| General information | | DisProt: | DP00128 | | Name: | Protein transport protein SEC9 | | Synonym(s): | SEC9_YEAST
Sec9p
| | First appeared in release: | Release 1.0 (08/01/2003) | | UniProt: | P40357 | | UniGene: | | | SwissProt: | SEC9_YEAST | | TrEMBL: | | | NCBI (GI): | 730733 | | Source organism: | Saccharomyces cerevisiae (Baker's yeast) | | Sequence length: | 651 | | Percent disordered: | 100% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MGLKKFFKIK PPEEATPEQN KDTLMELGIS VKNPSKKRKE KFAAYGKFAN DKAEDKVYAP - 60
PGYEQYARPQ DELEDLNASP LDANANEATA GSNRGSSGTQ DLGNGAESNS MQDPYAIEND - 120
DYRYDDDPYA RFQANKSNGR GSVNAAPYGD YGGGYNGTSL NSYNNDGPYS NQNTSNSWVN - 180
ANGRNSLNHS NSTLNVGPSR QTRQPPVSTS TNSLSLDQRS PLANPMQEKR NPYADMNSYG - 240
GAYDSNTNRS SGTRQGSSKN ANPYASMAND SYSNGNLNRS ANPYSSRSVR QPQSQQAPMT - 300
YTPSFIASDE AARNSEVDLN EEPRTGEFDF EEVYADKSAE NRAALDEPDL NAVMTNEDSI - 360
DLNASEVDHS SRQQQQQQWF MDEQQQQQQH FNATNNQYGD QRGYKTFEEI QKEEEARQQQ - 420
EEDEAVDEIK QEIKFTKQSS VASTRNTLKM AQDAERAGMN TLGMLGHQSE QLNNVEGNLD - 480
LMKVQNKVAD EKVAELKKLN RSILAVHVSN PFNSKRRRRE REEQLKNRKI EEKLMREQTS - 540
QQLSQSTQRI EGAMNANNNI SEVRERYQRK NVLEKAKRYQ FENDEEDDEM ELEIDRNLDQ - 600
IQQVSNRLKK MALTTGKELD SQQKRLNNIE ESTDDLDINL HMNTNRLAGI R
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| Functional narrative |
Protein transport protein Sec9 is an intrinsically disordered protein which is bound to the membrane of a cell. This member of the SNAP-25 family interacts with Sso1, Snc1, and Sec18 to form a SNARE complex which is essential to exocytosis and membrane fusion. These interactions lead to the formation of structure.
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered - Extended | | Name: | | | Location: | 1 - 651 | | Length: | 651 | | Region sequence: |
MGLKKFFKIKPPEEATPEQNKDTLMELGISVKNPSKKRKEKFAAYGKFANDKAEDKVYAP
PGYEQYARPQDELEDLNASPLDANANEATAGSNRGSSGTQDLGNGAESNSMQDPYAIEND
DYRYDDDPYARFQANKSNGRGSVNAAPYGDYGGGYNGTSLNSYNNDGPYSNQNTSNSWVN
ANGRNSLNHSNSTLNVGPSRQTRQPPVSTSTNSLSLDQRSPLANPMQEKRNPYADMNSYG
GAYDSNTNRSSGTRQGSSKNANPYASMANDSYSNGNLNRSANPYSSRSVRQPQSQQAPMT
YTPSFIASDEAARNSEVDLNEEPRTGEFDFEEVYADKSAENRAALDEPDLNAVMTNEDSI
DLNASEVDHSSRQQQQQQWFMDEQQQQQQHFNATNNQYGDQRGYKTFEEIQKEEEARQQQ
EEDEAVDEIKQEIKFTKQSSVASTRNTLKMAQDAERAGMNTLGMLGHQSEQLNNVEGNLD
LMKVQNKVADEKVAELKKLNRSILAVHVSNPFNSKRRRREREEQLKNRKIEEKLMREQTS
QQLSQSTQRIEGAMNANNNISEVRERYQRKNVLEKAKRYQFENDEEDDEMELEIDRNLDQ
IQQVSNRLKKMALTTGKELDSQQKRLNNIEESTDDLDINLHMNTNRLAGIR | | Modification type: | Native
| | PDB: | | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Protein-protein binding
| Detection methods:
| References:
- Fiebig KM, Rice LM, Pollock E, Brunger AT. "Folding intermediates of SNARE complex assembly." Nat Struct Biol. 1999; 6(2): 117-23. PubMed: 10048921
| Comments:Sec9 is completely disordered in isolation, but acquires some structure when forming a complex with Sso1.
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| Region 2 | | Type: | Disordered | | Name: | | | Location: | 401 - 651 | | Length: | 251 | | Region sequence: |
QRGYKTFEEIQKEEEARQQQEEDEAVDEIKQEIKFTKQSSVASTRNTLKMAQDAERAGMN
TLGMLGHQSEQLNNVEGNLDLMKVQNKVADEKVAELKKLNRSILAVHVSNPFNSKRRRRE
REEQLKNRKIEEKLMREQTSQQLSQSTQRIEGAMNANNNISEVRERYQRKNVLEKAKRYQ
FENDEEDDEMELEIDRNLDQIQQVSNRLKKMALTTGKELDSQQKRLNNIEESTDDLDINL
HMNTNRLAGIR | | Modification type: | Complex
Engineered
Fragment
| | PDB: | | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Protein-protein binding
| Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV (298 K; pH: 8.4; phosphate (buffer) 10 mM; sodium chloride 300 mM)
- Fluorescent probes (298 K; pH: 8.4; Sncl 2.5 uM; sodium chloride 300 mM; sodium phosphate 10 mM)
- SDS-PAGE gel, Aberrant mobility on
| References:
- Rice LM, Brennwald P, Brunger AT. "Formation of a yeast SNARE complex is accompanied by significant structural changes." FEBS Lett. 1997; 415(1): 49-55. PubMed: 9326367
| Comments:
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