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Database: UniProt
Entry: A0A3B4D1F2_PYGNA
LinkDB: A0A3B4D1F2_PYGNA
Original site: A0A3B4D1F2_PYGNA 
ID   A0A3B4D1F2_PYGNA        Unreviewed;       535 AA.
AC   A0A3B4D1F2;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Brain-specific angiogenesis inhibitor 1-associated protein 2 {ECO:0000256|ARBA:ARBA00018302};
OS   Pygocentrus nattereri (Red-bellied piranha).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Pygocentrus.
OX   NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000016694.1, ECO:0000313|Proteomes:UP000261440};
RN   [1] {ECO:0000313|Ensembl:ENSPNAP00000016694.1}
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   RefSeq; XP_017561447.1; XM_017705958.1.
DR   AlphaFoldDB; A0A3B4D1F2; -.
DR   Ensembl; ENSPNAT00000025255.1; ENSPNAP00000016694.1; ENSPNAG00000022859.1.
DR   GeneID; 108432239; -.
DR   CTD; 678518; -.
DR   GeneTree; ENSGT00940000153560; -.
DR   OMA; FSHQAKG; -.
DR   OrthoDB; 3059844at2759; -.
DR   Proteomes; UP000261440; 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; 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, ECO:0000256|SAM:Coils};
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          7..256
FT                   /note="IMD"
FT                   /evidence="ECO:0000259|PROSITE:PS51338"
FT   DOMAIN          391..454
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          305..389
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          126..153
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        334..362
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        370..388
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   535 AA;  59440 MW;  273717E1D216F061 CRC64;
     MVWTEDLAMS RTDEVHRITE NVYKTIMEQF NPCLRNFVAM GKNYEKALST VTFAAKGYFD
     ALVRMGELAS ESQGSKDLGD VLFQMAEVHR QIQVQLEEML KSFHTELLSE LEKKVELDAR
     YLTAALKKYQ MEHKSKSESL EKCQAELKKL RRKSQGSKNP SKYNDKELQY VETISSKQSE
     LDTFIAEGYK TALSEERRRY CFLVDRQCAV AKNSSAYHGK GKDLLTQKIP VWQQACSDPN
     KLPERAMLLV QQMASGSSTL LSSPLHSSKG NLVISDPIPG AQPLPVPPEL APFIGGGLGH
     QGRLMGPDGM SLVNGTTGLQ GEDYWGDGGV SQGRPASPQP QSQPQPQRQV SDVYSNTLPV
     RRPQPAKNKA SVGETRTLPR SSSMAAGLEK NGRSRVQAIF SHAAGDNSTL LSFTEGDIIT
     LLVPEARDGW HYGENEKNKM RGWFPFSYTR VLPDSDNDKL KVNLHHGKSS STGNLLERDD
     TSLPMPDYGL TARLLAQSLT QNRPRPYSMA GFTQPAIEDY DSHFAASLGP ELSRF
//
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