P36898 (BMR1B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Bone morphogenetic protein receptor type-1B
Short name=BMP type-1B receptor
Short name=BMPR-1B
EC=2.7.11.30

Alternative name(s):
Activin receptor-like kinase 6
Short name=ALK-6
Serine/threonine-protein kinase receptor R6
Short name=SKR6
CD_antigen=CDw293

Gene names

Name:	Bmpr1b
Synonyms:	Acvrlk6

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	502 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for BMP7/OP-1 and GDF5.
Catalytic activity	ATP + [receptor-protein] = ADP + [receptor-protein] phosphate.
Cofactor	Magnesium or manganese By similarity.
Subcellular location	Membrane; Single-pass type I membrane protein.
Sequence similarities	Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. TGFB receptor subfamily. Contains 1 GS domain. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Chondrogenesis
Cellular component	Membrane
Domain	Signal Transmembrane Transmembrane helix
Ligand	ATP-binding Magnesium Manganese Metal-binding Nucleotide-binding
Molecular function	Kinase Receptor Serine/threonine-protein kinase Transferase
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	BMP signaling pathway Inferred from mutant phenotype PubMed 11376112. Source: MGI cartilage condensation Inferred from mutant phenotype PubMed 10631181. Source: MGI dorsal/ventral pattern formation Inferred from genetic interaction PubMed 15673568. Source: MGI estrogen biosynthetic process Non-traceable author statement PubMed 11416163. Source: UniProtKB inflammatory response Inferred from expression pattern PubMed 12151307. Source: UniProtKB limb morphogenesis Inferred from electronic annotation. Source: Compara ovarian cumulus expansion Inferred from mutant phenotype PubMed 11416163. Source: UniProtKB positive regulation of bone mineralization Inferred from electronic annotation. Source: Compara positive regulation of osteoblast differentiation Inferred from electronic annotation. Source: Compara retina development in camera-type eye Inferred from mutant phenotype PubMed 12654290. Source: MGI retinal ganglion cell axon guidance Inferred from mutant phenotype PubMed 12654290. Source: MGI transforming growth factor beta receptor signaling pathway Traceable author statement PubMed 10631181. Source: MGI
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW transforming growth factor beta receptor activity, type I Inferred from mutant phenotype PubMed 11376112. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 13

13

Potential

Chain

14 – 502

489

Bone morphogenetic protein receptor type-1B

PRO_0000024413

Regions

Topological domain

14 – 126

113

Extracellular Potential

Transmembrane

127 – 148

22

Helical; Potential

Topological domain

149 – 502

354

Cytoplasmic Potential

Domain

174 – 203

30

GS

Domain

204 – 494

291

Protein kinase

Nucleotide binding

210 – 218

9

ATP By similarity

Sites

Active site

332

1

Proton acceptor By similarity

Binding site

231

1

ATP By similarity

Amino acid modifications

Disulfide bond

32 ↔ 53

Ref.4

Disulfide bond

34 ↔ 38

Ref.4

Disulfide bond

47 ↔ 71

Ref.4

Disulfide bond

81 ↔ 95

Ref.4

Disulfide bond

96 ↔ 102

Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

502

Helix Strand Turn

Details...

