SHLB1_MOUSE
ID SHLB1_MOUSE Reviewed; 365 AA.
AC Q9JK48; Q3TYR7; Q6A059; Q8CDS9; Q8VI52; Q9CT31;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Endophilin-B1;
DE AltName: Full=SH3 domain-containing GRB2-like protein B1;
GN Name=Sh3glb1; Synonyms=Kiaa0491;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), INTERACTION WITH DNM1; HTT;
RP BIN1 AND AMPH, AND SUBCELLULAR LOCATION.
RC STRAIN=BALB/cJ; TISSUE=Embryo;
RX PubMed=12456676; DOI=10.1074/jbc.m208568200;
RA Modregger J., Schmidt A.A., Ritter B., Huttner W.B., Plomann M.;
RT "Characterization of endophilin B1b, a brain-specific membrane-associated
RT lysophosphatidic acid acyl transferase with properties distinct from
RT endophilin A1.";
RL J. Biol. Chem. 278:4160-4167(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY, INTERACTION
RP WITH BAX AND PPP1CC, AND SUBCELLULAR LOCATION.
RC STRAIN=CD-1;
RX PubMed=17381077; DOI=10.1021/bi6025837;
RA Hrabchak C., Henderson H., Varmuza S.;
RT "A testis specific isoform of endophilin B1, endophilin B1t, interacts
RT specifically with protein phosphatase-1c gamma2 in mouse testis and is
RT abnormally expressed in PP1c gamma null mice.";
RL Biochemistry 46:4635-4644(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Natural killer cell;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Embryo, Inner ear, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Mammary gland;
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 [7]
RP FUNCTION, AND INTERACTION WITH BAX.
RX PubMed=16227588; DOI=10.1128/mcb.25.21.9369-9382.2005;
RA Takahashi Y., Karbowski M., Yamaguchi H., Kazi A., Wu J., Sebti S.M.,
RA Youle R.J., Wang H.G.;
RT "Loss of Bif-1 suppresses Bax/Bak conformational change and mitochondrial
RT apoptosis.";
RL Mol. Cell. Biol. 25:9369-9382(2005).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ARFGAP1.
RX PubMed=17086176; DOI=10.1038/ncb1503;
RA Yang J.S., Zhang L., Lee S.Y., Gad H., Luini A., Hsu V.W.;
RT "Key components of the fission machinery are interchangeable.";
RL Nat. Cell Biol. 8:1376-1382(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP ALTERNATIVE SPLICING, AND FUNCTION (ISOFORM 2).
RX PubMed=24523556; DOI=10.1523/jneurosci.4074-13.2014;
RA Wang D.B., Uo T., Kinoshita C., Sopher B.L., Lee R.J., Murphy S.P.,
RA Kinoshita Y., Garden G.A., Wang H.G., Morrison R.S.;
RT "Bax interacting factor-1 promotes survival and mitochondrial elongation in
RT neurons.";
RL J. Neurosci. 34:2674-2683(2014).
RN [11]
RP STRUCTURE BY NMR OF 296-365.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the SH3 domain of endophilin B1 (SH3G1B1).";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: May be required for normal outer mitochondrial membrane
CC dynamics. Required for coatomer-mediated retrograde transport in
CC certain cells (PubMed:17086176). May recruit other proteins to
CC membranes with high curvature. May promote membrane fusion (By
CC similarity). Involved in activation of caspase-dependent apoptosis by
CC promoting BAX/BAK1 activation (PubMed:16227588). Isoform 1 acts
CC proapoptotic in fibroblasts (PubMed:24523556). Involved in caspase-
CC independent apoptosis during nutrition starvation and involved in the
CC regulation of autophagy. Activates lipid kinase activity of PIK3C3
CC during autophagy probably by associating with the PI3K complex II
CC (PI3KC3-C2). Associated with PI3KC3-C2 during autophagy may regulate
CC the trafficking of ATG9A from the Golgi complex to the peripheral
CC cytoplasm for the formation of autophagosomes by inducing Golgi
CC membrane tubulation and fragmentation. Involved in regulation of
CC degradative endocytic trafficking and cytokinesis, probably in the
CC context of PI3KC3-C2 (By similarity). Isoform 2 acts antiapoptotic in
CC neuronal cells; involved in maintenance of mitochondrial morphology and
CC promotes neuronal viability (PubMed:24523556).
CC {ECO:0000250|UniProtKB:Q9Y371, ECO:0000269|PubMed:17086176,
CC ECO:0000269|PubMed:24523556}.
