BIN2_RAT
ID BIN2_RAT Reviewed; 507 AA.
AC Q68FR2;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Bridging integrator 2;
GN Name=Bin2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=23285027; DOI=10.1371/journal.pone.0052401;
RA Sanchez-Barrena M.J., Vallis Y., Clatworthy M.R., Doherty G.J.,
RA Veprintsev D.B., Evans P.R., McMahon H.T.;
RT "Bin2 is a membrane sculpting N-BAR protein that influences leucocyte
RT podosomes, motility and phagocytosis.";
RL PLoS ONE 7:E52401-E52401(2012).
CC -!- FUNCTION: Promotes cell motility and migration, probably via its
CC interaction with the cell membrane and with podosome proteins that
CC mediate interaction with the cytoskeleton. Modulates membrane curvature
CC and mediates membrane tubulation (By similarity). Plays a role in
CC podosome formation. Inhibits phagocytosis. {ECO:0000250,
CC ECO:0000269|PubMed:23285027}.
CC -!- SUBUNIT: Interacts with BIN1 and ARHGEF7 (via SH3 domain) (By
CC similarity). Homodimer. Interacts with ARHGEF6 (via SH3 domain),
CC SH3GL1, SH3GL2 and SH3GL3. Identified in a complex with ARHGEF6 and
CC GIT2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UBW5}. Cell
CC projection, podosome membrane {ECO:0000269|PubMed:23285027}; Peripheral
CC membrane protein {ECO:0000269|PubMed:23285027}; Cytoplasmic side
CC {ECO:0000269|PubMed:23285027}. Cytoplasm, cell cortex
CC {ECO:0000250|UniProtKB:Q9UBW5}. Cell projection, phagocytic cup
CC {ECO:0000250|UniProtKB:Q9UBW5}. Note=Associates with membranes enriched
CC in phosphoinositides. Detected in the actin-rich cell cortex at the
CC leading edge of migrating cells. Detected at podosomes, at an actin-
CC rich ring-like structure. {ECO:0000250|UniProtKB:Q9UBW5}.
CC -!- TISSUE SPECIFICITY: Detected in spleen, mast cells and macrophages (at
CC protein level). {ECO:0000269|PubMed:23285027}.
CC -!- DOMAIN: The BAR domain mediates dimerization and interaction with
CC membranes enriched in phosphatidylinositides. {ECO:0000250}.
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DR EMBL; BC079406; AAH79406.1; -; mRNA.
DR RefSeq; NP_001012223.1; NM_001012223.1.
DR AlphaFoldDB; Q68FR2; -.
DR SMR; Q68FR2; -.
DR BioGRID; 266251; 1.
DR STRING; 10116.ENSRNOP00000039630; -.
DR iPTMnet; Q68FR2; -.
DR PhosphoSitePlus; Q68FR2; -.
DR PaxDb; Q68FR2; -.
DR PRIDE; Q68FR2; -.
DR GeneID; 366988; -.
DR KEGG; rno:366988; -.
DR UCSC; RGD:1306789; rat.
DR CTD; 51411; -.
DR RGD; 1306789; Bin2.
DR VEuPathDB; HostDB:ENSRNOG00000031930; -.
DR eggNOG; KOG3771; Eukaryota.
DR HOGENOM; CLU_017859_7_0_1; -.
DR InParanoid; Q68FR2; -.
DR OMA; STMQNTH; -.
DR OrthoDB; 1366218at2759; -.
DR PhylomeDB; Q68FR2; -.
DR TreeFam; TF313542; -.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:Q68FR2; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000031930; Expressed in spleen and 19 other tissues.
DR Genevisible; Q68FR2; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR GO; GO:0001891; C:phagocytic cup; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0002102; C:podosome; ISS:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; ISS:UniProtKB.
DR GO; GO:0060326; P:cell chemotaxis; ISS:UniProtKB.
DR GO; GO:0006911; P:phagocytosis, engulfment; ISO:RGD.
DR GO; GO:0097320; P:plasma membrane tubulation; ISS:UniProtKB.
DR GO; GO:0071800; P:podosome assembly; ISS:UniProtKB.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR003005; Amphiphysin.
DR InterPro; IPR004148; BAR_dom.
DR InterPro; IPR028827; BIN2.
DR PANTHER; PTHR46514:SF1; PTHR46514:SF1; 1.
DR Pfam; PF03114; BAR; 1.
DR PRINTS; PR01251; AMPHIPHYSIN.
DR SMART; SM00721; BAR; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR PROSITE; PS51021; BAR; 1.
PE 1: Evidence at protein level;
KW Cell junction; Cell membrane; Cell projection; Coiled coil; Cytoplasm;
KW Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..507
FT /note="Bridging integrator 2"
FT /id="PRO_0000256141"
FT DOMAIN 28..244
FT /note="BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00361"
FT REGION 271..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..350
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBW5"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBW5"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBW5"
FT MOD_RES 439
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3Z6Q9"
FT MOD_RES 445
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 449
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3Z6Q9"
FT MOD_RES 461
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3Z6Q9"
SQ SEQUENCE 507 AA; 55118 MW; 5B6A7DB3FB18F0C8 CRC64;
MAEGKAGGAA GLFAKQMQKK FSRAQEKVLQ KLGKTVETKD ERFEQSASNF YQQQAEGHRL
YKDLKNFLSA VKVMRESSKR VSETLQEIYN SDWDGHEDLK AIVGNNDLLW EDYEEKLADQ
ALRTMENYVS QFSEVKERIA KRGRKLVDYD SARHHLEAVQ NAKKKDEAKM AKAEEDFSKA
QVVFEDLNQE LLEELPVLYN SRIGCYVTVF QNISNLRDVF YREMSKLNHS LYEVMSKLEK
QHSNKVFVVK GLSSSSRRSL VISPPVQTCT AFSPVSPVTS PTSPNALSVT SESESVSATA
EELTSEAVGE DSCESEESLK DEEADEDQSE TSSSEEEEDE DEDEDEEESL AACNGPTPTP
APTPAPASPA AEVKSQEEAA PCSPTSSLGR GQTGKEHSPP GEVVLRARAS SEGAEQSKRT
ASVQRTSAPP SRPPPPKASG GGLSSPPGSA EASKACHPRA SSDASSDPEP PETGEKEGTG
SSGPKEPHAS STKSATQVVS NDENTEL
