ID A0A3P9PJY1_POERE Unreviewed; 569 AA.
AC A0A3P9PJY1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Brain-specific angiogenesis inhibitor 1-associated protein 2 {ECO:0000256|ARBA:ARBA00018302};
GN Name=BAIAP2 {ECO:0000313|Ensembl:ENSPREP00000022196.1};
OS Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000022196.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000022196.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000022196.1};
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 RefSeq; XP_008435842.1; XM_008437620.2.
DR AlphaFoldDB; A0A3P9PJY1; -.
DR STRING; 8081.ENSPREP00000022196; -.
DR Ensembl; ENSPRET00000022427.1; ENSPREP00000022196.1; ENSPREG00000014992.1.
DR GeneID; 103481851; -.
DR KEGG; pret:103481851; -.
DR GeneTree; ENSGT00940000153560; -.
DR OMA; KNSYATX; -.
DR OrthoDB; 3059844at2759; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR Bgee; ENSPREG00000014992; Expressed in head.
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 Reference proteome {ECO:0000313|Proteomes:UP000242638};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 8..261
FT /note="IMD"
FT /evidence="ECO:0000259|PROSITE:PS51338"
FT DOMAIN 383..446
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 355..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..560
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 569 AA; 63427 MW; 1EC0389028EBBC0A CRC64;
MVVTDAPARM SRTDEVHRIT ENVYKNIMEQ FNPCLRNFIA MAKSYEKALT SVTFAAKGYF
DALVRMGEMA SESQGSKDLE EAAWDVLFQM AEVHRQIQIQ LEEMLKSFHN ELLTELEKKV
ELDARYLNAA LKKYQMEHKS KGESLEKCQA ELKKLRRKSQ GSKHPSKYGD KEMQFVEAIS
NKQSELDNYI AEGYKNALSE ERRRYCFLVD RQCAVAKNSS AYHNKGKELL SQKIPVWQQV
CAEPTKLPDR AMFLAQQMSG AAGGVPPGAL HPCISEPISG AKPLPMPPEL AALRAGAAMG
QQRLMDGAMP VMNGAAGGED YQQWMESKVA QGKASPQPQR HGAEVYSNTL PVRKAAPTKS
KTPQLETRTL PRSSSMAAGL ERNGRTRVQA VFSHAAGDNS TLLSFAEGDV ITLLVPEARD
GWHYGENEKT RMRGWFPFSY TRLVSESNGD TMRQLRVHNL HHGKSSSTGN LLEREDMPLP
GPDYGTHTRM SAQSTATLHR QQRPYSVAVP GFPQQGVEEY EPRFPTRSGP PSEPTVEAPA
KPLLPDDDEE HLDEAHYDSL ETSTATESP
//
