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NSFL1 cofactor p47 (p97 cofactor p47)

 NSF1C_MOUSE             Reviewed;         370 AA.
Q9CZ44; A2AT03; Q80Y15; Q8BYL3;
16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
05-JUL-2017, entry version 128.
RecName: Full=NSFL1 cofactor p47;
AltName: Full=p97 cofactor p47;
Name=Nsfl1c;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J; TISSUE=Embryo, and Hypothalamus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
STRAIN=C57BL/6J; TISSUE=Brain;
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]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-167, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Mast cell;
PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
Kawakami T., Salomon A.R.;
"Quantitative time-resolved phosphoproteomic analysis of mast cell
signaling.";
J. Immunol. 179:5864-5876(2007).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114 AND SER-176, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114; SER-176 AND
SER-272, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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) (By
similarity). {ECO:0000250}.
-!- 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 (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Golgi apparatus,
Golgi stack {ECO:0000250}. Chromosome {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9CZ44-1; Sequence=Displayed;
Name=2;
IsoId=Q9CZ44-2; Sequence=VSP_009264, VSP_009265, VSP_009266;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q9CZ44-3; Sequence=VSP_009264;
-!- PTM: Phosphorylated during mitosis. Phosphorylation inhibits
interaction with Golgi membranes and is required for the
fragmentation of the Golgi stacks during mitosis (By similarity).
{ECO:0000250}.
-!- SIMILARITY: Belongs to the NSFL1C family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AK013024; BAB28604.1; -; mRNA.
EMBL; AK039136; BAC30250.1; -; mRNA.
EMBL; AL928719; CAM23816.1; -; Genomic_DNA.
EMBL; BC050936; AAH50936.1; -; mRNA.
CCDS; CCDS16868.1; -. [Q9CZ44-3]
CCDS; CCDS71160.1; -. [Q9CZ44-1]
RefSeq; NP_001278003.1; NM_001291074.1. [Q9CZ44-1]
RefSeq; NP_938085.1; NM_198326.3. [Q9CZ44-3]
UniGene; Mm.419479; -.
ProteinModelPortal; Q9CZ44; -.
SMR; Q9CZ44; -.
BioGrid; 239751; 1.
IntAct; Q9CZ44; 6.
MINT; MINT-1869876; -.
STRING; 10090.ENSMUSP00000086542; -.
iPTMnet; Q9CZ44; -.
PhosphoSitePlus; Q9CZ44; -.
REPRODUCTION-2DPAGE; Q9CZ44; -.
EPD; Q9CZ44; -.
PaxDb; Q9CZ44; -.
PeptideAtlas; Q9CZ44; -.
PRIDE; Q9CZ44; -.
TopDownProteomics; Q9CZ44-1; -. [Q9CZ44-1]
TopDownProteomics; Q9CZ44-2; -. [Q9CZ44-2]
Ensembl; ENSMUST00000028949; ENSMUSP00000028949; ENSMUSG00000027455. [Q9CZ44-1]
Ensembl; ENSMUST00000089140; ENSMUSP00000086542; ENSMUSG00000027455. [Q9CZ44-3]
GeneID; 386649; -.
KEGG; mmu:386649; -.
CTD; 55968; -.
MGI; MGI:3042273; Nsfl1c.
eggNOG; KOG2086; Eukaryota.
eggNOG; ENOG410YGXU; LUCA.
GeneTree; ENSGT00520000055567; -.
HOGENOM; HOG000159961; -.
HOVERGEN; HBG054517; -.
InParanoid; Q9CZ44; -.
KO; K14012; -.
OMA; MRGEIPQ; -.
TreeFam; TF312973; -.
PRO; PR:Q9CZ44; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000027455; -.
CleanEx; MM_NSFL1C; -.
ExpressionAtlas; Q9CZ44; baseline and differential.
Genevisible; Q9CZ44; MM.
GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-SubCell.
GO; GO:0045111; C:intermediate filament cytoskeleton; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:1990730; C:VCP-NSFL1C complex; IEA:Ensembl.
GO; GO:0051117; F:ATPase binding; IEA:Ensembl.
GO; GO:0005543; F:phospholipid binding; IEA:Ensembl.
GO; GO:0019888; F:protein phosphatase regulator activity; IBA:GO_Central.
GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
GO; GO:0061025; P:membrane fusion; IBA:GO_Central.
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; IPR012989; SEP_domain.
InterPro; IPR009060; UBA-like.
InterPro; IPR029071; Ubiquitin-rel_dom.
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;
Alternative splicing; Chromosome; Complete proteome; Golgi apparatus;
Lipid-binding; Nucleus; Phosphoprotein; Reference proteome.
CHAIN 1 370 NSFL1 cofactor p47.
/FTId=PRO_0000210989.
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.
COMPBIAS 84 90 Poly-Glu.
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:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 140 140 Phosphoserine.
{ECO:0000250|UniProtKB:O35987}.
MOD_RES 167 167 Phosphotyrosine.
{ECO:0000244|PubMed:17947660}.
MOD_RES 176 176 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:21183079}.
MOD_RES 192 192 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UNZ2}.
MOD_RES 272 272 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
VAR_SEQ 93 93 R -> RSR (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_009264.
VAR_SEQ 262 262 S -> R (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_009265.
VAR_SEQ 263 370 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_009266.
CONFLICT 13 13 V -> A (in Ref. 1; BAC30250).
{ECO:0000305}.
SEQUENCE 370 AA; 40710 MW; 32C9C20F82125D58 CRC64;
MAEERQDALR EFVAVTGTEE 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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