ID A0A3B3V217_9TELE Unreviewed; 497 AA.
AC A0A3B3V217;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Brain-specific angiogenesis inhibitor 1-associated protein 2 {ECO:0000256|ARBA:ARBA00018302};
OS Poecilia latipinna (sailfin molly).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000019790.1, ECO:0000313|Proteomes:UP000261500};
RN [1] {ECO:0000313|Ensembl:ENSPLAP00000019790.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Adapter protein that links membrane-bound small G-proteins to
CC cytoplasmic effector proteins. Necessary for CDC42-mediated
CC reorganization of the actin cytoskeleton and for RAC1-mediated membrane
CC ruffling. Involved in the regulation of the actin cytoskeleton by WASF
CC family members and the Arp2/3 complex. Plays a role in neurite growth.
CC Acts syngeristically with ENAH to promote filipodia formation. Plays a
CC role in the reorganization of the actin cytoskeleton in response to
CC bacterial infection. Participates in actin bundling when associated
CC with EPS8, promoting filopodial protrusions.
CC {ECO:0000256|ARBA:ARBA00025545}.
CC -!- SUBCELLULAR LOCATION: Cell projection, filopodium
CC {ECO:0000256|ARBA:ARBA00004486}. Cell projection, ruffle
CC {ECO:0000256|ARBA:ARBA00004466}. Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
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DR AlphaFoldDB; A0A3B3V217; -.
DR Ensembl; ENSPLAT00000015161.1; ENSPLAP00000019790.1; ENSPLAG00000002215.1.
DR GeneTree; ENSGT00940000153560; -.
DR Proteomes; UP000261500; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR GO; GO:0008093; F:cytoskeletal anchor activity; IEA:InterPro.
DR GO; GO:0007009; P:plasma membrane organization; IEA:InterPro.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IEA:InterPro.
DR CDD; cd07646; I-BAR_IMD_IRSp53; 1.
DR CDD; cd11915; SH3_Irsp53; 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; IPR013606; I-BAR_dom.
DR InterPro; IPR027681; IRSp53/IRTKS/Pinkbar.
DR InterPro; IPR030128; IRSp53_I-BAR_dom.
DR InterPro; IPR035594; Irsp53_SH3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR14206; BRAIN-SPECIFIC ANGIOGENESIS INHIBITOR 1-ASSOCIATED PROTEIN 2; 1.
DR PANTHER; PTHR14206:SF3; BRAIN-SPECIFIC ANGIOGENESIS INHIBITOR 1-ASSOCIATED PROTEIN 2; 1.
DR Pfam; PF08397; IMD; 1.
DR Pfam; PF14604; SH3_9; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS51338; IMD; 1.
DR PROSITE; PS50002; SH3; 1.
PE 4: Predicted;
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 1..251
FT /note="IMD"
FT /evidence="ECO:0000259|PROSITE:PS51338"
FT DOMAIN 350..413
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 318..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 497 AA; 54934 MW; 466518F42ED5DB42 CRC64;
CFSQNTEEVH SYWEDYPHPT IMEQFNPCLR NFVAMGKNYE KALANVTFAA KGYFDALVRM
GELASESQGS KDLGDVLFQM AEVHRQIQVQ LEEMLKCFHN ELLSELEKKV DLDARYLTAA
LKKYQLEHKS KGESLEKCQG ELKKLRRKSQ GSKNPSKYGE KEMQFVETIS NKQTELDTFI
AEGYKTALSE ERRRYCFLVD RQCAVAKNSS AYHGKGKDLL TQKIPVWQQA CSDPNKLPDR
AMLLAQQMGS AALGGTSPLH SSKSNLVISD PIPGAQPLPV PPELAVFMGS GLGHPAAQGQ
SQVQPQRQVS DVYSNTLPVR RPAPAKNKNP VGETRTLPRS SSMAAGLEKN GRSRVQAIFS
HAAGDNSTLL SFSEGDVITL LVPEARDGWH YGENEKNKMR GWFPFSYTRV LMSFCSSSLH
HGKSSSTGNL LESDTSLPTP DYGLTARLLA QSLAQTRPRP YSMAGFAPQV LLNVASMKCA
DCTTVALVCL ICSIHLS
//
