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   27-MAR-2024, entry version 141.
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   GlyCosmos; Q8CJ69; 5 sites, No reported glycans.
DR   GlyGen; Q8CJ69; 5 sites.
DR   PhosphoSitePlus; Q8CJ69; -.
DR   MaxQB; Q8CJ69; -.
DR   PaxDb; 10090-ENSMUSP00000071872; -.
DR   ProteomicsDB; 265313; -.
DR   Antibodypedia; 12854; 201 antibodies from 24 providers.
DR   DNASU; 73230; -.
DR   Ensembl; ENSMUST00000071982.7; ENSMUSP00000071872.6; ENSMUSG00000031963.9.
DR   GeneID; 73230; -.
DR   KEGG; mmu:73230; -.
DR   UCSC; uc009oow.2; mouse.
DR   AGR; MGI:1920480; -.
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; 2906064at2759; -.
DR   PhylomeDB; Q8CJ69; -.
DR   TreeFam; TF343473; -.
DR   BioGRID-ORCS; 73230; 1 hit in 76 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 218 other cell types or tissues.
DR   ExpressionAtlas; Q8CJ69; baseline and differential.
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: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:0060391; P:positive regulation of SMAD protein signal transduction; 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:0032880; P:regulation of protein localization; IMP:MGI.
DR   GO; GO:0060395; P:SMAD protein signal transduction; IMP:MGI.
DR   GO; GO:0001657; P:ureteric bud development; IEP:UniProtKB.
DR   CDD; cd19941; TIL; 1.
DR   Gene3D; 6.20.200.20; -; 3.
DR   Gene3D; 2.10.70.10; Complement Module, domain 1; 2.
DR   Gene3D; 2.10.25.10; Laminin; 1.
DR   InterPro; IPR036084; Ser_inhib-like_sf.
DR   InterPro; IPR002919; TIL_dom.
DR   InterPro; IPR014853; VWF/SSPO/ZAN-like_Cys-rich_dom.
DR   InterPro; IPR001007; VWF_dom.
DR   InterPro; IPR001846; VWF_type-D.
DR   PANTHER; PTHR46698; CROSSVEINLESS 2; 1.
DR   PANTHER; PTHR46698:SF4; CROSSVEINLESS 2; 1.
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; SSF57603; FnI-like domain; 5.
DR   SUPFAM; SSF57567; Serine protease inhibitors; 1.
DR   PROSITE; PS01208; VWFC_1; 3.
DR   PROSITE; PS50184; VWFC_2; 2.
DR   PROSITE; PS51233; VWFD; 1.
DR   Genevisible; Q8CJ69; MM.
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
//