BAIP3_HUMAN
ID BAIP3_HUMAN Reviewed; 1187 AA.
AC O94812; A2A2B2; B2RCD7; B4DGS5; B4DIK3; B4DRK9; B4DRP1; E7EUB9; H3BUH8;
AC H3BVI3; H7C2Q1; O94839; Q2M226; Q658J2; Q76N05; Q96RZ3; Q9UJK1;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=BAI1-associated protein 3 {ECO:0000303|PubMed:9790924};
DE Short=BAP3 {ECO:0000303|PubMed:9790924};
DE AltName: Full=Brain-specific angiogenesis inhibitor I-associated protein 3 {ECO:0000303|PubMed:9790924};
GN Name=BAIAP3 {ECO:0000303|PubMed:28626000, ECO:0000312|HGNC:HGNC:948};
GN Synonyms=KIAA0734 {ECO:0000303|PubMed:12168954};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INTERACTION WITH ADGRB1, TISSUE
RP SPECIFICITY, AND VARIANT ALA-582.
RX PubMed=9790924; DOI=10.1006/bbrc.1998.9408;
RA Shiratsuchi T., Oda K., Nishimori H., Suzuki M., Takahashi E., Tokino T.,
RA Nakamura Y.;
RT "Cloning and characterization of BAP3 (BAI-associated protein 3), a C2
RT domain-containing protein that interacts with BAI1.";
RL Biochem. Biophys. Res. Commun. 251:158-165(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3; 4; 5 AND 6), AND
RP VARIANT ALA-582.
RC TISSUE=Brain, and Hippocampus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ALA-582.
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11157797; DOI=10.1093/hmg/10.4.339;
RA Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C.,
RA Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.;
RT "Sequence, structure and pathology of the fully annotated terminal 2 Mb of
RT the short arm of human chromosome 16.";
RL Hum. Mol. Genet. 10:339-352(2001).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-582.
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP 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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP FUNCTION, INTERACTION WITH VAMP3; VAMP4; STX6 AND STX16, SUBCELLULAR
RP LOCATION, AND TOPOLOGY.
RX PubMed=28626000; DOI=10.1083/jcb.201702099;
RA Zhang X., Jiang S., Mitok K.A., Li L., Attie A.D., Martin T.F.J.;
RT "BAIAP3, a C2 domain-containing Munc13 protein, controls the fate of dense-
RT core vesicles in neuroendocrine cells.";
RL J. Cell Biol. 216:2151-2166(2017).
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 (PubMed:28626000). Proposed to play a role in
CC hypothalamic neuronal firing by modulating gamma-aminobutyric acid
CC (GABA)ergic inhibitory neurotransmission (By similarity).
CC {ECO:0000250|UniProtKB:Q80TT2, ECO:0000269|PubMed:28626000}.
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
CC (PubMed:9790924). Interacts with endosomal SNARE proteins VAMP3, VAMP4,
CC STX6 and STX16; this interaction is increased in the presence of
CC calcium (PubMed:28626000). {ECO:0000269|PubMed:28626000,
CC ECO:0000269|PubMed:9790924}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:28626000}.
CC Recycling endosome membrane {ECO:0000269|PubMed:28626000}; Peripheral
CC membrane protein {ECO:0000305|PubMed:28626000}. Late endosome membrane
CC {ECO:0000269|PubMed:28626000}; Peripheral membrane protein
CC {ECO:0000305|PubMed:28626000}. Golgi apparatus, trans-Golgi network
CC membrane {ECO:0000269|PubMed:28626000}; Peripheral membrane protein
CC {ECO:0000305|PubMed:28626000}. Cell membrane
CC {ECO:0000269|PubMed:28626000}; Peripheral membrane protein
CC {ECO:0000305|PubMed:28626000}. Note=Rapidly recruited to the plasma
CC membrane and to Golgi structures in response to increased intracellular
CC calcium concentration. {ECO:0000269|PubMed:28626000}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=O94812-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O94812-2; Sequence=VSP_019231, VSP_019232;
CC Name=3;
CC IsoId=O94812-3; Sequence=VSP_019231, VSP_044673;
CC Name=4;
CC IsoId=O94812-5; Sequence=VSP_019231, VSP_047000;
CC Name=5;
CC IsoId=O94812-6; Sequence=VSP_019231;
CC Name=6;
CC IsoId=O94812-7; Sequence=VSP_019231, VSP_047001;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in brain (PubMed:9790924).
