NSF1C_MOUSE
ID NSF1C_MOUSE Reviewed; 370 AA.
AC Q9CZ44; A2AT03; Q80Y15; Q8BYL3;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=NSFL1 cofactor p47;
DE AltName: Full=p97 cofactor p47;
GN Name=Nsfl1c;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Hypothalamus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-167, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114 AND SER-176, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114; SER-176 AND SER-272, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Reduces the ATPase activity of VCP. Necessary for the
CC fragmentation of Golgi stacks during mitosis and for VCP-mediated
CC reassembly of Golgi stacks after mitosis. May play a role in VCP-
CC mediated formation of transitional endoplasmic reticulum (tER).
CC Inhibits the activity of CTSL (in vitro). Together with UBXN2B/p37,
CC regulates the centrosomal levels of kinase AURKA/Aurora A during
CC mitotic progression by promoting AURKA removal from centrosomes in
CC prophase. Also, regulates spindle orientation during mitosis.
CC {ECO:0000250|UniProtKB:O35987, ECO:0000250|UniProtKB:Q9UNZ2}.
CC -!- SUBUNIT: Part of a ternary complex containing STX5A, NSFL1C and VCP.
CC NSFL1C forms a homotrimer that binds to one end of a VCP homohexamer.
CC The complex binds to membranes enriched in phosphatidylethanolamine-
CC containing lipids and promotes Golgi membrane fusion. Interaction with
CC VCIP135 leads to dissociation of the complex via ATP hydrolysis by VCP.
CC Binds ubiquitin and mono-ubiquitinated proteins via its N-terminal UBA-
CC like domain when bound to VCP (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O35987}. Golgi
CC apparatus, Golgi stack {ECO:0000250|UniProtKB:O35987}. Chromosome
CC {ECO:0000250|UniProtKB:O35987}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:O35987}.
CC Note=Predominantly nuclear in interphase cells. Bound to the axial
CC elements of sex chromosomes in pachytene spermatocytes. A small
CC proportion of the protein is cytoplasmic, associated with Golgi stacks.
CC Localizes to centrosome during mitotic prophase and metaphase.
CC {ECO:0000250|UniProtKB:O35987}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9CZ44-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CZ44-2; Sequence=VSP_009264, VSP_009265, VSP_009266;
CC Name=3;
CC IsoId=Q9CZ44-3; Sequence=VSP_009264;
CC -!- PTM: Phosphorylated during mitosis. Phosphorylation inhibits
CC interaction with Golgi membranes and is required for the fragmentation
CC of the Golgi stacks during mitosis (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NSFL1C family. {ECO:0000305}.
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DR EMBL; AK013024; BAB28604.1; -; mRNA.
DR EMBL; AK039136; BAC30250.1; -; mRNA.
DR EMBL; AL928719; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC050936; AAH50936.1; -; mRNA.
DR CCDS; CCDS16868.1; -. [Q9CZ44-3]
DR CCDS; CCDS71160.1; -. [Q9CZ44-1]
DR RefSeq; NP_001278003.1; NM_001291074.1. [Q9CZ44-1]
DR RefSeq; NP_938085.1; NM_198326.3. [Q9CZ44-3]
DR AlphaFoldDB; Q9CZ44; -.
DR BMRB; Q9CZ44; -.
DR SMR; Q9CZ44; -.
DR BioGRID; 239751; 33.
DR ComplexPortal; CPX-264; Nsfl1c-Vcp complex.
DR IntAct; Q9CZ44; 5.
DR MINT; Q9CZ44; -.
DR STRING; 10090.ENSMUSP00000086542; -.
DR iPTMnet; Q9CZ44; -.
DR PhosphoSitePlus; Q9CZ44; -.
DR REPRODUCTION-2DPAGE; Q9CZ44; -.
DR CPTAC; non-CPTAC-3852; -.
DR EPD; Q9CZ44; -.
DR jPOST; Q9CZ44; -.
DR MaxQB; Q9CZ44; -.
DR PaxDb; Q9CZ44; -.
DR PeptideAtlas; Q9CZ44; -.
