Reviewed, UniProtKB/Swiss-Prot O60242 (BAI3_HUMAN)

Names and origin

Protein names

Recommended name:
    Brain-specific angiogenesis inhibitor 3

Gene names

Name:	BAI3
Synonyms:	KIAA0550

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1522 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Might be involved in angiogenesis inhibition and suppression of glioblastoma.
Subcellular location	Cell membrane; Multi-pass membrane protein.
Tissue specificity	Strongly expressed in brain. Also detected in heart. Reduced expression is observed in some glioblastoma cell lines.
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.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Coding sequence diversity	Polymorphism
Domain	Repeat Signal Transmembrane
Molecular function	G-protein coupled receptor Receptor Transducer
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	neuropeptide signaling pathway Inferred from electronic annotation. Source: InterPro
Cellular component	integral to membrane Traceable author statement. Source: GDB plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	brain-specific angiogenesis inhibitor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 24	24	Potential
	Chain	25 – 1522	1498	Brain-specific angiogenesis inhibitor 3		PRO_0000012865
Regions
	Topological domain	25 – 880	856	Extracellular Potential
	Transmembrane	881 – 901	21	1 Potential
	Topological domain	902 – 910	9	Cytoplasmic Potential
	Transmembrane	911 – 931	21	2 Potential
	Topological domain	932 – 939	8	Extracellular Potential
	Transmembrane	940 – 960	21	3 Potential
	Topological domain	961 – 981	21	Cytoplasmic Potential
	Transmembrane	982 – 1002	21	4 Potential
	Topological domain	1003 – 1023	21	Extracellular Potential
	Transmembrane	1024 – 1044	21	5 Potential
	Topological domain	1045 – 1098	54	Cytoplasmic Potential
	Transmembrane	1099 – 1119	21	6 Potential
	Topological domain	1120 – 1125	6	Extracellular Potential
	Transmembrane	1126 – 1146	21	7 Potential
	Topological domain	1147 – 1522	376	Cytoplasmic Potential
	Domain	30 – 159	130	CUB
	Domain	291 – 343	53	TSP type-1 1
	Domain	345 – 398	54	TSP type-1 2
	Domain	400 – 453	54	TSP type-1 3
	Domain	455 – 508	54	TSP type-1 4
	Domain	816 – 868	53	GPS
	Compositional bias	942 – 945	4	Poly-Thr
	Compositional bias	1173 – 1176	4	Poly-Ser
Amino acid modifications
	Modified residue	619	1	Phosphoserine Ref.7
	Modified residue	1220	1	Phosphoserine By similarity
	Modified residue	1411	1	Phosphoserine By similarity
	Glycosylation	51	1	N-linked (GlcNAc...) Potential
	Glycosylation	54	1	N-linked (GlcNAc...) Potential
	Glycosylation	82	1	N-linked (GlcNAc...) Potential
	Glycosylation	105	1	N-linked (GlcNAc...) Potential
	Glycosylation	241	1	N-linked (GlcNAc...) Potential
	Glycosylation	337	1	N-linked (GlcNAc...) Potential
	Glycosylation	418	1	N-linked (GlcNAc...) Potential
	Glycosylation	540	1	N-linked (GlcNAc...) Potential
	Glycosylation	625	1	N-linked (GlcNAc...) Potential
	Glycosylation	779	1	N-linked (GlcNAc...) Potential
	Glycosylation	812	1	N-linked (GlcNAc...) Potential
	Glycosylation	828	1	N-linked (GlcNAc...) Potential
	Glycosylation	937	1	N-linked (GlcNAc...) Potential
	Disulfide bond	30 ↔ 55		By similarity
	Disulfide bond	303 ↔ 336		By similarity
	Disulfide bond	307 ↔ 342		By similarity
	Disulfide bond	318 ↔ 326		By similarity
	Disulfide bond	357 ↔ 392		By similarity
	Disulfide bond	361 ↔ 397		By similarity
	Disulfide bond	372 ↔ 382		By similarity
	Disulfide bond	412 ↔ 447		By similarity
	Disulfide bond	416 ↔ 452		By similarity
	Disulfide bond	427 ↔ 437		By similarity
	Disulfide bond	467 ↔ 502		By similarity
	Disulfide bond	471 ↔ 507		By similarity
	Disulfide bond	482 ↔ 492		By similarity
Natural variations
	Natural variant	503	1	S → N: dbSNP rs1932618. Ref.4 Ref.5		VAR_046525