CC Also expressed in nonneural tissues such as breast and testes
CC epithelium (PubMed:12498718). {ECO:0000269|PubMed:12498718,
CC ECO:0000269|PubMed:9790924}.
CC -!- SIMILARITY: Belongs to the unc-13 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA34454.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG57886.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB017111; BAA34710.1; -; Genomic_DNA.
DR EMBL; AB018277; BAA34454.2; ALT_INIT; mRNA.
DR EMBL; AK294744; BAG57886.1; ALT_SEQ; mRNA.
DR EMBL; AK295645; BAG58515.1; -; mRNA.
DR EMBL; AK299309; BAG61321.1; -; mRNA.
DR EMBL; AK299358; BAG61353.1; -; mRNA.
DR EMBL; AK315059; BAG37534.1; -; mRNA.
DR EMBL; AL834321; CAH56376.1; -; mRNA.
DR EMBL; AE006467; AAK61275.1; -; Genomic_DNA.
DR EMBL; AL031709; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471112; EAW85670.1; -; Genomic_DNA.
DR EMBL; BC104966; AAI04967.1; -; mRNA.
DR EMBL; BC112129; AAI12130.1; -; mRNA.
DR CCDS; CCDS10434.1; -. [O94812-1]
DR CCDS; CCDS55978.1; -. [O94812-6]
DR CCDS; CCDS55979.1; -. [O94812-7]
DR CCDS; CCDS58402.1; -. [O94812-3]
DR CCDS; CCDS58403.1; -. [O94812-5]
DR CCDS; CCDS66894.1; -. [O94812-2]
DR PIR; JE0347; JE0347.
DR RefSeq; NP_001186025.1; NM_001199096.1. [O94812-7]
DR RefSeq; NP_001186026.1; NM_001199097.1. [O94812-6]
DR RefSeq; NP_001186027.1; NM_001199098.1. [O94812-3]
DR RefSeq; NP_001186028.1; NM_001199099.1. [O94812-5]
DR RefSeq; NP_001273393.1; NM_001286464.1. [O94812-2]
DR RefSeq; NP_003924.2; NM_003933.4. [O94812-1]
DR AlphaFoldDB; O94812; -.
DR SMR; O94812; -.
DR BioGRID; 114450; 5.
DR IntAct; O94812; 3.
DR MINT; O94812; -.
DR STRING; 9606.ENSP00000324510; -.
DR iPTMnet; O94812; -.
DR PhosphoSitePlus; O94812; -.
DR BioMuta; BAIAP3; -.
DR jPOST; O94812; -.
DR MassIVE; O94812; -.
DR PaxDb; O94812; -.
DR PeptideAtlas; O94812; -.
DR PRIDE; O94812; -.
DR ProteomicsDB; 18396; -.
DR ProteomicsDB; 188; -.
DR ProteomicsDB; 42936; -.
DR ProteomicsDB; 43226; -.
DR ProteomicsDB; 45064; -.
DR ProteomicsDB; 50452; -. [O94812-1]
DR ProteomicsDB; 50453; -. [O94812-2]
DR Antibodypedia; 23051; 141 antibodies from 25 providers.
DR DNASU; 8938; -.
DR Ensembl; ENST00000324385.9; ENSP00000324510.5; ENSG00000007516.14. [O94812-1]
DR Ensembl; ENST00000397488.6; ENSP00000380625.2; ENSG00000007516.14. [O94812-2]
DR Ensembl; ENST00000421665.6; ENSP00000409533.2; ENSG00000007516.14. [O94812-7]
DR Ensembl; ENST00000426824.8; ENSP00000407242.4; ENSG00000007516.14. [O94812-6]
DR Ensembl; ENST00000562208.5; ENSP00000458134.1; ENSG00000007516.14. [O94812-3]
DR Ensembl; ENST00000568887.5; ENSP00000457644.1; ENSG00000007516.14. [O94812-5]
DR Ensembl; ENST00000628027.2; ENSP00000487275.1; ENSG00000007516.14. [O94812-2]
DR GeneID; 8938; -.
DR KEGG; hsa:8938; -.
DR MANE-Select; ENST00000426824.8; ENSP00000407242.4; NM_001199097.2; NP_001186026.1. [O94812-6]
DR UCSC; uc002clj.4; human. [O94812-1]
DR CTD; 8938; -.
DR DisGeNET; 8938; -.
DR GeneCards; BAIAP3; -.
DR HGNC; HGNC:948; BAIAP3.
DR HPA; ENSG00000007516; Group enriched (brain, pituitary gland).
DR MIM; 604009; gene.
DR neXtProt; NX_O94812; -.
DR OpenTargets; ENSG00000007516; -.
DR PharmGKB; PA25252; -.
DR VEuPathDB; HostDB:ENSG00000007516; -.
DR eggNOG; KOG1328; Eukaryota.
DR GeneTree; ENSGT00730000110939; -.
DR HOGENOM; CLU_003295_2_0_1; -.
DR InParanoid; O94812; -.
DR OMA; NTNGIQY; -.
DR OrthoDB; 72416at2759; -.
DR PhylomeDB; O94812; -.
DR TreeFam; TF315526; -.
DR PathwayCommons; O94812; -.
DR SignaLink; O94812; -.
DR BioGRID-ORCS; 8938; 11 hits in 1068 CRISPR screens.
DR GeneWiki; BAIAP3; -.
DR GenomeRNAi; 8938; -.
DR Pharos; O94812; Tbio.
DR PRO; PR:O94812; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; O94812; protein.
DR Bgee; ENSG00000007516; Expressed in right uterine tube and 133 other tissues.
DR ExpressionAtlas; O94812; baseline and differential.
DR Genevisible; O94812; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0055038; C:recycling endosome membrane; IDA:UniProtKB.
DR GO; GO:0099503; C:secretory vesicle; IBA:GO_Central.
DR GO; GO:0032588; C:trans-Golgi network membrane; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; IDA:UniProtKB.
DR GO; GO:0000149; F:SNARE binding; IDA:UniProtKB.
DR GO; GO:0019905; F:syntaxin binding; IPI:UniProtKB.
DR GO; GO:1990502; P:dense core granule maturation; IMP:UniProtKB.
DR GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IPI:MGI.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:UniProtKB.
DR GO; GO:0001956; P:positive regulation of neurotransmitter secretion; IMP:UniProtKB.
DR GO; GO:1905413; P:regulation of dense core granule exocytosis; IDA:UniProtKB.
DR GO; GO:0032228; P:regulation of synaptic transmission, GABAergic; ISS:UniProtKB.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IDA: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 Alternative splicing; Calcium; Cell membrane; Cytoplasm; Endosome;
KW Exocytosis; Golgi apparatus; Membrane; Metal-binding; Reference proteome;
KW Repeat; Transport.
