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Database: UniProt
Entry: A0A093PQZ4_9PASS
LinkDB: A0A093PQZ4_9PASS
Original site: A0A093PQZ4_9PASS 
ID   A0A093PQZ4_9PASS        Unreviewed;       484 AA.
AC   A0A093PQZ4;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Brain-specific angiogenesis inhibitor 1-associated protein 2 {ECO:0000256|ARBA:ARBA00018302};
DE   Flags: Fragment;
GN   ORFNames=N305_07934 {ECO:0000313|EMBL:KFW79233.1};
OS   Manacus vitellinus (golden-collared manakin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Pipridae; Manacus.
OX   NCBI_TaxID=328815 {ECO:0000313|EMBL:KFW79233.1, ECO:0000313|Proteomes:UP000053258};
RN   [1] {ECO:0000313|EMBL:KFW79233.1, ECO:0000313|Proteomes:UP000053258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N305 {ECO:0000313|EMBL:KFW79233.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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   EMBL; KL670490; KFW79233.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093PQZ4; -.
DR   STRING; 328815.ENSMVIP00005018122; -.
DR   Proteomes; UP000053258; 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: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; PF07653; SH3_2; 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   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053258};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          1..232
FT                   /note="IMD"
FT                   /evidence="ECO:0000259|PROSITE:PS51338"
FT   DOMAIN          358..421
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          282..356
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          425..470
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        310..355
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        425..443
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFW79233.1"
FT   NON_TER         484
FT                   /evidence="ECO:0000313|EMBL:KFW79233.1"
SQ   SEQUENCE   484 AA;  53684 MW;  36B65306B9CE9C19 CRC64;
     TIMEQFNPSL RNFISMGKTY EKALASMTYA AKGYFDALVK MGELASESQG SKELGDVLFQ
     MAEVHRQIQN QLEEMLKSFH NELLTQLEQK VELDSRYLSA ALKKYQTEQR SKGDSLDKCQ
     AELKKLRKKS QGSKNPQKYS DKELQYIEAI SNKQGELENY VSDGYKTALT EERRRFCFLV
     EKQCAVAKSA ITYHAKGKEM LTQKLPLWQE SCSDPNKIPD RAIQLMQQMA ASSNGTIMPS
     PLSTSKSNLI ISDPIPGAKP LPVPPELAPF VGRMSAQEAM PVMNGVSGPD SDGYNHWSEM
     KPAQPKSLSP PQPQKQLSDS YSNTLPVRKN VPPKNSYASA ENKTLPRSSS MAAGLERNGR
     TRVQAIFSHA AGDNSTLLSF KEGDLITLLV PEARDGWHYG ESEKTKMRGW FPFSYTRVLD
     NDGSERVHTS LQQGKSSSTG NLLDKDDIAI PPPDYGMASQ AFPAQGGSTF KQRPYSVAVP
     ALSQ
//
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