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Q61288

- ACVL1_MOUSE

UniProt

Q61288 - ACVL1_MOUSE

Protein

Serine/threonine-protein kinase receptor R3

Gene

Acvrl1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    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

    Magnesium or manganese.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 receptor activity, type I Source: Ensembl
    2. ATP binding Source: UniProtKB-KW
    3. metal ion binding Source: UniProtKB-KW
    4. protein binding Source: DFLAT
    5. receptor signaling protein serine/threonine kinase activity Source: Ensembl
    6. 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 vessel morphogenesis Source: MGI
    4. blood vessel remodeling Source: BHF-UCL
    5. BMP signaling pathway Source: MGI
    6. cellular response to BMP stimulus Source: Ensembl
    7. cellular response to transforming growth factor beta stimulus Source: BHF-UCL
    8. endothelial cell activation Source: DFLAT
    9. endothelial tube morphogenesis Source: Ensembl
    10. in utero embryonic development Source: MGI
    11. lymphangiogenesis Source: BHF-UCL
    12. lymphatic endothelial cell differentiation Source: BHF-UCL
    13. negative regulation of blood vessel endothelial cell migration Source: Ensembl
    14. negative regulation of cell growth Source: Ensembl
    15. negative regulation of DNA biosynthetic process Source: Ensembl
    16. negative regulation of endothelial cell differentiation Source: DFLAT
    17. negative regulation of endothelial cell proliferation Source: DFLAT
    18. negative regulation of focal adhesion assembly Source: Ensembl
    19. positive regulation of angiogenesis Source: MGI
    20. positive regulation of BMP signaling pathway Source: DFLAT
    21. positive regulation of endothelial cell differentiation Source: DFLAT
    22. positive regulation of endothelial cell proliferation Source: DFLAT
    23. positive regulation of pathway-restricted SMAD protein phosphorylation Source: Ensembl
    24. positive regulation of transcription, DNA-templated Source: DFLAT
    25. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    26. protein heterooligomerization Source: Ensembl
    27. regulation of blood pressure Source: Ensembl
    28. retina vasculature development in camera-type eye Source: BHF-UCL
    29. transforming growth factor beta receptor signaling pathway Source: MGI
    30. venous blood vessel development Source: BHF-UCL
    31. wound healing, spreading of epidermal cells Source: Ensembl

    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: Chromosome 15

    Organism-specific databases

    MGIiMGI:1338946. Acvrl1.

    Subcellular locationi

    GO - Cellular componenti

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

    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

    ArrayExpressiQ61288.
    BgeeiQ61288.
    CleanExiMM_ACVRL1.
    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...

    Topological domain

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

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei120 – 14021HelicalSequence AnalysisAdd
    BLAST

    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.
    GeneTreeiENSGT00730000110868.
    HOGENOMiHOG000230587.
    HOVERGENiHBG054502.
    InParanoidiQ91YR0.
    KOiK13594.
    OMAiWHVRRRQ.
    OrthoDBiEOG7Q8CN3.
    TreeFamiTF314724.

    Family and domain databases

    InterProiIPR000472. 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]
    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

    MTLGSFRRGL LMLSVAFGLT RGDLAKPSKL VNCTCESPHC KRPFCQGSWC    50
    TVVLVREQGR HPQVYRGCGS LNQELCLGRP TEFLNHHCCY RSFCNHNVSL 100
    MLEATQTPSE EPEVDAHLPL ILGPVLALPV LVALGALGLW RVRRRQEKQR 150
    DLHSDLGESS LILKASEQAD SMLGDFLDSD CTTGSGSGLP FLVQRTVARQ 200
    VALVECVGKG RYGEVWRGSW HGESVAVKIF SSRDEQSWFR ETEIYNTVLL 250
    RHDNILGFIA SDMTSRNSST QLWLITHYHE HGSLYDFLQR QTLEPQLALR 300
    LAVSAACGLA HLHVEIFGTQ GKPAIAHRDL KSRNVLVKSN LQCCIADLGL 350
    AVMHSQSSDY LDIGNNPRVG TKRYMAPEVL DEHIRTDCFE SYKWTDIWAF 400
    GLVLWEIARR TIINGIVEDY RPPFYDMVPN DPSFEDMKKV VCVDQQTPTI 450
    PNRLAADPVL SGLAQMMREC WYPNPSARLT ALRIKKTLQK LSHNPEKPKV 500
    IH 502
    Length:502
    Mass (Da):56,519
    Last modified:July 27, 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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS37215.1.
    PIRi I48241.
    JC4337.
    RefSeqi NP_001264186.1. NM_001277257.1.
    NP_001264187.1. NM_001277258.1.
    NP_001264188.1. NM_001277259.1.
    NP_033742.2. NM_009612.3.
    UniGenei Mm.279542.

    3D structure databases

    ProteinModelPortali Q61288.
    SMRi Q61288. Positions 30-103, 171-491.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 197957. 1 interaction.
    DIPi DIP-47635N.
    IntActi Q61288. 4 interactions.
    MINTi MINT-4086807.

    PTM databases

    PhosphoSitei Q61288.

    Proteomic databases

    PaxDbi Q61288.
    PRIDEi Q61288.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000000542 ; ENSMUSP00000000542 ; ENSMUSG00000000530 .
    ENSMUST00000117984 ; ENSMUSP00000113505 ; ENSMUSG00000000530 .
    ENSMUST00000119063 ; ENSMUSP00000113536 ; ENSMUSG00000000530 .
    ENSMUST00000120028 ; ENSMUSP00000113297 ; ENSMUSG00000000530 .
    ENSMUST00000120754 ; ENSMUSP00000112490 ; ENSMUSG00000000530 .
    ENSMUST00000121718 ; ENSMUSP00000114027 ; ENSMUSG00000000530 .
    GeneIDi 11482.
    KEGGi mmu:11482.
    UCSCi uc007xsm.1. mouse.

    Organism-specific databases

    CTDi 94.
    MGIi MGI:1338946. Acvrl1.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00730000110868.
    HOGENOMi HOG000230587.
    HOVERGENi HBG054502.
    InParanoidi Q91YR0.
    KOi K13594.
    OMAi WHVRRRQ.
    OrthoDBi EOG7Q8CN3.
    TreeFami TF314724.

    Enzyme and pathway databases

    BRENDAi 2.7.10.2. 3474.

    Miscellaneous databases

    NextBioi 278836.
    PROi Q61288.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q61288.
    Bgeei Q61288.
    CleanExi MM_ACVRL1.
    Genevestigatori Q61288.

    Family and domain databases

    InterProi IPR000472. 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 ]
    PANTHERi PTHR23255. PTHR23255. 1 hit.
    Pfami PF01064. Activin_recp. 1 hit.
    PF00069. Pkinase. 1 hit.
    PF08515. TGF_beta_GS. 1 hit.
    [Graphical view ]
    SMARTi SM00467. GS. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS51256. GS. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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].

    Entry informationi

    Entry nameiACVL1_MOUSE
    AccessioniPrimary (citable) accession number: Q61288
    Secondary accession number(s): Q61289, Q91YR0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 138 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