FT CHAIN 1..1187
FT /note="BAI1-associated protein 3"
FT /id="PRO_0000064819"
FT DOMAIN 176..335
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 663..784
FT /note="MHD1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00587"
FT DOMAIN 888..996
FT /note="MHD2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00588"
FT DOMAIN 1010..1136
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 55..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 211
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 217
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 295
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 297
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1040
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1041
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1041
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1047
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1105
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1105
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1107
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1107
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1107
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1110
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1113
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1113
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT VAR_SEQ 1..35
FT /note="Missing (in isoform 2, isoform 3, isoform 4, isoform
FT 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_019231"
FT VAR_SEQ 108
FT /note="E -> EAWGSPCRQSPHPGPHTQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_019232"
FT VAR_SEQ 136..163
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047000"
FT VAR_SEQ 136..158
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044673"
FT VAR_SEQ 355..390
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047001"
FT VARIANT 582
FT /note="D -> A (in dbSNP:rs1132356)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005,
FT ECO:0000269|PubMed:9790924"
FT /id="VAR_026667"
FT VARIANT 879
FT /note="S -> I (in dbSNP:rs36074509)"
FT /id="VAR_050687"
FT CONFLICT 216
FT /note="S -> G (in Ref. 4; BAG61321)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="S -> G (in Ref. 4; BAG57886)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="M -> T (in Ref. 4; BAG61353)"
FT /evidence="ECO:0000305"
FT CONFLICT 422
FT /note="E -> G (in Ref. 4; BAG61353)"
FT /evidence="ECO:0000305"
FT CONFLICT 599
FT /note="V -> L (in Ref. 4; BAG61321)"
FT /evidence="ECO:0000305"
FT CONFLICT O94812-2:87
FT /note="P -> T (in Ref. 5; CAH56376)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1187 AA; 131901 MW; E38EF36E91BE7DEB CRC64;
MRPRGAAFAA GPPGDLHLGT AIGFAGAIWR SRSPAMSTLL DIKSSVLRQV QVCPSFRRRT
EQDPGSASAD PQEPATGAWK PGDGVEFFAH MRLMLKKGEG RQGLPCLEVP LRSGSPAPPE
PVDPSLGLRA LAPEEVEMLY EEALYTVLYR AGTMGPDQVD DEEALLSYLQ QVFGTSLEEH
TEAIERVRKA KAPTYALKVS VMRAKNLLAK DPNGFSDPYC MLGILPASDA TREPRAQKEQ
RFGFRKGSKR GGPLPAKCIQ VTEVKSSTLN PVWKEHFLFE IEDVSTDQLH LDIWDHDDDV
SLVEACRKLN EVIGLKGMGR YFKQIVKSAR ANGTAGPTED HTDDFLGCLN IPVREVPVAG
VDRWFKLEPR SSASRVQGHC HLVLKLITTQ RDTAMSQRGR SGFLSHLLLL SHLLRLEHSA
EEPNSSSWRG ELSTPAATIL CLHGAQSNLS PLQLAVLHWQ VSSRHHQTCT LDYSYLLGLL
EDMQAHWEEA PSLPQEQEES LADSLSAFSE FGLQLLRQLR DYFPATNSTA VHRLELLLKC
LGKLQLFQPS FEICPFESEL NMDIAAALKR GNREWYDRIL NDKSPREQPG PQRLPGLVVL
ADAVYDDLQF CYSVYASLFH SILNVDVFTL TFRQLERLVA EEAWVLTEEL SPKMTLEVAS
GLFELYLTLA DLQRFWDSIP GRDSRSLALA GIHAPFLPAV KLWFQVLRDQ AKWRLQGAVD
MDTLEPVDAS SRHSSSAATA GLCLSHIQEL WVRLAWPDPA QAQGLGTQLG QDVCEATLFY
TELLRKKVDT QPGAAGEAVS EALCVVLNNV ELVRKAAGQA LKGLAWPEGA TGPEGVLPRP
LLSCTQALDD DLQREAHTVT AHLTSKMVGD IRKYVQHISL SPDSIQNDEA VAPLMKYLDE
KLALLNASLV KGNLSRVLEA LWELLLQAIL QALGANRDVS ADFYSRFHFT LEALVSFFHA
EGQGLPLESL RDGSYKRLKE ELRLHKCSTR ECIEQFYLDK LKQRTLEQNR FGRLSVRCHY
EAAEQRLAVE VLHAADLLPL DANGLSDPFV IVELGPPHLF PLVRSQRTQV KTRTLHPVYD
ELFYFSVPAE ACRRRAACVL FTVMDHDWLS TNDFAGEAAL GLGGVTGVAR PQVGGGARAG
QPVTLHLCRP RAQVRSALRR LEGRTSKEAQ EFVKKLKELE KCMEADP
