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Protein

Protein transport protein SEC7

Gene

SEC7

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May play a role in vesicular budding and traffic between compartments of the Golgi apparatus.

GO - Molecular functioni

  • ARF guanyl-nucleotide exchange factor activity Source: SGD

GO - Biological processi

  • autophagosome assembly Source: SGD
  • ER to Golgi vesicle-mediated transport Source: SGD
  • intra-Golgi vesicle-mediated transport Source: SGD
  • protein transport Source: UniProtKB-KW
  • regulation of ARF protein signal transduction Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-29759-MONOMER.
ReactomeiR-SCE-6811438. Intra-Golgi traffic.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein transport protein SEC7
Gene namesi
Name:SEC7
Ordered Locus Names:YDR170C
ORF Names:YD9395.01C, YD9489.05C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR170C.
SGDiS000002577. SEC7.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: SGD
  • Golgi-associated vesicle Source: SGD
  • late endosome Source: SGD
  • trans-Golgi network Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Golgi apparatus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 20092009Protein transport protein SEC7PRO_0000120214Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei212 – 2121PhosphoserineCombined sources
Modified residuei215 – 2151PhosphoserineCombined sources
Modified residuei334 – 3341PhosphothreonineCombined sources
Modified residuei447 – 4471PhosphoserineCombined sources
Modified residuei452 – 4521PhosphoserineCombined sources
Modified residuei455 – 4551PhosphoserineCombined sources
Cross-linki797 – 797Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei807 – 8071PhosphoserineCombined sources
Modified residuei1226 – 12261PhosphoserineCombined sources
Modified residuei1240 – 12401PhosphothreonineCombined sources
Modified residuei1741 – 17411PhosphoserineCombined sources
Modified residuei1752 – 17521PhosphoserineCombined sources

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP11075.
PRIDEiP11075.

PTM databases

iPTMnetiP11075.

Interactioni

Protein-protein interaction databases

BioGridi32221. 104 interactions.
DIPiDIP-830N.
IntActiP11075. 55 interactions.
MINTiMINT-616341.

Structurei

Secondary structure

1
2009
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi830 – 84011Combined sources
Helixi842 – 85110Combined sources
Beta strandi854 – 8563Combined sources
Helixi860 – 86910Combined sources
Helixi875 – 8839Combined sources
Helixi887 – 89812Combined sources
Helixi907 – 9159Combined sources
Helixi924 – 94118Combined sources
Helixi949 – 96719Combined sources
Beta strandi970 – 9723Combined sources
Helixi977 – 9837Combined sources
Turni984 – 9874Combined sources
Helixi995 – 100713Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4OIYX-ray1.50A/B824-1010[»]
ProteinModelPortaliP11075.
SMRiP11075. Positions 823-1010.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini824 – 1010187SEC7PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi89 – 213125Asp/Glu-rich (highly acidic)Add
BLAST

Domaini

The highly charged acidic domain may serve a structural role to interact with lipids or proteins on the cytoplasmic surface of the Golgi apparatus.

Sequence similaritiesi

Contains 1 SEC7 domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00760000119036.
HOGENOMiHOG000181045.
InParanoidiP11075.
KOiK18442.
OMAiHEDTHES.
OrthoDBiEOG725DRW.

