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Q3UHD1 (BAI1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Brain-specific angiogenesis inhibitor 1
Gene names
Name:Bai1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1582 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Likely to be a potent inhibitor of angiogenesis in brain and may play a significant role as a mediator of the p53 signal in suppression of glioblastoma. May function in cell adhesion and signal transduction in the brain By similarity. Ref.4 Ref.5

Subunit structure

Interacts with MAGI1, MAGI3, BAIAP2 and PHYHIP By similarity. Interacts with ELMO1 and DOCK1. When bound to ELMO1 and DOCK1, it may act as a module to promote the engulfment. Ref.1 Ref.5

Subcellular location

Cell membrane; Multi-pass membrane protein By similarity. Note: Likely to be concentrated at cell-cell adhesion sites By similarity.

Tissue specificity

Specifically expressed in brain. Ref.1

Developmental stage

Observed only on embryonic brain not in other tissues. Ref.1

Domain

The TSP1 repeats inhibit in vivo angiogenesis in rat cornea induced by BFGF.

Post-translational modification

The endogenous protein is proteolytically cleaved into 2 subunits, an extracellular subunit and a seven-transmembrane subunit By similarity.

Sequence similarities

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

Contains 1 GPS domain.

Contains 5 TSP type-1 domains.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Select]
Isoform 1 (identifier: Q3UHD1-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q3UHD1-2)

The sequence of this isoform is not available.
Note: Observed very weakly in the kidney, skeletal muscle, skin, stomach, thymus and brain from embryonic day 18. By neonatal day 1, the expression is targeted only to the brain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3333 Potential
Chain34 – 15821549Brain-specific angiogenesis inhibitor 1
PRO_0000245046

Regions

Topological domain34 – 948915Extracellular Potential
Transmembrane949 – 96921Helical; Name=1; Potential
Topological domain970 – 98011Cytoplasmic Potential
Transmembrane981 – 100121Helical; Name=2; Potential
Topological domain1002 – 10087Extracellular Potential
Transmembrane1009 – 102921Helical; Name=3; Potential
Topological domain1030 – 105223Cytoplasmic Potential
Transmembrane1053 – 107321Helical; Name=4; Potential
Topological domain1074 – 109320Extracellular Potential
Transmembrane1094 – 111421Helical; Name=5; Potential
Topological domain1115 – 113622Cytoplasmic Potential
Transmembrane1137 – 115721Helical; Name=6; Potential
Topological domain1158 – 11669Extracellular Potential
Transmembrane1167 – 118721Helical; Name=7; Potential
Topological domain1188 – 1582395Cytoplasmic Potential
Domain261 – 31555TSP type-1 1
Domain354 – 40754TSP type-1 2
Domain409 – 46254TSP type-1 3
Domain467 – 52054TSP type-1 4
Domain522 – 57554TSP type-1 5
Domain881 – 93858GPS
Motif231 – 2333Cell attachment site Potential
Compositional bias1382 – 144968Pro-rich

Amino acid modifications

Glycosylation641N-linked (GlcNAc...) Potential
Glycosylation4011N-linked (GlcNAc...) Potential
Glycosylation6071N-linked (GlcNAc...) Potential
Glycosylation6921N-linked (GlcNAc...) Potential
Glycosylation8441N-linked (GlcNAc...) Potential
Glycosylation8771N-linked (GlcNAc...) Potential
Glycosylation8811N-linked (GlcNAc...) Potential
Disulfide bond273 ↔ 309 By similarity
Disulfide bond277 ↔ 314 By similarity
Disulfide bond288 ↔ 299 By similarity
Disulfide bond366 ↔ 400 By similarity
Disulfide bond370 ↔ 406 By similarity
Disulfide bond381 ↔ 390 By similarity
Disulfide bond421 ↔ 456 By similarity
Disulfide bond425 ↔ 461 By similarity
Disulfide bond436 ↔ 446 By similarity
Disulfide bond479 ↔ 514 By similarity
Disulfide bond483 ↔ 519 By similarity
Disulfide bond494 ↔ 504 By similarity
Disulfide bond534 ↔ 569 By similarity
Disulfide bond538 ↔ 574 By similarity
Disulfide bond549 ↔ 559 By similarity
Disulfide bond581 ↔ 616 By similarity
Disulfide bond604 ↔ 634 By similarity
Disulfide bond884 ↔ 921 By similarity
Disulfide bond909 ↔ 923 By similarity

Experimental info

Sequence conflict2641W → L in AAN86966. Ref.1
Sequence conflict275 – 28612RDCGG…QTRTR → AGLRGRPANSNP in AAN86966. Ref.1
Sequence conflict3001E → K in AAN86966. Ref.1
Sequence conflict8211D → G in BAE28021. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: 6D1AA6D46E2E223B