DR PRIDE; Q9CZ44; -.
DR ProteomicsDB; 253020; -. [Q9CZ44-1]
DR ProteomicsDB; 253021; -. [Q9CZ44-2]
DR ProteomicsDB; 253022; -. [Q9CZ44-3]
DR TopDownProteomics; Q9CZ44-1; -. [Q9CZ44-1]
DR TopDownProteomics; Q9CZ44-2; -. [Q9CZ44-2]
DR Antibodypedia; 23083; 110 antibodies from 27 providers.
DR DNASU; 386649; -.
DR Ensembl; ENSMUST00000028949; ENSMUSP00000028949; ENSMUSG00000027455. [Q9CZ44-1]
DR Ensembl; ENSMUST00000089140; ENSMUSP00000086542; ENSMUSG00000027455. [Q9CZ44-3]
DR GeneID; 386649; -.
DR KEGG; mmu:386649; -.
DR CTD; 55968; -.
DR MGI; MGI:3042273; Nsfl1c.
DR VEuPathDB; HostDB:ENSMUSG00000027455; -.
DR eggNOG; KOG2086; Eukaryota.
DR GeneTree; ENSGT00520000055567; -.
DR InParanoid; Q9CZ44; -.
DR OMA; EHQAFYA; -.
DR TreeFam; TF312973; -.
DR Reactome; R-MMU-9013407; RHOH GTPase cycle.
DR BioGRID-ORCS; 386649; 12 hits in 74 CRISPR screens.
DR ChiTaRS; Nsfl1c; mouse.
DR PRO; PR:Q9CZ44; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9CZ44; protein.
DR Bgee; ENSMUSG00000027455; Expressed in embryonic brain and 73 other tissues.
DR ExpressionAtlas; Q9CZ44; baseline and differential.
DR Genevisible; Q9CZ44; MM.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0031616; C:spindle pole centrosome; ISO:MGI.
DR GO; GO:1990730; C:VCP-NSFL1C complex; IPI:ComplexPortal.
DR GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR GO; GO:0005543; F:phospholipid binding; ISO:MGI.
DR GO; GO:0043130; F:ubiquitin binding; ISO:MGI.
DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; ISO:MGI.
DR GO; GO:0007030; P:Golgi organization; ISO:MGI.
DR GO; GO:0061025; P:membrane fusion; ISO:MGI.
DR GO; GO:1904780; P:negative regulation of protein localization to centrosome; ISO:MGI.
DR GO; GO:0031468; P:nuclear membrane reassembly; IBA:GO_Central.
DR GO; GO:0046604; P:positive regulation of mitotic centrosome separation; ISO:MGI.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.30.420.210; -; 1.
DR InterPro; IPR036241; NSFL1C_SEP_dom_sf.
DR InterPro; IPR012989; SEP_domain.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR001012; UBX_dom.
DR Pfam; PF08059; SEP; 1.
DR Pfam; PF00789; UBX; 1.
DR SMART; SM00553; SEP; 1.
DR SMART; SM00166; UBX; 1.
DR SUPFAM; SSF102848; SSF102848; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS51399; SEP; 1.
DR PROSITE; PS50033; UBX; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromosome; Cytoplasm; Cytoskeleton; Golgi apparatus;
KW Lipid-binding; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..370
FT /note="NSFL1 cofactor p47"
FT /id="PRO_0000210989"
FT DOMAIN 179..244
FT /note="SEP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00732"
FT DOMAIN 291..368
FT /note="UBX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00215"
FT REGION 54..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 80..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 109..115
FT /note="Nuclear localization signal"
FT MOTIF 172..175
FT /note="Nuclear localization signal"
FT COMPBIAS 54..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UNZ2"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UNZ2"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35987"
FT MOD_RES 167
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UNZ2"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 93
FT /note="R -> RSR (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_009264"
FT VAR_SEQ 262
FT /note="S -> R (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_009265"
FT VAR_SEQ 263..370
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_009266"
FT CONFLICT 13
FT /note="V -> A (in Ref. 1; BAC30250)"
FT /evidence="ECO:0000305"
SQ 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
