PACER_BOVIN
ID PACER_BOVIN Reviewed; 663 AA.
AC A7E316;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Protein associated with UVRAG as autophagy enhancer {ECO:0000250|UniProtKB:Q9H714};
DE Short=Pacer {ECO:0000250|UniProtKB:Q9H714};
DE AltName: Full=Protein Rubicon-like {ECO:0000305};
GN Name=RUBCNL {ECO:0000250|UniProtKB:Q9H714};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Regulator of autophagy that promotes autophagosome maturation
CC by facilitating the biogenesis of phosphatidylinositol 3-phosphate
CC (PtdIns(3)P) in late steps of autophagy. Acts by antagonizing RUBCN,
CC thereby stimulating phosphatidylinositol 3-kinase activity of the
CC PI3K/PI3KC3 complex. Following anchorage to the autophagosomal SNARE
CC STX17, promotes the recruitment of PI3K/PI3KC3 and HOPS complexes to
CC the autophagosome to regulate the fusion specificity of autophagosomes
CC with late endosomes/lysosomes. Binds phosphoinositides
CC phosphatidylinositol 3-phosphate (PtdIns(3)P), 4-phosphate (PtdIns(4)P)
CC and 5-phosphate (PtdIns(5)P) (By similarity). In addition to its role
CC in autophagy, acts as a regulator of lipid and glycogen homeostasis (By
CC similarity). May act as a tumor suppressor (By similarity).
CC {ECO:0000250|UniProtKB:Q3TD16, ECO:0000250|UniProtKB:Q9H714}.
CC -!- SUBUNIT: Interacts with UVRAG; the interaction is direct and promotes
CC association with the PI3K/PI3KC3 and HOPS complexes. Interacts with
CC STX17. {ECO:0000250|UniProtKB:Q9H714}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome membrane
CC {ECO:0000250|UniProtKB:Q9H714}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9H714}. Note=Associates with late autophagic
CC structure. Recruitment to autophagosome membrane is promoted by
CC autophagic stimuli. {ECO:0000250|UniProtKB:Q9H714}.
CC -!- PTM: Acetylated by KAT5/TIP60 under autophagy induction, promoting
CC autophagosome maturation and lipid metabolism. Lys-484 and Lys-574
CC constitute the key sites for tuning function in autophagy.
CC {ECO:0000250|UniProtKB:Q9H714}.
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DR EMBL; BC151662; AAI51663.1; -; mRNA.
DR RefSeq; NP_001095511.1; NM_001102041.2.
DR RefSeq; XP_010809010.1; XM_010810708.2.
DR RefSeq; XP_010809011.1; XM_010810709.2.
DR RefSeq; XP_010809012.1; XM_010810710.2.
DR AlphaFoldDB; A7E316; -.
DR SMR; A7E316; -.
DR STRING; 9913.ENSBTAP00000017794; -.
DR PaxDb; A7E316; -.
DR PRIDE; A7E316; -.
DR Ensembl; ENSBTAT00000017794; ENSBTAP00000017794; ENSBTAG00000013371.
DR GeneID; 517231; -.
DR KEGG; bta:517231; -.
DR CTD; 80183; -.
DR VEuPathDB; HostDB:ENSBTAG00000013371; -.
DR VGNC; VGNC:34213; RUBCNL.
DR eggNOG; KOG1829; Eukaryota.
DR GeneTree; ENSGT00940000160585; -.
DR HOGENOM; CLU_027575_0_0_1; -.
DR InParanoid; A7E316; -.
DR OrthoDB; 177737at2759; -.
DR TreeFam; TF317067; -.
DR Proteomes; UP000009136; Chromosome 12.
DR Bgee; ENSBTAG00000013371; Expressed in neutrophil and 103 other tissues.
DR ExpressionAtlas; A7E316; baseline and differential.
DR GO; GO:0000421; C:autophagosome membrane; ISS:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:1901981; F:phosphatidylinositol phosphate binding; IBA:GO_Central.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; ISS:UniProtKB.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; ISS:UniProtKB.
DR GO; GO:0010314; F:phosphatidylinositol-5-phosphate binding; ISS:UniProtKB.
DR GO; GO:0097352; P:autophagosome maturation; ISS:UniProtKB.
DR GO; GO:0061910; P:autophagosome-endosome fusion; IBA:GO_Central.
DR GO; GO:0061909; P:autophagosome-lysosome fusion; ISS:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0070873; P:regulation of glycogen metabolic process; ISS:UniProtKB.
DR GO; GO:0019216; P:regulation of lipid metabolic process; ISS:UniProtKB.
DR InterPro; IPR025258; Zf-RING_9.
DR Pfam; PF13901; zf-RING_9; 1.
DR SMART; SM01175; DUF4206; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Autophagy; Cytoplasmic vesicle; Lipid metabolism;
KW Lipid-binding; Membrane; Reference proteome.
FT CHAIN 1..663
FT /note="Protein associated with UVRAG as autophagy enhancer"
FT /id="PRO_0000350566"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..235
FT /note="Interaction with UVRAG"
FT /evidence="ECO:0000250|UniProtKB:Q9H714"
FT COMPBIAS 65..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 484
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9H714"
FT MOD_RES 534
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9H714"
FT MOD_RES 574
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9H714"
FT MOD_RES 634
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9H714"
SQ SEQUENCE 663 AA; 73604 MW; 856EBAAC10AE8277 CRC64;
MVSQSSGRQD SPVDPWEGVS DDPGNTDGLP SLLDTEHPFC PSDIRFTRHR AAWINPPCAQ
QQLQDASPQV LAVGNRESHT ASNTKSPLGT SPLSLGDSVV ETSLPKGTTD SLGSSSAWGT
AGNGSDSSVT LKEERAGLPR RCPHTSLITS SKTVSGPPCP EDGRAFFKPS QLTASADADA
VQVGGRTVSS NSFSPEAFVL PVDAEKENAH FYVADMIISV MEKMKCNILS QQHTETWSTE
EAGRSLGNSR ADLEGTFYTH VKQESGSSTS SDSGYEGCVL QVSPVVETPT FSEVTEEDCK
CDFDDFVIVE LGDFSNTTEP CGCSSDTSKS VIHEPNFNSA ELIAKELYRV FRKCWMLAEV
HYQLTGSLDA AGSIVINEER VQKDFESSTD VVQEIKLKSR IRGTGDWAPP RFQIIFDIHP
PLKRDLVVIA QNFFCAGCGT PIEPKFVKRL RYCEYLGKYF CDCCHSYSES CIPARILRMW
DFRKYYVSNF SKRLLDHIWH EPIFNLLHVS HGLYTKAKEL DRVREIQEQL FHIKKLLKTC
RFAESTLKEF EQLPGHLTEA LHLFSLEDMV KVKKGLLAPL LKDILKASLE HVASCELCQG
KGFICEFCRS TAVIFPFQTA TCRRCSACRA CFHKQCFQSS KCPRCARITA RRRLLESLPS
AAT
