NSF1C_PONAB
ID NSF1C_PONAB Reviewed; 370 AA.
AC Q5RBG3;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=NSFL1 cofactor p47;
DE AltName: Full=p97 cofactor p47;
GN Name=NSFL1C;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 levels 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 -!- 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; CR858685; CAH90897.1; -; mRNA.
DR RefSeq; NP_001125510.1; NM_001132038.1.
DR AlphaFoldDB; Q5RBG3; -.
DR BMRB; Q5RBG3; -.
DR SMR; Q5RBG3; -.
DR STRING; 9601.ENSPPYP00000012121; -.
DR Ensembl; ENSPPYT00000012599; ENSPPYP00000012121; ENSPPYG00000039067.
DR GeneID; 100172420; -.
DR KEGG; pon:100172420; -.
DR CTD; 55968; -.
DR eggNOG; KOG2086; Eukaryota.
DR GeneTree; ENSGT00520000055567; -.
DR HOGENOM; CLU_029402_0_0_1; -.
DR InParanoid; Q5RBG3; -.
DR OMA; EHQAFYA; -.
DR TreeFam; TF312973; -.
DR Proteomes; UP000001595; Chromosome 20.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Chromosome; Cytoplasm; Cytoskeleton; Golgi apparatus; Lipid-binding;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..370
FT /note="NSFL1 cofactor p47"
FT /id="PRO_0000304738"
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..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..289
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:0000250|UniProtKB:Q9UNZ2"
FT MOD_RES 140
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:O35987"
FT MOD_RES 167
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZ44"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZ44"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UNZ2"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UNZ2"
SQ SEQUENCE 370 AA; 40573 MW; 79364617F940B9F9 CRC64;
MAAERQEALR EFVAVTGAEE DRARFFLESA GWDLQIALAS FYEDGGDEDI VTISQATPSS
VSRGTAPSDN RVTSFRDLIH DQDEDEEEEE GQRFYAGGSE RSGQQIVGPP RKKSPNELVD
DLFKGAKEHG AVAVERVTKS PGETSKPRPF AGGGYRLGAA PEEESAYVAG EKRQHSSQDV
HVVLKLWKSG FSLDNGELRS YQDPSNAQFL ESIRRGEVPA ELRRLAHGGQ VNLDMEDHRD
EDFVKPKGAF KAFTGEGQKL GSTAPQVLST SSPAQQAENE AKASSSILID ESEPTTNIQI
RLADGGRLVQ KFNHSHRISD IRLFIVDARP AMAATSFILM TTFPNKELAD ESQTLKEANL
LNAVIVQRLT