CC -!- SUBUNIT: Homodimer, and heterodimer with SH3GLB2 (By similarity). Binds
CC BAX; induction of apoptosis augments BAX binding (PubMed:16227588,
CC PubMed:17381077). Binds DNM1, HTT, AMPH, BIN1 and ARFGAP1
CC (PubMed:12456676, PubMed:17086176). Interacts with UVRAG; UVRAG bridges
CC the interaction to BECN1 indicative for an association with the PI3K
CC complex II (PI3KC3-C2) (By similarity). Isoform 3 interacts with
CC PPP1CC; this interaction leads to the inhibition of phosphatase
CC activity (PubMed:17381077). {ECO:0000250|UniProtKB:Q9Y371,
CC ECO:0000269|PubMed:12456676, ECO:0000269|PubMed:16227588,
CC ECO:0000269|PubMed:17086176, ECO:0000269|PubMed:17381077}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17381077}. Golgi
CC apparatus membrane {ECO:0000269|PubMed:17086176}; Peripheral membrane
CC protein {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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Endophilin B1a, Bif-1 {ECO:0000303|PubMed:17381077};
CC IsoId=Q9JK48-1; Sequence=Displayed;
CC Name=2; Synonyms=Endophilin B1b;
CC IsoId=Q9JK48-2; Sequence=VSP_009277;
CC Name=3; Synonyms=Endophilin-B1t {ECO:0000303|PubMed:17381077};
CC IsoId=Q9JK48-3; Sequence=VSP_058266;
CC -!- TISSUE SPECIFICITY: Isoform 1 is widely expressed. Isoform 2 is brain-
CC specific. Isoform 3 is predominantly expressed in testis, but it is
CC also detected in liver and, at much lower levels, in skin, stomach and
CC ovary. {ECO:0000269|PubMed:17381077}.
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 -!- MISCELLANEOUS: Fibroblasts with a reduced level of Sh3glb1 show a
CC defect in retrograde transport between the Golgi apparatus and the
CC endoplasmic reticulum.
CC -!- SIMILARITY: Belongs to the endophilin family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to have lysophosphatidic acid
CC acyltransferase activity, but by homology with SH3GL2/endophilin A1 is
CC unlikely to have this activity. {ECO:0000305|PubMed:12456676}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32237.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF263364; AAF73438.1; -; mRNA.
DR EMBL; AF272946; AAL59846.1; -; mRNA.
DR EMBL; DQ205686; ABA54268.1; -; mRNA.
DR EMBL; AK172959; BAD32237.1; ALT_INIT; mRNA.
DR EMBL; AK029647; BAC26545.1; -; mRNA.
DR EMBL; AK011371; BAB27575.3; -; mRNA.
DR EMBL; AK158415; BAE34495.1; -; mRNA.
DR EMBL; AC134404; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC024362; AAH24362.1; -; mRNA.
DR CCDS; CCDS17885.1; -. [Q9JK48-1]
DR CCDS; CCDS80042.1; -. [Q9JK48-3]
DR CCDS; CCDS80043.1; -. [Q9JK48-2]
DR RefSeq; NP_001268966.1; NM_001282037.1. [Q9JK48-2]
DR RefSeq; NP_001268971.1; NM_001282042.1. [Q9JK48-3]
DR RefSeq; NP_062337.1; NM_019464.3. [Q9JK48-1]
DR PDB; 1X43; NMR; -; A=298-365.
DR PDBsum; 1X43; -.
DR AlphaFoldDB; Q9JK48; -.
DR SMR; Q9JK48; -.
DR BioGRID; 207716; 5.
DR IntAct; Q9JK48; 2.
DR STRING; 10090.ENSMUSP00000129800; -.
DR iPTMnet; Q9JK48; -.
DR PhosphoSitePlus; Q9JK48; -.
DR SwissPalm; Q9JK48; -.
DR REPRODUCTION-2DPAGE; Q9JK48; -.
DR EPD; Q9JK48; -.
DR MaxQB; Q9JK48; -.
DR PaxDb; Q9JK48; -.
DR PeptideAtlas; Q9JK48; -.
DR PRIDE; Q9JK48; -.
DR ProteomicsDB; 257005; -. [Q9JK48-1]
DR ProteomicsDB; 257006; -. [Q9JK48-2]
DR ProteomicsDB; 257007; -. [Q9JK48-3]
DR Antibodypedia; 2824; 559 antibodies from 37 providers.
DR DNASU; 54673; -.
DR Ensembl; ENSMUST00000163279; ENSMUSP00000129800; ENSMUSG00000037062. [Q9JK48-1]
DR Ensembl; ENSMUST00000198254; ENSMUSP00000143312; ENSMUSG00000037062. [Q9JK48-2]
DR Ensembl; ENSMUST00000199531; ENSMUSP00000143433; ENSMUSG00000037062. [Q9JK48-3]
DR GeneID; 54673; -.
DR KEGG; mmu:54673; -.
DR UCSC; uc008rpt.2; mouse. [Q9JK48-1]
DR UCSC; uc008rpw.2; mouse. [Q9JK48-2]
DR CTD; 51100; -.
DR MGI; MGI:1859730; Sh3glb1.
DR VEuPathDB; HostDB:ENSMUSG00000037062; -.
DR eggNOG; KOG3725; Eukaryota.
DR GeneTree; ENSGT00940000155667; -.
DR HOGENOM; CLU_043817_1_1_1; -.
DR InParanoid; Q9JK48; -.
DR OMA; ETTYYAQ; -.
DR OrthoDB; 803053at2759; -.
DR PhylomeDB; Q9JK48; -.
DR TreeFam; TF313281; -.
DR BioGRID-ORCS; 54673; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Sh3glb1; mouse.
DR EvolutionaryTrace; Q9JK48; -.
DR PRO; PR:Q9JK48; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9JK48; protein.
DR Bgee; ENSMUSG00000037062; Expressed in blood and 253 other tissues.
DR ExpressionAtlas; Q9JK48; baseline and differential.
DR Genevisible; Q9JK48; MM.
DR GO; GO:0000421; C:autophagosome membrane; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IC:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0030496; C:midbody; ISO:MGI.
DR GO; GO:0005740; C:mitochondrial envelope; ISO:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR GO; GO:0005504; F:fatty acid binding; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0042171; F:lysophosphatidic acid acyltransferase activity; IDA:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0051084; P:'de novo' post-translational protein folding; IDA:MGI.
DR GO; GO:0006915; P:apoptotic process; ISO:MGI.
DR GO; GO:0048102; P:autophagic cell death; IMP:UniProtKB.
DR GO; GO:0034198; P:cellular response to amino acid starvation; ISO:MGI.
DR GO; GO:0042149; P:cellular response to glucose starvation; ISO:MGI.
DR GO; GO:0090148; P:membrane fission; ISO:MGI.
DR GO; GO:0061024; P:membrane organization; IBA:GO_Central.
DR GO; GO:0007005; P:mitochondrion organization; IMP:UniProtKB.
DR GO; GO:1902254; P:negative regulation of intrinsic apoptotic signaling pathway by p53 class mediator; IMP:UniProtKB.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IDA:MGI.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IDA:MGI.
DR GO; GO:2000786; P:positive regulation of autophagosome assembly; IMP:UniProtKB.
DR GO; GO:0010508; P:positive regulation of autophagy; IMP:UniProtKB.
DR GO; GO:1903861; P:positive regulation of dendrite extension; ISO:MGI.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; ISO:MGI.
DR GO; GO:1902255; P:positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator; IDA:UniProtKB.
DR GO; GO:1903527; P:positive regulation of membrane tubulation; ISO:MGI.
DR GO; GO:0051388; P:positive regulation of neurotrophin TRK receptor signaling pathway; ISO:MGI.
DR GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IMP:UniProtKB.
DR GO; GO:1900740; P:positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; IMP:MGI.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISO:MGI.
DR GO; GO:1903778; P:protein localization to vacuolar membrane; IMP:UniProtKB.
DR GO; GO:0032801; P:receptor catabolic process; ISO:MGI.
DR GO; GO:0032465; P:regulation of cytokinesis; ISO:MGI.
DR GO; GO:2000641; P:regulation of early endosome to late endosome transport; ISO:MGI.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Apoptosis; Coiled coil;
KW Cytoplasm; Cytoplasmic vesicle; Golgi apparatus; Lipid-binding; Membrane;
KW Mitochondrion; Mitochondrion outer membrane; Phosphoprotein;
KW Reference proteome; SH3 domain.
FT CHAIN 1..365
FT /note="Endophilin-B1"
FT /id="PRO_0000146754"
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..186
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"
FT VAR_SEQ 190
FT /note="S -> SQLNSARPEGDNIMIWAEEVTK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12456676"
FT /id="VSP_009277"
FT VAR_SEQ 356..365
FT /note="Missing (in isoform 3)"
FT /id="VSP_058266"
FT CONFLICT 159
FT /note="A -> T (in Ref. 4; BAB27575)"
FT /evidence="ECO:0000305"
FT STRAND 308..314
FT /evidence="ECO:0007829|PDB:1X43"
FT STRAND 331..335
FT /evidence="ECO:0007829|PDB:1X43"
FT STRAND 344..349
FT /evidence="ECO:0007829|PDB:1X43"
FT STRAND 352..357
FT /evidence="ECO:0007829|PDB:1X43"
FT HELIX 358..360
FT /evidence="ECO:0007829|PDB:1X43"
FT STRAND 361..363
FT /evidence="ECO:0007829|PDB:1X43"
SQ SEQUENCE 365 AA; 40855 MW; 1FC02795693142FB CRC64;
MNIMDFNVKK LAADAGTFLS RAVQFTEEKL GQAEKTELDA HLENLLSKAE CTKIWTEKIM
KQTEVLLQPN PNARIEEFVY EKLDRKAPSR INNPELLGQY MIDAGTEFGP GTAYGNALIK
CGETQKRIGT ADRELIQTSA LNFLTPLRNF IEGDYKTIAK ERKLLQNKRL DLDAAKTRLK
KAKAAETKSS SEQELRITQS EFDRQAEITR LLLEGISSTH AHHLRCLNDF VEAQMTYYAQ
CYQYMLDLQK QLGSFPSNYL SNNNQTSGTP VPYALSNAIG PSAQASTGSL VITCPSNLND
LKESSNNRKA RVLYDYDAAN STELSLLADE VITVFSVVGM DSDWLMGERG NQKGKVPITY
LELLN