Family and domain databases

Gene3Di1.10.1000.11. 1 hit.
InterProiIPR016024. ARM-type_fold.
IPR032629. DCB_dom.
IPR023394. Sec7_alpha_orthog.
IPR015403. Sec7_C.
IPR000904. Sec7_dom.
IPR032691. Sec7_N.
[Graphical view]
PfamiPF16213. DCB. 1 hit.
PF09324. DUF1981. 1 hit.
PF01369. Sec7. 1 hit.
PF12783. Sec7_N. 1 hit.
[Graphical view]
SMARTiSM00222. Sec7. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 2 hits.
SSF48425. SSF48425. 1 hit.
PROSITEiPS50190. SEC7. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P11075-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEQNSVVNA EKGDGEISSN VETASSVNPS VKPQNAIKEE AKETNGEDQK
60 70 80 90 100
CKGPENAGST AETKETSNDA TNGMKTPEET EDTNDKRHDD EGEDGDEDED
110 120 130 140 150
EDEDEDEDNG DEDDEDVDSS SSETSSEDGE DSESVSGEST ESSSGEDEES
160 170 180 190 200
DESDGNTSNS SSGDESGSEE EEEEEEEEEE EENAGEPAIA HQDSVPTNDS
210 220 230 240 250
TAPRSTHTRN ISLSSNGSNT NSTIILVKTT LETILNDKDI KKNSNAQKAI
260 270 280 290 300
ERTLQKFKEF DPQTTNNPHY VDSILVFEAL RASCRTKSSK VQSLALDCLS
310 320 330 340 350
KLFSFRSLDE TLLVNPPDSL ASNDQRQDAA DGITPPPKQK IIDAAIDTIS
360 370 380 390 400
DCFQGEGTDD RVELQIVRAL SSCILEEDSS SLCHGASLLK AIRTIYNVFV
410 420 430 440 450
FSLNPSNQGI AQATLTQIIS SVYDKIDLKQ STSSAVSLST KNHQQQSAIE
460 470 480 490 500
LSEASENAET PAPLTLENMD KLNDDEERLM DAQQPDSIAI TNQDLAVKDA
510 520 530 540 550
FLVFRVMAKI CAKPLETELD MRSHAVRSKL LSLHIIYSII KDHIDVFLSH
560 570 580 590 600
NIFLPGKERV CFIDSIRQYL RLVLSRNAAS PLAPVFEVTL EIMWLLIANL
610 620 630 640 650
RADFVKEIPV FLTEIYFPIS ELTTSTSQQK RYFLSVIQRI CNDPRTLVEF
660 670 680 690 700
YLNYDCNPGM PNVMEITVDY LTRLALTRVE ITQTQRSYYD EQISKSLSTY
710 720 730 740 750
NFSQLPLLTS SNLSSSPDVG QVNLLFPLDF ALKMVSLNCI VSVLRSLSSW
760 770 780 790 800
AHKALNPNTH TANKVLLNTT SSARQESRSS LSNDVRSSIM TSNDDFKPTY
810 820 830 840 850
EDEESRSLSS QNIDADDPTQ FENLKLRKTA LSECIAIFNN KPKKAIPVLI
860 870 880 890 900
KKGFLKDDSP ISIAKWLLET EGLDMAAVGD YLGEGDDKNI AIMHAFVDEF
910 920 930 940 950
DFTGMSIVDA LRSFLQSFRL PGEGQKIDRF MLKFAERFVD QNPGVFSKAD
960 970 980 990 1000
TAYVLSYSLI MLNTDLHSSQ IKNKMSLQEF LENNEGIDNG RDLPRDFLEG
1010 1020 1030 1040 1050
LFNEIANNEI KLISEQHQAM LSGDTNLVQQ QQSAFNFFNS RDLTREAYNQ
1060 1070 1080 1090 1100
VSKEISSKTE LVFKNLNKNK GGPDVYYAAS HVEHVKSIFE TLWMSFLAAL
1110 1120 1130 1140 1150
TPPFKDYDDI DTTNKCLEGL KISIKIASTF RINDARTSFV GALVQFCNLQ
1160 1170 1180 1190 1200
NLEEIKVKNV NAMVILLEVA LSEGNYLEGS WKDILLVVSQ MERLQLISKG
1210 1220 1230 1240 1250
IDRDTVPDVA QARVANPRVS YESSRSNNTS FFDVWGKKAT PTELAQEKHH
1260 1270 1280 1290 1300
NQTLSPEISK FISSSELVVL MDNIFTKSSE LSGNAIVDFI KALTAVSLEE
1310 1320 1330 1340 1350
IESSENASTP RMFSLQKMVD VCYYNMDRIK LEWTPLWAVM GKAFNKIATN
1360 1370 1380 1390 1400
SNLAVVFFAI DSLRQLSMRF LDIEELSGFE FQHDFLKPFE YTVQNSGNTE
1410 1420 1430 1440 1450
VQEMIIECFR NFILTKSESI KSGWKPILES LQYTARSSTE SIVLKTQLLV
1460 1470 1480 1490 1500
SNDIVTNHFE NVFSQEDAFS ELVGVFREIT KNKRFQKLSL HALESLRKMT
1510 1520 1530 1540 1550
QNVADICFYN ENKTEEERKH NDALLRGKDI FQDVWFPMLF CFNDTIMTAE
1560 1570 1580 1590 1600
DLEVRSRALN YMFDALVAYG GKFNDDFWEK ICKKLLFPIF GVLSKHWEVN
1610 1620 1630 1640 1650
QFNSHDDLSV WLSTTLIQAL RNLIALFTHY FESLNRMLDG FLGLLVSCIC
1660 1670 1680 1690 1700
QENDTIARIG RSCLQQLILQ NVSKFNEYHW NQIGDVFDKL FDLTTANELF
1710 1720 1730 1740 1750
DYDPLQQGRK SSVSHHQTTN DTSQHSDDDS NDRRENDSNI SETVERAHQE
1760 1770 1780 1790 1800
ESSEDVGGDM VETLNGQTKL NNGNSVPTVK DELNPKPASL SIPKKTKHMK
1810 1820 1830 1840 1850
RNESNEDIRR RINIKNSIVV KCVLQLLMIE LLNELFENED FAHCIPYKEA
1860 1870 1880 1890 1900
IRITRLLEKS YEFSRDFNED YGLRTRLVEA RVVDKIPNLL KQETSAAAVL
1910 1920 1930 1940 1950
LDIMFQLYLN DDEKKADLIT RLITICIQVV EGYVSLDDRT MERSINAWRS
1960 1970 1980 1990 2000
VIVEILQGYY EFDDEDFRLY CPAMYALVIQ ILDKSVPTEL RHAIKQFLSR

