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O60242 (BAI3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Brain-specific angiogenesis inhibitor 3
Gene names
Name:BAI3
Synonyms:KIAA0550
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1522 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May regulate the number of excitatory synapses that are formed on hippocampus neurons. Has no effect on inhibitory synapses. Might be involved in angiogenesis inhibition and suppression of glioblastoma.

Subunit structure

Interacts with C1QL1, C1QL2, C1QL3 and C1QL4. Ref.8

Subcellular location

Cell membrane; Multi-pass membrane protein Ref.8 Ref.9.

Tissue specificity

Strongly expressed in brain. Also detected in heart. Reduced expression is observed in some glioblastoma cell lines.

Post-translational modification

The endogenous protein is proteolytically cleaved into 2 subunits, an extracellular subunit and a seven-transmembrane subunit. Does not undergo autocatalytic cleavage (in vitro). Ref.9

Sequence similarities

Belongs to the G-protein coupled receptor 2 family. LN-TM7 subfamily.

Contains 1 CUB domain.

Contains 1 GPS domain.

Contains 4 TSP type-1 domains.

Sequence caution

The sequence BAA25476.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 15221498Brain-specific angiogenesis inhibitor 3
PRO_0000012865

Regions

Topological domain25 – 880856Extracellular Potential
Transmembrane881 – 90121Helical; Name=1; Potential
Topological domain902 – 9109Cytoplasmic Potential
Transmembrane911 – 93121Helical; Name=2; Potential
Topological domain932 – 9398Extracellular Potential
Transmembrane940 – 96021Helical; Name=3; Potential
Topological domain961 – 98121Cytoplasmic Potential
Transmembrane982 – 100221Helical; Name=4; Potential
Topological domain1003 – 102321Extracellular Potential
Transmembrane1024 – 104421Helical; Name=5; Potential
Topological domain1045 – 109854Cytoplasmic Potential
Transmembrane1099 – 111921Helical; Name=6; Potential
Topological domain1120 – 11256Extracellular Potential
Transmembrane1126 – 114621Helical; Name=7; Potential
Topological domain1147 – 1522376Cytoplasmic Potential
Domain30 – 159130CUB
Domain291 – 34353TSP type-1 1
Domain345 – 39854TSP type-1 2
Domain400 – 45354TSP type-1 3
Domain455 – 50854TSP type-1 4
Domain816 – 86853GPS
Compositional bias942 – 9454Poly-Thr
Compositional bias1173 – 11764Poly-Ser

Amino acid modifications

Modified residue6191Phosphoserine Ref.7
Glycosylation511N-linked (GlcNAc...) Potential
Glycosylation541N-linked (GlcNAc...) Potential
Glycosylation821N-linked (GlcNAc...) Potential
Glycosylation1051N-linked (GlcNAc...) Potential
Glycosylation2411N-linked (GlcNAc...) Potential
Glycosylation3371N-linked (GlcNAc...) Potential
Glycosylation4181N-linked (GlcNAc...) Potential
Glycosylation5401N-linked (GlcNAc...) Ref.9
Glycosylation6251N-linked (GlcNAc...) Ref.9
Glycosylation7791N-linked (GlcNAc...) Potential
Glycosylation8121N-linked (GlcNAc...) Potential
Glycosylation8281N-linked (GlcNAc...) Potential
Glycosylation9371N-linked (GlcNAc...) Potential
Disulfide bond30 ↔ 55 By similarity
Disulfide bond303 ↔ 336 By similarity
Disulfide bond307 ↔ 342 By similarity
Disulfide bond318 ↔ 326 By similarity
Disulfide bond357 ↔ 392 By similarity
Disulfide bond361 ↔ 397 By similarity
Disulfide bond372 ↔ 382 By similarity
Disulfide bond412 ↔ 447 By similarity
Disulfide bond416 ↔ 452 By similarity
Disulfide bond427 ↔ 437 By similarity
Disulfide bond467 ↔ 502 By similarity
Disulfide bond471 ↔ 507 By similarity
Disulfide bond482 ↔ 492 By similarity
Disulfide bond514 ↔ 549 Ref.9
Disulfide bond537 ↔ 567 Ref.9
Disulfide bond819 ↔ 851 Ref.9
Disulfide bond839 ↔ 853 Ref.9

Natural variations

Natural variant5031N → S. Ref.1 Ref.2 Ref.6
Corresponds to variant rs1932618 [ dbSNP | Ensembl ].
VAR_046525

Secondary structure

....................................................... 1522
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O60242 [UniParc].

