SH3G2_CHICK
ID SH3G2_CHICK Reviewed; 353 AA.
AC Q8AXV1;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Endophilin-A1;
DE AltName: Full=Endophilin-1;
DE AltName: Full=SH3 domain-containing GRB2-like protein 1;
DE AltName: Full=SH3p4;
GN Name=SH3GL2 {ECO:0000250|UniProtKB:O35179};
GN Synonyms=SH3P4 {ECO:0000312|EMBL:CAD27935.1};
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:CAD27935.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INTERACTION WITH SYNJ1
RP AND DNM1.
RC TISSUE=Brain {ECO:0000312|EMBL:CAD27935.1};
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 synaptic vesicle endocytosis. May recruit other
CC proteins to membranes with high curvature (By similarity).
CC {ECO:0000250|UniProtKB:O35179}.
CC -!- SUBUNIT: Monomer; in cytoplasm. Homodimer; when associated with
CC membranes. Associates with MAP4K3. This interaction appears to regulate
CC MAP4K3-mediated JNK activation (By similarity). Interacts with SYNJ1
CC and DNM1. {ECO:0000250|UniProtKB:O35179, ECO:0000269|PubMed:12606338}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O35179}.
CC Membrane {ECO:0000250|UniProtKB:O35179}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O35179}. Early endosome
CC {ECO:0000250|UniProtKB:Q62420}. Presynapse
CC {ECO:0000250|UniProtKB:O35179}.
CC -!- TISSUE SPECIFICITY: Highly expressed in brain.
CC {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. The BAR
CC domain dimer forms a rigid crescent shaped bundle of helices with the
CC pair of second amphipathic helices protruding towards the membrane-
CC binding surface (By similarity). {ECO:0000250|UniProtKB:O35179}.
CC -!- SIMILARITY: Belongs to the endophilin family. {ECO:0000255}.
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DR EMBL; AJ439350; CAD27935.1; -; mRNA.
DR RefSeq; NP_989861.1; NM_204530.1.
DR AlphaFoldDB; Q8AXV1; -.
DR SMR; Q8AXV1; -.
DR BioGRID; 675497; 4.
DR STRING; 9031.ENSGALP00000024312; -.
DR PaxDb; Q8AXV1; -.
DR Ensembl; ENSGALT00000024358; ENSGALP00000024312; ENSGALG00000015096.
DR GeneID; 395203; -.
DR KEGG; gga:395203; -.
DR CTD; 6456; -.
DR VEuPathDB; HostDB:geneid_395203; -.
DR eggNOG; KOG1118; Eukaryota.
DR GeneTree; ENSGT00940000154737; -.
DR HOGENOM; CLU_047887_0_0_1; -.
DR InParanoid; Q8AXV1; -.
DR OMA; XIRQASS; -.
DR OrthoDB; 788657at2759; -.
DR PhylomeDB; Q8AXV1; -.
DR Reactome; R-GGA-177504; Retrograde neurotrophin signalling.
DR Reactome; R-GGA-182971; EGFR downregulation.
DR Reactome; R-GGA-2132295; MHC class II antigen presentation.
DR Reactome; R-GGA-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-GGA-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-GGA-437239; Recycling pathway of L1.
DR Reactome; R-GGA-6807004; Negative regulation of MET activity.
DR Reactome; R-GGA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-GGA-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:Q8AXV1; -.
DR Proteomes; UP000000539; Chromosome Z.
DR Bgee; ENSGALG00000015096; Expressed in cerebellum and 2 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; 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; IPR035824; Endophilin_A_SH3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
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 Cell projection; Coiled coil; Cytoplasm; Endocytosis; Endosome;
KW Lipid-binding; Membrane; Reference proteome; SH3 domain; Synapse.
FT CHAIN 1..353
FT /note="Endophilin-A1"
FT /id="PRO_0000309487"
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..125
FT /note="Binds and tubulates liposomes"
FT /evidence="ECO:0000250|UniProtKB:O35179"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 243..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 181..201
FT /evidence="ECO:0000255"
FT COMPBIAS 243..259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 353 AA; 39934 MW; F21FF31337641018 CRC64;
MSVAGLKKQF HKATQKVSEK VGGAEGTKLD DDFKEMERKV DVTSRAVMEI MAKTIEYLQP
NPASRAKLSM INTMSKIRGQ EKGPGYPQAE ALLADAMLKF GRELGEECNF GPALADVGEA
MKELSEVKDS LDMEVKQNFI DPLQNLHDKD LREIQHHLKK MEGRRLDFDY KKKRQGKLPD
EELRQALEKF DESKEIAESS MFNLLEMDIE QVSQLSALVQ AQLEYHKQAT QILQRVTSKL
EDRIKEASSQ PKREYQPKPR MSLDFTSGGD NTQHNGGISH ATTPKPAGAH MDQPCCRALY
DFEPENEGEL GFKEGDIITL TNQIDENWYE GMLHGQSGFF PINYVDILVP LPN
