SH3G1_BOVIN
ID SH3G1_BOVIN Reviewed; 368 AA.
AC Q2KJA1; Q1JPK1;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Endophilin-A2;
DE AltName: Full=Endophilin-2;
DE AltName: Full=SH3 domain protein 2B;
DE AltName: Full=SH3 domain-containing GRB2-like protein 1;
GN Name=SH3GL1 {ECO:0000312|EMBL:AAI05445.1};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1] {ECO:0000312|EMBL:ABF57308.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2] {ECO:0000312|EMBL:AAI05445.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford {ECO:0000312|EMBL:AAI05445.1};
RC TISSUE=Fetal liver {ECO:0000312|EMBL:AAI05445.1};
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Implicated in endocytosis. May recruit other proteins to
CC membranes with high curvature (By similarity).
CC {ECO:0000250|UniProtKB:O35964}.
CC -!- SUBUNIT: Interacts with ARC, SYNJ1 and DNM1. Interacts with PDCD6IP.
CC Interacts with BIN2 (By similarity). {ECO:0000250}.
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 -!- 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; BT025352; ABF57308.1; -; mRNA.
DR EMBL; BC105444; AAI05445.1; -; mRNA.
DR RefSeq; NP_001039595.1; NM_001046130.2.
DR RefSeq; XP_005208990.1; XM_005208933.2.
DR AlphaFoldDB; Q2KJA1; -.
DR SMR; Q2KJA1; -.
DR STRING; 9913.ENSBTAP00000007890; -.
DR PaxDb; Q2KJA1; -.
DR PRIDE; Q2KJA1; -.
DR Ensembl; ENSBTAT00000007890; ENSBTAP00000007890; ENSBTAG00000006007.
DR GeneID; 512719; -.
DR KEGG; bta:512719; -.
DR CTD; 6455; -.
DR VEuPathDB; HostDB:ENSBTAG00000006007; -.
DR VGNC; VGNC:34572; SH3GL1.
DR eggNOG; KOG1118; Eukaryota.
DR GeneTree; ENSGT00940000154737; -.
DR HOGENOM; CLU_047887_0_0_1; -.
DR InParanoid; Q2KJA1; -.
DR OMA; QYLSETM; -.
DR OrthoDB; 788657at2759; -.
DR TreeFam; TF313281; -.
DR Reactome; R-BTA-182971; EGFR downregulation.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000006007; Expressed in esophagus and 106 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:0005829; C:cytosol; IEA:Ensembl.
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:0042802; F:identical protein binding; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Cell junction; Cell projection; Coiled coil; Cytoplasm; Endocytosis;
KW Endosome; Lipid-binding; Membrane; Phosphoprotein; Reference proteome;
KW SH3 domain.
FT CHAIN 1..368
FT /note="Endophilin-A2"
FT /id="PRO_0000309485"
FT DOMAIN 18..249
FT /note="BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00361"
FT DOMAIN 306..365
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..308
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 284..298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99961"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99961"
FT MOD_RES 298
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99961"
FT MOD_RES 315
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q62419"
FT CONFLICT 285
FT /note="A -> AA (in Ref. 1; ABF57308)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 368 AA; 41455 MW; 58FD0A362875628F CRC64;
MSVAGLKKQF YKASQLVSEK VGGAEGTKLD DDFKEMEKKV DVTSKAVTEV LARTIEYLQP
NPASRAKLTM LNTVSKIRGQ VKNPGYPQSE GLLGECMIRH GKELGGESNF GDALLDAGES
MKRLAEVKDS LDIEVKQNFI DPLQNLCDKD LKEIQHHLKK LEGRRLDFDY KKKRQGKIPD
EELRQAMEKF EESKEVAETS MHHLLETDIE QVSQLSALVD AQLDYHRQAV QILDELADKL
KRRMREASSR PKREYKPKPR ELLDLGEPEQ SNGGFPCAAA PKITASSSFR SSDKPVRTPS
RSMPPLDQPS CKALYDFEPE NDGELGFHEG DIITLTNQID ENWYEGMLDG QSGFFPLSYV
EVLVPLPQ
