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NSF1C_CHICK
ID   NSF1C_CHICK             Reviewed;         369 AA.
AC   Q5ZK10;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=NSFL1 cofactor p47;
DE   AltName: Full=p97 cofactor p47;
GN   Name=NSFL1C; ORFNames=RCJMB04_13o20;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(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).
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   -!- 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}. Note=Predominantly nuclear in
CC       interphase cells. A small proportion of the protein is cytoplasmic,
CC       associated with Golgi stacks. Localizes to centrosome during mitotic
CC       prophase and metaphase. {ECO:0000250|UniProtKB:O35987}.
CC   -!- SIMILARITY: Belongs to the NSFL1C family. {ECO:0000305}.
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DR   EMBL; AJ720274; CAG31933.1; -; mRNA.
DR   RefSeq; NP_001026030.1; NM_001030859.1.
DR   AlphaFoldDB; Q5ZK10; -.
DR   SMR; Q5ZK10; -.
DR   STRING; 9031.ENSGALP00000038618; -.
DR   PaxDb; Q5ZK10; -.
DR   Ensembl; ENSGALT00000086660; ENSGALP00000063425; ENSGALG00000006182.
DR   GeneID; 419268; -.
DR   KEGG; gga:419268; -.
DR   CTD; 55968; -.
DR   VEuPathDB; HostDB:geneid_419268; -.
DR   eggNOG; KOG2086; Eukaryota.
DR   GeneTree; ENSGT00520000055567; -.
DR   HOGENOM; CLU_029402_0_0_1; -.
DR   InParanoid; Q5ZK10; -.
DR   OMA; EHQAFYA; -.
DR   OrthoDB; 1175850at2759; -.
DR   PhylomeDB; Q5ZK10; -.
DR   Reactome; R-GGA-9013407; RHOH GTPase cycle.
DR   PRO; PR:Q5ZK10; -.
DR   Proteomes; UP000000539; Chromosome 20.
DR   Bgee; ENSGALG00000006182; Expressed in testis and 14 other tissues.
DR   ExpressionAtlas; Q5ZK10; baseline and differential.
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:1990730; C:VCP-NSFL1C complex; IEA:Ensembl.
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:0000132; P:establishment of mitotic spindle orientation; IEA:Ensembl.
DR   GO; GO:0007030; P:Golgi organization; ISS:AgBase.
DR   GO; GO:0061025; P:membrane fusion; ISS:AgBase.
DR   GO; GO:1904780; P:negative regulation of protein localization to centrosome; IEA:Ensembl.
DR   GO; GO:0031468; P:nuclear membrane reassembly; IBA:GO_Central.
DR   GO; GO:0046604; P:positive regulation of mitotic centrosome separation; IEA:Ensembl.
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   2: Evidence at transcript level;
KW   Cytoplasm; Cytoskeleton; Golgi apparatus; Lipid-binding; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..369
FT                   /note="NSFL1 cofactor p47"
FT                   /id="PRO_0000304739"
FT   DOMAIN          178..243
FT                   /note="SEP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00732"
FT   DOMAIN          291..367
FT                   /note="UBX"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00215"
FT   REGION          46..115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          133..156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          260..280
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        52..68
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   369 AA;  40641 MW;  B39CBE86F02FFD96 CRC64;
     MADREEALRE FVAVTGAEEE RARFFLESAG WDLQIALASF YEDGGDEDIL TLPQPTPSSV
     SRGTAASDHR VTSFRDLVHA QEDDDEEEEG QRFYAGGSER SGQQIVGPPR KKSPNELVED
     LFKGAKEHGA VAVDRTAKSS GESSKPKPFA GGGYRLGATP EEESAYVAGE RRHNSVQDVH
     VVLKLWKTGF SLDSGELRSY QDPSNAQFLD DIRRGEVPAE LRRLARGGQV NLDMEDHRDE
     EYVKPKSVFK AFTGEGQKLG STAPQVLSTS SPAQQAENEA KASSAIAIDE SEPVTNIQIR
     LADGGRLVQK FNHNHRIRDI RLFIVDARPA MAATSFVLMT TFPNKELTDE NQTLKEANLL
     NAVIVQRLT
 
 
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