VGELYLSTD
Length:2,009
Mass (Da):226,886
Last modified:November 1, 1997 - v2
Checksum:i02B2D370DD2E4661
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti188 – 1881A → S in AAB04031 (PubMed:3042778).Curated
Sequence conflicti399 – 4002FV → LL (PubMed:3042778).Curated
Sequence conflicti402 – 4021S → C (PubMed:3042778).Curated
Sequence conflicti1031 – 10344QQSA → PAIC (PubMed:3042778).Curated
Sequence conflicti1036 – 10372NF → QL (PubMed:3042778).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03918 Genomic DNA. Translation: AAB04031.1.
Z46727 Genomic DNA. Translation: CAA86696.1.
Z47813 Genomic DNA. Translation: CAA87801.1.
BK006938 Genomic DNA. Translation: DAA12011.1.
PIRiS49764.
RefSeqiNP_010454.3. NM_001180477.3.

Genome annotation databases

EnsemblFungiiYDR170C; YDR170C; YDR170C.
GeneIDi851748.
KEGGisce:YDR170C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03918 Genomic DNA. Translation: AAB04031.1.
Z46727 Genomic DNA. Translation: CAA86696.1.
Z47813 Genomic DNA. Translation: CAA87801.1.
BK006938 Genomic DNA. Translation: DAA12011.1.
PIRiS49764.
RefSeqiNP_010454.3. NM_001180477.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4OIYX-ray1.50A/B824-1010[»]
ProteinModelPortaliP11075.
SMRiP11075. Positions 823-1010.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32221. 104 interactions.
DIPiDIP-830N.
IntActiP11075. 55 interactions.
MINTiMINT-616341.

PTM databases

iPTMnetiP11075.

Proteomic databases

MaxQBiP11075.
PRIDEiP11075.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR170C; YDR170C; YDR170C.
GeneIDi851748.
KEGGisce:YDR170C.

Organism-specific databases

EuPathDBiFungiDB:YDR170C.
SGDiS000002577. SEC7.

Phylogenomic databases

GeneTreeiENSGT00760000119036.
HOGENOMiHOG000181045.
InParanoidiP11075.
KOiK18442.
OMAiHEDTHES.
OrthoDBiEOG725DRW.

Enzyme and pathway databases

BioCyciYEAST:G3O-29759-MONOMER.
ReactomeiR-SCE-6811438. Intra-Golgi traffic.

Miscellaneous databases

PROiP11075.

Family and domain databases

Gene3Di1.10.1000.11. 1 hit.
InterProiIPR016024. ARM-type_fold.
IPR032629. DCB_dom.
IPR023394. Sec7_alpha_orthog.
IPR015403. Sec7_C.
IPR000904. Sec7_dom.
IPR032691. Sec7_N.
[Graphical view]
PfamiPF16213. DCB. 1 hit.
PF09324. DUF1981. 1 hit.
PF01369. Sec7. 1 hit.
PF12783. Sec7_N. 1 hit.
[Graphical view]
SMARTiSM00222. Sec7. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 2 hits.
SSF48425. SSF48425. 1 hit.
PROSITEiPS50190. SEC7. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "SEC7 encodes an unusual, high molecular weight protein required for membrane traffic from the yeast Golgi apparatus."
    Achstetter T., Franzusoff A., Field C., Schekman R.
    J. Biol. Chem. 263:11711-11717(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Localization of components involved in protein transport and processing through the yeast Golgi apparatus."
    Franzusoff A., Redding K., Crosby J., Fuller R.S., Schekman R.
    J. Cell Biol. 112:27-37(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
    Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
    Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: YAL6B.
  7. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212; SER-215; SER-807; SER-1226 AND THR-1240, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  8. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-334; SER-447 AND SER-1226, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212; SER-447; SER-452; SER-455; SER-1226; THR-1240; SER-1741 AND SER-1752, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-797, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSEC7_YEAST
AccessioniPrimary (citable) accession number: P11075
Secondary accession number(s): D6VSF1, Q03960, Q04139
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 1, 1997
Last modified: July 6, 2016
This is version 157 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 3670 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.