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Serine/threonine-protein kinase receptor R3 (SKR3) (EC 2.7.11.30) (Activin receptor-like kinase 1) (ALK-1) (TGF-B superfamily receptor type I) (TSR-I)

 ACVL1_MOUSE             Reviewed;         502 AA.
Q61288; Q61289; Q91YR0;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
22-NOV-2017, entry version 162.
RecName: Full=Serine/threonine-protein kinase receptor R3;
Short=SKR3;
EC=2.7.11.30;
AltName: Full=Activin receptor-like kinase 1;
Short=ALK-1;
AltName: Full=TGF-B superfamily receptor type I;
Short=TSR-I;
Flags: Precursor;
Name=Acvrl1; Synonyms=Acvrlk1, Alk-1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lung;
PubMed=7488127; DOI=10.1006/bbrc.1995.2594;
Wu X., Robinson C.E., Fong H.W., Crabtree J.S., Rodriguez B.R.,
Roe B.A., Gimble J.M.;
"Cloning and characterization of the murine activin receptor like
kinase-1 (ALK-1) homolog.";
Biochem. Biophys. Res. Commun. 216:78-83(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Placenta;
PubMed=7750489; DOI=10.1210/endo.136.6.7750489;
Dewulf N., Verschueren K., Lonnoy O., Moren A., Grimsby S.,
Spiegle K., Miyazono K., Huylebroeck D., ten Dijke P.;
"Distinct spatial and temporal expression patterns of two type I
receptors for bone morphogenetic proteins during mouse
embryogenesis.";
Endocrinology 136:2652-2663(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154; SER-159 AND
SER-160, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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. {ECO:0000250|UniProtKB:P37023}.
-!- CATALYTIC ACTIVITY: ATP + [receptor-protein] = ADP + [receptor-
protein] phosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P37023}; Single-pass type I membrane
protein {ECO:0000255}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
protein kinase family. TGFB receptor subfamily. {ECO:0000305}.
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EMBL; L48015; AAB03642.1; -; mRNA.
EMBL; Z31664; CAA83484.1; -; mRNA.
EMBL; AK160915; BAE36089.1; -; mRNA.
EMBL; AK170870; BAE42083.1; -; mRNA.
EMBL; CH466550; EDL04061.1; -; Genomic_DNA.
EMBL; CH466550; EDL04063.1; -; Genomic_DNA.
EMBL; BC015083; AAH15083.1; -; mRNA.
CCDS; CCDS37215.1; -.
PIR; I48241; I48241.
PIR; JC4337; JC4337.
RefSeq; NP_001264186.1; NM_001277257.1.
RefSeq; NP_001264187.1; NM_001277258.1.
RefSeq; NP_001264188.1; NM_001277259.1.
RefSeq; NP_033742.2; NM_009612.3.
UniGene; Mm.279542; -.
ProteinModelPortal; Q61288; -.
SMR; Q61288; -.
BioGrid; 197957; 1.
DIP; DIP-47635N; -.
IntAct; Q61288; 5.
MINT; MINT-4086807; -.
STRING; 10090.ENSMUSP00000000542; -.
BindingDB; Q61288; -.
iPTMnet; Q61288; -.
PhosphoSitePlus; Q61288; -.
MaxQB; Q61288; -.
PaxDb; Q61288; -.
PeptideAtlas; Q61288; -.
PRIDE; Q61288; -.
Ensembl; ENSMUST00000000542; ENSMUSP00000000542; ENSMUSG00000000530.
Ensembl; ENSMUST00000117984; ENSMUSP00000113505; ENSMUSG00000000530.
Ensembl; ENSMUST00000119063; ENSMUSP00000113536; ENSMUSG00000000530.
Ensembl; ENSMUST00000120028; ENSMUSP00000113297; ENSMUSG00000000530.
Ensembl; ENSMUST00000120754; ENSMUSP00000112490; ENSMUSG00000000530.
Ensembl; ENSMUST00000121718; ENSMUSP00000114027; ENSMUSG00000000530.
GeneID; 11482; -.
KEGG; mmu:11482; -.
UCSC; uc007xsm.2; mouse.
CTD; 94; -.
MGI; MGI:1338946; Acvrl1.
eggNOG; KOG2052; Eukaryota.
eggNOG; ENOG410XQT0; LUCA.
GeneTree; ENSGT00760000118876; -.
HOGENOM; HOG000230587; -.
HOVERGEN; HBG054502; -.
InParanoid; Q61288; -.
KO; K13594; -.
OMA; WHVRRRQ; -.
OrthoDB; EOG091G0BIU; -.
TreeFam; TF314724; -.
BRENDA; 2.7.10.2; 3474.
Reactome; R-MMU-201451; Signaling by BMP.