FASTA1,582173,297
        10         20         30         40         50         60 
MRGQAAAPGP IWILAPLLLL LLLLGRWARA ASGADIGPGT EQCTTLVQGK FFGYFSAAAV 

        70         80         90        100        110        120 
FPANASRCSW TLRNPDPRRY TLYMKVAKAP APCSGPGRVR TYQFDSFLES TRTYLGVESF 

       130        140        150        160        170        180 
DEVLRLCDSS APLAFLQASK QFLQMQRQQP PQDGDLGPQG EFPSSSDDFS VEYLVVGNRN 

       190        200        210        220        230        240 
PSHAACQMLC RWLDACLAGS RSSHPCGIMQ TPCACLGGDV GDPASSPLVP RGDVCLRDGV 

       250        260        270        280        290        300 
AGGPENCLTS LTQDRGGHGS AGGWKLWSLW GECTRDCGGG LQTRTRTCLP TLGVEGGGCE 

       310        320        330        340        350        360 
GVLEEGRLCN RKACGPTGRS SSRSQSLRST DARRREEFGD ELQQFGFPSP QTGDPAAEEW 

       370        380        390        400        410        420 
SPWSVCSSTC GEGWQTRTRF CVSSSYSTQC SGPLREQRLC NNSAVCPVHG AWDEWSPWSL 

       430        440        450        460        470        480 
CSSTCGRGFR DRTRTCRPPQ FGGNPCEGPE KQTKFCNIAL CPGRAVDGNW NEWSSWSTCS 

       490        500        510        520        530        540 
ASCSQGRQQR TRECNGPSYG GAECQGHWVE TRDCFLQQCP VDGKWQAWAS WGSCSVTCGG 

       550        560        570        580        590        600 
GSQRRERVCS GPFFGGAACQ GPQDEYRQCG AQRCPEPHEI CDEDNFGAVV WKETPAGEVA 

       610        620        630        640        650        660 
AVRCPRNATG LILRRCELDE EGIAFWEPPT YIRCVSIDYR NIQMMTREHL AKAQRGLPGE 

       670        680        690        700        710        720 
GVSEVIQTLL EISQDGTSYS GDLLSTIDVL RNMTEIFRRA YYSPTPGDVQ NFVQIISNLL 

       730        740        750        760        770        780 
AEENRDKWEE AQLMGPNAKE LFRLVEDFVD VIGFRMKDLR DAYQVTDNLV LSIHKLPASG 

       790        800        810        820        830        840 
ATDISFPMKG WRATGDWAKV PEDRVTVSKS VFSTGLAEAD DSSVFVVGTV LYRNLGSFLA 

       850        860        870        880        890        900 
LQRNTTVLNS KVISVTVKPP PRSLLTPLEI EFAHMYNGTT NQTCILWDET DGPSSSAPPQ 

       910        920        930        940        950        960 
LGPWSWRGCR TVPLDALRTR CLCDRLSTFA ILAQLSADAT MDKVTVPSVT LIVGCGVSSL 

       970        980        990       1000       1010       1020 
TLLMLVIIYV SVWRYIRSER SVILINFCLS IISSNALILI GQTQTRNKVV CTLVAAFLHF 

      1030       1040       1050       1060       1070       1080 
FFLSSFCWVL TEAWQSYMAV TGRLRSRLVR KRFLCLGWGL PALVVAISVG FTKAKGYSTM 

      1090       1100       1110       1120       1130       1140 
NYCWLSLEGG LLYAFVGPAA AVVLVNMVIG ILVFNKLVSK DGITDKKLKE RAGASLWSSC 

      1150       1160       1170       1180       1190       1200 
VVLPLLALTW MSAVLAVTDR RSALFQILFA VFDSLEGFVI VMVHCILRRE VQDAVKCRVV 

      1210       1220       1230       1240       1250       1260 
DRQEEGNGDS GGSFQNGHAQ LMTDFEKDVD LACRSVLNKD IAACRTATIT GTFKRPSLPE 

      1270       1280       1290       1300       1310       1320 
EEKMKLAKGP PPTFNSLPAN VSKLHLHGSP RYPGGPLPDF PNHSLTLKKD KAPKSSFIGD 

      1330       1340       1350       1360       1370       1380 
GDIFKKLDSE LSRAQEKALD TSYVILPTAT ATLRPKPKEE PKYSINIDQM PQTRLIHLSM 

      1390       1400       1410       1420       1430       1440 
APDASFPTRS PPAREPPGGA PPEVPPVQPP PPPPPPPPPP QQPIPPPPTL EPAPPSLGDT 

      1450       1460       1470       1480       1490       1500 
GEPAAHPGPS SGAGAKNENV ATLSVSSLER RKSRYAELDF EKIMHTRKRH QDMFQDLNRK 

      1510       1520       1530       1540       1550       1560 
LQHAAEKEKE VPGADSKPEK QQTPNKRAWE SLRKPHGTPA WVKKELEPLP PSPLELRSVE 

      1570       1580 
WEKAGATIPL VGQDIIDLQT EV 

« Hide

Isoform 2 (Sequence not available).

