ID A0A3L8SDV8_CHLGU Unreviewed; 402 AA.
AC A0A3L8SDV8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Endophilin-B2 {ECO:0000256|ARBA:ARBA00040331};
DE AltName: Full=SH3 domain-containing GRB2-like protein B2 {ECO:0000256|ARBA:ARBA00042180};
GN ORFNames=DV515_00008836 {ECO:0000313|EMBL:RLW00538.1};
OS Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC Chloebia.
OX NCBI_TaxID=44316 {ECO:0000313|EMBL:RLW00538.1, ECO:0000313|Proteomes:UP000276834};
RN [1] {ECO:0000313|EMBL:RLW00538.1, ECO:0000313|Proteomes:UP000276834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red01 {ECO:0000313|EMBL:RLW00538.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:RLW00538.1};
RX PubMed=30282656;
RA Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT "A non-coding region near Follistatin controls head colour polymorphism in
RT the Gouldian finch.";
RL Proc. R. Soc. B 285:0-0(2018).
CC -!- SUBUNIT: Homodimer, and heterodimer with SH3GLB1.
CC {ECO:0000256|ARBA:ARBA00038771}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the endophilin family.
CC {ECO:0000256|ARBA:ARBA00006697}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RLW00538.1}.
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DR EMBL; QUSF01000027; RLW00538.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L8SDV8; -.
DR STRING; 44316.ENSEGOP00005008285; -.
DR Ensembl; ENSEGOT00005009452; ENSEGOP00005008285; ENSEGOG00005006429.
DR OMA; QMSFYAQ; -.
DR Proteomes; UP000276834; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR CDD; cd07617; BAR_Endophilin_B2; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 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 PANTHER; PTHR14167:SF68; ENDOPHILIN-B2; 1.
DR PANTHER; PTHR14167; SH3 DOMAIN-CONTAINING; 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; BAR/IMD domain-like; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS51021; BAR; 1.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000276834};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 24..287
FT /note="BAR"
FT /evidence="ECO:0000259|PROSITE:PS51021"
FT DOMAIN 342..402
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
SQ SEQUENCE 402 AA; 44758 MW; DEB395F4B396F062 CRC64;
MEFNVKKLAS DAGVFFSRAM QFTEEKLGQA EKTELDAHFE NLLARADCTK NWTEKILRQT
EVLLQPNPSA RVEEFLYEKL DRKVPSRVTN GELLAQYMTE AANDFGPGTP YGKTLIKVGE
TQRRLGAAER EFIRSASISF LTPLRNFLEG DWRTISKERR ILQNRRLDLD ACKARLKKAK
AAEAKAAAVP DFQETRPRNY VLSASASALW SDEVEKAEHE LRLTQTEFDR QAEVTRLLLE
GISSTHVNHL RCLHEFVESQ TNYYAQCYQF MLDLQKQLGR FSGTFVGNAE SASPAAATSS
PAVAAATLPA VPTIPVVPTI VGVPNTVAEG VLNPKEVKPP ASGTRRARVL YDYEAADSTE
LALLADEMIT VYSLPGMDPD WLIGERGNQK GKVPVTYLEL LS
//