PRO; PR:Q61288; -.
Proteomes; UP000000589; Chromosome 15.
Bgee; ENSMUSG00000000530; -.
CleanEx; MM_ACVRL1; -.
ExpressionAtlas; Q61288; baseline and differential.
Genevisible; Q61288; MM.
GO; GO:0009986; C:cell surface; ISO:MGI.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0048185; F:activin binding; ISO:MGI.
GO; GO:0016361; F:activin receptor activity, type I; ISO:MGI.
GO; GO:0005524; F:ATP binding; ISO:MGI.
GO; GO:0098821; F:BMP receptor activity; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:MGI.
GO; GO:0004702; F:signal transducer, downstream of receptor, with serine/threonine kinase activity; IEA:Ensembl.
GO; GO:0046332; F:SMAD binding; ISO:MGI.
GO; GO:0050431; F:transforming growth factor beta binding; ISO:MGI.
GO; GO:0005025; F:transforming growth factor beta receptor activity, type I; IEA:Ensembl.
GO; GO:0005024; F:transforming growth factor beta-activated receptor activity; ISO:MGI.
GO; GO:0001525; P:angiogenesis; IMP:MGI.
GO; GO:0060840; P:artery development; IMP:BHF-UCL.
GO; GO:0008015; P:blood circulation; ISO:MGI.
GO; GO:0048514; P:blood vessel morphogenesis; IMP:MGI.
GO; GO:0001974; P:blood vessel remodeling; IMP:BHF-UCL.
GO; GO:0030509; P:BMP signaling pathway; IMP:MGI.
GO; GO:0071773; P:cellular response to BMP stimulus; ISO:MGI.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IDA:BHF-UCL.
GO; GO:0035912; P:dorsal aorta morphogenesis; IMP:BHF-UCL.
GO; GO:0003203; P:endocardial cushion morphogenesis; IMP:BHF-UCL.
GO; GO:0042118; P:endothelial cell activation; TAS:DFLAT.
GO; GO:0061154; P:endothelial tube morphogenesis; ISO:MGI.
GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
GO; GO:0001946; P:lymphangiogenesis; IMP:BHF-UCL.
GO; GO:0060836; P:lymphatic endothelial cell differentiation; IMP:BHF-UCL.
GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; ISO:MGI.
GO; GO:0007162; P:negative regulation of cell adhesion; ISO:MGI.
GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI.
GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI.
GO; GO:0008285; P:negative regulation of cell proliferation; ISO:MGI.
GO; GO:2000279; P:negative regulation of DNA biosynthetic process; ISO:MGI.
GO; GO:0045602; P:negative regulation of endothelial cell differentiation; IDA:DFLAT.
GO; GO:0010596; P:negative regulation of endothelial cell migration; ISO:MGI.
GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IDA:DFLAT.
GO; GO:0051895; P:negative regulation of focal adhesion assembly; ISO:MGI.
GO; GO:0010629; P:negative regulation of gene expression; IMP:BHF-UCL.
GO; GO:0045766; P:positive regulation of angiogenesis; IGI:MGI.
GO; GO:0030513; P:positive regulation of BMP signaling pathway; IDA:DFLAT.
GO; GO:0045603; P:positive regulation of endothelial cell differentiation; IDA:DFLAT.
GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IDA:DFLAT.
GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:DFLAT.
GO; GO:0051291; P:protein heterooligomerization; IEA:Ensembl.
GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
GO; GO:0008217; P:regulation of blood pressure; ISO:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0061298; P:retina vasculature development in camera-type eye; IMP:BHF-UCL.
GO; GO:0007165; P:signal transduction; ISO:MGI.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:MGI.
GO; GO:0060841; P:venous blood vessel development; IMP:BHF-UCL.
GO; GO:0035313; P:wound healing, spreading of epidermal cells; ISO:MGI.
InterPro; IPR003605; GS_dom.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008271; Ser/Thr_kinase_AS.
InterPro; IPR000333; TGFB_receptor.
PANTHER; PTHR23255; PTHR23255; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF08515; TGF_beta_GS; 1.
SMART; SM00467; GS; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51256; GS; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
Angiogenesis; ATP-binding; Cell membrane; Complete proteome;
Disulfide bond; Glycoprotein; Kinase; Magnesium; Manganese; Membrane;
Metal-binding; Nucleotide-binding; Phosphoprotein; Receptor;
Reference proteome; Serine/threonine-protein kinase; Signal;
Transferase; Transmembrane; Transmembrane helix.
SIGNAL 1 22 {ECO:0000255}.
CHAIN 23 502 Serine/threonine-protein kinase receptor
R3.
/FTId=PRO_0000024421.
TOPO_DOM 23 119 Extracellular. {ECO:0000255}.
