[1]	NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. TISSUE=Ovary; DOI=10.1038/339355a0; PubMed=2657434 [NCBI, ExPASy, EBI, Israel, Japan] Wilson D.W., Wilcox C.A., Flynn G.C., Chen E., Kuang W.-J., Henzel W.J., Block M.R., Ullrich A., Rothman J.E.; "A fusion protein required for vesicle-mediated transport in both mammalian cells and yeast."; Nature 339:355-359(1989).
[2]	FUNCTION. DOI=10.1038/339397a0; PubMed=2542798 [NCBI, ExPASy, EBI, Israel, Japan] Beckers C.J.M., Block M.R., Glick B.S., Rothman J.E., Balch W.E.; "Vesicular transport between the endoplasmic reticulum and the Golgi stack requires the NEM-sensitive fusion protein."; Nature 339:397-398(1989).
[3]	X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 497-742. DOI=10.1016/S0092-8674(00)81593-7; PubMed=9727495 [NCBI, ExPASy, EBI, Israel, Japan] Lenzen C.U., Steinmann D., Whiteheart S.W., Weis W.I.; "Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein."; Cell 94:525-536(1998).
[4]	ERRATUM. Lenzen C.U., Steinmann D., Whiteheart S.W., Weis W.I.; Cell 95:289-289(1998).
[5]	X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 489-735. DOI=10.1038/1843; PubMed=9731775 [NCBI, ExPASy, EBI, Israel, Japan] Yu R.C., Hanson P.I., Jahn R., Bruenger A.T.; "Structure of the ATP-dependent oligomerization domain of N-ethylmaleimide sensitive factor complexed with ATP."; Nat. Struct. Biol. 5:803-811(1998).
[6]	X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-205. DOI=10.1016/S1097-2765(00)80191-4; PubMed=10445031 [NCBI, ExPASy, EBI, Israel, Japan] Yu R.C., Jahn R., Brunger A.T.; "NSF N-terminal domain crystal structure: models of NSF function."; Mol. Cell 4:97-107(1999).
[7]	X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-203. DOI=10.1038/11097; PubMed=10559905 [NCBI, ExPASy, EBI, Israel, Japan] May A.P., Misura K.M., Whiteheart S.W., Weis W.I.; "Crystal structure of the amino-terminal domain of N-ethylmaleimide-sensitive fusion protein."; Nat. Cell Biol. 1:175-182(1999).

Comments

FUNCTION: Required for vesicle-mediated transport. Catalyzes the fusion of transport vesicles within the Golgi cisternae. Is also required for transport from the endoplasmic reticulum to the Golgi stack. Seem to function as a fusion protein required for the delivery of cargo proteins to all compartments of the Golgi stack independent of vesicle origin.
CATALYTIC ACTIVITY: ATP + H₂O = ADP + phosphate.
COFACTOR: Binds 1 magnesium ion per subunit.
SUBUNIT: Interacts with GABARAP and GABARAPL2 (By similarity). Homohexamer.
INTERACTION:
Q9H0R8:GABARAPL1 (xeno); NbExp=1; IntAct=EBI-925742, EBI-746969;
P19491:Gria2 (xeno); NbExp=1; IntAct=EBI-925742, EBI-77718;
P19492:Gria3 (xeno); NbExp=1; IntAct=EBI-925742, EBI-77764;
SUBCELLULAR LOCATION: Cytoplasm.
SIMILARITY: Belongs to the AAA ATPase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X15652; CAA33678.1; ALT_INIT; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S04235; S04235.

3D structure databases

PDB

1D2N; X-ray; 1.75 A; A=487-743.	[ExPASy / RCSB / EBI]
1NSF; X-ray; 1.90 A; A=478-744.	[ExPASy / RCSB / EBI]
1QCS; X-ray; 1.90 A; A=1-205.	[ExPASy / RCSB / EBI]
1QDN; X-ray; 2.30 A; A/B/C=1-203.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1D2N; -.
1NSF; -.
1QCS; -.
1QDN; -.

ModBase

P18708.

Protein-protein interaction databases

IntAct

P18708; -.

Ontologies

GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.

Family and domain databases

InterPro

IPR003593; AAA+_ATPase_core.
IPR003959; AAA_ATPase_core.
IPR003960; AAA_ATPase_CS.
IPR003338; ATPaseVAT_N.
IPR004201; Cdc48_2.
IPR001984; Peptidase_S16.
Graphical view of domain structure.

Pfam

PF00004; AAA; 2.
PF02933; CDC48_2; 1.
PF02359; CDC48_N; 1.
Pfam graphical view of domain structure.

PRINTS

PR00830; ENDOLAPTASE.

SMART

SM00382; AAA; 2.
SMART graphical view of domain structure.

PROSITE

PS00674; AAA; 1.

BLOCKS

P18708.

Phylogenomic databases

HOVERGEN

P18708; -.

