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NSFL1 cofactor p47 (XY body-associated protein XY40) (p97 cofactor p47)

 NSF1C_RAT               Reviewed;         370 AA.
O35987;
16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
22-NOV-2017, entry version 148.
RecName: Full=NSFL1 cofactor p47;
AltName: Full=XY body-associated protein XY40;
AltName: Full=p97 cofactor p47;
Name=Nsfl1c;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 200-209; 283-292 AND
323-328, AND TISSUE SPECIFICITY.
STRAIN=Wistar; TISSUE=Spermatocyte;
PubMed=9297509; DOI=10.1007/s004120050252;
Alsheimer M., Imamichi Y., Heid H., Benavente R.;
"Molecular characterization and expression pattern of XY body-
associated protein XY40 of the rat.";
Chromosoma 106:308-314(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 11-22; 94-101;
157-172; 189-214; 260-282; 323-346 AND 357-368, IDENTIFICATION BY MASS
SPECTROMETRY, FUNCTION, INTERACTION WITH VCP, SUBCELLULAR LOCATION,
AND TISSUE SPECIFICITY.
TISSUE=Liver;
PubMed=9214505; DOI=10.1038/40411;
Kondo H., Rabouille C., Newman R., Levine T.P., Pappin D.,
Freemont P., Warren G.;
"p47 is a cofactor for p97-mediated membrane fusion.";
Nature 388:75-78(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 200-214 AND 283-301, AND IDENTIFICATION BY MASS
SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
Lubec G., Chen W.-Q.;
Submitted (APR-2007) to UniProtKB.
[5]
TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=1495983; DOI=10.1073/pnas.89.15.6938;
Smith A., Benavente R.;
"Meiosis-specific protein selectively associated with sex chromosomes
of rat pachytene spermatocytes.";
Proc. Natl. Acad. Sci. U.S.A. 89:6938-6942(1992).
[6]
INTERACTION WITH STX5A.
PubMed=9506515; DOI=10.1016/S0092-8674(00)81128-9;
Rabouille C., Kondo H., Newman R., Hui N., Freemont P., Warren G.;
"Syntaxin 5 is a common component of the NSF- and p97-mediated
reassembly pathways of Golgi cisternae from mitotic Golgi fragments in
vitro.";
Cell 92:603-610(1998).
[7]
FUNCTION.
PubMed=9824302; DOI=10.1016/S0014-5793(98)01232-0;
Meyer H.H., Kondo H., Warren G.;
"The p47 co-factor regulates the ATPase activity of the membrane
fusion protein, p97.";
FEBS Lett. 437:255-257(1998).
[8]
INTERACTION WITH VCP.
PubMed=10811609; DOI=10.1093/emboj/19.10.2181;
Meyer H.H., Shorter J.G., Seemann J., Pappin D., Warren G.;
"A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to
ubiquitin and nuclear transport pathways.";
EMBO J. 19:2181-2192(2000).
[9]
FUNCTION.
PubMed=10930451; DOI=10.1091/mbc.11.8.2529;
Roy L., Bergeron J.J.M., Lavoie C., Hendriks R., Gushue J., Fazel A.,
Pelletier A., Morre D.J., Subramaniam V.N., Hong W., Paiement J.;
"Role of p97 and syntaxin 5 in the assembly of transitional
endoplasmic reticulum.";
Mol. Biol. Cell 11:2529-2542(2000).
[10]
INTERACTION WITH MEMBRANES.
PubMed=12146947; DOI=10.1021/bi0259195;
Pecheur E.-I., Martin I., Maier O., Bakowsky U., Ruysschaert J.-M.,
Hoekstra D.;
"Phospholipid species act as modulators in p97/p47-mediated fusion of
Golgi membranes.";
Biochemistry 41:9813-9823(2002).
[11]
FUNCTION, AND MUTAGENESIS OF PHE-41.
PubMed=12411482; DOI=10.1093/emboj/cdf579;
Meyer H.H., Wang Y., Warren G.;
"Direct binding of ubiquitin conjugates by the mammalian p97 adaptor
complexes, p47 and Ufd1-Npl4.";
EMBO J. 21:5645-5652(2002).
[12]
INTERACTION WITH VCIP135.
PubMed=12473691; DOI=10.1083/jcb.200208112;
Uchiyama K., Jokitalo E., Kano F., Murata M., Zhang X., Canas B.,
Newman R., Rabouille C., Pappin D., Freemont P., Kondo H.;
"VCIP135, a novel essential factor for p97/p47-mediated membrane
fusion, is required for Golgi and ER assembly in vivo.";
J. Cell Biol. 159:855-866(2002).
[13]
PHOSPHORYLATION AT SER-140, MUTAGENESIS OF THR-57; LYS-112; SER-114;
SER-140; ARG-173 AND SER-272, AND SUBCELLULAR LOCATION.
