.S., Schekman R.;
RT "Localization of components involved in protein transport and processing
RT through the yeast Golgi apparatus.";
RL J. Cell Biol. 112:27-37(1991).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212; SER-215; SER-807;
RP SER-1226 AND THR-1240, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 THR-334; SER-447 AND SER-1226,
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212; SER-447; SER-452;
RP SER-455; SER-1226; THR-1240; SER-1741 AND SER-1752, 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).
RN [11]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-797, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: May play a role in vesicular budding and traffic between
CC compartments of the Golgi apparatus.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus. Note=Associated with
CC the peripheral Golgi membrane.
CC -!- DOMAIN: The highly charged acidic domain may serve a structural role to
CC interact with lipids or proteins on the cytoplasmic surface of the
CC Golgi apparatus.
CC -!- MISCELLANEOUS: Present with 3670 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; J03918; AAB04031.1; -; Genomic_DNA.
DR EMBL; Z46727; CAA86696.1; -; Genomic_DNA.
DR EMBL; Z47813; CAA87801.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12011.1; -; Genomic_DNA.
DR PIR; S49764; S49764.
DR RefSeq; NP_010454.3; NM_001180477.3.
DR PDB; 4OIY; X-ray; 1.50 A; A/B=824-1010.
DR PDBsum; 4OIY; -.
DR AlphaFoldDB; P11075; -.
DR SMR; P11075; -.
DR BioGRID; 32221; 294.
DR DIP; DIP-830N; -.
DR IntAct; P11075; 59.
DR MINT; P11075; -.
DR STRING; 4932.YDR170C; -.
DR CarbonylDB; P11075; -.
DR iPTMnet; P11075; -.
DR MaxQB; P11075; -.
DR PaxDb; P11075; -.
DR PRIDE; P11075; -.
DR EnsemblFungi; YDR170C_mRNA; YDR170C; YDR170C.
DR GeneID; 851748; -.
DR KEGG; sce:YDR170C; -.
DR SGD; S000002577; SEC7.
DR VEuPathDB; FungiDB:YDR170C; -.
DR eggNOG; KOG0929; Eukaryota.
DR HOGENOM; CLU_000691_1_1_1; -.
DR InParanoid; P11075; -.
DR OMA; LLWNMEM; -.
DR BioCyc; YEAST:G3O-29759-MON; -.
DR PRO; PR:P11075; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P11075; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005798; C:Golgi-associated vesicle; IDA:SGD.
DR GO; GO:0005770; C:late endosome; IDA:SGD.
DR GO; GO:0005802; C:trans-Golgi network; IDA:SGD.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:SGD.
DR GO; GO:0000045; P:autophagosome assembly; IMP:SGD.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:SGD.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IMP:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR CDD; cd00171; Sec7; 1.
DR Gene3D; 1.10.1000.11; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR032629; DCB_dom.
DR InterPro; IPR015403; Sec7_C.
DR InterPro; IPR023394; Sec7_C_sf.
DR InterPro; IPR000904; Sec7_dom.
DR InterPro; IPR035999; Sec7_dom_sf.
DR InterPro; IPR032691; Sec7_N.
DR Pfam; PF16213; DCB; 1.
DR Pfam; PF09324; DUF1981; 1.
DR Pfam; PF01369; Sec7; 1.
DR Pfam; PF12783; Sec7_N; 1.
DR SMART; SM00222; Sec7; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF48425; SSF48425; 1.
DR PROSITE; PS50190; SEC7; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Golgi apparatus; Isopeptide bond; Phosphoprotein;
KW Protein transport; Reference proteome; Transport; Ubl conjugation.
FT CHAIN 1..2009
FT /note="Protein transport protein SEC7"
FT /id="PRO_0000120214"
FT DOMAIN 824..1010
FT /note="SEC7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00189"
FT REGION 1..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 771..814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1708..1803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..135
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..184
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..795
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..810
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1721..1755
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1764..1779
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 334
