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Protein

Serine/threonine-protein kinase receptor R3

Gene

Acvrl1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

ATP + [receptor-protein] = ADP + [receptor-protein] phosphate.

Cofactori

Mg2+By similarity, Mn2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei228 – 2281ATPPROSITE-ProRule annotation
Active sitei329 – 3291Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi207 – 2159ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. activin binding Source: MGI
  2. activin receptor activity, type I Source: MGI
  3. ATP binding Source: MGI
  4. metal ion binding Source: UniProtKB-KW
  5. protein kinase binding Source: MGI
  6. protein serine/threonine kinase activity Source: MGI
  7. receptor signaling protein serine/threonine kinase activity Source: Ensembl
  8. SMAD binding Source: MGI
  9. transforming growth factor beta-activated receptor activity Source: MGI
  10. transforming growth factor beta binding Source: MGI
  11. transforming growth factor beta receptor activity, type I Source: Ensembl

GO - Biological processi

  1. angiogenesis Source: MGI
  2. artery development Source: BHF-UCL
  3. blood circulation Source: MGI
  4. blood vessel morphogenesis Source: MGI
  5. blood vessel remodeling Source: BHF-UCL
  6. BMP signaling pathway Source: MGI
  7. cellular response to BMP stimulus Source: MGI
  8. cellular response to transforming growth factor beta stimulus Source: BHF-UCL
  9. endothelial cell activation Source: DFLAT
  10. endothelial tube morphogenesis Source: MGI
  11. in utero embryonic development Source: MGI
  12. lymphangiogenesis Source: BHF-UCL
  13. lymphatic endothelial cell differentiation Source: BHF-UCL
  14. negative regulation of blood vessel endothelial cell migration Source: MGI
  15. negative regulation of cell adhesion Source: MGI
  16. negative regulation of cell growth Source: MGI
  17. negative regulation of cell migration Source: MGI
  18. negative regulation of cell proliferation Source: MGI
  19. negative regulation of DNA biosynthetic process Source: MGI
  20. negative regulation of endothelial cell differentiation Source: DFLAT
  21. negative regulation of endothelial cell migration Source: MGI
  22. negative regulation of endothelial cell proliferation Source: DFLAT
  23. negative regulation of focal adhesion assembly Source: MGI
  24. positive regulation of angiogenesis Source: MGI
  25. positive regulation of BMP signaling pathway Source: DFLAT
  26. positive regulation of endothelial cell differentiation Source: DFLAT
  27. positive regulation of endothelial cell proliferation Source: DFLAT
  28. positive regulation of pathway-restricted SMAD protein phosphorylation Source: MGI
  29. positive regulation of transcription, DNA-templated Source: DFLAT
  30. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  31. protein heterooligomerization Source: Ensembl
  32. protein phosphorylation Source: MGI
  33. regulation of blood pressure Source: MGI
  34. regulation of transcription, DNA-templated Source: MGI
  35. retina vasculature development in camera-type eye Source: BHF-UCL
  36. signal transduction Source: MGI
  37. transforming growth factor beta receptor signaling pathway Source: MGI
  38. venous blood vessel development Source: BHF-UCL
  39. wound healing, spreading of epidermal cells Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Receptor, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Angiogenesis

Keywords - Ligandi

ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.2. 3474.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase receptor R3 (EC:2.7.11.30)
Short name:
SKR3
Alternative name(s):
Activin receptor-like kinase 1
Short name:
ALK-1
TGF-B superfamily receptor type I
Short name:
TSR-I
Gene namesi
Name:Acvrl1
Synonyms:Acvrlk1, Alk-1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:1338946. Acvrl1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini23 – 11997ExtracellularSequence AnalysisAdd
BLAST
Transmembranei120 – 14021HelicalSequence AnalysisAdd
BLAST
Topological domaini141 – 502362CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cell surface Source: MGI
  2. dendrite Source: Ensembl
  3. integral component of plasma membrane Source: MGI
  4. neuronal cell body Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence AnalysisAdd
BLAST
Chaini23 – 502480Serine/threonine-protein kinase receptor R3PRO_0000024421Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi32 – 321N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi33 ↔ 50By similarity
Disulfide bondi35 ↔ 40By similarity
Disulfide bondi45 ↔ 68By similarity
Disulfide bondi76 ↔ 88By similarity
Disulfide bondi89 ↔ 94By similarity
Glycosylationi97 – 971N-linked (GlcNAc...)Sequence Analysis
Modified residuei154 – 1541Phosphoserine1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ61288.
PRIDEiQ61288.

PTM databases

PhosphoSiteiQ61288.

Expressioni

Gene expression databases

BgeeiQ61288.
CleanExiMM_ACVRL1.
ExpressionAtlasiQ61288. baseline and differential.
GenevestigatoriQ61288.

Interactioni

Protein-protein interaction databases

BioGridi197957. 1 interaction.
DIPiDIP-47635N.
IntActiQ61288. 4 interactions.
MINTiMINT-4086807.

Structurei

3D structure databases

ProteinModelPortaliQ61288.
SMRiQ61288. Positions 30-103, 171-491.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini171 – 20030GSPROSITE-ProRule annotationAdd
BLAST
Domaini201 – 502302Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni72 – 754Mediates specificity for BMP ligandBy similarity

Sequence similaritiesi

Contains 1 GS domain.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118876.
HOGENOMiHOG000230587.
HOVERGENiHBG054502.
InParanoidiQ61288.
KOiK13594.
OMAiWHVRRRQ.
OrthoDBiEOG7Q8CN3.
TreeFamiTF314724.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR000472. TFB_recept_I/II_C.
IPR003605. TGF_beta_rcpt_GS.
IPR000333. TGFB_receptor.
[Graphical view]
PANTHERiPTHR23255. PTHR23255. 1 hit.
PfamiPF01064. Activin_recp. 1 hit.
PF00069. Pkinase. 1 hit.
PF08515. TGF_beta_GS. 1 hit.
[Graphical view]
SMARTiSM00467. GS. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51256. GS. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q61288-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTLGSFRRGL LMLSVAFGLT RGDLAKPSKL VNCTCESPHC KRPFCQGSWC
60 70 80 90 100
TVVLVREQGR HPQVYRGCGS LNQELCLGRP TEFLNHHCCY RSFCNHNVSL
110 120 130 140 150
MLEATQTPSE EPEVDAHLPL ILGPVLALPV LVALGALGLW RVRRRQEKQR
160 170 180 190 200
DLHSDLGESS LILKASEQAD SMLGDFLDSD CTTGSGSGLP FLVQRTVARQ
210 220 230 240 250
VALVECVGKG RYGEVWRGSW HGESVAVKIF SSRDEQSWFR ETEIYNTVLL
260 270 280 290 300
RHDNILGFIA SDMTSRNSST QLWLITHYHE HGSLYDFLQR QTLEPQLALR
310 320 330 340 350
LAVSAACGLA HLHVEIFGTQ GKPAIAHRDL KSRNVLVKSN LQCCIADLGL
360 370 380 390 400
AVMHSQSSDY LDIGNNPRVG TKRYMAPEVL DEHIRTDCFE SYKWTDIWAF
410 420 430 440 450
GLVLWEIARR TIINGIVEDY RPPFYDMVPN DPSFEDMKKV VCVDQQTPTI
460 470 480 490 500
PNRLAADPVL SGLAQMMREC WYPNPSARLT ALRIKKTLQK LSHNPEKPKV

IH
Length:502
Mass (Da):56,519
Last modified:July 26, 2011 - v2
Checksum:i439510D3CC740D65
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti17 – 171F → L in CAA83484 (PubMed:7750489).Curated
Sequence conflicti21 – 211R → Q (PubMed:7750489).Curated
Sequence conflicti23 – 231D → R (PubMed:7750489).Curated
Sequence conflicti25 – 262AK → RR in AAB03642 (PubMed:7488127).Curated
Sequence conflicti305 – 3051A → P in CAA83484 (PubMed:7750489).Curated
Sequence conflicti358 – 3592SD → NE in CAA83484 (PubMed:7750489).Curated
Sequence conflicti366 – 3661N → T in CAA83484 (PubMed:7750489).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS37215.1.
PIRiI48241.
JC4337.
RefSeqiNP_001264186.1. NM_001277257.1.
NP_001264187.1. NM_001277258.1.
NP_001264188.1. NM_001277259.1.
NP_033742.2. NM_009612.3.
UniGeneiMm.279542.

