Skip Header

Contribute Send feedback
Read comments (?) or add your own

P98063 (BMP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 117. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bone morphogenetic protein 1
Short name=BMP-1
EC=3.4.24.19
Alternative name(s):
Mammalian tolloid protein
Short name=mTld
Procollagen C-proteinase
Short name=PCP
Gene names
Name:Bmp1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length991 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cleaves the C-terminal propeptides of procollagen I, II and III. Induces cartilage and bone formation. May participate in dorsoventral patterning during early development by cleaving chordin (CHRD) By similarity. Responsible for the proteolytic activation of lysyl oxidase LOX. Ref.4

Catalytic activity

Cleavage of the C-terminal propeptide at Ala-|-Asp in type I and II procollagens and at Arg-|-Asp in type III.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Enzyme regulation

Activity is increased by the procollagen C-endopeptidase enhancer protein.

Subunit structure

Interacts with POSTN, the interaction promotes deposition on the extracellular matrix. Ref.4

Subcellular location

Golgi apparatus › trans-Golgi network. Secreted › extracellular space › extracellular matrix. Note: Co-localizes with POSTN in the Golgi. Ref.4

Tissue specificity

At high levels in embryonic maternal deciduum and floor plate region of the neural tube. Less in developing membranous and endochondral bone, submucosa of intestine, dermis of skin and the mesenchyme of spleen and lung.

Sequence similarities

Belongs to the peptidase M12A family.

Contains 5 CUB domains.

Contains 2 EGF-like domains.

Sequence caution

The sequence AAA37306.1 differs from that shown. Reason: Frameshift at positions 24 and 61.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Propeptide26 – 125100 Potential
PRO_0000028891
Chain126 – 991866Bone morphogenetic protein 1
PRO_0000028892

Regions

Domain327 – 439113CUB 1
Domain440 – 551112CUB 2
Domain552 – 59342EGF-like 1; calcium-binding Potential
Domain596 – 707112CUB 3
Domain708 – 74841EGF-like 2; calcium-binding Potential
Domain752 – 864113CUB 4
Domain865 – 981117CUB 5
Region126 – 326201Metalloprotease

Sites

Active site2191 By similarity
Metal binding2181Zinc; catalytic By similarity
Metal binding2221Zinc; catalytic By similarity
Metal binding2281Zinc; catalytic By similarity

Amino acid modifications

Glycosylation961N-linked (GlcNAc...) Potential
Glycosylation1471N-linked (GlcNAc...) Potential
Glycosylation3371N-linked (GlcNAc...) Potential
Glycosylation3681N-linked (GlcNAc...) Potential
Glycosylation6041N-linked (GlcNAc...) Potential
Disulfide bond188 ↔ 191 By similarity
Disulfide bond327 ↔ 353 By similarity
Disulfide bond380 ↔ 402 By similarity
Disulfide bond440 ↔ 466 By similarity
Disulfide bond493 ↔ 515 By similarity
Disulfide bond556 ↔ 568 By similarity
Disulfide bond564 ↔ 577 By similarity
Disulfide bond579 ↔ 592 By similarity
Disulfide bond596 ↔ 622 By similarity
Disulfide bond649 ↔ 671 By similarity
Disulfide bond712 ↔ 723 By similarity
Disulfide bond719 ↔ 732 By similarity
Disulfide bond734 ↔ 747 By similarity
Disulfide bond752 ↔ 778 By similarity
Disulfide bond805 ↔ 827 By similarity
Disulfide bond865 ↔ 895 By similarity
Disulfide bond922 ↔ 944 By similarity

Experimental info

Sequence conflict395 – 3973APL → VWV in AAA37306. Ref.1
Sequence conflict5191K → N in AAA37306. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P98063 [UniParc].

Last modified October 3, 2012. Version 2.
Checksum: F838441CF1DA9F1A

FASTA991111,666
        10         20         30         40         50         60 
MPGVARPPLP LLSLPLLLLL LLLPRAGRPL DLADYTYDLG EEDAPELLNY KDPCKAAAFL 

        70         80         90        100        110        120 
GDIALDEEDL RAFQVQQAAV LRQQTARRPS IKAAGNSSAL GGQGTSGQPQ RESRGRWRGR 

       130        140        150        160        170        180 
PRSRRAATSR PERVWPDGVI PFVIGGNFTG SQRAVFRQAM RHWEKHTCVT FLERTDEDSY 

       190        200        210        220        230        240 
IVFTYRPCGC CSYVGRRGGG PQAISIGKNC DKFGIVVHEL GHVIGFWHEH TRPDRDRHVS 

       250        260        270        280        290        300 
IVRENIQPGQ EYNFLKMEVQ EVESLGETYD FDSIMHYARN TFSRGIFLDT IVPKYEVNGV 

       310        320        330        340        350        360 
KPSIGQRTRL SKGDIAQARK LYKCPACGET LQDSTGNFSS PEYPNGYSAH MHCVWRISVT 

       370        380        390        400        410        420 
PGEKIILNFT SMDLYRSRLC WYDYVEVRDG FWRKAPLRGR FCGGKLPEPI VSTDSRLWVE 

