NSF1C_DICDI
ID NSF1C_DICDI Reviewed; 415 AA.
AC Q54BQ5;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=NSFL1 cofactor p47 homolog;
GN Name=nsfl1c; ORFNames=DDB_G0293498;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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) (By
CC similarity). {ECO:0000250}.
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 Regulates the centrosomal levels of kinase aurK/Aurora during mitotic
CC progression by promoting aurK removal from centrosomes in prophase.
CC Also, regulates spindle orientation during mitosis.
CC {ECO:0000250|UniProtKB:O35987, ECO:0000250|UniProtKB:Q9UNZ2}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O35987}. Golgi
CC apparatus, Golgi stack {ECO:0000250|UniProtKB:O35987}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:O35987}.
CC -!- SIMILARITY: Belongs to the NSFL1C family. {ECO:0000305}.
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DR EMBL; AAFI02000217; EAL60684.1; -; Genomic_DNA.
DR RefSeq; XP_629097.1; XM_629095.1.
DR AlphaFoldDB; Q54BQ5; -.
DR SMR; Q54BQ5; -.
DR BioGRID; 1254259; 1.
DR STRING; 44689.DDB0304493; -.
DR PaxDb; Q54BQ5; -.
DR EnsemblProtists; EAL60684; EAL60684; DDB_G0293498.
DR GeneID; 8629256; -.
DR KEGG; ddi:DDB_G0293498; -.
DR dictyBase; DDB_G0293498; -.
DR eggNOG; KOG2086; Eukaryota.
DR HOGENOM; CLU_029402_4_1_1; -.
DR InParanoid; Q54BQ5; -.
DR OMA; EHQAFYA; -.
DR PhylomeDB; Q54BQ5; -.
DR Reactome; R-DDI-9013407; RHOH GTPase cycle.
DR PRO; PR:Q54BQ5; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-SubCell.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR GO; GO:0061025; P:membrane fusion; IBA:GO_Central.
DR GO; GO:0031468; P:nuclear membrane reassembly; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR CDD; cd14349; UBA_CF106; 1.
DR Gene3D; 3.30.420.210; -; 1.
DR InterPro; IPR039517; C6orf106_UBA-like.
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 3: Inferred from homology;
KW Cytoplasm; Cytoskeleton; Golgi apparatus; Lipid-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..415
FT /note="NSFL1 cofactor p47 homolog"
FT /id="PRO_0000328492"
FT DOMAIN 213..279
FT /note="SEP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00732"
FT DOMAIN 337..413
FT /note="UBX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00215"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 39..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 415 AA; 45471 MW; 9C0FF5752972A30A CRC64;
MSDHSEAIAT FQSITGASKE ESTFYLESHD WDLEKAAQTF TTLQEEENQR NDQPQIEEDY
EDEEEEDDHR DPMPASRPVY SKPVAKTVSK KAPAGGRVGG IRTLSDFNND DHDDHDHSDG
DDDEDDRSQQ YFTGGEKSGL VVESAPKKGK NGGSGDIVND VFDSAKRHGA VASNEKKVEK
PDSFDSVGYQ LGATDQGNRN VSKPKEKDPN SQVVEVKVTF WNQGFTIDDG PLRKYDNPEN
KELLDDIQRG IVPRELQKKA TTPNGLSVTL INNHNQDYVE PAKPKYVAFS GGGQTLGSSS
TSTNNNNNNN NNNNNRATTT STTTTSTPNV SSINVDQSQP TTTVQIRLAN GSRLSTTFNH
SHTLQDVINY INSSSGSNQS FDLLTGFPQK PVTNPTSTTL KDAGLLNALL IQKLK