PubMed=12810701; DOI=10.1083/jcb.200303048;
Uchiyama K., Jokitalo E., Lindman M., Jackman M., Kano F., Murata M.,
Zhang X., Kondo H.;
"The localization and phosphorylation of p47 are important for Golgi
disassembly-assembly during the cell cycle.";
J. Cell Biol. 161:1067-1079(2003).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114 AND SER-176, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=16641100; DOI=10.1073/pnas.0600895103;
Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
"Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
regulation of aquaporin-2 phosphorylation at two sites.";
Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114 AND SER-176, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[16]
STRUCTURE BY NMR OF 282-370, AND INTERACTION WITH VCP.
PubMed=11478859; DOI=10.1006/jmbi.2001.4864;
Yuan X., Shaw A., Zhang X., Kondo H., Lally J., Freemont P.S.,
Matthews S.;
"Solution structure and interaction surface of the C-terminal domain
from p47: a major p97-cofactor involved in SNARE disassembly.";
J. Mol. Biol. 311:255-263(2001).
[17]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 244-370, INTERACTION WITH
VCP, AND MUTAGENESIS OF ARG-301; 342-THR--ASN-345; PHE-343 AND
ASN-345.
PubMed=14988733; DOI=10.1038/sj.emboj.7600139;
Dreveny I., Kondo H., Uchiyama K., Shaw A., Zhang X., Freemont P.S.;
"Structural basis of the interaction between the AAA ATPase p97/VCP
and its adaptor protein p47.";
EMBO J. 23:1030-1039(2004).
[18]
STRUCTURE BY NMR OF 1-46 IN COMPLEX WITH UBIQUITIN, STRUCTURE BY NMR
OF 171-246, AND INTERACTION WITH VCP.
PubMed=15029246; DOI=10.1038/sj.emboj.7600152;
Yuan X., Simpson P., McKeown C., Kondo H., Uchiyama K., Wallis R.,
Dreveny I., Keetch C., Zhang X., Robinson C., Freemont P.,
Matthews S.;
"Structure, dynamics and interactions of p47, a major adaptor of the
AAA ATPase, p97.";
EMBO J. 23:1463-1473(2004).
-!- FUNCTION: Reduces the ATPase activity of VCP. Necessary for the
fragmentation of Golgi stacks during mitosis and for VCP-mediated
reassembly of Golgi stacks after mitosis. May play a role in VCP-
mediated formation of transitional endoplasmic reticulum (tER).
{ECO:0000269|PubMed:10930451, ECO:0000269|PubMed:12411482,
ECO:0000269|PubMed:9214505, ECO:0000269|PubMed:9824302}.
-!- SUBUNIT: Part of a ternary complex containing STX5A, NSFL1C and
VCP. NSFL1C forms a homotrimer that binds to one end of a VCP
homohexamer. The complex binds to membranes enriched in
phosphatidylethanolamine-containing lipids and promotes Golgi
membrane fusion. Interaction with VCIP135 leads to dissociation of
the complex via ATP hydrolysis by VCP. Binds ubiquitin and mono-
ubiquitinated proteins via its N-terminal UBA-like domain when
bound to VCP. {ECO:0000269|PubMed:10811609,
ECO:0000269|PubMed:11478859, ECO:0000269|PubMed:12146947,
ECO:0000269|PubMed:12473691, ECO:0000269|PubMed:14988733,
ECO:0000269|PubMed:15029246, ECO:0000269|PubMed:9214505,
ECO:0000269|PubMed:9506515}.
-!- INTERACTION:
P46462:Vcp; NbExp=12; IntAct=EBI-1993760, EBI-399011;
Q01853:Vcp (xeno); NbExp=8; IntAct=EBI-1993760, EBI-80597;
-!- SUBCELLULAR LOCATION: Nucleus. Golgi apparatus, Golgi stack.
Chromosome. Note=Predominantly nuclear in interphase cells. Bound
to the axial elements of sex chromosomes in pachytene
spermatocytes. A small proportion of the protein is cytoplasmic,
associated with Golgi stacks.
-!- TISSUE SPECIFICITY: Highly expressed in heart, brain, spleen,
lung, liver, muscle, kidney and testis.
{ECO:0000269|PubMed:1495983, ECO:0000269|PubMed:9214505,
ECO:0000269|PubMed:9297509}.
-!- DEVELOPMENTAL STAGE: Highly expressed in pachytene spermatocytes
during spermatogenesis.
