ID   A0A2K5K502_COLAP        Unreviewed;       339 AA.
AC   A0A2K5K502;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=NSFL1 cofactor p47 {ECO:0000256|ARBA:ARBA00019548};
DE   AltName: Full=p97 cofactor p47 {ECO:0000256|ARBA:ARBA00030329};
OS   Colobus angolensis palliatus (Peters' Angolan colobus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Colobus.
OX   NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000036193.1, ECO:0000313|Proteomes:UP000233080};
RN   [1] {ECO:0000313|Ensembl:ENSCANP00000036193.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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_011798779.1; XM_011943389.1.
DR   AlphaFoldDB; A0A2K5K502; -.
DR   Ensembl; ENSCANT00000059441.1; ENSCANP00000036193.1; ENSCANG00000041770.1.
DR   GeneID; 105512783; -.
DR   CTD; 55968; -.
DR   OMA; EHQAFYA; -.
DR   OrthoDB; 5483331at2759; -.
DR   Proteomes; UP000233080; 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:UP000233080}.
FT   DOMAIN          148..213
FT                   /note="SEP"
FT                   /evidence="ECO:0000259|PROSITE:PS51399"
FT   DOMAIN          260..337
FT                   /note="UBX"
FT                   /evidence="ECO:0000259|PROSITE:PS50033"
FT   REGION          80..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          230..258
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   339 AA;  37298 MW;  CF1F55398BB3B35B CRC64;
     MAAERQEALR EFVAVTGAEE DRARFFLESA GWDLQIALAS FYEDGGDEDI VTISQATPSS
     VSRGTAPSDS RVTSFRDLIH DQDEDEEEEE GQRFYAGGSE RSGQQIVGPP RKKSPNELVD
     DLFKGAKEHG AVAVERVTKS PGETSKPRVH VVLKLWKSGF SLDNGELRSY QDPSNAQFLE
     SIRRGEVPAE LRRLAHGGQV NLDMEDHRDE DFVKPKGAFK AFTGEGQKLG STAPQVLSTS
     SPAQQAENEA KASSSILIDE SEPTTNIQIR LADGGRLVQK FNHSHRISDI RLFIVDARPA
     MAATSFILMT TFPNKELADE SQTLKEANLL NAVIVQRLT
//