SEC5/YDR166C Protein Information Help

Standard Name Sec5p 1, 2
Systematic Name Ydr166cp
ORF Classification Verified
Description Essential 107kDa subunit of the exocyst complex; the exocyst mediates polarized targeting and tethering of post-Golgi secretory vesicles to active sites of exocytosis at the plasma membrane prior to SNARE-mediated fusion; involved in assembly of the exocyst complex; required with Sec3p for ER inheritance where it promotes anchoring of the cortical ER at the bud tip (3, 4, 5)
Name Description SECretory 6
Experimental Data
Molecules/cell 3400 7
Predicted Sequence Formatted Sequence or sequence in FASTA format
Length (a.a.) 971
Molecular Weight (Da) 112,120
Isoelectric Point (pI) 5.66

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Post-translational Modifications PhosphoGRID | PhosphoPep Database
Domains/motifs See the graphical view and list of proteins that share domains/motifs in common with Sec5p (InterPro)
Physical Interactions There are 80 total physical interactions (BioGRID)
Homologs PDB Homologs | BLASTP | BLASTP v. fungi | Fungal Alignment | Synteny Viewer
External Sequence Databases EBI: UPI0000053255 | P89102
MIPS: YDR166C
NCBI: 1781309 | 2498890 | 398365919 | 642275 | 899413 | NP_010450.3
GenBank/EMBL/DDBJ: DAA12006.1 | Y08788 | Z47813 | Z50046
Amino Acid Sequence (or in FASTA format)
       1  MDRFQIGDEQ LLRFYQLKTI NPTHSWAQDS SKLNNEEATS NELGVETSFD
      51  ILKDFKYGNQ ISIDKESRAY LNDESLSYIR DPLNGQEMSK ELQHLPNDSM
     101  RLNYLVNSKQ FNVKAFLRDM HKQDSFNDLN NSLDRLDSDI QDQSIHLKQL
     151  VGKNFTKYVK IKNKLDQIYK EFDEKTNEKN QCDSPKENQI NVESLNKKVD
     201  EVIRTTTFKL KPLMDNYQKI LNYQATKKFI ELNKFYFNLP KSLKRCLTNN
     251  DFNEFIIEYS KGLTLRRRFN QSSDASQSLV IKRIWTQIEN LLVTYKDLIW
     301  NSLINSNFNI DQPQETILSL FSKLLNLENF INNNQRESES GNKNTTSSSN
     351  ENPILRWMSI KMNGFQNELN ELSGHMISKI IHSQRLILQN NTNQDKSQGC
     401  VELSYYLKIN QLFQIISDTG KDSEGLKSTV EPNKVNTISG TSYLNLNCQP
     451  SSQGLTDSPT IIEMWLLILK YINDLWKICD QFIEFWEHIE KFLDGTYQNS
     501  IINEKRKENI LIGDSNIIES YQKSLILKEE QINEVRLKGE EFITSVSQNL
     551  ISFFTSSQSS LPSSLKDSTG DITRSNKDSG SPLDYGFIPP NCNGLSCLRY
     601  LPKIVEPILK FSTELAQLNI TTNGITICRN TLSTIINRCV GAISSTKLRD
     651  ISNFYQLENW QVYETVTFSS KSQDSSKNLT FEYGVTQFPE IVTSFQEVSI
     701  KTTRDLLFAY EKLPIINGIS VVSYPSKQLL TGIEIQQIIS MEAVLEAILK
     751  NAAKDKDNPR NSHTILTLTN LQYFRECAFP NILQYFDDAF EWNLASKNLE
     801  LFSLLSKMES SIFGNYLSDL KINLRDTLEE KFHEINWPMY TSNSFRVGDY
     851  IIEALMILIV VHSECFRIGP QLIHKILIET QIFIARYLFE AFKPYVGNLS
     901  NDGSLQIIVD LEFFQKVMGP LLEKDTEATL RACLQNCFQN DTNRLQKCIN
     951  EINPIVSANL KRTAIQFAAF S*                              

external links for Sec5p
Homologs Interaction Resources Protein databases/Other Localization Resources
BLASTP (NCBI) BioGRID SCOP Superfamily YPL+
Ashbya (AGD) BOND GPMdb (Mass Spec.) YeastGFP
Aspergillus (AspGD) BioPIXIE MIPS YeastRC Public Image Repository
YGOB CYC2008 (complexes) Pfam domains
YOGY Complexome YeastRC Structure Prediction (Seattle)

DIP


GeneMANIA


YeastRC Mass Spec (Seattle)

References cited on this page View Complete Literature Guide for Sec5p
1) Novick P, et al.  (1980) Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway. Cell 21(1):205-15
2) Fields, C. and Schekman, R.  (1985) Personal Communication, Mortimer Map Edition 9
3) TerBush DR, et al.  (1996) The Exocyst is a multiprotein complex required for exocytosis in Saccharomyces cerevisiae. EMBO J 15(23):6483-94
4) TerBush DR and Novick P  (1995) Sec6, Sec8, and Sec15 are components of a multisubunit complex which localizes to small bud tips in Saccharomyces cerevisiae. J Cell Biol 130(2):299-312
5) Wiederkehr A, et al.  (2004) Functional specialization within a vesicle tethering complex: bypass of a subset of exocyst deletion mutants by Sec1p or Sec4p. J Cell Biol 167(5):875-87
6) Novick P and Schekman R  (1979) Secretion and cell-surface growth are blocked in a temperature-sensitive mutant of Saccharomyces cerevisiae. Proc Natl Acad Sci U S A 76(4):1858-62
7) Ghaemmaghami S, et al.  (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41