SH3G1_CHICK
ID SH3G1_CHICK Reviewed; 367 AA.
AC Q8AXV0;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Endophilin-A2;
DE AltName: Full=Endophilin-2;
DE AltName: Full=SH3 domain-containing GRB2-like protein 2;
DE AltName: Full=SH3p8;
GN Name=SH3GL1 {ECO:0000250|UniProtKB:O35964};
GN Synonyms=SH3P8 {ECO:0000312|EMBL:CAD27936.1};
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:CAD27936.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP INTERACTION WITH SYNJ1 AND DNM1.
RC TISSUE=Brain {ECO:0000312|EMBL:CAD27936.1};
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).
CC {ECO:0000250|UniProtKB:O35180}.
CC -!- SUBUNIT: Interacts with ARC (By similarity). Interacts with SYNJ1 and
CC DNM1. {ECO:0000250|UniProtKB:O35964, ECO:0000269|PubMed:12606338}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O35964}. Early
CC endosome membrane {ECO:0000250|UniProtKB:O35964}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:O35964}. Cell projection, podosome
CC {ECO:0000250}. Note=Associated with postsynaptic endosomes in
CC hippocampal neurons. {ECO:0000250|UniProtKB:O35964}.
CC -!- TISSUE SPECIFICITY: Highest level in central region of the theca of
CC developing follicles (at protein level). Expressed at highest level in
CC brain and testis, at high level in kidney, lung and stroma, low level
CC in spleen and adrenal gland (at protein level). Expressed in most
CC tissue with highest levels in small ovarian follicles, brain and
CC testis. {ECO:0000269|PubMed:12606338}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout follicle development with
CC highest level in small white follicles. Expressed in granulosa cells,
CC theca cells and post-ovulatory sacs of developing follicles.
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.
CC {ECO:0000250|UniProtKB:O35179}.
CC -!- SIMILARITY: Belongs to the endophilin family. {ECO:0000255}.
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DR EMBL; AJ439351; CAD27936.1; -; mRNA.
DR RefSeq; NP_989860.1; NM_204529.1.
DR AlphaFoldDB; Q8AXV0; -.
DR SMR; Q8AXV0; -.
DR BioGRID; 675496; 4.
DR STRING; 9031.ENSGALP00000001688; -.
DR PaxDb; Q8AXV0; -.
DR GeneID; 395202; -.
DR KEGG; gga:395202; -.
DR CTD; 6455; -.
DR VEuPathDB; HostDB:geneid_395202; -.
DR eggNOG; KOG1118; Eukaryota.
DR HOGENOM; CLU_047887_0_0_1; -.
DR InParanoid; Q8AXV0; -.
DR OrthoDB; 788657at2759; -.
DR PhylomeDB; Q8AXV0; -.
DR TreeFam; TF313281; -.
DR PRO; PR:Q8AXV0; -.
DR Proteomes; UP000000539; Unplaced.
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:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IBA:GO_Central.
DR GO; GO:0002102; C:podosome; 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; IPR028501; Endophilin-A.
DR InterPro; IPR035824; Endophilin_A_SH3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR14167:SF63; PTHR14167:SF63; 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 Cell junction; Cell projection; Coiled coil; Cytoplasm; Endocytosis;
KW Endosome; Lipid-binding; Membrane; Reference proteome; SH3 domain.
FT CHAIN 1..367
FT /note="Endophilin-A2"
FT /id="PRO_0000309486"
FT DOMAIN 18..249
FT /note="BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00361"
FT DOMAIN 305..364
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 REGION 243..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 181..250
FT /evidence="ECO:0000255"
FT COMPBIAS 243..265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 367 AA; 41732 MW; 6FE55BFD418D3053 CRC64;
MSVAGLKKQF YKASQLVSEK VGGAEGTKLD DDFKEMEKKV DLTSKAVTEV LTRTIEYLQP
NPASRAKLTM LNTMSKIRGQ VKNPGYPQSE GLLGESMIRY GKELGEDSNF GDALLDAGES
MKRLAEVKDS LDIEVKQNFI DPLQNLCDKD LKEIQHHLKK LEGRRLDFDY KKKRQGKIPD
EELRQAMEKF EESKEVAETS MHNLLETDIE QVSQLSALVD AQLDYHRQAV QILDELAEKL
KRRMREASSR PRREYKPKPR ETYDFGESDQ SNGGFSCTPT PKVSASSSFR SDKPFRTSVR
SIPHLDQPCC KALYDFEPEN DGELGFKEGD IITLTNQIDE NWYEGMINGQ SGFFPLNYVE
VLVPLPQ
