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Database: UniProt
Entry: K7DSH5_PANTR
LinkDB: K7DSH5_PANTR
Original site: K7DSH5_PANTR 
ID   K7DSH5_PANTR            Unreviewed;       521 AA.
AC   K7DSH5; A0A2J8JGF8;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=Brain-specific angiogenesis inhibitor 1-associated protein 2 {ECO:0000256|ARBA:ARBA00018302};
GN   Name=BAIAP2 {ECO:0000313|EMBL:JAA41527.1,
GN   ECO:0000313|Ensembl:ENSPTRP00000067105.1, ECO:0000313|VGNC:VGNC:9131};
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598 {ECO:0000313|EMBL:JAA41527.1};
RN   [1] {ECO:0000313|Ensembl:ENSPTRP00000067105.1, ECO:0000313|Proteomes:UP000002277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16136131; DOI=10.1038/nature04072;
RG   Chimpanzee sequencing and analysis consortium;
RT   "Initial sequence of the chimpanzee genome and comparison with the human
RT   genome.";
RL   Nature 437:69-87(2005).
RN   [2] {ECO:0000313|EMBL:JAA41527.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Skeletal muscle {ECO:0000313|EMBL:JAA41527.1}, Skin
RC   {ECO:0000313|EMBL:JAA25001.1}, and Smooth vascular
RC   {ECO:0000313|EMBL:JAA16597.1};
RA   Maudhoo M.D., Meehan D.T., Norgren R.B.Jr.;
RT   "De novo assembly of the reference chimpanzee transcriptome from NextGen
RT   mRNA sequences.";
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSPTRP00000067105.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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   EMBL; AACZ04061189; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; GABF01005548; JAA16597.1; -; mRNA.
DR   EMBL; GABD01008099; JAA25001.1; -; mRNA.
DR   EMBL; GABE01003212; JAA41527.1; -; mRNA.
DR   RefSeq; XP_016788609.1; XM_016933120.1.
DR   Ensembl; ENSPTRT00000079091.1; ENSPTRP00000067105.1; ENSPTRG00000009750.5.
DR   GeneID; 454951; -.
DR   CTD; 10458; -.
DR   VGNC; VGNC:9131; BAIAP2.
DR   GeneTree; ENSGT00940000153560; -.
DR   OrthoDB; 3059844at2759; -.
DR   Proteomes; UP000002277; Chromosome 17.
DR   Bgee; ENSPTRG00000009750; Expressed in temporal lobe and 20 other cell types or tissues.
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   2: Evidence at transcript level;
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:UP000002277};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          1..250
FT                   /note="IMD"
FT                   /evidence="ECO:0000259|PROSITE:PS51338"
FT   DOMAIN          374..437
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          296..369
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        322..367
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   521 AA;  57329 MW;  9D2DC6D5087C849B CRC64;
     MSLSRSEEMH RLTENVYKTI MEQFNPSLRN FIAMGKNYEK ALAGVTYAAK GYFDALVKMG
     ELASESQGSK ELGDVLFQMA EVHRQIQNQL EEMLKSFHNE LLTQLEQKVE LDSRYLSAAL
     KKYQTEQRSK GDALDKCQAE LKKLRKKSQG SKNPQKYSDK ELQYIDAISN KQGELENYVS
     DGYKTALTEE RRRFCFLVEK QCAVAKNSAA YHSKGKELLA QKLPLWQQAC ADPSKIPERA
     VQLMQQVASN GATLPSALSA SKSNLVISDP IPGAKPLPVP PELAPFVGRM SAQESTPIMN
     GVAGPDGEDY SPWADRKAAQ PKSLSPPQSQ SKLSDSYSNT LPVRKSVTPK NSYATTENKT
     LPRSSSMAAG LERNGRMRVK AIFSHAAGDN STLLSFKEGD LITLLVPEAR DGWHYGESEK
     TKMRGWFPFS YTRVLDSDGS DRLHMSLQQG KSSSTGNLLD KDDLAIPPPD YGAASRAFPA
     QTASGFKQRP YSVAVPAFSQ GLDDYGARSM SSGSGTLVST V
//
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