Other

ProtoNet

P18708.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; ATP-binding; Cytoplasm; Direct protein sequencing; Hydrolase; Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein; Protein transport; Repeat; Transport.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 744`	`744`	`Vesicle-fusing ATPase.`	`PRO_0000084562`
`NP_BIND`	`260 267`	`8`	`ATP (Potential).`
`NP_BIND`	`543 550`	`8`	`ATP (Potential).`
`METAL`	`550 550`		`Magnesium.`
`MOD_RES`	`259 259`		`Phosphotyrosine (By similarity).`
`STRAND`	`4 10`	`7`
`HELIX`	`14 18`	`5`
`STRAND`	`22 24`	`3`
`TURN`	`26 28`	`3`
`STRAND`	`34 40`	`7`
`STRAND`	`43 51`	`9`
`STRAND`	`59 62`	`4`
`HELIX`	`64 70`	`7`
`STRAND`	`77 83`	`7`
`HELIX`	`87 90`	`4`
`STRAND`	`91 102`	`12`
`HELIX`	`104 106`	`3`
`STRAND`	`111 113`	`3`
`HELIX`	`114 125`	`12`
`STRAND`	`129 131`	`3`
`STRAND`	`135 140`	`6`
`STRAND`	`143 154`	`12`
`STRAND`	`173 176`	`4`
`STRAND`	`182 187`	`6`
`STRAND`	`194 200`	`7`
`TURN`	`500 502`	`3`
`HELIX`	`512 530`	`19`
`STRAND`	`535 542`	`8`
`HELIX`	`549 560`	`12`
`STRAND`	`563 568`	`6`
`HELIX`	`570 572`	`3`
`HELIX`	`578 593`	`16`
`STRAND`	`595 602`	`8`
`HELIX`	`605 608`	`4`
`TURN`	`613 616`	`4`
`HELIX`	`620 629`	`10`
`STRAND`	`639 647`	`9`
`HELIX`	`649 654`	`6`
`TURN`	`658 660`	`3`
`STRAND`	`661 666`	`6`
`STRAND`	`670 672`	`3`
`HELIX`	`673 683`	`11`
`HELIX`	`688 698`	`11`
`STRAND`	`701 705`	`5`
`HELIX`	`707 717`	`11`
`HELIX`	`722 724`	`3`
`HELIX`	`725 735`	`11`

Sequence information

Length: 744 AA [This is the length of the unprocessed precursor]

Molecular weight: 82536 Da [This is the MW of the unprocessed precursor]

CRC64: F3E0CEB2CF1BD582 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAGRSMQAAR CPTDELSLSN CAVVSEKDYQ SGQHVIVRTS PNHKYIFTLR THPSVVPGSV 

        70         80         90        100        110        120 
AFSLPQRKWA GLSIGQEIEV ALYSFDKAKQ CIGTMTIEID FLQKKNIDSN PYDTDKMAAE 

       130        140        150        160        170        180 
FIQQFNNQAF SVGQQLVFSF NDKLFGLLVK DIEAMDPSIL KGEPASGKRQ KIEVGLVVGN 

       190        200        210        220        230        240 
SQVAFEKAEN SSLNLIGKAK TKENRQSIIN PDWNFEKMGI GGLDKEFSDI FRRAFASRVF 

       250        260        270        280        290        300 
PPEIVEQMGC KHVKGILLYG PPGCGKTLLA RQIGKMLNAR EPKVVNGPEI LNKYVGESEA 

       310        320        330        340        350        360 
NIRKLFADAE EEQRRLGANS GLHIIIFDEI DAICKQRGSM AGSTGVHDTV VNQLLSKIDG 

       370        380        390        400        410        420 
VEQLNNILVI GMTNRPDLID EALLRPGRLE VKMEIGLPDE KGRLQILHIH TARMRGHQLL 

       430        440        450        460        470        480 
SADVDIKELA VETKNFSGAE LEGLVRAAQS TAMNRHIKAS TKVEVDMEKA ESLQVTRGDF 

       490        500        510        520        530        540 
LASLENDIKP AFGTNQEDYA SYIMNGIIKW GDPVTRVLDD GELLVQQTKN SDRTPLVSVL 

       550        560        570        580        590        600 
LEGPPHSGKT ALAAKIAEES NFPFIKICSP DKMIGFSETA KCQAMKKIFD DAYKSQLSCV 

       610        620        630        640        650        660 
VVDDIERLLD YVPIGPRFSN LVLQALLVLL KKAPPQGRKL LIIGTTSRKD VLQEMEMLNA 

       670        680        690        700        710        720 
FSTTIHVPNI ATGEQLLEAL ELLGNFKDKE RTTIAQQVKG KKVWIGIKKL LMLIEMSLQM 

       730        740 
DPEYRVRKFL ALLREEGASP LDFD

P18708 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools