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Q61288 (ACVL1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 136. 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

Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase receptor R3

Short name=SKR3
EC=2.7.11.30
Alternative name(s):
Activin receptor-like kinase 1
Short name=ALK-1
TGF-B superfamily receptor type I
Short name=TSR-I
Gene names
Name:Acvrl1
Synonyms:Acvrlk1, Alk-1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length502 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Type I receptor for TGF-beta family ligands BMP9/GDF2 and BMP10 and important regulator of normal blood vessel development. 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. May bind activin as well.

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 processAngiogenesis
   Cellular componentMembrane
   DomainSignal
Transmembrane
Transmembrane helix
   LigandATP-binding
Magnesium
Manganese
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Receptor
Serine/threonine-protein kinase
Transferase
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processBMP signaling pathway

Inferred from mutant phenotype PubMed 22783020. Source: MGI

angiogenesis

Inferred from mutant phenotype PubMed 10716993PubMed 11062473. Source: MGI

artery development

Inferred from mutant phenotype PubMed 19903896. Source: BHF-UCL

blood vessel morphogenesis

Inferred from mutant phenotype PubMed 17530030PubMed 17911384. Source: MGI

blood vessel remodeling

Inferred from mutant phenotype PubMed 19903896. Source: BHF-UCL

cellular response to BMP stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to transforming growth factor beta stimulus

Inferred from direct assay PubMed 19494318. Source: BHF-UCL

endothelial cell activation

Traceable author statement PubMed 20406889. Source: DFLAT

endothelial tube morphogenesis

Inferred from electronic annotation. Source: Ensembl

in utero embryonic development

Inferred from mutant phenotype PubMed 17911384. Source: MGI

lymphangiogenesis

Inferred from mutant phenotype PubMed 19903896. Source: BHF-UCL

lymphatic endothelial cell differentiation

Inferred from mutant phenotype PubMed 19903896. Source: BHF-UCL

negative regulation of DNA biosynthetic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of blood vessel endothelial cell migration

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell growth

Inferred from electronic annotation. Source: Ensembl

negative regulation of endothelial cell differentiation

Inferred from direct assay PubMed 20406889. Source: DFLAT

negative regulation of endothelial cell proliferation

Inferred from direct assay PubMed 20406889. Source: DFLAT

negative regulation of focal adhesion assembly

Inferred from electronic annotation. Source: Ensembl

positive regulation of BMP signaling pathway

Inferred from direct assay PubMed 20406889. Source: DFLAT

positive regulation of angiogenesis

Inferred from genetic interaction PubMed 23868260. Source: MGI

positive regulation of endothelial cell differentiation

Inferred from direct assay PubMed 20406889. Source: DFLAT

positive regulation of endothelial cell proliferation

Inferred from direct assay PubMed 20406889. Source: DFLAT

positive regulation of pathway-restricted SMAD protein phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 20406889. Source: DFLAT

protein heterooligomerization

Inferred from electronic annotation. Source: Ensembl

regulation of blood pressure

Inferred from electronic annotation. Source: Ensembl

retina vasculature development in camera-type eye

Inferred from mutant phenotype PubMed 19903896. Source: BHF-UCL

transforming growth factor beta receptor signaling pathway

Inferred from direct assay PubMed 14580334. Source: MGI

venous blood vessel development

Inferred from mutant phenotype PubMed 19903896. Source: BHF-UCL

wound healing, spreading of epidermal cells

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell surface

Inferred from electronic annotation. Source: Ensembl

dendrite

Inferred from electronic annotation. Source: Ensembl

integral component of plasma membrane

Inferred from electronic annotation. Source: Ensembl

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

activin receptor activity, type I

Inferred from electronic annotation. Source: Ensembl

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 20406889. Source: DFLAT

receptor signaling protein serine/threonine kinase activity

Inferred from electronic annotation. Source: Ensembl

transforming growth factor beta receptor activity, type I

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 502480Serine/threonine-protein kinase receptor R3
PRO_0000024421

Regions

Topological domain23 – 11997Extracellular Potential
Transmembrane120 – 14021Helical; Potential
Topological domain141 – 502362Cytoplasmic Potential
Domain171 – 20030GS
Domain201 – 502302Protein kinase
Nucleotide binding207 – 2159ATP By similarity
Region72 – 754Mediates specificity for BMP ligand By similarity

Sites

Active site3291Proton acceptor By similarity
Binding site2281ATP By similarity

Amino acid modifications

Modified residue1541Phosphoserine Ref.6
Glycosylation321N-linked (GlcNAc...) Potential
Glycosylation971N-linked (GlcNAc...) Potential
Disulfide bond33 ↔ 50 By similarity
Disulfide bond35 ↔ 40 By similarity
Disulfide bond45 ↔ 68 By similarity
Disulfide bond76 ↔ 88 By similarity
Disulfide bond89 ↔ 94 By similarity

Experimental info

Sequence conflict171F → L in CAA83484. Ref.2
Sequence conflict211R → Q Ref.2
Sequence conflict231D → R Ref.2
Sequence conflict25 – 262AK → RR in AAB03642. Ref.1
Sequence conflict3051A → P in CAA83484. Ref.2
Sequence conflict358 – 3592SD → NE in CAA83484. Ref.2
Sequence conflict3661N → T in CAA83484. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q61288 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 439510D3CC740D65

