ID A0A096MA62_POEFO Unreviewed; 631 AA.
AC A0A096MA62;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Brain-specific angiogenesis inhibitor 1-associated protein 2 {ECO:0000256|ARBA:ARBA00018302};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000028303.1, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000028303.1}
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}. 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 EMBL; AYCK01003736; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A096MA62; -.
DR Ensembl; ENSPFOT00000031105.1; ENSPFOP00000028303.1; ENSPFOG00000008600.2.
DR GeneTree; ENSGT00940000153560; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
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: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; cd11779; SH3_Irsp53_BAIAP2L; 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; 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:SF6; 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, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000028760};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 1..249
FT /note="IMD"
FT /evidence="ECO:0000259|PROSITE:PS51338"
FT DOMAIN 441..514
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 280..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 104..145
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 287..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 631 AA; 69161 MW; BB2D56D2D0D77A97 CRC64;
MSRTEEINKM TENVYKGILD QFNPSLKNFV TMGKHYEKAL TGVTVAAKGY FDALVKLGEL
ASDSQGSKEL GDTLFQMAEV HRQIQVQLED VLKLFHSEML AQLEQKLELD IKYLTATLKK
YQSERRSQSE SIERCQSQLK KLRRKSQGSR HPNKYGDREM QFVELMSRRQ GELDALVATG
YKSALTEERR RYCFLVDRQC CVTKLLINYH SKVRELLSQK LSSWQQSCSQ PTKLPERALN
LLRHTAPQTP GAAGIAEVLR HTKLGTAQPE QRVSVQEVPP LLNGSPHAFR TASSTAAAAP
GSSRGASPQH TSTPLSTSVS PLSDGGPSAS DTATSLLLAS NTSNLSPSLI PSTVMSLSQI
SQSSSSSQGM TLPILHSAPH SPPLSHSAPL SRALTPVQLL HQQKSGDVSA TATLPLPRRP
VSEMRLGGFQ GSSLPRVLPL SGVTHVEALF AHTPGALDGA GGSLGGGACL LHFLPGDNIT
LLISEPRDGW HYGQNERTGR KGWFPFSYTQ PQHSRRDHRE GSLLLSKANS TSTGQLDKLV
SAGLPALTPE SEEERSLPPQ RVSTFRPRPY SMADSNKVRR LNCRASQPRV FYLQITSDLR
ASPPSPTRPN PFAHVRLRKT VTNDRSAPII E
//
