Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q8CJ69 (BMPER_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
BMP-binding endothelial regulator protein
Alternative name(s):
Bone morphogenetic protein-binding endothelial cell precursor-derived regulator
Protein crossveinless-2
Short name=mCV2
Gene names
Name:Bmper
Synonyms:Cv2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length685 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Inhibitor of bone morphogenetic protein (BMP) function, it may regulate BMP responsiveness of osteoblasts and chondrocytes By similarity.

Subunit structure

Interacts with BMP4. Ref.2

Subcellular location

Secreted Ref.1.

Developmental stage

At E9<.0 day, expressed in the ventral tail bud and also in the closing anterior neuropore and in the roof of the neural tube, at E10.5, also expressed in mesonephric ridge. Ref.1

Sequence similarities

Contains 1 TIL (trypsin inhibitory-like) domain.

Contains 5 VWFC domains.

Contains 1 VWFD domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3939 Potential
Chain40 – 685646BMP-binding endothelial regulator protein
PRO_0000020821

Regions

Domain50 – 10556VWFC 1
Domain108 – 16356VWFC 2
Domain164 – 22562VWFC 3
Domain238 – 28952VWFC 4
Domain299 – 35860VWFC 5
Domain363 – 574212VWFD
Domain629 – 68254TIL

Amino acid modifications

Glycosylation301N-linked (GlcNAc...) Potential
Glycosylation1161N-linked (GlcNAc...) Potential
Glycosylation2551N-linked (GlcNAc...) Potential
Glycosylation3181N-linked (GlcNAc...) Potential
Glycosylation4411N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict1511N → K in AAH66153. Ref.3
Sequence conflict224 – 23512CLGQR…FDLPF → MFGSEKSIRPSL in BAB29213. Ref.4
Sequence conflict3501R → G in AAP88382. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8CJ69 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 4FF98D53E2C57656

FASTA68576,148
        10         20         30         40         50         60 
MLWFFSVRAL AERPCRRSPG ITCCVLLLLN CSGVPMSLAS SFLTGSVAKC ENEGEVLQIP 

        70         80         90        100        110        120 
FITDNPCIMC VCLNKEVTCK REKCPVLSRD CALAIKQRGA CCERCKGCTH EGRTYNSSFK 

       130        140        150        160        170        180 
WQTPAEPCVL RQCQEGVVTE SEVRCVVHCK NPAEHQGACC PTCPGCVFEG VQYREGEEFQ 

       190        200        210        220        230        240 
PEGNKCITCS CVGGRTQCVR EVCPILSCPQ HLSHTPSGQC CPKCLGQRKV FDLPFGSCLF 

       250        260        270        280        290        300 
RSDVYDNGAS FVYDNCTVCT CKDSTMVCKK KCSHPGVCNS DEDACCEDCL LRVPPEDIKV 

       310        320        330        340        350        360 
CKFGSKIFRD GEMWSSVNCS ICACVKGKTE CRKKQCVPVS SCPQGKILNR KGCCPICTEK 

       370        380        390        400        410        420 
PGVCTVFGDP HYNTFDGRTF NFQGTCQYVL TKDCSSPASP FQVLVKNDAR RTRSFSWTKS 

       430        440        450        460        470        480 
VELMLGESTV SLQQHLTVRW NGSRIALPCH TPHFHIDLDG YLLKVTTRAG LEISWDGDSF 

       490        500        510        520        530        540 
VEVMAAPHLK GKLCGLCGNY NGHKRDDLIG GDGNFKFDVD DFAESWRVES NEFCNRPQRK 

       550        560        570        580        590        600 
PVPELCQGTV KVKLRAHREC QKLKSWEFQT CHSTVDYTTF YRSCVTDMCE CPVHKNCYCE 

       610        620        630        640        650        660 
SFLAYTRACQ REGIKVHWEP QQSCAATQCK HGAVYDTCGP GCVKTCDNWN EIGPCNKPCI 

       670        680 
AGCHCPANLV LHKGRCIKPV LCPQR 

« Hide

References

« Hide 'large scale' references
[1]"Mouse Crossveinless-2 is the vertebrate homolog of a Drosophila extracellular regulator of BMP signaling."
Coffinier C., Ketpura N., Tran U., Geissert D., De Robertis E.M.
Mech. Dev. 119:S179-S184(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
Strain: C57BL/6J.
[2]"BMPER, a novel endothelial cell precursor-derived protein, antagonizes bone morphogenetic protein signaling and endothelial cell differentiation."
Moser M., Binder O., Wu Y., Aitsebaomo J., Ren R., Bode C., Bautch V.L., Conlon F.L., Patterson C.
Mol. Cell. Biol. 23:5664-5679(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH BMP4.
Strain: Swiss Webster.
[3]"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].
Strain: CD-1.
Tissue: Mammary tumor and Neural stem cell.
[4]"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] OF 224-685.
Strain: C57BL/6J.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF454954 mRNA. Translation: AAN45857.1.
AY263358 mRNA. Translation: AAP88382.1.
BC042718 mRNA. Translation: AAH42718.1.
BC066153 mRNA. Translation: AAH66153.1.
AK014221 mRNA. Translation: BAB29213.1.
CCDSCCDS22929.1.
RefSeqNP_082748.1. NM_028472.2.
UniGeneMm.335020.

3D structure databases

ProteinModelPortalQ8CJ69.
SMRQ8CJ69. Positions 42-107.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid215850. 1 interaction.

PTM databases

PhosphoSiteQ8CJ69.

Proteomic databases

PRIDEQ8CJ69.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000071982; ENSMUSP00000071872; ENSMUSG00000031963.
GeneID73230.
KEGGmmu:73230.
UCSCuc009oow.1. mouse.

Organism-specific databases

CTD168667.
MGIMGI:1920480. Bmper.

Phylogenomic databases

eggNOGNOG283828.
GeneTreeENSGT00730000110288.
HOGENOMHOG000234284.
HOVERGENHBG050704.
InParanoidQ8CJ69.
OMAEFCNRPQ.
OrthoDBEOG7G7KNN.
PhylomeDBQ8CJ69.
TreeFamTF343473.

Gene expression databases

BgeeQ8CJ69.
CleanExMM_BMPER.
GenevestigatorQ8CJ69.

Family and domain databases

InterProIPR002919. TIL_dom.
IPR014853. Unchr_dom_Cys-rich.
IPR001007. VWF_C.
IPR001846. VWF_type-D.
[Graphical view]
PfamPF08742. C8. 1 hit.
PF01826. TIL. 1 hit.
PF00093. VWC. 2 hits.
PF00094. VWD. 1 hit.
[Graphical view]
SMARTSM00832. C8. 1 hit.
SM00214. VWC. 5 hits.
SM00216. VWD. 1 hit.
[Graphical view]
SUPFAMSSF57567. SSF57567. 1 hit.
PROSITEPS01208. VWFC_1. 3 hits.
PS50184. VWFC_2. 2 hits.
PS51233. VWFD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio337713.
PMAP-CutDBQ8CJ69.
PROQ8CJ69.
SOURCESearch...

Entry information

Entry nameBMPER_MOUSE
AccessionPrimary (citable) accession number: Q8CJ69
Secondary accession number(s): Q7TN57, Q80UZ1, Q9CXM8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 88 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