-!- PTM: Phosphorylated during mitosis. Phosphorylation inhibits
interaction with Golgi membranes and is required for the
fragmentation of the Golgi stacks during mitosis.
{ECO:0000269|PubMed:12810701}.
-!- SIMILARITY: Belongs to the NSFL1C family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; Y10769; CAA71742.1; -; mRNA.
EMBL; AB002086; BAA21659.1; -; mRNA.
EMBL; BC072464; AAH72464.1; -; mRNA.
RefSeq; NP_114187.1; NM_031981.2.
UniGene; Rn.2771; -.
PDB; 1I42; NMR; -; A=282-370.
PDB; 1JRU; NMR; -; A=282-370.
PDB; 1S3S; X-ray; 2.90 A; G/H/I=244-370.
PDB; 1V92; NMR; -; A=1-46.
PDB; 1VAZ; NMR; -; A=171-246.
PDBsum; 1I42; -.
PDBsum; 1JRU; -.
PDBsum; 1S3S; -.
PDBsum; 1V92; -.
PDBsum; 1VAZ; -.
ProteinModelPortal; O35987; -.
SMR; O35987; -.
BioGrid; 249844; 4.
CORUM; O35987; -.
IntAct; O35987; 18.
MINT; MINT-1954288; -.
STRING; 10116.ENSRNOP00000011654; -.
iPTMnet; O35987; -.
PhosphoSitePlus; O35987; -.
PaxDb; O35987; -.
PRIDE; O35987; -.
Ensembl; ENSRNOT00000011654; ENSRNOP00000011654; ENSRNOG00000008604.
GeneID; 83809; -.
KEGG; rno:83809; -.
UCSC; RGD:619952; rat.
CTD; 55968; -.
RGD; 619952; Nsfl1c.
eggNOG; KOG2086; Eukaryota.
eggNOG; ENOG410YGXU; LUCA.
GeneTree; ENSGT00520000055567; -.
HOGENOM; HOG000159961; -.
HOVERGEN; HBG054517; -.
InParanoid; O35987; -.
KO; K14012; -.
OMA; MRGEIPQ; -.
OrthoDB; EOG091G0QFZ; -.
PhylomeDB; O35987; -.
EvolutionaryTrace; O35987; -.
PRO; PR:O35987; -.
Proteomes; UP000002494; Chromosome 3.
Bgee; ENSRNOG00000008604; -.
ExpressionAtlas; O35987; baseline and differential.
Genevisible; O35987; RN.
GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IDA:ParkinsonsUK-UCL.
GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-SubCell.
GO; GO:0045111; C:intermediate filament cytoskeleton; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:1990730; C:VCP-NSFL1C complex; IPI:ParkinsonsUK-UCL.
GO; GO:0051117; F:ATPase binding; IPI:RGD.
GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
GO; GO:0019888; F:protein phosphatase regulator activity; IBA:GO_Central.
GO; GO:0043130; F:ubiquitin binding; IDA:BHF-UCL.
GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
GO; GO:0007030; P:Golgi organization; IDA:RGD.
GO; GO:0061025; P:membrane fusion; IDA:RGD.
GO; GO:0031468; P:nuclear envelope reassembly; IBA:GO_Central.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
InterPro; IPR036241; NSFL1C_SEP_dom_sf.
InterPro; IPR012989; SEP_domain.
InterPro; IPR009060; UBA-like_sf.
InterPro; IPR029071; Ubiquitin-like_domsf.
InterPro; IPR001012; UBX_dom.
Pfam; PF08059; SEP; 1.
Pfam; PF00789; UBX; 1.
SMART; SM00553; SEP; 1.
SMART; SM00166; UBX; 1.
SUPFAM; SSF102848; SSF102848; 1.
SUPFAM; SSF46934; SSF46934; 1.
SUPFAM; SSF54236; SSF54236; 1.
PROSITE; PS51399; SEP; 1.
PROSITE; PS50033; UBX; 1.
1: Evidence at protein level;
3D-structure; Chromosome; Complete proteome;
Direct protein sequencing; Golgi apparatus; Lipid-binding; Nucleus;
Phosphoprotein; Reference proteome.
CHAIN 1 370 NSFL1 cofactor p47.
/FTId=PRO_0000210990.
DOMAIN 179 244 SEP. {ECO:0000255|PROSITE-
ProRule:PRU00732}.
DOMAIN 291 368 UBX. {ECO:0000255|PROSITE-
ProRule:PRU00215}.
MOTIF 109 115 Nuclear localization signal.
MOTIF 172 175 Nuclear localization signal.
MOD_RES 74 74 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UNZ2}.
MOD_RES 102 102 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UNZ2}.
MOD_RES 114 114 Phosphoserine.
{ECO:0000244|PubMed:16641100,
ECO:0000244|PubMed:22673903}.
MOD_RES 140 140 Phosphoserine; by CDK1.
{ECO:0000269|PubMed:12810701}.
MOD_RES 167 167 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9CZ44}.
MOD_RES 176 176 Phosphoserine.
{ECO:0000244|PubMed:16641100,
ECO:0000244|PubMed:22673903}.
MOD_RES 192 192 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UNZ2}.
MOD_RES 272 272 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UNZ2}.
MUTAGEN 41 41 F->A: Reduces ubiquitin binding and Golgi
reassembly.
{ECO:0000269|PubMed:12411482}.
MUTAGEN 57 57 T->A: No effect on phosphorylation.
{ECO:0000269|PubMed:12810701}.
MUTAGEN 112 112 K->T: Strongly reduces nuclear location.
{ECO:0000269|PubMed:12810701}.
MUTAGEN 114 114 S->A: No effect on phosphorylation.
{ECO:0000269|PubMed:12810701}.
MUTAGEN 140 140 S->A: Abolishes phosphorylation by CDK1.
{ECO:0000269|PubMed:12810701}.
MUTAGEN 140 140 S->D: Strongly reduces binding to Golgi
membranes. {ECO:0000269|PubMed:12810701}.
MUTAGEN 173 173 R->T: Strongly reduces nuclear location.
{ECO:0000269|PubMed:12810701}.
MUTAGEN 272 272 S->A: No effect on phosphorylation.
{ECO:0000269|PubMed:12810701}.
MUTAGEN 301 301 R->A: Reduced interaction with VCP.
{ECO:0000269|PubMed:14988733}.
MUTAGEN 342 345 TFPN->AG: Strongly reduced interaction
with VCP. {ECO:0000269|PubMed:14988733}.
MUTAGEN 343 343 F->S: Reduced interaction with VCP.
{ECO:0000269|PubMed:14988733}.
MUTAGEN 345 345 N->A: Reduced interaction with VCP.
{ECO:0000269|PubMed:14988733}.
HELIX 4 15 {ECO:0000244|PDB:1V92}.
HELIX 20 29 {ECO:0000244|PDB:1V92}.
HELIX 35 43 {ECO:0000244|PDB:1V92}.
STRAND 181 187 {ECO:0000244|PDB:1VAZ}.
STRAND 190 192 {ECO:0000244|PDB:1VAZ}.
STRAND 198 200 {ECO:0000244|PDB:1VAZ}.
HELIX 206 215 {ECO:0000244|PDB:1VAZ}.
HELIX 221 224 {ECO:0000244|PDB:1VAZ}.
STRAND 227 229 {ECO:0000244|PDB:1VAZ}.
STRAND 232 237 {ECO:0000244|PDB:1VAZ}.
TURN 239 241 {ECO:0000244|PDB:1VAZ}.
HELIX 275 286 {ECO:0000244|PDB:1S3S}.
STRAND 298 302 {ECO:0000244|PDB:1S3S}.
TURN 303 306 {ECO:0000244|PDB:1S3S}.
STRAND 307 311 {ECO:0000244|PDB:1S3S}.
STRAND 314 316 {ECO:0000244|PDB:1I42}.
HELIX 318 328 {ECO:0000244|PDB:1S3S}.
HELIX 331 333 {ECO:0000244|PDB:1S3S}.
STRAND 337 341 {ECO:0000244|PDB:1S3S}.
TURN 342 345 {ECO:0000244|PDB:1S3S}.
HELIX 355 358 {ECO:0000244|PDB:1S3S}.
STRAND 364 369 {ECO:0000244|PDB:1S3S}.
SEQUENCE 370 AA; 40680 MW; 60C81402E5C58134 CRC64;
MAEERQDALR EFVAVTGAEE DRARFFLESA GWDLQIALAS FYEDGGDEDI VTISQATPSS
VSRGTAPSDN RVTSFRDLIH DQDEEEEEEE GQRFYAGGSE RSGQQIVGPP RKKSPNELVD
DLFKGAKEHG AVAVERVTKS PGETSKPRPF AGGGYRLGAA PEEESAYVAG ERRRHSGQDV
HVVLKLWKTG FSLDNGDLRS YQDPSNAQFL ESIRRGEVPA ELRRLAHGGQ VNLDMEDHRD
EDFVKPKGAF KAFTGEGQKL GSTAPQVLNT SSPAQQAENE AKASSSILIN EAEPTTNIQI
RLADGGRLVQ KFNHSHRISD IRLFIVDARP AMAATSFVLM TTFPNKELAD ENQTLKEANL
LNAVIVQRLT


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