Beta strand

30 – 33

4

Beta strand

35 – 37

3

Beta strand

46 – 59

14

Beta strand

64 – 72

9

Helix

77 – 80

4

Beta strand

91 – 96

6

Helix

102 – 105

4

Sequences

	Sequence		Length	Mass (Da)
	P36898 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: AB29681F3FF5A361	FASTA	502	56,944
	10 20 30 40 50 60 MLLRSSGKLN VGTKKEDGES TAPTPRPKIL RCKCHHHCPE DSVNNICSTD GYCFTMIEED 70 80 90 100 110 120 DSGMPVVTSG CLGLEGSDFQ CRDTPIPHQR RSIECCTERN ECNKDLHPTL PPLKDRDFVD 130 140 150 160 170 180 GPIHHKALLI SVTVCSLLLV LIILFCYFRY KRQEARPRYS IGLEQDETYI PPGESLRDLI 190 200 210 220 230 240 EQSQSSGSGS GLPLLVQRTI AKQIQMVKQI GKGRYGEVWM GKWRGEKVAV KVFFTTEEAS 250 260 270 280 290 300 WFRETEIYQT VLMRHENILG FIAADIKGTG SWTQLYLITD YHENGSLYDY LKSTTLDAKS 310 320 330 340 350 360 MLKLAYSSVS GLCHLHTEIF STQGKPAIAH RDLKSKNILV KKNGTCCIAD LGLAVKFISD 370 380 390 400 410 420 TNEVDIPPNT RVGTKRYMPP EVLDESLNRN HFQSYIMADM YSFGLILWEI ARRCVSGGIV 430 440 450 460 470 480 EEYQLPYHDL VPSDPSYEDM REIVCMKKLR PSFPNRWSSD ECLRQMGKLM TECWAQNPAS 490 500 RLTALRVKKT LAKMSESQDI KL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of type I receptors for transforming growth factor-beta and activin." ten Dijke P., Yamashita H., Ichijo H., Franzen P., Laiho M., Miyazono K., Heldin C.-H. Science 264:101-104(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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. , 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/6J. Tissue: Head and Hypothalamus.
[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 and Retina.
[4]	"Crystal structure analysis reveals a spring-loaded latch as molecular mechanism for GDF-5-type I receptor specificity." Kotzsch A., Nickel J., Seher A., Sebald W., Muller T.D. EMBO J. 28:937-947(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 14-126 IN COMPLEX WITH HUMAN GDF5, DISULFIDE BONDS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z23143 mRNA. Translation: CAA80674.1.
AK086130 mRNA. Translation: BAC39617.1.
AK162844 mRNA. Translation: BAE37078.1.
BC065106 mRNA. Translation: AAH65106.1.
BC065143 mRNA. Translation: AAH65143.1.

IPI

IPI00128197.

PIR

A53444.

RefSeq

NP_031586.1. NM_007560.3.

UniGene

Mm.39089.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3EVS	X-ray	2.10	C	14-126	[»]

ProteinModelPortal

P36898.

SMR

P36898. Positions 29-113, 174-500.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-252N.

MINT

MINT-124245.

PTM databases

PhosphoSite

P36898.

Proteomic databases

PaxDb

P36898.

PRIDE

P36898.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000029948; ENSMUSP00000029948; ENSMUSG00000052430.
ENSMUST00000098568; ENSMUSP00000096167; ENSMUSG00000052430.
ENSMUST00000106230; ENSMUSP00000101837; ENSMUSG00000052430.
ENSMUST00000106232; ENSMUSP00000101839; ENSMUSG00000052430.

GeneID

12167.

KEGG

mmu:12167.

Organism-specific databases

CTD

658.

MGI

MGI:107191. Bmpr1b.

Phylogenomic databases

eggNOG

COG0515.

GeneTree

ENSGT00560000076615.

HOGENOM

HOG000230587.

HOVERGEN

HBG054502.

InParanoid

P36898.

KO

K13578.

OMA

DGPIHHK.

OrthoDB

EOG40P46G.

Enzyme and pathway databases

BRENDA

2.7.10.2. 3474.

Gene expression databases

ArrayExpress

P36898.

Bgee

P36898.

CleanEx

MM_BMPR1B.

Genevestigator

P36898.

GermOnline

ENSMUSG00000052430. Mus musculus.

Family and domain databases

InterPro

IPR000472. Activin_rcpt.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR003605. TGF_beta_rcpt_GS.
[Graphical view]

Pfam

PF01064. Activin_recp. 1 hit.
PF00069. Pkinase. 1 hit.
PF08515. TGF_beta_GS. 1 hit.
[Graphical view]

SMART

SM00467. GS. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

PROSITE

PS51256. GS. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

BMPR1B. mouse.

EvolutionaryTrace

P36898.

NextBio

280535.

SOURCE

Search...

Entry information

Entry name

BMR1B_MOUSE

Accession

Primary (citable) accession number: P36898
Secondary accession number(s): Q3TRF2

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	April 3, 2013
This is version 129 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program