SHLB1_PONAB
ID SHLB1_PONAB Reviewed; 365 AA.
AC Q5R8P5;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Endophilin-B1;
DE AltName: Full=SH3 domain-containing GRB2-like protein B1;
GN Name=SH3GLB1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May be required for normal outer mitochondrial membrane
CC dynamics. Required for coatomer-mediated retrograde transport in
CC certain cells. May recruit other proteins to membranes with high
CC curvature. May promote membrane fusion. Involved in activation of
CC caspase-dependent apoptosis by promoting BAX/BAK1 activation. Involved
CC in caspase-independent apoptosis during nutrition starvation and
CC involved in the regulation of autophagy. Activates lipid kinase
CC activity of PIK3C3 during autophagy probably by associating with the
CC PI3K complex II (PI3KC3-C2). Associated with PI3KC3-C2 during autophagy
CC may regulate the trafficking of ATG9A from the Golgi complex to the
CC peripheral cytoplasm for the formation of autophagosomes by inducing
CC Golgi membrane tubulation and fragmentation. Involved in regulation of
CC degradative endocytic trafficking and cytokinesis, probably in the
CC context of PI3KC3-C2 (By similarity). {ECO:0000250|UniProtKB:Q9JK48,
CC ECO:0000250|UniProtKB:Q9Y371}.
CC -!- SUBUNIT: Homodimer, and heterodimer with SH3GLB2. Binds BAX; induction
CC of apoptosis augments BAX binding. Binds DNM1, HTT, AMPH, BIN1 and
CC ARFGAP1. Interacts with UVRAG; UVRAG bridges the interaction to BECN1
CC indicative for an association with the PI3K complex II (PI3KC3-C2)
CC STOPPED Homodimer, and heterodimer with SH3GLB2. Binds BAX. Binds DNM1,
CC HTT, AMPH, BIN1 and ARFGAP1 (By similarity).
CC {ECO:0000250|UniProtKB:Q9JK48, ECO:0000250|UniProtKB:Q9Y371}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6AYE2,
CC ECO:0000250|UniProtKB:Q9Y371}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q6AYE2, ECO:0000250|UniProtKB:Q9JK48,
CC ECO:0000250|UniProtKB:Q9Y371}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q6AYE2}. Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q9Y371}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9Y371}. Cytoplasmic vesicle, autophagosome
CC membrane {ECO:0000250|UniProtKB:Q9Y371}. Midbody
CC {ECO:0000250|UniProtKB:Q9Y371}. Note=Association with the Golgi
CC apparatus depends on the cell type. Following starvation colocalizes
CC with ATG5 and LC3 autophagy-related protein(s)on autophagosomal
CC membranes. {ECO:0000250|UniProtKB:Q9Y371}.
CC -!- DOMAIN: An N-terminal amphipathic helix, the BAR domain and a second
CC amphipathic helix inserted into helix 1 of the BAR domain (N-BAR
CC domain) induce membrane curvature and bind curved membranes.
CC {ECO:0000250}.
CC -!- DOMAIN: The SH3 domain is required and sufficient for the interaction
CC with UVRAG. {ECO:0000250|UniProtKB:Q9Y371}.
CC -!- PTM: Phosphorylated at Thr-145 by CDK5; this phosphorylation is
CC required for autophagy induction in starved neurons and facilitates
CC homodimerization. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the endophilin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAH91865.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR859706; CAH91865.1; ALT_INIT; mRNA.
DR RefSeq; NP_001126080.1; NM_001132608.1.
DR AlphaFoldDB; Q5R8P5; -.
DR SMR; Q5R8P5; -.
DR STRING; 9601.ENSPPYP00000001374; -.
DR Ensembl; ENSPPYT00000001419; ENSPPYP00000001374; ENSPPYG00000001185.
DR GeneID; 100173032; -.
DR KEGG; pon:100173032; -.
DR CTD; 51100; -.
DR eggNOG; KOG3725; Eukaryota.
DR GeneTree; ENSGT00940000155667; -.
DR HOGENOM; CLU_043817_1_1_1; -.
DR InParanoid; Q5R8P5; -.
DR OrthoDB; 803053at2759; -.
DR TreeFam; TF313281; -.
DR Proteomes; UP000001595; Chromosome 1.
DR GO; GO:0000421; C:autophagosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR CDD; cd07616; BAR_Endophilin_B1; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR004148; BAR_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR028503; SH3GLB1.
DR InterPro; IPR035695; SH3GLB1_BAR.
DR PANTHER; PTHR14167:SF52; PTHR14167:SF52; 1.
DR Pfam; PF03114; BAR; 1.
DR Pfam; PF14604; SH3_9; 1.
DR SMART; SM00721; BAR; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51021; BAR; 1.
DR PROSITE; PS50002; SH3; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Apoptosis; Coiled coil; Cytoplasm; Cytoplasmic vesicle;
KW Golgi apparatus; Lipid-binding; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Phosphoprotein; Reference proteome;
KW SH3 domain.
FT CHAIN 1..365
FT /note="Endophilin-B1"
FT /id="PRO_0000285844"
FT DOMAIN 27..261
FT /note="BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00361"
FT DOMAIN 305..365
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..37
FT /note="Required for membrane binding"
FT /evidence="ECO:0000250|UniProtKB:Q9Y371"
FT REGION 1..30
FT /note="Membrane-binding amphipathic helix"
FT /evidence="ECO:0000250"
FT COILED 155..195
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y371"
FT MOD_RES 145
FT /note="Phosphothreonine; by CDK5"
FT /evidence="ECO:0000250|UniProtKB:Q9Y371"
SQ SEQUENCE 365 AA; 40796 MW; 42C2AEA57A0B350E CRC64;
MNIMDFNVKK LAADAGTFLS RAVQFTEEKL GQAEKTELDA HLENLLSKAE CTKIWTEKIM
KQTEVLLQPN PNARIEEFVY EKLDRKAPSR INNPELLGQY MIDAGTEFGP GTAYGNALIK
CGETQKRIGT ADRELIQTSA LNFLTPLRNF IEGDYKTIAK ERKLLQNKRL DLDAAKTRLK
KAKAAETRNS SEQELRITQS EFDRQAEITR LLLEGISSTH AHHLRCLNDF VEAQMTYYAQ
CYQYMLDLQK QLGSFPSNYL SNNNQTSVTP VPSVLPNAIG SSAMASTSGL VITSPSNLSD
LKECSGSRKA RVLYDYDAAN STELSLLADE VITVFSVVGM DSDWLMGERG NQKGKVPITY
LELLN