Sequences

	Sequence		Length	Mass (Da)
	O60242-1 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: D22D0A5D4BB62502	FASTA	1,522	171,491
	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 RCSEQRCPAP 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

References

	« Hide 'large scale' referencesShow '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: 9533023] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. 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: 9628581] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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: 12168954] [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. , 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: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ASN-503.
[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. , 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], VARIANT ASN-503.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-619, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB005299 mRNA. Translation: BAA25363.1. AB011122 mRNA. Translation: BAA25476.2. Different initiation. AL133378 , AL158051, AL160401, AL356117, AL359714, AL391807 Genomic DNA. Translation: CAC34969.2. AL359714 , AL133378, AL158051, AL160401, AL356117, AL391807 Genomic DNA. Translation: CAH71522.1. AL356117 , AL133378, AL158051, AL160401, AL359714, AL391807 Genomic DNA. Translation: CAH71772.1. AL160401 , AL133378, AL158051, AL356117, AL359714, AL391807 Genomic DNA. Translation: CAH73864.1. AL158051 , AL133378, AL160401, AL356117, AL359714, AL391807 Genomic DNA. Translation: CAI19625.1. AL391807 , AL133378, AL158051, AL160401, AL356117, AL359714 Genomic DNA. Translation: CAI21673.1. CH471051 Genomic DNA. Translation: EAW48837.1. BC111720 mRNA. Translation: AAI11721.1.
IPI	IPI00028448.
PIR	T00028. T00326.
RefSeq	NP_001695.1.
UniGene	Hs.13261
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	O60242.
Protein family/group databases
GPCRDB	Search...
PTM databases
PhosphoSite	O60242.
Proteomic databases
PRIDE	O60242.
Genome annotation databases
Ensembl	ENST00000238918; ENSP00000238918; ENSG00000135298; Homo sapiens. [Genome view] ENST00000370598; ENSP00000359630; ENSG00000135298; Homo sapiens. [Genome view]
GeneID	577.
KEGG	hsa:577.
UCSC	uc003pev.2. human.
Organism-specific databases
CTD	577.
GeneCards	GC06P069404.
H-InvDB	HIX0019135.
HGNC	HGNC:945. BAI3.
HPA	HPA015963.
MIM	602684. gene.
PharmGKB	PA25249.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
HOGENOM	HBG714232.
HOVERGEN	O60242.
InParanoid	O60242.
Enzyme and pathway databases
Reactome	REACT_14797. Signaling by GPCR.
Gene expression databases
ArrayExpress	O60242.
Bgee	O60242.
CleanEx	HS_BAI3.
Genevestigator	O60242.
GermOnline	ENSG00000135298. Homo sapiens.
Family and domain databases
InterPro	IPR000859. CUB. IPR017981. GPCR_2-like. IPR008077. GPCR_2_brain-spec_angio_inhib. IPR001879. GPCR_2_extracellular. IPR000832. GPCR_2_secretin-like. IPR017983. GPCR_2_secretin-like_CS. IPR000203. GPS_dom. IPR000884. Thrombospondin_1_rpt. [Graphical view]
Pfam	PF00002. 7tm_2. 1 hit. PF01825. GPS. 1 hit. PF02793. HRM. 1 hit. PF00090. TSP_1. 4 hits. [Graphical view]
PRINTS	PR01694. BAIPRECURSOR. PR00249. GPCRSECRETIN.
SMART	SM00303. GPS. 1 hit. SM00008. HormR. 1 hit. SM00209. TSP1. 4 hits. [Graphical view]
PROSITE	PS01180. CUB. 1 hit. PS00649. G_PROTEIN_RECEP_F2_1. False negative. 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]
ProtoNet	Search...
Other Resources
NextBio	2355.
SOURCE	Search...

Entry information

Entry name

BAI3_HUMAN

Accession

Primary (citable) accession number: O60242
Secondary accession number(s): O60297 , Q2NKN6, Q5VY37, Q9BX54

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	August 1, 1998
Last modified:	December 15, 2009
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.