ID A0A091QSB1_9GRUI Unreviewed; 249 AA.
AC A0A091QSB1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Endophilin-A2 {ECO:0000256|ARBA:ARBA00040340};
DE AltName: Full=Endophilin-2 {ECO:0000256|ARBA:ARBA00043171};
DE Flags: Fragment;
GN ORFNames=N332_03321 {ECO:0000313|EMBL:KFQ30088.1};
OS Mesitornis unicolor (brown roatelo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Gruiformes; Mesitornithidae; Mesitornis.
OX NCBI_TaxID=54374 {ECO:0000313|EMBL:KFQ30088.1, ECO:0000313|Proteomes:UP000053369};
RN [1] {ECO:0000313|EMBL:KFQ30088.1, ECO:0000313|Proteomes:UP000053369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N332 {ECO:0000313|EMBL:KFQ30088.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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 EMBL; KK802927; KFQ30088.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091QSB1; -.
DR Proteomes; UP000053369; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
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; PR00452; SH3DOMAIN.
DR PRINTS; PR01887; SPECTRNALPHA.
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:UP000053369};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 1..139
FT /note="BAR"
FT /evidence="ECO:0000259|PROSITE:PS51021"
FT DOMAIN 196..249
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 134..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ30088.1"
FT NON_TER 249
FT /evidence="ECO:0000313|EMBL:KFQ30088.1"
SQ SEQUENCE 249 AA; 28321 MW; D06E0CD701CB3883 CRC64;
GDALLDAGES MKRLAEVKDS LDIEVKQNFI DPLQNLCDKD LKEIQHHLKK LEGRRLDFDY
KKKRQGKIPD EELRQAMEKF EESKEVAETS MHNLLETDIE QVSQLSALVD AQLDYHRQAV
QILDELAEKL KRRMREASSR PRREYKPKPR ETYDFGDADQ SNGGFSCNPP PKVSGKGSAG
GPAYLFPPQP LPAAPLDQPC CKALYDFEPE NDGELGFKEG DIITLTNQID ENWYEGMING
QSGFFPLKY
//