       430        440        450        460        470        480 
FRSSSNWVGK GFFAVYEAIC GGDVKKDNGH IQSPNYPDDY RPSKVCIWRI QVSEGFHVGL 

       490        500        510        520        530        540 
TFQSFEIERH DSCAYDYLEV RDGHSESSNL IGRYCGYEKP DDIKSTSSRL WLKFVSDGSI 

       550        560        570        580        590        600 
NKAGFAVNFF KEVDECSRPN RGGCEQRCLN TLGSYKCSCD PGYELAPDKR RCEAACGGFL 

       610        620        630        640        650        660 
TKLNGSITSP GWPKEYPPNK NCIWQLVAPT QYRISLQFDF FETEGNDVCK YDFVEVRSGL 

       670        680        690        700        710        720 
TADSKLHGKF CGSEKPEVIT SQYNNMRVEF KSDNTVSKKG FKAHFFSDKD ECSKDNGGCQ 

       730        740        750        760        770        780 
QDCVNTFGSY ECQCRSGFVL HDNKHDCKEA GCEHKVTSTS GTITSPNWPD KYPSKKECTW 

       790        800        810        820        830        840 
AISSTPGHRV KLTFVEMDIE SQPECAYDHL EVFDGRDAKA PVLGRFCGSK KPEPVLATGN 

       850        860        870        880        890        900 
RMFLRFYSDN SVQRKGFQAS HSTECGGQVR ADVKTKDLYS HAQFGDNNYP GGVDCEWVIV 

       910        920        930        940        950        960 
AEEGYGVELV FQTFEVEEET DCGYDYIELF DGYDSTAPRL GRYCGSGPPE EVYSAGDSVL 

       970        980        990 
VKFHSDDTIS KKGFHLRYTS TKFQDTLHSR K

« Hide

References

« Hide 'large scale' references
[1]"Embryonic expression of mouse bone morphogenetic protein-1 (BMP-1), which is related to the Drosophila dorsoventral gene tolloid and encodes a putative astacin metalloendopeptidase."
Fukagawa M., Noboru S., Hogan B.L.M., Jones C.M.
Dev. Biol. 163:175-183(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6.
Tissue: Embryo.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[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: C57BL/6.
Tissue: Brain.
[4]"Interaction between periostin and BMP-1 promotes proteolytic activation of lysyl oxidase."
Maruhashi T., Kii I., Saito M., Kudo A.
J. Biol. Chem. 285:13294-13303(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH POSTN, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L24755 mRNA. Translation: AAA37306.1. Frameshift.
AC122268 Genomic DNA. No translation available.
BC066062 mRNA. Translation: AAH66062.1.
IPIIPI00125182.
IPI00469541.
PIRI49540.
RefSeqNP_033885.2. NM_009755.3.
UniGeneMm.27757.

3D structure databases

HSSPHSSP built from PDB template 1APQ based on UniProtKB P00736.
ProteinModelPortalP98063.
SMRP98063. Positions 126-981.
ModBaseSearch...

Protein family/group databases

MEROPSM12.005.

PTM databases

PhosphoSiteP98063.

Proteomic databases

PaxDbP98063.
PRIDEP98063.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000022693; ENSMUSP00000022693; ENSMUSG00000022098.
GeneID12153.
KEGGmmu:12153.

Organism-specific databases

CTD649.
MGIMGI:88176. Bmp1.

Phylogenomic databases

eggNOGNOG70307.
GeneTreeENSGT00700000104171.
HOGENOMHOG000236339.
HOVERGENHBG004859.
KOK05502.
OMAVLVRFHS.
OrthoDBEOG4FTVZV.

Gene expression databases

CleanExMM_BMP1.
GenevestigatorP98063.
GermOnlineENSMUSG00000022098. Mus musculus.

Family and domain databases

Gene3D2.60.120.290. 5 hits.
3.40.390.10. 1 hit.
InterProIPR015446. BMP_1/tolloid-like.
IPR000859. CUB_dom.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR024079. MetalloPept_cat_dom.
IPR001506. Peptidase_M12A.
IPR006026. Peptidase_Metallo.
[Graphical view]
PfamPF01400. Astacin. 1 hit.
PF00431. CUB. 5 hits.
PF07645. EGF_CA. 2 hits.
[Graphical view]
PIRSFPIRSF001199. BMP_1/tolloid-like. 1 hit.
PRINTSPR00480. ASTACIN.
SMARTSM00042. CUB. 5 hits.
SM00179. EGF_CA. 2 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMSSF49854. CUB. 5 hits.
PROSITEPS00010. ASX_HYDROXYL. 2 hits.
PS01180. CUB. 5 hits.
PS00022. EGF_1. False negative.
PS01186. EGF_2. 2 hits.
PS50026. EGF_3. 2 hits.
PS01187. EGF_CA. 2 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio280487.
SOURCESearch...

Entry information

Entry nameBMP1_MOUSE
AccessionPrimary (citable) accession number: P98063
Secondary accession number(s): Q6NZM2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: October 3, 2012
Last modified: May 1, 2013
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents