BMPER_MOUSE
ID BMPER_MOUSE Reviewed; 685 AA.
AC Q8CJ69; Q7TN57; Q80UZ1; Q9CXM8;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=BMP-binding endothelial regulator protein;
DE AltName: Full=Bone morphogenetic protein-binding endothelial cell precursor-derived regulator;
DE AltName: Full=Protein crossveinless-2;
DE Short=mCV2;
DE Flags: Precursor;
GN Name=Bmper; Synonyms=Cv2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J;
RX PubMed=14516682; DOI=10.1016/s0925-4773(03)00113-8;
RA Coffinier C., Ketpura N., Tran U., Geissert D., De Robertis E.M.;
RT "Mouse Crossveinless-2 is the vertebrate homolog of a Drosophila
RT extracellular regulator of BMP signaling.";
RL Mech. Dev. 119:S179-S184(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH BMP4.
RC STRAIN=Swiss Webster;
RX PubMed=12897139; DOI=10.1128/mcb.23.16.5664-5679.2003;
RA Moser M., Binder O., Wu Y., Aitsebaomo J., Ren R., Bode C., Bautch V.L.,
RA Conlon F.L., Patterson C.;
RT "BMPER, a novel endothelial cell precursor-derived protein, antagonizes
RT bone morphogenetic protein signaling and endothelial cell
RT differentiation.";
RL Mol. Cell. Biol. 23:5664-5679(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CD-1; TISSUE=Mammary tumor, and Neural stem cell;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 224-685.
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
CC -!- FUNCTION: Inhibitor of bone morphogenetic protein (BMP) function, it
CC may regulate BMP responsiveness of osteoblasts and chondrocytes.
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with BMP4. {ECO:0000269|PubMed:12897139}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14516682}.
CC -!- DEVELOPMENTAL STAGE: At 9.0 dpc, expressed in the ventral tail bud and
CC also in the closing anterior neuropore and in the roof of the neural
CC tube, at 10.5 dpc, also expressed in mesonephric ridge.
CC {ECO:0000269|PubMed:14516682}.
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DR EMBL; AF454954; AAN45857.1; -; mRNA.
DR EMBL; AY263358; AAP88382.1; -; mRNA.
DR EMBL; BC042718; AAH42718.1; -; mRNA.
DR EMBL; BC066153; AAH66153.1; -; mRNA.
DR EMBL; AK014221; BAB29213.1; -; mRNA.
DR CCDS; CCDS22929.1; -.
DR RefSeq; NP_082748.1; NM_028472.2.
DR AlphaFoldDB; Q8CJ69; -.
DR SMR; Q8CJ69; -.
DR BioGRID; 215850; 3.
DR STRING; 10090.ENSMUSP00000071872; -.
DR GlyGen; Q8CJ69; 5 sites.
DR PhosphoSitePlus; Q8CJ69; -.
DR MaxQB; Q8CJ69; -.
DR PaxDb; Q8CJ69; -.
DR PRIDE; Q8CJ69; -.
DR ProteomicsDB; 265313; -.
DR Antibodypedia; 12854; 179 antibodies from 24 providers.
DR DNASU; 73230; -.
DR Ensembl; ENSMUST00000071982; ENSMUSP00000071872; ENSMUSG00000031963.
DR GeneID; 73230; -.
DR KEGG; mmu:73230; -.
DR UCSC; uc009oow.2; mouse.
DR CTD; 168667; -.
DR MGI; MGI:1920480; Bmper.
DR VEuPathDB; HostDB:ENSMUSG00000031963; -.
DR eggNOG; KOG1216; Eukaryota.
DR GeneTree; ENSGT00940000156485; -.
DR HOGENOM; CLU_018024_2_0_1; -.
DR InParanoid; Q8CJ69; -.
DR OMA; WHFANSW; -.
DR OrthoDB; 1104860at2759; -.
DR PhylomeDB; Q8CJ69; -.
DR TreeFam; TF343473; -.
DR BioGRID-ORCS; 73230; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Bmper; mouse.
DR PRO; PR:Q8CJ69; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8CJ69; protein.
DR Bgee; ENSMUSG00000031963; Expressed in metanephric mesenchyme and 216 other tissues.
DR ExpressionAtlas; Q8CJ69; baseline and differential.
DR Genevisible; Q8CJ69; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0001568; P:blood vessel development; IBA:GO_Central.
DR GO; GO:0002043; P:blood vessel endothelial cell proliferation involved in sprouting angiogenesis; ISO:MGI.
DR GO; GO:0030509; P:BMP signaling pathway; IMP:MGI.
DR GO; GO:0007182; P:common-partner SMAD protein phosphorylation; IMP:MGI.
DR GO; GO:0042118; P:endothelial cell activation; ISO:MGI.
DR GO; GO:0048839; P:inner ear development; IDA:MGI.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IDA:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:1903672; P:positive regulation of sprouting angiogenesis; ISO:MGI.
DR GO; GO:0045765; P:regulation of angiogenesis; IBA:GO_Central.
DR GO; GO:0010594; P:regulation of endothelial cell migration; ISO:MGI.
DR GO; GO:0060393; P:regulation of pathway-restricted SMAD protein phosphorylation; ISO:MGI.
DR GO; GO:0032880; P:regulation of protein localization; IMP:MGI.
DR GO; GO:0001657; P:ureteric bud development; IEP:UniProtKB.
DR InterPro; IPR036084; Ser_inhib-like_sf.
DR InterPro; IPR002919; TIL_dom.
DR InterPro; IPR014853; Unchr_dom_Cys-rich.
DR InterPro; IPR001007; VWF_dom.
DR InterPro; IPR001846; VWF_type-D.
DR Pfam; PF08742; C8; 1.
DR Pfam; PF01826; TIL; 1.
DR Pfam; PF00093; VWC; 2.
DR Pfam; PF00094; VWD; 1.
DR SMART; SM00832; C8; 1.
DR SMART; SM00214; VWC; 5.
DR SMART; SM00216; VWD; 1.
DR SUPFAM; SSF57567; SSF57567; 1.
DR PROSITE; PS01208; VWFC_1; 3.
DR PROSITE; PS50184; VWFC_2; 2.
DR PROSITE; PS51233; VWFD; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..39
FT /evidence="ECO:0000255"
FT CHAIN 40..685
FT /note="BMP-binding endothelial regulator protein"
FT /id="PRO_0000020821"
FT DOMAIN 50..105
FT /note="VWFC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 108..163
FT /note="VWFC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 164..225
FT /note="VWFC 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 238..289
FT /note="VWFC 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 299..358
FT /note="VWFC 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 362..535
FT /note="VWFD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 629..682
FT /note="TIL"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 364..497
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 386..534
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT CONFLICT 151
FT /note="N -> K (in Ref. 3; AAH66153)"
FT /evidence="ECO:0000305"
FT CONFLICT 224..235
FT /note="CLGQRKVFDLPF -> MFGSEKSIRPSL (in Ref. 4; BAB29213)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="R -> G (in Ref. 2; AAP88382)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 685 AA; 76148 MW; 4FF98D53E2C57656 CRC64;
MLWFFSVRAL AERPCRRSPG ITCCVLLLLN CSGVPMSLAS SFLTGSVAKC ENEGEVLQIP
FITDNPCIMC VCLNKEVTCK REKCPVLSRD CALAIKQRGA CCERCKGCTH EGRTYNSSFK
WQTPAEPCVL RQCQEGVVTE SEVRCVVHCK NPAEHQGACC PTCPGCVFEG VQYREGEEFQ
PEGNKCITCS CVGGRTQCVR EVCPILSCPQ HLSHTPSGQC CPKCLGQRKV FDLPFGSCLF
RSDVYDNGAS FVYDNCTVCT CKDSTMVCKK KCSHPGVCNS DEDACCEDCL LRVPPEDIKV
CKFGSKIFRD GEMWSSVNCS ICACVKGKTE CRKKQCVPVS SCPQGKILNR KGCCPICTEK
PGVCTVFGDP HYNTFDGRTF NFQGTCQYVL TKDCSSPASP FQVLVKNDAR RTRSFSWTKS
VELMLGESTV SLQQHLTVRW NGSRIALPCH TPHFHIDLDG YLLKVTTRAG LEISWDGDSF
VEVMAAPHLK GKLCGLCGNY NGHKRDDLIG GDGNFKFDVD DFAESWRVES NEFCNRPQRK
PVPELCQGTV KVKLRAHREC QKLKSWEFQT CHSTVDYTTF YRSCVTDMCE CPVHKNCYCE
SFLAYTRACQ REGIKVHWEP QQSCAATQCK HGAVYDTCGP GCVKTCDNWN EIGPCNKPCI
AGCHCPANLV LHKGRCIKPV LCPQR
