SH3G3_CHICK
ID SH3G3_CHICK Reviewed; 353 AA.
AC Q8AXU9;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Endophilin-A3;
DE AltName: Full=Endophilin-3;
DE AltName: Full=SH3 domain-containing GRB2-like protein 3;
DE AltName: Full=SH3p13;
GN Name=SH3GL3 {ECO:0000250|UniProtKB:O35180};
GN Synonyms=SH3P13 {ECO:0000312|EMBL:CAD27937.1};
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:0000305, ECO:0000312|EMBL:CAD27937.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, INTERACTION WITH SYNJ1 AND DNM1, AND DISRUPTION PHENOTYPE.
RC TISSUE=Brain {ECO:0000312|EMBL:CAD27937.1};
RX PubMed=12606338; DOI=10.1095/biolreprod.102.012427;
RA Hirayama S., Bajari T.M., Nimpf J., Schneider W.J.;
RT "Receptor-mediated chicken oocyte growth: differential expression of
RT endophilin isoforms in developing follicles.";
RL Biol. Reprod. 68:1850-1860(2003).
CC -!- FUNCTION: Implicated in endocytosis. May recruit other proteins to
CC membranes with high curvature (By similarity). Implicated in
CC endocytosis of yolk proteins during oogenesis.
CC {ECO:0000250|UniProtKB:O35180, ECO:0000269|PubMed:12606338}.
CC -!- SUBUNIT: Interacts with ARC (By similarity). Interacts with SYNJ1 and
CC DNM1. {ECO:0000250|UniProtKB:O35180, ECO:0000269|PubMed:12606338}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O35180}. Early
CC endosome membrane {ECO:0000250|UniProtKB:O35180}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:O35180}. Note=Associated with
CC postsynaptic endosomes in hippocampal neurons.
CC {ECO:0000250|UniProtKB:O35180}.
CC -!- TISSUE SPECIFICITY: Highest level in a region associated with
CC endocytosis of yolk proteins in developing oocytes (at protein level).
CC Highest level in small ovarian follicles. High levels in brain and
CC testis. Lower level in adrenal glands. {ECO:0000269|PubMed:12606338}.
CC -!- DEVELOPMENTAL STAGE: Expressed in early stages of follicle development
CC up to large white follicles with highest level in small white
CC follicles. {ECO:0000269|PubMed:12606338}.
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|UniProtKB:O35179}.
CC -!- DISRUPTION PHENOTYPE: Hens express reduced levels of SH3GL3 in ovarian
CC follicles prior to uptake of yolk proteins.
CC {ECO:0000269|PubMed:12606338}.
CC -!- SIMILARITY: Belongs to the endophilin family. {ECO:0000255}.
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DR EMBL; AJ439352; CAD27937.1; -; mRNA.
DR RefSeq; NP_989859.1; NM_204528.1.
DR AlphaFoldDB; Q8AXU9; -.
DR SMR; Q8AXU9; -.
DR BioGRID; 675495; 4.
DR STRING; 9031.ENSGALP00000009724; -.
DR PaxDb; Q8AXU9; -.
DR GeneID; 395201; -.
DR KEGG; gga:395201; -.
DR CTD; 6457; -.
DR VEuPathDB; HostDB:geneid_395201; -.
DR eggNOG; KOG1118; Eukaryota.
DR InParanoid; Q8AXU9; -.
DR OrthoDB; 788657at2759; -.
DR PhylomeDB; Q8AXU9; -.
DR PRO; PR:Q8AXU9; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IBA:GO_Central.
DR GO; GO:0098793; C:presynapse; IBA:GO_Central.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0016191; P:synaptic vesicle uncoating; IBA:GO_Central.
DR CDD; cd07615; BAR_Endophilin_A3; 1.
DR CDD; cd11803; SH3_Endophilin_A; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR004148; BAR_dom.
DR InterPro; IPR028501; Endophilin-A.
DR InterPro; IPR032469; Endophilin-A3_BAR.
DR InterPro; IPR035824; Endophilin_A_SH3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR14167:SF45; PTHR14167:SF45; 1.
DR Pfam; PF03114; BAR; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
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 Coiled coil; Cytoplasm; Endocytosis; Endosome; Lipid-binding; Membrane;
KW Reference proteome; SH3 domain.
FT CHAIN 1..353
FT /note="Endophilin-A3"
FT /id="PRO_0000309488"
FT DOMAIN 18..249
FT /note="BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00361"
FT DOMAIN 291..350
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..21
FT /note="Membrane-binding amphipathic helix"
FT /evidence="ECO:0000250|UniProtKB:O35179"
FT REGION 60..87
FT /note="Required for dimerization upon membrane association"
FT /evidence="ECO:0000250|UniProtKB:O35179"
FT REGION 218..254
FT /note="Interaction with ARC"
FT /evidence="ECO:0000250|UniProtKB:O35964"
FT COILED 180..201
FT /evidence="ECO:0000255"
SQ SEQUENCE 353 AA; 40005 MW; 4512C0731DD3768C CRC64;
MSVAGLKKQF HKASQLFSEK ISGAEGTKLD EEFQEMERKI DVTNKAVAEL LSKSTEYLQP
NPAYRAKLGM LNTMSKIRGQ VKTTGYPQTE GLLGDCMIRY GRELGDDSMF GLALLDAGES
MKQMAEVKDS LDINVKQNFI DPLQLLQDKD LKEIGHHLKK LEGRRLDYDY KKKRLGKIPD
EEVKQAVEKF EESKELAERS MFNFLENDVE QVSQLAVFVE AALDYHKQST EILEDLQSKL
QNRINVASSR PKREFKPKPV ITTTLETGDN QQHNGIAYSS SIKSSGSSMH VDQPCCQALY
DFEPENEGEL GFKEGDIITL TNQIDENWYE GMLNGESGFF PHNYVEVMVP LPQ
