BAIP3_MOUSE
ID BAIP3_MOUSE Reviewed; 1134 AA.
AC Q80TT2; E9QQ76; Q6RUT4;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=BAI1-associated protein 3;
DE Short=BAP3;
DE AltName: Full=Brain-specific angiogenesis inhibitor I-associated protein 3 {ECO:0000303|PubMed:23698091};
DE Short=Baiap3 {ECO:0000303|PubMed:23698091};
GN Name=Baiap3 {ECO:0000303|PubMed:12498718, ECO:0000303|PubMed:23698091,
GN ECO:0000312|MGI:MGI:2685783};
GN Synonyms=Gm937, Kiaa0734 {ECO:0000303|PubMed:12693553};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RA Brathwaite M.E., Waeltz P., Qian Y., Dudekula D., Schlessinger D.,
RA Nagaraja R.;
RT "Genomic sequence analysis in the mouse T-complex region.";
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12498718; DOI=10.1016/s1535-6108(02)00205-2;
RA Palmer R.E., Lee S.B., Wong J.C., Reynolds P.A., Zhang H., Truong V.,
RA Oliner J.D., Gerald W.L., Haber D.A.;
RT "Induction of BAIAP3 by the EWS-WT1 chimeric fusion implicates regulated
RT exocytosis in tumorigenesis.";
RL Cancer Cell 2:497-505(2002).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=23698091; DOI=10.2119/molmed.2013.00033;
RA Wojcik S.M., Tantra M., Stepniak B., Man K.N., Mueller-Ribbe K.,
RA Begemann M., Ju A., Papiol S., Ronnenberg A., Gurvich A., Shin Y.,
RA Augustin I., Brose N., Ehrenreich H.;
RT "Genetic markers of a Munc13 protein family member, BAIAP3, are gender
RT specifically associated with anxiety and benzodiazepine abuse in mice and
RT humans.";
RL Mol. Med. 19:135-148(2013).
CC -!- FUNCTION: Functions in endosome to Golgi retrograde transport. In
CC response to calcium influx, may interact with SNARE fusion receptors
CC and membrane phospholipids to mediate endosome fusion with the trans-
CC Golgi network. By promoting the recycling of secretory vesicle
CC transmembrane proteins, it indirectly controls dense-core secretory
CC vesicle biogenesis, maturation and their ability to mediate the
CC constitutive and regulated secretion of neurotransmitters and hormones.
CC May regulate behavior and food intake by controlling calcium-stimulated
CC exocytosis of neurotransmitters including NPY and serotonin and
CC hormones like insulin (By similarity). Proposed to play a role in
CC hypothalamic neuronal firing by modulating gamma-aminobutyric acid
CC (GABA)ergic inhibitory neurotransmission (Probable).
CC {ECO:0000250|UniProtKB:O94812, ECO:0000305|PubMed:23698091}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC Note=Binds 3 Ca(2+) ions per C2 domain. {ECO:0000255|PROSITE-
CC ProRule:PRU00041};
CC -!- SUBUNIT: Interacts with ADGRB1, this interaction is direct. Interacts
CC with endosomal SNARE proteins VAMP3, VAMP4, STX6 and STX16; this
CC interaction is increased in the presence of calcium.
CC {ECO:0000250|UniProtKB:O94812}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12498718}.
CC Recycling endosome membrane {ECO:0000250|UniProtKB:O94812}; Peripheral
CC membrane protein {ECO:0000250|UniProtKB:O94812}. Late endosome membrane
CC {ECO:0000250|UniProtKB:O94812}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O94812}. Golgi apparatus, trans-Golgi network
CC membrane {ECO:0000250|UniProtKB:O94812}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O94812}. Cell membrane
CC {ECO:0000250|UniProtKB:O94812}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O94812}. Note=Rapidly recruited to the plasma
CC membrane and to Golgi structures in response to increased intracellular
CC calcium concentration. {ECO:0000250|UniProtKB:O94812}.
CC -!- TISSUE SPECIFICITY: Prominently expressed in brain structures including
CC hypothalamus, amygdala, stria terminalis and periaqueductal gray (at
CC protein level). Expressed in nonneuronal tissues, including placenta,
CC lung, pancreas, spleen, and testes. Within placenta, expression is
CC restricted to the syncytiotrophoblasts. {ECO:0000269|PubMed:12498718,
CC ECO:0000269|PubMed:23698091}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice are viable, fertile and have overall
CC normal development. Behavioral phenotyping show increased
CC susceptibility to pentylenetetrazole-induced seizures, increased
CC anxiety in females, and benzodiazepine tolerance in males.
CC {ECO:0000269|PubMed:23698091}.
CC -!- SIMILARITY: Belongs to the unc-13 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65640.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK122358; BAC65640.1; ALT_INIT; Transcribed_RNA.
DR EMBL; AY491413; AAS21653.1; -; Genomic_DNA.
DR EMBL; AC122454; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; Q80TT2; -.
DR SMR; Q80TT2; -.
DR STRING; 10090.ENSMUSP00000138188; -.
DR iPTMnet; Q80TT2; -.
DR PhosphoSitePlus; Q80TT2; -.
DR PaxDb; Q80TT2; -.
DR PRIDE; Q80TT2; -.
DR ProteomicsDB; 265202; -.
DR MGI; MGI:2685783; Baiap3.
DR eggNOG; KOG1328; Eukaryota.
DR InParanoid; Q80TT2; -.
DR ChiTaRS; Baiap3; mouse.
DR PRO; PR:Q80TT2; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q80TT2; protein.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0031902; C:late endosome membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
DR GO; GO:0099503; C:secretory vesicle; IBA:GO_Central.
DR GO; GO:0032588; C:trans-Golgi network membrane; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; ISS:UniProtKB.
DR GO; GO:0000149; F:SNARE binding; ISS:UniProtKB.
DR GO; GO:0019905; F:syntaxin binding; ISO:MGI.
DR GO; GO:1990502; P:dense core granule maturation; ISO:MGI.
DR GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IDA:SynGO.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; ISS:UniProtKB.
DR GO; GO:0001956; P:positive regulation of neurotransmitter secretion; ISS:UniProtKB.
DR GO; GO:0050795; P:regulation of behavior; IMP:UniProtKB.
DR GO; GO:1905413; P:regulation of dense core granule exocytosis; ISO:MGI.
DR GO; GO:0032228; P:regulation of synaptic transmission, GABAergic; IMP:UniProtKB.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISS:UniProtKB.
DR Gene3D; 2.60.40.150; -; 2.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR010439; MUN_dom.
DR InterPro; IPR014770; Munc13_1.
DR InterPro; IPR014772; Munc13_dom-2.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF06292; MUN; 1.
DR SMART; SM00239; C2; 2.
DR SUPFAM; SSF49562; SSF49562; 2.
DR PROSITE; PS50004; C2; 2.
DR PROSITE; PS51258; MHD1; 1.
DR PROSITE; PS51259; MHD2; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell membrane; Cytoplasm; Endosome; Exocytosis; Golgi apparatus;
KW Membrane; Metal-binding; Reference proteome; Repeat; Transport.
FT CHAIN 1..1134
FT /note="BAI1-associated protein 3"
FT /id="PRO_0000064820"
FT DOMAIN 139..298
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 610..731
FT /note="MHD1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00587"
FT DOMAIN 835..943
FT /note="MHD2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00588"
FT DOMAIN 957..1083
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 22..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 174
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 180
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 258
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 260
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 987
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 988
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 988
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 994
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1052
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1052
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1054
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1054
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1054
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1057
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1060
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1060
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT CONFLICT 178..179
FT /note="Missing (in Ref. 2; AAS21653)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="Y -> D (in Ref. 2; AAS21653)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="P -> S (in Ref. 1; BAC65640 and 2; AAS21653)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="Q -> R (in Ref. 2; AAS21653)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="S -> N (in Ref. 1; BAC65640 and 2; AAS21653)"
FT /evidence="ECO:0000305"
FT CONFLICT 584
FT /note="G -> R (in Ref. 1; BAC65640)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1134 AA; 127075 MW; F6040BDD91E008E5 CRC64;
MSTLLDIKSS VLRQVQVCPS FRRKTEQEPE VTNSQEPPTG AWKPGDGVEF FAHMRLILKK
GDGRQGLPCP EVLLRSGSPA PAEPVDPNRG LRTLTQEEVE MLYEEALYTV LHRAGTMGPD
QVDDEEVLLS YLQQVFGTSS EEHMEAIMRV KKAKAPTYAL KVSVMRAKNL LAKDPNGFSD
PYCMLGILPA SSAPQEPSGQ KEQRFGFRKG SKRSSPLPAK CIQVTEVKNS TLNPVWKEHF
LFEIDDVNTD QLHLDIWDHD DDVSLAEACR KLNEVIGLKG MTRYFKQIVK SARANGTAGP
TEDHTDDFLG CLNIPIREVP VAGADRWFKL EPRSSASRVQ GDCHLVLKLI TTQRDTVMSQ
RGRSGFLSYL LLLSRVLRFE HRVEEPNSSS WRGELSGPGT TVLCLHGAQS NLSPLQLAVL
HWQVSSRHHQ TRTLDYGYLL GLLEDVQAHW EEAASLPQEQ EESLADSFSA FSEFGLRLLR
QLRDYFPATN STAVYRLELL LKCLEKLQLF QPAFEICPFE TELSMDIAAA LKRGNREWYD
QLLNTKSPRE QPGPQRLAGL VELADIIYED LQLCYGVYAS LFHGQVAEEA WVLTEELSPK
MNLEVASGLF ELYLTLADTQ RFWSCIPGRE SRSLALAGIH TPFLPAVKLW LQVLRDQAKW
RLQGAVDVDT LEPVDAASKH SSSAATASLC LSHIQELWVR LAWPDPSQAQ GLGTQLSQDM
CEASLFYTEL LRKKVDTQPG AAGEAVSEQL CVVLNNVELV RRASGQALRG LAWSEGASGL
EGVLPRPLLS CIQALDEDLH REAHTVTAHL TSKMVADIRK YIQHISLSPD SIQNDEAVAP
LLKYLDEKLA LLNDALVKEN LNRVLEALWE LLLQAILQAL SANRDVSADF YGRFHFTLEA
LVSFFHAEGQ GLPLENLRDG SYKRLQEELR LHKCSTRECI EQFYLDKLKQ RSLEQNRFGR
LTVRCHYEAA EQRLAVEVLH AADLLPLDAN GLSDPFVIVE LGPPHLFPLV RSQRTQVKAR
TLHPVYDELF HFSVPAEACR RRGACVLFTV MDHDWLSTND FAGEAALGLG GISGIARPHV
GGGMRPGQPI TLHLRRPRAQ VRSALRMLEG RTSREAQEFV KKLKELEKCM EADL