FASTA50256,519
        10         20         30         40         50         60 
MTLGSFRRGL LMLSVAFGLT RGDLAKPSKL VNCTCESPHC KRPFCQGSWC TVVLVREQGR 

        70         80         90        100        110        120 
HPQVYRGCGS LNQELCLGRP TEFLNHHCCY RSFCNHNVSL MLEATQTPSE EPEVDAHLPL 

       130        140        150        160        170        180 
ILGPVLALPV LVALGALGLW RVRRRQEKQR DLHSDLGESS LILKASEQAD SMLGDFLDSD 

       190        200        210        220        230        240 
CTTGSGSGLP FLVQRTVARQ VALVECVGKG RYGEVWRGSW HGESVAVKIF SSRDEQSWFR 

       250        260        270        280        290        300 
ETEIYNTVLL RHDNILGFIA SDMTSRNSST QLWLITHYHE HGSLYDFLQR QTLEPQLALR 

       310        320        330        340        350        360 
LAVSAACGLA HLHVEIFGTQ GKPAIAHRDL KSRNVLVKSN LQCCIADLGL AVMHSQSSDY 

       370        380        390        400        410        420 
LDIGNNPRVG TKRYMAPEVL DEHIRTDCFE SYKWTDIWAF GLVLWEIARR TIINGIVEDY 

       430        440        450        460        470        480 
RPPFYDMVPN DPSFEDMKKV VCVDQQTPTI PNRLAADPVL SGLAQMMREC WYPNPSARLT 

       490        500 
ALRIKKTLQK LSHNPEKPKV IH 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of the murine activin receptor like kinase-1 (ALK-1) homolog."
Wu X., Robinson C.E., Fong H.W., Crabtree J.S., Rodriguez B.R., Roe B.A., Gimble J.M.
Biochem. Biophys. Res. Commun. 216:78-83(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Lung.
[2]"Distinct spatial and temporal expression patterns of two type I receptors for bone morphogenetic proteins during mouse embryogenesis."
Dewulf N., Verschueren K., Lonnoy O., Moren A., Grimsby S., Spiegle K., Miyazono K., Huylebroeck D., ten Dijke P.
Endocrinology 136:2652-2663(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Placenta.
[3]"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].
Strain: C57BL/6J and NOD.
[4]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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: FVB/N.
Tissue: Mammary tumor.
[6]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L48015 mRNA. Translation: AAB03642.1.
Z31664 mRNA. Translation: CAA83484.1.
AK160915 mRNA. Translation: BAE36089.1.
AK170870 mRNA. Translation: BAE42083.1.
CH466550 Genomic DNA. Translation: EDL04061.1.
CH466550 Genomic DNA. Translation: EDL04063.1.
BC015083 mRNA. Translation: AAH15083.1.
CCDSCCDS37215.1.
PIRI48241.
JC4337.
RefSeqNP_001264186.1. NM_001277257.1.
NP_001264187.1. NM_001277258.1.
NP_001264188.1. NM_001277259.1.
NP_033742.2. NM_009612.3.
UniGeneMm.279542.

3D structure databases

ProteinModelPortalQ61288.
SMRQ61288. Positions 30-103, 171-491.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid197957. 1 interaction.
DIPDIP-47635N.
IntActQ61288. 4 interactions.
MINTMINT-4086807.

PTM databases

PhosphoSiteQ61288.

Proteomic databases

PaxDbQ61288.
PRIDEQ61288.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000000542; ENSMUSP00000000542; ENSMUSG00000000530.
ENSMUST00000117984; ENSMUSP00000113505; ENSMUSG00000000530.
ENSMUST00000119063; ENSMUSP00000113536; ENSMUSG00000000530.
ENSMUST00000120028; ENSMUSP00000113297; ENSMUSG00000000530.
ENSMUST00000120754; ENSMUSP00000112490; ENSMUSG00000000530.
ENSMUST00000121718; ENSMUSP00000114027; ENSMUSG00000000530.
GeneID11482.
KEGGmmu:11482.
UCSCuc007xsm.1. mouse.

Organism-specific databases

CTD94.
MGIMGI:1338946. Acvrl1.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00730000110868.
HOGENOMHOG000230587.
HOVERGENHBG054502.
InParanoidQ91YR0.
KOK13594.
OMAWHVRRRQ.
OrthoDBEOG7Q8CN3.
TreeFamTF314724.

Enzyme and pathway databases

BRENDA2.7.10.2. 3474.

Gene expression databases

ArrayExpressQ61288.
BgeeQ61288.
CleanExMM_ACVRL1.
GenevestigatorQ61288.

Family and domain databases

InterProIPR000472. Activin_rcpt.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR003605. TGF_beta_rcpt_GS.
IPR000333. TGFB_receptor.
[Graphical view]
PANTHERPTHR23255. PTHR23255. 1 hit.
PfamPF01064. Activin_recp. 1 hit.
PF00069. Pkinase. 1 hit.
PF08515. TGF_beta_GS. 1 hit.
[Graphical view]
SMARTSM00467. GS. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS51256. GS. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio278836.
PROQ61288.
SOURCESearch...

Entry information

Entry nameACVL1_MOUSE
AccessionPrimary (citable) accession number: Q61288
Secondary accession number(s): Q61289, Q91YR0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 136 of the entry and version 2 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

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

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