ID A0A3Q3LHL2_9TELE Unreviewed; 349 AA.
AC A0A3Q3LHL2;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Endophilin-A2 {ECO:0000256|ARBA:ARBA00040340};
DE AltName: Full=Endophilin-2 {ECO:0000256|ARBA:ARBA00043171};
OS Mastacembelus armatus (zig-zag eel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000013638.1, ECO:0000313|Proteomes:UP000261640};
RN [1] {ECO:0000313|Ensembl:ENSMAMP00000013638.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Implicated in endocytosis. May recruit other proteins to
CC membranes with high curvature. {ECO:0000256|ARBA:ARBA00024839}.
CC -!- SUBCELLULAR LOCATION: Cell projection, podosome
CC {ECO:0000256|ARBA:ARBA00004188}. Cytoplasm
CC {ECO:0000256|ARBA:ARBA00004496}. Early endosome membrane
CC {ECO:0000256|ARBA:ARBA00004220}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004220}. Endosome membrane
CC {ECO:0000256|ARBA:ARBA00004481}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004481}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the endophilin family.
CC {ECO:0000256|ARBA:ARBA00006697}.
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DR AlphaFoldDB; A0A3Q3LHL2; -.
DR Ensembl; ENSMAMT00000014015.2; ENSMAMP00000013638.1; ENSMAMG00000009226.2.
DR GeneTree; ENSGT00940000154737; -.
DR Proteomes; UP000261640; Unplaced.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0002102; C:podosome; IEA:UniProtKB-SubCell.
DR CDD; cd07592; BAR_Endophilin_A; 1.
DR CDD; cd11803; SH3_Endophilin_A; 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; IPR035824; Endophilin_A_SH3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR14167:SF63; ENDOPHILIN-A2; 1.
DR PANTHER; PTHR14167; SH3 DOMAIN-CONTAINING; 1.
DR Pfam; PF03114; BAR; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00499; P67PHOX.
DR PRINTS; PR00452; SH3DOMAIN.
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 Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Reference proteome {ECO:0000313|Proteomes:UP000261640};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 18..249
FT /note="BAR"
FT /evidence="ECO:0000259|PROSITE:PS51021"
FT DOMAIN 287..346
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 243..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 349 AA; 39572 MW; EC7CA3F6CD4375EC CRC64;
MSVAGFKKQF YKASQLMSEK VGGAEGTKLD EDFKDLERRA DVTSKAVVEV INKTSEYLQP
NPASRAKLSM LNTVSKIRGQ VKSPGYPQPE GLLGECMTKY GRDMGEDTNF GGALIDVGES
MKRMAEVKDS LDIDVKQNFI DPLQAVAEKD IKDIQHHLKK LEGRRLDYDY KKKRQGKIHD
EEIRQALEKF HESKEMAESS MYNLLETDVE QVSELSSFVE SLLQYHRQAS QILEELSSKL
RERVNDAQNR PRREYTPKPR QTFEYEETEQ SNGGYSPAAA SPPAYSPADP CCKALYDFDP
ENDGELGFHE GDIITLVSRI DENWFQGTLH GKSGYFPNNY VEVVVPLPH
//