ID A0A6J0SZP0_9SAUR Unreviewed; 584 AA.
AC A0A6J0SZP0;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 08-OCT-2025, sequence version 2.
DT 28-JAN-2026, entry version 23.
DE SubName: Full=Bridging integrator 2 isoform X2 {ECO:0000313|RefSeq:XP_020640220.2};
GN Name=BIN2 {ECO:0000313|RefSeq:XP_020640220.2};
OS Pogona vitticeps (central bearded dragon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Acrodonta; Agamidae; Amphibolurinae; Pogona.
OX NCBI_TaxID=103695 {ECO:0000313|Proteomes:UP001652642, ECO:0000313|RefSeq:XP_020640220.2};
RN [1] {ECO:0000313|Proteomes:UP001652642}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG RefSeq;
RL Submitted (MAY-2025) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_020640220.2}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR RefSeq; XP_020640220.2; XM_020784561.2.
DR AlphaFoldDB; A0A6J0SZP0; -.
DR GeneID; 110074418; -.
DR CTD; 51411; -.
DR Proteomes; UP001652642; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0001891; C:phagocytic cup; IEA:TreeGrafter.
DR GO; GO:0002102; C:podosome; IEA:TreeGrafter.
DR GO; GO:0005543; F:phospholipid binding; IEA:TreeGrafter.
DR GO; GO:0006911; P:phagocytosis, engulfment; IEA:TreeGrafter.
DR GO; GO:0097320; P:plasma membrane tubulation; IEA:TreeGrafter.
DR GO; GO:0071800; P:podosome assembly; IEA:TreeGrafter.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 2.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR003005; Amphiphysin.
DR InterPro; IPR004148; BAR_dom.
DR InterPro; IPR048886; Bin2_C.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR46514; AMPHIPHYSIN; 1.
DR PANTHER; PTHR46514:SF1; BRIDGING INTEGRATOR 2; 1.
DR Pfam; PF03114; BAR; 1.
DR Pfam; PF21532; Bin2_C; 1.
DR PRINTS; PR01251; AMPHIPHYSIN.
DR SMART; SM00721; BAR; 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 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP001652642};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 1..193
FT /note="BAR"
FT /evidence="ECO:0000259|PROSITE:PS51021"
FT DOMAIN 512..583
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 227..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 67..139
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 227..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..401
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..471
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 584 AA; 64779 MW; 30F6B4B13E34F2EB CRC64;
MAEGKTGSAG LFAKRVQKQL SRAQEKVLQK LGKTVETKDE QFEQSALNFQ QQQSNDLLWE
DYEEKLADQA VRTMENYLSQ FNEIKERIGK RGRKLVDYDS SRHHLEALQN AKKKDDVKIA
KAEEEFYKAQ AVFEELNKEL REELPVLYSS RIACYVNIFQ NISNLRDIFY KEMSKLNHDL
YDVMSKLEKQ HSNKVFIIKG LSSNRGSLVI SSPVSPTSPA FMLAENSVSE TQASAPDTPS
KHNGEFASAA KTASVPSGVS ETKEEIPASL ATASQSKEED VAKSTLSSVS EPKDENQAMN
LETPLSVSKG TPKKVDEVAN HIAVEILSEA VHEAAGKVQN VSKDSEDTEQ PPSINNIEAD
ETCKEDRGSA PQARDGIPSL LKQEIEHSQD ETQAEESDPE GEVLSLSERS ICPEDNLQDP
SSSIQDQVNR QEVSSTTNGG MTSALPKAGA IQQQKPGTRE ATCQDHEKAE VDSSSDGSME
EIEVSPKVTN TQTISNFFSE DKTEDYVKFP LGFMFKAQAT EAHASEDEDH LQFGEGETIF
VLSDAQAEEQ GFLMGIKERD WKESQDMQQK GIFPPHLIKT VPLE
//