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 447
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 452
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 455
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 807
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 1226
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 1240
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 1741
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1752
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CROSSLNK 797
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CONFLICT 188
FT /note="A -> S (in Ref. 1; AAB04031)"
FT /evidence="ECO:0000305"
FT CONFLICT 399..400
FT /note="FV -> LL (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 402
FT /note="S -> C (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 1031..1034
FT /note="QQSA -> PAIC (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 1036..1037
FT /note="NF -> QL (in Ref. 1)"
FT /evidence="ECO:0000305"
FT HELIX 830..840
FT /evidence="ECO:0007829|PDB:4OIY"
FT HELIX 842..851
FT /evidence="ECO:0007829|PDB:4OIY"
FT STRAND 854..856
FT /evidence="ECO:0007829|PDB:4OIY"
FT HELIX 860..869
FT /evidence="ECO:0007829|PDB:4OIY"
FT HELIX 875..883
FT /evidence="ECO:0007829|PDB:4OIY"
FT HELIX 887..898
FT /evidence="ECO:0007829|PDB:4OIY"
FT HELIX 907..915
FT /evidence="ECO:0007829|PDB:4OIY"
FT HELIX 924..941
FT /evidence="ECO:0007829|PDB:4OIY"
FT HELIX 949..967
FT /evidence="ECO:0007829|PDB:4OIY"
FT STRAND 970..972
FT /evidence="ECO:0007829|PDB:4OIY"
FT HELIX 977..983
FT /evidence="ECO:0007829|PDB:4OIY"
FT TURN 984..987
FT /evidence="ECO:0007829|PDB:4OIY"
FT HELIX 995..1007
FT /evidence="ECO:0007829|PDB:4OIY"
SQ SEQUENCE 2009 AA; 226886 MW; 02B2D370DD2E4661 CRC64;
MSEQNSVVNA EKGDGEISSN VETASSVNPS VKPQNAIKEE AKETNGEDQK CKGPENAGST
AETKETSNDA TNGMKTPEET EDTNDKRHDD EGEDGDEDED EDEDEDEDNG DEDDEDVDSS
SSETSSEDGE DSESVSGEST ESSSGEDEES DESDGNTSNS SSGDESGSEE EEEEEEEEEE
EENAGEPAIA HQDSVPTNDS TAPRSTHTRN ISLSSNGSNT NSTIILVKTT LETILNDKDI
KKNSNAQKAI ERTLQKFKEF DPQTTNNPHY VDSILVFEAL RASCRTKSSK VQSLALDCLS
KLFSFRSLDE TLLVNPPDSL ASNDQRQDAA DGITPPPKQK IIDAAIDTIS DCFQGEGTDD
RVELQIVRAL SSCILEEDSS SLCHGASLLK AIRTIYNVFV FSLNPSNQGI AQATLTQIIS
SVYDKIDLKQ STSSAVSLST KNHQQQSAIE LSEASENAET PAPLTLENMD KLNDDEERLM
DAQQPDSIAI TNQDLAVKDA FLVFRVMAKI CAKPLETELD MRSHAVRSKL LSLHIIYSII
KDHIDVFLSH NIFLPGKERV CFIDSIRQYL RLVLSRNAAS PLAPVFEVTL EIMWLLIANL
RADFVKEIPV FLTEIYFPIS ELTTSTSQQK RYFLSVIQRI CNDPRTLVEF YLNYDCNPGM
PNVMEITVDY LTRLALTRVE ITQTQRSYYD EQISKSLSTY NFSQLPLLTS SNLSSSPDVG
QVNLLFPLDF ALKMVSLNCI VSVLRSLSSW AHKALNPNTH TANKVLLNTT SSARQESRSS
LSNDVRSSIM TSNDDFKPTY EDEESRSLSS QNIDADDPTQ FENLKLRKTA LSECIAIFNN
KPKKAIPVLI KKGFLKDDSP ISIAKWLLET EGLDMAAVGD YLGEGDDKNI AIMHAFVDEF
DFTGMSIVDA LRSFLQSFRL PGEGQKIDRF MLKFAERFVD QNPGVFSKAD TAYVLSYSLI
MLNTDLHSSQ IKNKMSLQEF LENNEGIDNG RDLPRDFLEG LFNEIANNEI KLISEQHQAM
LSGDTNLVQQ QQSAFNFFNS RDLTREAYNQ VSKEISSKTE LVFKNLNKNK GGPDVYYAAS
HVEHVKSIFE TLWMSFLAAL TPPFKDYDDI DTTNKCLEGL KISIKIASTF RINDARTSFV
GALVQFCNLQ NLEEIKVKNV NAMVILLEVA LSEGNYLEGS WKDILLVVSQ MERLQLISKG
IDRDTVPDVA QARVANPRVS YESSRSNNTS FFDVWGKKAT PTELAQEKHH NQTLSPEISK
FISSSELVVL MDNIFTKSSE LSGNAIVDFI KALTAVSLEE IESSENASTP RMFSLQKMVD
VCYYNMDRIK LEWTPLWAVM GKAFNKIATN SNLAVVFFAI DSLRQLSMRF LDIEELSGFE
FQHDFLKPFE YTVQNSGNTE VQEMIIECFR NFILTKSESI KSGWKPILES LQYTARSSTE
SIVLKTQLLV SNDIVTNHFE NVFSQEDAFS ELVGVFREIT KNKRFQKLSL HALESLRKMT
QNVADICFYN ENKTEEERKH NDALLRGKDI FQDVWFPMLF CFNDTIMTAE DLEVRSRALN
YMFDALVAYG GKFNDDFWEK ICKKLLFPIF GVLSKHWEVN QFNSHDDLSV WLSTTLIQAL
RNLIALFTHY FESLNRMLDG FLGLLVSCIC QENDTIARIG RSCLQQLILQ NVSKFNEYHW
NQIGDVFDKL FDLTTANELF DYDPLQQGRK SSVSHHQTTN DTSQHSDDDS NDRRENDSNI
SETVERAHQE ESSEDVGGDM VETLNGQTKL NNGNSVPTVK DELNPKPASL SIPKKTKHMK
RNESNEDIRR RINIKNSIVV KCVLQLLMIE LLNELFENED FAHCIPYKEA IRITRLLEKS
YEFSRDFNED YGLRTRLVEA RVVDKIPNLL KQETSAAAVL LDIMFQLYLN DDEKKADLIT
RLITICIQVV EGYVSLDDRT MERSINAWRS VIVEILQGYY EFDDEDFRLY CPAMYALVIQ
ILDKSVPTEL RHAIKQFLSR VGELYLSTD
