BI2L2_BOVIN
ID BI2L2_BOVIN Reviewed; 529 AA.
AC E1BFE9;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 2;
DE Short=BAI1-associated protein 2-like protein 2;
DE AltName: Full=Planar intestinal- and kidney-specific BAR domain protein;
DE Short=Pinkbar;
GN Name=BAIAP2L2;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19390049; DOI=10.1126/science.1169588;
RG The bovine genome sequencing and analysis consortium;
RT "The genome sequence of taurine cattle: a window to ruminant biology and
RT evolution.";
RL Science 324:522-528(2009).
CC -!- FUNCTION: Phosphoinositides-binding protein that induces the formation
CC of planar or gently curved membrane structures. Binds to
CC phosphoinositides, including to phosphatidylinositol 4,5-bisphosphate
CC (PtdIns(4,5)P2) headgroups. There seems to be no clear preference for a
CC specific phosphoinositide (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Cell junction {ECO:0000250}. Cytoplasmic vesicle
CC membrane {ECO:0000250}. Note=Localizes to RAB13-positive vesicles and
CC to the plasma membrane at intercellular contacts. {ECO:0000250}.
CC -!- DOMAIN: The IMD domain consisting of an antiparallel dimer of three-
CC helix bundles, featuring on one side a positively charged. The N-
CC terminal alpha-helix inserts into the lipid bilayer. Also forms
CC homodimers and homooligomers. The residue Trp-141 is essential for
CC oligomer formation (By similarity). {ECO:0000250}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAFC03031682; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAFC03051115; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; E1BFE9; -.
DR SMR; E1BFE9; -.
DR STRING; 9913.ENSBTAP00000020331; -.
DR PaxDb; E1BFE9; -.
DR eggNOG; ENOG502QW6V; Eukaryota.
DR HOGENOM; CLU_025877_1_1_1; -.
DR InParanoid; E1BFE9; -.
DR TreeFam; TF325648; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0051764; P:actin crosslink formation; IBA:GO_Central.
DR GO; GO:0051017; P:actin filament bundle assembly; IBA:GO_Central.
DR GO; GO:0007009; P:plasma membrane organization; IEA:InterPro.
DR GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; IBA:GO_Central.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IBA:GO_Central.
DR CDD; cd11914; SH3_BAIAP2L2; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR013606; I-BAR_dom.
DR InterPro; IPR027681; IRSp53/IRTKS/Pinkbar.
DR InterPro; IPR030126; Pinkbar.
DR InterPro; IPR035593; Pinkbar_SH3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR14206; PTHR14206; 1.
DR PANTHER; PTHR14206:SF5; PTHR14206:SF5; 1.
DR Pfam; PF08397; IMD; 1.
DR Pfam; PF14604; SH3_9; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51338; IMD; 1.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW Cell junction; Cell membrane; Cytoplasmic vesicle; Lipid-binding; Membrane;
KW Phosphoprotein; Reference proteome; SH3 domain.
FT CHAIN 1..529
FT /note="Brain-specific angiogenesis inhibitor 1-associated
FT protein 2-like protein 2"
FT /id="PRO_0000412902"
FT DOMAIN 1..239
FT /note="IMD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00668"
FT DOMAIN 329..392
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 221..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80Y61"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80Y61"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80Y61"
FT MOD_RES 479
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80Y61"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80Y61"
SQ SEQUENCE 529 AA; 59190 MW; C7E5092C80382399 CRC64;
MAPEMDQFYR STMAIYKSIL EQFNPALENL VYLGNNYLRA FHALSEAAEV YFNAIQKIGE
QALQSSTSQI LGEILVQMSD TQRHLNSDLE VVVQTFHGDL LQHMEKNTKL DMQFIKDSRQ
HYEMEYRHRA ANLEKSMSQL WRMERKRDKN AREMKESVNR LHAQMQAFVS ESQRAAELEE
KRRYRFLAEK HLLLSNTFLQ FFGRARGMLQ NRVLLWKEQS EASRSPSRAH SPGLLGPVLG
PPYPSGRLTP TRLDMPQRAL GEFGSPRSRH GSGSYGPEPA EARSASQLEP DHRRSLPRTP
SASSLYSSST QRSRSNSFGE RPGGGGGGGG ARRVRALVSH SEGANHTLLR FSAGDVVEVL
VPEAQNGWLY GKLEGSSSSG WFPEAYVKPL DELPVNPMNP LNPVTSMNPR SPVNELPSRL
RSYPLRGSHS LDDLLDRPGN STASSDYWDG QSRSRTPSHI PSRTPSPAPT PLPSSRRSSM
GSMGVASDVK KLASWEQQPP ELFPRGTNPF ATVKLRPTVT NDRSAPLIR
