ID A0A2U4CLV0_TURTR Unreviewed; 381 AA.
AC A0A2U4CLV0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=NSFL1 cofactor p47 {ECO:0000256|ARBA:ARBA00019548};
DE AltName: Full=p97 cofactor p47 {ECO:0000256|ARBA:ARBA00030329};
GN Name=NSFL1C {ECO:0000313|RefSeq:XP_019806414.1};
OS Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Delphinidae; Tursiops.
OX NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_019806414.1};
RN [1] {ECO:0000313|RefSeq:XP_019806414.1}
RP IDENTIFICATION.
RC TISSUE=Spleen {ECO:0000313|RefSeq:XP_019806414.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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. {ECO:0000256|ARBA:ARBA00025968}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Golgi apparatus,
CC Golgi stack {ECO:0000256|ARBA:ARBA00004348}.
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DR RefSeq; XP_019806414.1; XM_019950855.2.
DR AlphaFoldDB; A0A2U4CLV0; -.
DR GeneID; 101332083; -.
DR InParanoid; A0A2U4CLV0; -.
DR OrthoDB; 5483331at2759; -.
DR Proteomes; UP000245320; Chromosome 15.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR CDD; cd14348; UBA_p47; 1.
DR CDD; cd17162; UBX_UBXN2C; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 3.30.420.210; SEP domain; 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 PANTHER; PTHR23333:SF24; NSFL1 COFACTOR P47; 1.
DR PANTHER; PTHR23333; UBX DOMAIN CONTAINING PROTEIN; 1.
DR Pfam; PF08059; SEP; 1.
DR Pfam; PF14555; UBA_4; 1.
DR Pfam; PF00789; UBX; 1.
DR SMART; SM00553; SEP; 1.
DR SMART; SM00166; UBX; 1.
DR SUPFAM; SSF102848; NSFL1 (p97 ATPase) cofactor p47, SEP domain; 1.
DR SUPFAM; SSF46934; UBA-like; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS51399; SEP; 1.
DR PROSITE; PS50033; UBX; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Reference proteome {ECO:0000313|Proteomes:UP000245320}.
FT DOMAIN 190..255
FT /note="SEP"
FT /evidence="ECO:0000259|PROSITE:PS51399"
FT DOMAIN 302..379
FT /note="UBX"
FT /evidence="ECO:0000259|PROSITE:PS50033"
FT REGION 54..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 381 AA; 41853 MW; 4BF4248898ECE1E7 CRC64;
MAAERQDSLR EFVAVTGAEE DRARFFLESA GWDLQIALAS FYEDGGDEDI VTISQATPSS
VSRGTAPSDN RVTSFRDLIH DQDEDEEDEE GQRFEPDGPD LRNRFYAGGS ERSGQQIVGP
PRKKSPNELV DDLFKGAKEH GAVAVERVTK SPGETSKPRP FAGGGYRLGA APEEESAYVA
GERRRHSGQD VHVVLKLWKS GFSLDNGELR SYQDPSNAQF LESIRRGEVP AELRRLAHGG
QVNLDMEDHR DEDFVKPKGA FRAFTGEGQK LGSTAPPVLN TSSPAQQAEN EAKASSSISV
DESQPTTNIQ IRLADGGRLV QKFNHSHRIS DIRLFIVDAR PAMAATSFVL MTTFPNKELA
DESQTLKEAN LLNAVIVQRL T
//