TRANSMEM 120 140 Helical. {ECO:0000255}.
TOPO_DOM 141 502 Cytoplasmic. {ECO:0000255}.
DOMAIN 171 200 GS. {ECO:0000255|PROSITE-
ProRule:PRU00585}.
DOMAIN 201 502 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 207 215 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 72 75 Mediates specificity for BMP ligand.
{ECO:0000250}.
ACT_SITE 329 329 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 228 228 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 154 154 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 159 159 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 160 160 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CARBOHYD 32 32 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 97 97 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 33 50 {ECO:0000250|UniProtKB:P37023}.
DISULFID 35 40 {ECO:0000250|UniProtKB:P37023}.
DISULFID 45 68 {ECO:0000250|UniProtKB:P37023}.
DISULFID 76 88 {ECO:0000250|UniProtKB:P37023}.
DISULFID 89 94 {ECO:0000250|UniProtKB:P37023}.
CONFLICT 17 17 F -> L (in Ref. 2; CAA83484).
{ECO:0000305}.
CONFLICT 21 21 R -> Q (in Ref. 2). {ECO:0000305}.
CONFLICT 23 23 D -> R (in Ref. 2). {ECO:0000305}.
CONFLICT 25 26 AK -> RR (in Ref. 1; AAB03642).
{ECO:0000305}.
CONFLICT 305 305 A -> P (in Ref. 2; CAA83484).
{ECO:0000305}.
CONFLICT 358 359 SD -> NE (in Ref. 2; CAA83484).
{ECO:0000305}.
CONFLICT 366 366 N -> T (in Ref. 2; CAA83484).
{ECO:0000305}.
SEQUENCE 502 AA; 56519 MW; 439510D3CC740D65 CRC64;
MTLGSFRRGL LMLSVAFGLT RGDLAKPSKL VNCTCESPHC KRPFCQGSWC TVVLVREQGR
HPQVYRGCGS LNQELCLGRP TEFLNHHCCY RSFCNHNVSL MLEATQTPSE EPEVDAHLPL
ILGPVLALPV LVALGALGLW RVRRRQEKQR DLHSDLGESS LILKASEQAD SMLGDFLDSD
CTTGSGSGLP FLVQRTVARQ VALVECVGKG RYGEVWRGSW HGESVAVKIF SSRDEQSWFR
ETEIYNTVLL RHDNILGFIA SDMTSRNSST QLWLITHYHE HGSLYDFLQR QTLEPQLALR
LAVSAACGLA HLHVEIFGTQ GKPAIAHRDL KSRNVLVKSN LQCCIADLGL AVMHSQSSDY
LDIGNNPRVG TKRYMAPEVL DEHIRTDCFE SYKWTDIWAF GLVLWEIARR TIINGIVEDY
RPPFYDMVPN DPSFEDMKKV VCVDQQTPTI PNRLAADPVL SGLAQMMREC WYPNPSARLT
ALRIKKTLQK LSHNPEKPKV IH


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E0015m ELISA kit Activin receptor-like kinase 3,Acvrlk3,ALK-3,BMP type-1A receptor,BMP-2_BMP-4 receptor,Bmpr,Bmpr1a,BMPR-1A,Bone morphogenetic protein receptor type-1A,Mouse,Mus musculus,Serine_threonine-pr 96T
U0015m CLIA Activin receptor-like kinase 3,Acvrlk3,ALK-3,BMP type-1A receptor,BMP-2_BMP-4 receptor,Bmpr,Bmpr1a,BMPR-1A,Bone morphogenetic protein receptor type-1A,Mouse,Mus musculus,Serine_threonine-protein 96T
E0015m ELISA Activin receptor-like kinase 3,Acvrlk3,ALK-3,BMP type-1A receptor,BMP-2_BMP-4 receptor,Bmpr,Bmpr1a,BMPR-1A,Bone morphogenetic protein receptor type-1A,Mouse,Mus musculus,Serine_threonine-protein 96T
EIAAB13074 Eck,Epha2,Ephrin type-A receptor 2,Epithelial cell kinase,Mouse,Mus musculus,Myk2,Sek2,Tyrosine-protein kinase receptor ECK,Tyrosine-protein kinase receptor MPK-5,Tyrosine-protein kinase receptor SEK-
EIAAB13105 Ephb2,Ephrin type-B receptor 2,Epth3,Mouse,Mus musculus,Neural kinase,Nuk,Nuk receptor tyrosine kinase,Sek3,Tyrosine-protein kinase receptor EPH-3,Tyrosine-protein kinase receptor SEK-3
18-661-15094 Receptor-interacting serine-threonine kinase 3 - Receptor interacting protein 3 Polyclonal 0.1 mg


 

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