References

« Hide 'large scale' references
[1]"Characterization of mouse brain-specific angiogenesis inhibitor 1 (BAI1) and phytanoyl-CoA alpha-hydroxylase-associated protein 1, a novel BAI1-binding protein."
Koh J.T., Lee Z.H., Ahn K.Y., Kim J.-K., Bae C.S., Kim H.-H., Kee H.J., Kim K.K.
Brain Res. Mol. Brain Res. 87:223-237(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INTERACTION WITH PHYHIP.
Strain: ICR.
Tissue: Brain.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Brain.
[3]Lubec G., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 1255-1268, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
[4]"Overexpression of the p53-inducible brain-specific angiogenesis inhibitor 1 suppresses efficiently tumour angiogenesis."
Duda D.G., Sunamura M., Lozonschi L., Yokoyama T., Yatsuoka T., Motoi F., Horii A., Tani K., Asano S., Nakamura Y., Matsuno S.
Br. J. Cancer 86:490-496(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"BAI1 is an engulfment receptor for apoptotic cells upstream of the ELMO/Dock180/Rac module."
Park D., Tosello-Trampont A.-C., Elliott M.R., Lu M., Haney L.B., Ma Z., Klibanov A.L., Mandell J.W., Ravichandran K.S.
Nature 450:430-434(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ELMO1 AND DOCK1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY168408 mRNA. Translation: AAN86966.1.
AK147494 mRNA. Translation: BAE27949.1.
AK147456 mRNA. Translation: BAE27923.1.
AK147459 mRNA. Translation: BAE27926.1.
AK147607 mRNA. Translation: BAE28021.1.
CCDSCCDS70635.1. [Q3UHD1-1]
RefSeqNP_778156.2. NM_174991.3. [Q3UHD1-1]
UniGeneMm.43133.

3D structure databases

ProteinModelPortalQ3UHD1.
SMRQ3UHD1. Positions 262-401, 410-934, 946-1187.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid223612. 2 interactions.
DIPDIP-37711N.
IntActQ3UHD1. 1 interaction.

Chemistry

GuidetoPHARMACOLOGY174.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteQ3UHD1.

Proteomic databases

MaxQBQ3UHD1.
PaxDbQ3UHD1.
PRIDEQ3UHD1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000042035; ENSMUSP00000046097; ENSMUSG00000034730. [Q3UHD1-1]
GeneID107831.
KEGGmmu:107831.
UCSCuc007wco.1. mouse. [Q3UHD1-1]

Organism-specific databases

CTD575.
MGIMGI:1933736. Bai1.

Phylogenomic databases

eggNOGNOG285547.
GeneTreeENSGT00690000101769.
HOGENOMHOG000230916.
HOVERGENHBG004813.
InParanoidQ3UHD1.
KOK04596.
OMADSKPEKQ.
OrthoDBEOG7KDF90.
PhylomeDBQ3UHD1.
TreeFamTF331634.

Gene expression databases

ArrayExpressQ3UHD1.
BgeeQ3UHD1.
CleanExMM_BAI1.
GenevestigatorQ3UHD1.

Family and domain databases

InterProIPR022624. DUF3497.
IPR017981. GPCR_2-like.
IPR008077. GPCR_2_brain-spec_angio_inhib.
IPR001879. GPCR_2_extracellular_dom.
IPR000832. GPCR_2_secretin-like.
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. 5 hits.
[Graphical view]
PRINTSPR01694. BAIPRECURSOR.
PR00249. GPCRSECRETIN.
SMARTSM00303. GPS. 1 hit.
SM00008. HormR. 1 hit.
SM00209. TSP1. 5 hits.
[Graphical view]
SUPFAMSSF82895. SSF82895. 5 hits.
PROSITEPS50227. G_PROTEIN_RECEP_F2_3. 1 hit.
PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
PS50221. GPS. 1 hit.
PS50092. TSP1. 5 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio359547.
PROQ3UHD1.
SOURCESearch...

Entry information

Entry nameBAI1_MOUSE
AccessionPrimary (citable) accession number: Q3UHD1
Secondary accession number(s): Q3UH36, Q8CGM0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: October 11, 2005
Last modified: July 9, 2014
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries