ID A0A2Y9D9S4_TRIMA Unreviewed; 370 AA.
AC A0A2Y9D9S4;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=NSFL1 cofactor p47 {ECO:0000256|ARBA:ARBA00019548};
DE AltName: Full=p97 cofactor p47 {ECO:0000256|ARBA:ARBA00030329};
GN Name=LOC101352501 {ECO:0000313|RefSeq:XP_004370555.1};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_004370555.1};
RN [1] {ECO:0000313|RefSeq:XP_004370555.1}
RP IDENTIFICATION.
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_004370555.1; XM_004370498.2.
DR AlphaFoldDB; A0A2Y9D9S4; -.
DR GeneID; 101352501; -.
DR OrthoDB; 5483331at2759; -.
DR Proteomes; UP000248480; Unplaced.
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:UP000248480}.
FT DOMAIN 179..244
FT /note="SEP"
FT /evidence="ECO:0000259|PROSITE:PS51399"
FT DOMAIN 291..368
FT /note="UBX"
FT /evidence="ECO:0000259|PROSITE:PS50033"
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 REGION 261..290
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"
SQ SEQUENCE 370 AA; 40586 MW; 978B7DBC707B19ED CRC64;
MAAERQDALR EFVAVTGADE DRARFYLESA GWDLQIALAS FYEDGGDEDI VTISQATPSS
VSRGTAPSDN RVTSFRDLIH DQDDEEEEEE GQRFYAGGSE RSGQQIVGPP RKKSPNELVD
DLFKGAKEHG AVAVERVSKS PGETSKPRPF AGGGYRLGAA PEEESAYVAG ERRRHSGQDV
HVVLKLWKSG FSLDNGELRN YQDPSNAQFL ESIRRGEVPA ELRRLAHGGQ VNLDMEDHRD
EDFVKPKGAF KAFTGEGQKL GSTAPQVLNT SSPAQQAENE AKASSSISIN ESEPTTNIQI
RLADGGRLVQ KFNHSHRISD IRLFIVDARP AMAATSFVLM TTFPNKELAD ESQTLKEANL
LNAVIVQRLT
//