Genome annotation databases

EnsembliENSMUST00000000542; ENSMUSP00000000542; ENSMUSG00000000530.
ENSMUST00000117984; ENSMUSP00000113505; ENSMUSG00000000530.
ENSMUST00000119063; ENSMUSP00000113536; ENSMUSG00000000530.
ENSMUST00000120028; ENSMUSP00000113297; ENSMUSG00000000530.
ENSMUST00000120754; ENSMUSP00000112490; ENSMUSG00000000530.
ENSMUST00000121718; ENSMUSP00000114027; ENSMUSG00000000530.
GeneIDi11482.
KEGGimmu:11482.
UCSCiuc007xsm.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS37215.1.
PIRiI48241.
JC4337.
RefSeqiNP_001264186.1. NM_001277257.1.
NP_001264187.1. NM_001277258.1.
NP_001264188.1. NM_001277259.1.
NP_033742.2. NM_009612.3.
UniGeneiMm.279542.

3D structure databases

ProteinModelPortaliQ61288.
SMRiQ61288. Positions 30-103, 171-491.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi197957. 1 interaction.
DIPiDIP-47635N.
IntActiQ61288. 4 interactions.
MINTiMINT-4086807.

Chemistry

BindingDBiQ61288.

PTM databases

PhosphoSiteiQ61288.

Proteomic databases

PaxDbiQ61288.
PRIDEiQ61288.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000000542; ENSMUSP00000000542; ENSMUSG00000000530.
ENSMUST00000117984; ENSMUSP00000113505; ENSMUSG00000000530.
ENSMUST00000119063; ENSMUSP00000113536; ENSMUSG00000000530.
ENSMUST00000120028; ENSMUSP00000113297; ENSMUSG00000000530.
ENSMUST00000120754; ENSMUSP00000112490; ENSMUSG00000000530.
ENSMUST00000121718; ENSMUSP00000114027; ENSMUSG00000000530.
GeneIDi11482.
KEGGimmu:11482.
UCSCiuc007xsm.1. mouse.

Organism-specific databases

CTDi94.
MGIiMGI:1338946. Acvrl1.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118876.
HOGENOMiHOG000230587.
HOVERGENiHBG054502.
InParanoidiQ61288.
KOiK13594.
OMAiWHVRRRQ.
OrthoDBiEOG7Q8CN3.
TreeFamiTF314724.

Enzyme and pathway databases

BRENDAi2.7.10.2. 3474.

Miscellaneous databases

NextBioi278836.
PROiQ61288.
SOURCEiSearch...

Gene expression databases

BgeeiQ61288.
CleanExiMM_ACVRL1.
ExpressionAtlasiQ61288. baseline and differential.
GenevestigatoriQ61288.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR000472. TFB_recept_I/II_C.
IPR003605. TGF_beta_rcpt_GS.
IPR000333. TGFB_receptor.
[Graphical view]
PANTHERiPTHR23255. PTHR23255. 1 hit.
PfamiPF01064. Activin_recp. 1 hit.
PF00069. Pkinase. 1 hit.
PF08515. TGF_beta_GS. 1 hit.
[Graphical view]
SMARTiSM00467. GS. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51256. GS. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1994) [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(1994) [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.
    , 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(2004) [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 (AUG-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(2003) [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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiACVL1_MOUSE
AccessioniPrimary (citable) accession number: Q61288
Secondary accession number(s): Q61289, Q91YR0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 14, 1998
Last sequence update: July 26, 2011
Last modified: March 31, 2015
This is version 143 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.