Last modified November 2, 2010. Version 2.
Checksum: D22D0A5CF59E811F

FASTA1,522171,518
        10         20         30         40         50         60 
MKAVRNLLIY IFSTYLLVMF GFNAAQDFWC STLVKGVIYG SYSVSEMFPK NFTNCTWTLE 

        70         80         90        100        110        120 
NPDPTKYSIY LKFSKKDLSC SNFSLLAYQF DHFSHEKIKD LLRKNHSIMQ LCNSKNAFVF 

       130        140        150        160        170        180 
LQYDKNFIQI RRVFPTNFPG LQKKGEEDQK SFFEFLVLNK VSPSQFGCHV LCTWLESCLK 

       190        200        210        220        230        240 
SENGRTESCG IMYTKCTCPQ HLGEWGIDDQ SLILLNNVVL PLNEQTEGCL TQELQTTQVC 

       250        260        270        280        290        300 
NLTREAKRPP KEEFGMMGDH TIKSQRPRSV HEKRVPQEQA DAAKFMAQTG ESGVEEWSQW 

       310        320        330        340        350        360 
STCSVTCGQG SQVRTRTCVS PYGTHCSGPL RESRVCNNTA LCPVHGVWEE WSPWSLCSFT 

       370        380        390        400        410        420 
CGRGQRTRTR SCTPPQYGGR PCEGPETHHK PCNIALCPVD GQWQEWSSWS QCSVTCSNGT 

       430        440        450        460        470        480 
QQRSRQCTAA AHGGSECRGP WAESRECYNP ECTANGQWNQ WGHWSGCSKS CDGGWERRIR 

       490        500        510        520        530        540 
TCQGAVITGQ QCEGTGEEVR RCNEQRCPAP YEICPEDYLM SMVWKRTPAG DLAFNQCPLN 

       550        560        570        580        590        600 
ATGTTSRRCS LSLHGVAFWE QPSFARCISN EYRHLQHSIK EHLAKGQRML AGDGMSQVTK 

       610        620        630        640        650        660 
TLLDLTQRKN FYAGDLLMSV EILRNVTDTF KRASYIPASD GVQNFFQIVS NLLDEENKEK 

       670        680        690        700        710        720 
WEDAQQIYPG SIELMQVIED FIHIVGMGMM DFQNSYLMTG NVVASIQKLP AASVLTDINF 

       730        740        750        760        770        780 
PMKGRKGMVD WARNSEDRVV IPKSIFTPVS SKELDESSVF VLGAVLYKNL DLILPTLRNY 

       790        800        810        820        830        840 
TVINSKIIVV TIRPEPKTTD SFLEIELAHL ANGTLNPYCV LWDDSKTNES LGTWSTQGCK 

       850        860        870        880        890        900 
TVLTDASHTK CLCDRLSTFA ILAQQPREII MESSGTPSVT LIVGSGLSCL ALITLAVVYA 

       910        920        930        940        950        960 
ALWRYIRSER SIILINFCLS IISSNILILV GQTQTHNKSI CTTTTAFLHF FFLASFCWVL 

       970        980        990       1000       1010       1020 
TEAWQSYMAV TGKIRTRLIR KRFLCLGWGL PALVVATSVG FTRTKGYGTD HYCWLSLEGG 

      1030       1040       1050       1060       1070       1080 
LLYAFVGPAA AVVLVNMVIG ILVFNKLVSR DGILDKKLKH RAGQMSEPHS GLTLKCAKCG 

      1090       1100       1110       1120       1130       1140 
VVSTTALSAT TASNAMASLW SSCVVLPLLA LTWMSAVLAM TDKRSILFQI LFAVFDSLQG 

      1150       1160       1170       1180       1190       1200 
FVIVMVHCIL RREVQDAFRC RLRNCQDPIN ADSSSSFPNG HAQIMTDFEK DVDIACRSVL 

      1210       1220       1230       1240       1250       1260 
HKDIGPCRAA TITGTLSRIS LNDDEEEKGT NPEGLSYSTL PGNVISKVII QQPTGLHMPM 

      1270       1280       1290       1300       1310       1320 
SMNELSNPCL KKENSELRRT VYLCTDDNLR GADMDIVHPQ ERMMESDYIV MPRSSVNNQP 

      1330       1340       1350       1360       1370       1380 
SMKEESKMNI GMETLPHERL LHYKVNPEFN MNPPVMDQFN MNLEQHLAPQ EHMQNLPFEP 

      1390       1400       1410       1420       1430       1440 
RTAVKNFMAS ELDDNAGLSR SETGSTISMS SLERRKSRYS DLDFEKVMHT RKRHMELFQE 

      1450       1460       1470       1480       1490       1500 
LNQKFQTLDR FRDIPNTSSM ENPAPNKNPW DTFKNPSEYP HYTTINVLDT EAKDALELRP 

