SHLB1_CHICK
ID SHLB1_CHICK Reviewed; 366 AA.
AC Q5ZIR1;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Endophilin-B1;
DE AltName: Full=SH3 domain-containing GRB2-like protein B1;
GN Name=SH3GLB1 {ECO:0000250|UniProtKB:Q9Y371}; ORFNames=RCJMB04_24b23;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1] {ECO:0000312|EMBL:CAG32382.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB {ECO:0000312|EMBL:CAG32382.1};
RC TISSUE=Bursa of Fabricius {ECO:0000312|EMBL:CAG32382.1};
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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 (By similarity).
CC {ECO:0000250|UniProtKB:Q9Y371}.
CC -!- SUBUNIT: Homodimer, and heterodimer with SH3GLB2. Binds BAX. Binds
CC DNM1, HTT, AMPH, BIN1 and ARFGAP1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9JK48,
CC ECO:0000250|UniProtKB:Q9Y371}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9JK48, ECO:0000250|UniProtKB:Q9Y371};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q9JK48,
CC ECO:0000250|UniProtKB:Q9Y371}. 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}. Note=Association with the Golgi
CC apparatus depends on the cell type. {ECO:0000250|UniProtKB:Q9JK48,
CC 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 -!- SIMILARITY: Belongs to the endophilin family. {ECO:0000255}.
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DR EMBL; AJ720723; CAG32382.1; -; mRNA.
DR RefSeq; NP_001006534.1; NM_001006534.1.
DR AlphaFoldDB; Q5ZIR1; -.
DR SMR; Q5ZIR1; -.
DR STRING; 9031.ENSGALP00000007174; -.
DR PaxDb; Q5ZIR1; -.
DR Ensembl; ENSGALT00000007186; ENSGALP00000007174; ENSGALG00000006284.
DR GeneID; 424522; -.
DR KEGG; gga:424522; -.
DR CTD; 51100; -.
DR VEuPathDB; HostDB:geneid_424522; -.
DR eggNOG; KOG3725; Eukaryota.
DR GeneTree; ENSGT00940000155667; -.
DR HOGENOM; CLU_043817_1_1_1; -.
DR InParanoid; Q5ZIR1; -.
DR PhylomeDB; Q5ZIR1; -.
DR PRO; PR:Q5ZIR1; -.
DR Proteomes; UP000000539; Chromosome 8.
DR Bgee; ENSGALG00000006284; Expressed in spermatid and 14 other tissues.
DR ExpressionAtlas; Q5ZIR1; baseline and differential.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
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 GO; GO:0061024; P:membrane organization; IBA:GO_Central.
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 Apoptosis; Coiled coil; Cytoplasm; Golgi apparatus; Lipid-binding;
KW Membrane; Mitochondrion; Mitochondrion outer membrane; Reference proteome;
KW SH3 domain.
FT CHAIN 1..366
FT /note="Endophilin-B1"
FT /id="PRO_0000307712"
FT DOMAIN 27..261
FT /note="BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00361"
FT DOMAIN 306..366
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 34..54
FT /evidence="ECO:0000255"
FT COILED 160..185
FT /evidence="ECO:0000255"
SQ SEQUENCE 366 AA; 40795 MW; 9A2588591537F2E1 CRC64;
MNIMDFNMKK LAADAGTFLS RAVQFTEEKL GQAEKTELDA HLENLLSKAE CTKQWTEKIM
KQTEVLLQPN PNARIEEFFY EKLDRKAPSR MNNPELLGQY MIDAGNEFGP GTAYGNALIK
CGETQKQIGT ADRELIQTSA INFLTPLRNF IEGDYKTITK ERKLLQNKRL DLDAAKTRLK
KAKVAEARAA SEQEVRITQS EFDRQAEITR LLLEGISSTH AHHLRCLNDF VEAQMTYYAQ
CYKYMLDLQK QLGSFPSTFL SNNNQSSSAP VQSVSTPSVL ASASASLPSV SNSVVTSGIS
ELKSSSGSRK ARVLYDYDAA NSSELSLLAD EVITVYSIPG MDSDWLMGER GNQKGKVPIT
YLELLN
