SHLB1_RAT
ID SHLB1_RAT Reviewed; 365 AA.
AC Q6AYE2;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Endophilin-B1;
DE AltName: Full=SH3 domain-containing GRB2-like protein B1;
GN Name=Sh3glb1 {ECO:0000312|EMBL:AAH79085.1};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000312|EMBL:AAH79085.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung {ECO:0000312|EMBL:AAH79085.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2] {ECO:0000305}
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DOMAIN.
RX PubMed=11604418; DOI=10.1083/jcb.200107075;
RA Farsad K., Ringstad N., Takei K., Floyd S.R., Rose K., De Camilli P.;
RT "Generation of high curvature membranes mediated by direct endophilin
RT bilayer interactions.";
RL J. Cell Biol. 155:193-200(2001).
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) (By
CC similarity). {ECO:0000250|UniProtKB:Q9JK48,
CC ECO:0000250|UniProtKB:Q9Y371}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11604418}. Golgi
CC apparatus membrane {ECO:0000269|PubMed:11604418}; Peripheral membrane
CC protein {ECO:0000269|PubMed:11604418}. Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q9JK48, ECO:0000250|UniProtKB:Q9Y371};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q9JK48,
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:Q9JK48, ECO:0000250|UniProtKB:Q9Y371,
CC ECO:0000269|PubMed:11604418}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, heart, lung and spleen. Low
CC level in liver and testis. {ECO:0000269|PubMed:11604418}.
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:0000269|PubMed:11604418}.
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:0000255}.
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DR EMBL; BC079085; AAH79085.1; -; mRNA.
DR RefSeq; NP_001011929.1; NM_001011929.1.
DR AlphaFoldDB; Q6AYE2; -.
DR SMR; Q6AYE2; -.
DR BioGRID; 253783; 1.
DR IntAct; Q6AYE2; 3.
DR STRING; 10116.ENSRNOP00000017771; -.
DR iPTMnet; Q6AYE2; -.
DR PhosphoSitePlus; Q6AYE2; -.
DR jPOST; Q6AYE2; -.
DR PaxDb; Q6AYE2; -.
DR PRIDE; Q6AYE2; -.
DR Ensembl; ENSRNOT00000017770; ENSRNOP00000017771; ENSRNOG00000012957.
DR GeneID; 292156; -.
DR KEGG; rno:292156; -.
DR CTD; 51100; -.
DR RGD; 1304859; Sh3glb1.
DR eggNOG; KOG3725; Eukaryota.
DR GeneTree; ENSGT00940000155667; -.
DR HOGENOM; CLU_043817_1_1_1; -.
DR InParanoid; Q6AYE2; -.
DR OrthoDB; 803053at2759; -.
DR PRO; PR:Q6AYE2; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000012957; Expressed in testis and 19 other tissues.
DR ExpressionAtlas; Q6AYE2; baseline and differential.
DR Genevisible; Q6AYE2; RN.
DR GO; GO:0000421; C:autophagosome membrane; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005769; C:early endosome; IDA:RGD.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0030496; C:midbody; ISO:RGD.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0008021; C:synaptic vesicle; IDA:RGD.
DR GO; GO:0005504; F:fatty acid binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0042171; F:lysophosphatidic acid acyltransferase activity; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0051084; P:'de novo' post-translational protein folding; ISO:RGD.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0048102; P:autophagic cell death; ISO:RGD.
DR GO; GO:0034198; P:cellular response to amino acid starvation; ISO:RGD.
DR GO; GO:0042149; P:cellular response to glucose starvation; ISO:RGD.
DR GO; GO:0090148; P:membrane fission; ISO:RGD.
DR GO; GO:0061024; P:membrane organization; IBA:GO_Central.
DR GO; GO:0007005; P:mitochondrion organization; ISO:RGD.
DR GO; GO:1902254; P:negative regulation of intrinsic apoptotic signaling pathway by p53 class mediator; ISO:RGD.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; ISO:RGD.
DR GO; GO:0008654; P:phospholipid biosynthetic process; ISO:RGD.
DR GO; GO:2000786; P:positive regulation of autophagosome assembly; ISO:RGD.
DR GO; GO:0010508; P:positive regulation of autophagy; ISO:RGD.
DR GO; GO:1903861; P:positive regulation of dendrite extension; IMP:RGD.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; IMP:RGD.
DR GO; GO:1902255; P:positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator; ISO:RGD.
DR GO; GO:1903527; P:positive regulation of membrane tubulation; ISO:RGD.
DR GO; GO:0051388; P:positive regulation of neurotrophin TRK receptor signaling pathway; IMP:RGD.
DR GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; ISO:RGD.
DR GO; GO:1900740; P:positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISO:RGD.
DR GO; GO:1903778; P:protein localization to vacuolar membrane; ISO:RGD.
DR GO; GO:0032801; P:receptor catabolic process; ISO:RGD.
DR GO; GO:0032465; P:regulation of cytokinesis; ISO:RGD.
DR GO; GO:2000641; P:regulation of early endosome to late endosome transport; IMP:RGD.
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_0000307711"
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|UniProtKB:Q9Y371"
FT COILED 156..185
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; 40787 MW; AF6950A4820FB470 CRC64;
MNIMDFNVKK LAADAGTFLS RAVQFTEEKL GQAEKTELDA HLENLLSKAE CTKVWTEKIM
KQTEVLLQPN PNARIEEFVY EKLDRKAPSR INNPELLGQY MIDAGTEFGP GTAYGNALIK
CGETQKRIGT ADRELIQTSA LNFLTPLRNF IEGDYKTIAK ERKLLQNKRL DLDAAKTRLK
KAKAAETKSS SEQELRITQS EFDRQAEITR LLLEGISSTH AHHLRCLNDF VEAQMTYYAQ
CYQYMLDLQK QLGSFPSNYV SNNNQTSGTP VPYTLSNTIG PSAVASTGSL VITCPPNLSD
LKDSSSTRKA RVLYDYDAAN STELSLLADE VITVFSVVGM DSDWLMGERG NQKGKVPITY
LELLN