      1510       1520 
AEWEKCLNLP LDVQEGDFQT EV 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of BAI2 and BAI3, novel genes homologous to brain-specific angiogenesis inhibitor 1 (BAI1)."
Shiratsuchi T., Nishimori H., Ichise H., Nakamura Y., Tokino T.
Cytogenet. Cell Genet. 79:103-108(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-503.
Tissue: Fetal brain.
[2]"Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-503.
Tissue: Brain.
[3]"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION TO 643-665 AND C-TERMINUS.
[4]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-503.
[7]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-619, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"The cell-adhesion G protein-coupled receptor BAI3 is a high-affinity receptor for C1q-like proteins."
Bolliger M.F., Martinelli D.C., Sudhof T.C.
Proc. Natl. Acad. Sci. U.S.A. 108:2534-2539(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH C1QL1; C1QL2; C1QL3 AND C1QL4.
[9]"A novel evolutionarily conserved domain of cell-adhesion GPCRs mediates autoproteolysis."
Arac D., Boucard A.A., Bolliger M.F., Nguyen J., Soltis S.M., Sudhof T.C., Brunger A.T.
EMBO J. 31:1364-1378(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 498-868, PROTEOLYTIC PROCESSING, GLYCOSYLATION AT ASN-540 AND ASN-625, DISULFIDE BONDS, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB005299 mRNA. Translation: BAA25363.1.
AB011122 mRNA. Translation: BAA25476.2. Different initiation.
AL133378 expand/collapse EMBL AC list , AL158051, AL160401, AL356117, AL359714, AL391807 Genomic DNA. Translation: CAC34969.2.
AL359714 expand/collapse EMBL AC list , AL133378, AL158051, AL160401, AL356117, AL391807 Genomic DNA. Translation: CAH71522.1.
AL356117 expand/collapse EMBL AC list , AL133378, AL158051, AL160401, AL359714, AL391807 Genomic DNA. Translation: CAH71772.1.
AL160401 expand/collapse EMBL AC list , AL133378, AL158051, AL356117, AL359714, AL391807 Genomic DNA. Translation: CAH73864.1.
AL158051 expand/collapse EMBL AC list , AL133378, AL160401, AL356117, AL359714, AL391807 Genomic DNA. Translation: CAI19625.1.
AL391807 expand/collapse EMBL AC list , AL133378, AL158051, AL160401, AL356117, AL359714 Genomic DNA. Translation: CAI21673.1.
CH471051 Genomic DNA. Translation: EAW48837.1.
BC111720 mRNA. Translation: AAI11721.1.
PIRT00028.
T00326.
RefSeqNP_001695.1. NM_001704.2.
XP_005248809.1. XM_005248752.1.
UniGeneHs.13261.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4DLOX-ray2.30A/B498-868[»]
ProteinModelPortalO60242.
SMRO60242. Positions 508-866.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107053. 1 interaction.
DIPDIP-56121N.
IntActO60242. 1 interaction.
STRING9606.ENSP00000238918.

Protein family/group databases

MEROPSS63.030.
GPCRDBSearch...

PTM databases

PhosphoSiteO60242.

Proteomic databases

PaxDbO60242.
PRIDEO60242.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000370598; ENSP00000359630; ENSG00000135298.
GeneID577.
KEGGhsa:577.
UCSCuc003pev.4. human.

Organism-specific databases

CTD577.
GeneCardsGC06P069404.
HGNCHGNC:945. BAI3.
HPAHPA015963.
MIM602684. gene.
neXtProtNX_O60242.
PharmGKBPA25249.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG146816.
HOGENOMHOG000230916.
HOVERGENHBG004813.
InParanoidO60242.
KOK04598.
OMALPTLRNY.
OrthoDBEOG7KDF90.
PhylomeDBO60242.
TreeFamTF331634.

Gene expression databases

ArrayExpressO60242.
BgeeO60242.
CleanExHS_BAI3.
GenevestigatorO60242.

Family and domain databases

InterProIPR000859. CUB_dom.
IPR022624. DUF3497.
IPR017981. GPCR_2-like.
IPR008077. GPCR_2_brain-spec_angio_inhib.
IPR001879. GPCR_2_extracellular_dom.
IPR000832. GPCR_2_secretin-like.
IPR017983. GPCR_2_secretin-like_CS.
IPR000203. GPS.
IPR000884. Thrombospondin_1_rpt.
[Graphical view]
PfamPF00002. 7tm_2. 1 hit.
PF12003. DUF3497. 1 hit.
PF01825. GPS. 1 hit.
PF02793. HRM. 1 hit.
PF00090. TSP_1. 4 hits.
[Graphical view]
PRINTSPR01694. BAIPRECURSOR.
PR00249. GPCRSECRETIN.
SMARTSM00303. GPS. 1 hit.
SM00008. HormR. 1 hit.
SM00209. TSP1. 4 hits.
[Graphical view]
SUPFAMSSF82895. SSF82895. 4 hits.
PROSITEPS01180. CUB. 1 hit.
PS00650. G_PROTEIN_RECEP_F2_2. 1 hit.
PS50227. G_PROTEIN_RECEP_F2_3. 1 hit.
PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
PS50221. GPS. 1 hit.
PS50092. TSP1. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSBAI3. human.
GeneWikiBrain-specific_angiogenesis_inhibitor_3.
GenomeRNAi577.
NextBio2355.
PROO60242.
SOURCESearch...

Entry information

Entry nameBAI3_HUMAN
AccessionPrimary (citable) accession number: O60242
Secondary accession number(s): O60297 expand/collapse secondary AC list , Q2NKN6, Q5VY37, Q9BX54
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 2, 2010
Last modified: April 16, 2014
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries