ID   BAIP2_BOVIN             Reviewed;         521 AA.
AC   Q5EAD0;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   24-JAN-2024, entry version 124.
DE   RecName: Full=Brain-specific angiogenesis inhibitor 1-associated protein 2;
DE            Short=BAI-associated protein 2;
DE            Short=BAI1-associated protein 2;
GN   Name=BAIAP2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. Interacts with CDC42 and RAC1 that have been
CC       activated by GTP binding. Interacts with ATN1, ADGRB1, DIAPH1, EPS8,
CC       SHANK1, SHANK2, SHANK3, TIAM1, WASF1 and WASF2. Interacts with ENAH
CC       after recruitment of CDC42 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}. Cell projection, filopodium
CC       {ECO:0000250}. Cell projection, ruffle {ECO:0000250}. Cytoplasm,
CC       cytoskeleton {ECO:0000250}. Note=Detected throughout the cytoplasm in
CC       the absence of specific binding partners. Detected in filopodia and
CC       close to membrane ruffles. Recruited to actin pedestals that are formed
CC       upon infection by bacteria at bacterial attachment sites (By
CC       similarity). {ECO:0000250}.
CC   -!- DOMAIN: The IMD domain forms a coiled coil. The isolated domain can
CC       induce actin bundling and filopodia formation. In the absence of G-
CC       proteins intramolecular interaction between the IMD and the SH3 domain
CC       gives rise to an auto-inhibited state of the protein. Interaction of
CC       the IMD with RAC1 or CDC42 leads to activation (By similarity).
CC       {ECO:0000250}.
CC   -!- DOMAIN: The SH3 domain interacts with ATN1, ADGRB1, WASF1, WASF2,
CC       SHANK1, DIAPH1 and ENAH. {ECO:0000250}.
CC   -!- PTM: Phosphorylated on tyrosine residues by INSR in response to insulin
CC       treatment. {ECO:0000250}.
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DR   EMBL; BT020639; AAX08656.1; -; mRNA.
DR   RefSeq; NP_001017937.1; NM_001017937.1.
DR   RefSeq; XP_015314409.1; XM_015458923.1.
DR   AlphaFoldDB; Q5EAD0; -.
DR   SMR; Q5EAD0; -.
DR   STRING; 9913.ENSBTAP00000040235; -.
DR   PaxDb; 9913-ENSBTAP00000040235; -.
DR   Ensembl; ENSBTAT00000025350.5; ENSBTAP00000025350.4; ENSBTAG00000019044.5.
DR   Ensembl; ENSBTAT00000078735.1; ENSBTAP00000061820.1; ENSBTAG00000019044.5.
DR   GeneID; 507837; -.
DR   KEGG; bta:507837; -.
DR   CTD; 10458; -.
DR   VEuPathDB; HostDB:ENSBTAG00000019044; -.
DR   VGNC; VGNC:26412; BAIAP2.
DR   eggNOG; ENOG502QUM6; Eukaryota.
DR   GeneTree; ENSGT00940000153560; -.
DR   InParanoid; Q5EAD0; -.
DR   Reactome; R-BTA-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR   Reactome; R-BTA-4420097; VEGFA-VEGFR2 Pathway.
DR   Reactome; R-BTA-5663213; RHO GTPases Activate WASPs and WAVEs.
DR   Reactome; R-BTA-9013149; RAC1 GTPase cycle.
DR   Reactome; R-BTA-9013423; RAC3 GTPase cycle.
DR   Proteomes; UP000009136; Chromosome 19.
DR   Bgee; ENSBTAG00000019044; Expressed in esophagus and 101 other cell types or tissues.
DR   ExpressionAtlas; Q5EAD0; baseline and differential.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR   GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR   GO; GO:0008093; F:cytoskeletal anchor activity; IEA:InterPro.
DR   GO; GO:0070064; F:proline-rich region binding; ISS:UniProtKB.
DR   GO; GO:0051764; P:actin crosslink formation; ISS:UniProtKB.
DR   GO; GO:0051017; P:actin filament bundle assembly; ISS:UniProtKB.
DR   GO; GO:0007009; P:plasma membrane organization; IEA:InterPro.
DR   GO; GO:0030838; P:positive regulation of actin filament polymerization; IBA:GO_Central.
DR   GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISS:UniProtKB.
DR   GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
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; Coiled coil; Cytoplasm; Cytoskeleton; Membrane;
KW   Phosphoprotein; Reference proteome; SH3 domain.
FT   CHAIN           1..521
FT                   /note="Brain-specific angiogenesis inhibitor 1-associated
FT                   protein 2"
FT                   /id="PRO_0000064814"
FT   DOMAIN          1..250
FT                   /note="IMD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00668"
FT   DOMAIN          375..438
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   REGION          297..370
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          450..471
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          132..153
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        318..368
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         262
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UQB8"
FT   MOD_RES         324
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UQB8"
FT   MOD_RES         326
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UQB8"
FT   MOD_RES         337
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UQB8"
FT   MOD_RES         341
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UQB8"
FT   MOD_RES         347
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UQB8"
FT   MOD_RES         361
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UQB8"
FT   MOD_RES         367
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UQB8"
FT   MOD_RES         385
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UQB8"
FT   MOD_RES         396
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BKX1"
FT   MOD_RES         455
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UQB8"
SQ   SEQUENCE   521 AA;  57566 MW;  283D43FE6B9FD1D7 CRC64;
     MSLSRSEEMH RLTENVYKTI MEQFNPSLRN FIAMGKNYEK ALAGVTYAAK GYFDALVKMG
     ELASESQGSK ELGDVLFQMA EVHRQIQNQL EEMLKSFHNE LLTQLEQKVE LDSRYLSAAL
     KKYQTEQRSK GDALDKCQAE LKKLRKKSQG SKNPQKYSDK ELQYIDAIGN KQGELESYVS
     DGYKTALTEE RRRFCFLVEK QCAVAKNSAA YHSKGKELLA QKLPLWQQAC ADPNKIPDRA
     VQLMQQMGNS NGSILPSGLS ASKSNLVISD PIPGAKPLPV PPELAPFVGR LSAQENAPVM
     NGVSGPDSED YNPWADRKAT QPKSTSPPQS QSKLSDSYSN TLPVRKSVAP KNSYATTENK
     TLPRSSSMAA GLERNGRMRV KAIFSHAAGD NSTLLSFKEG DLITLLVPEA RDGWHYGESE
     KTKMRGWFPF SYTRVLDNDG GDRLHMSLQQ GKSSSTGNLL DKEDLALPPP DYGTSSRAFP
     TQTAGAFKQR PYSVAVPAFS QGLDDYGARA VSSADVEVAR F
//