Reviewed, UniProtKB/Swiss-Prot P37172 (ACVR1_MOUSE)

Names and origin

Protein names

Recommended name:
    Activin receptor type-1
    EC=2.7.11.30
Alternative name(s):
    Activin receptor type I
      Short name=ACTR-I
    Serine/threonine-protein kinase receptor R1
      Short name=SKR1
    TGF-B superfamily receptor type I
      Short name=TSR-I
    TSK-7L

Gene names

Name:	Acvr1
Synonyms:	Acvrlk2, Tgfb1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	509 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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 activin. May be involved in left-right pattern formation during embryogenesis.
Catalytic activity	ATP + [receptor-protein] = ADP + [receptor-protein] phosphate.
Cofactor	Magnesium or manganese By similarity.
Subcellular location	Membrane; Single-pass type I membrane protein.
Tissue specificity	Expressed in normal parenchymal cells, endothelial cells, fibroblasts and tumor-derived epithelial cells.
Developmental stage	Highly expressed in the node and midline and weakly expressed in E8.5 embryos and in the lateral plate mesoderm.
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
Cellular component	Membrane
Domain	Signal Transmembrane
Ligand	ATP-binding Magnesium Manganese Metal-binding Nucleotide-binding
Molecular function	Kinase Receptor Serine/threonine-protein kinase Transferase
PTM	Glycoprotein Phosphoprotein
Gene Ontology (GO)
Biological process	acute inflammatory response Inferred from expression pattern. Source: UniProtKB determination of left/right symmetry Ref.5 Inferred from mutant phenotype. Source: MGI gastrulation with mouth forming second Inferred from mutant phenotype. Source: MGI germ cell development Inferred from mutant phenotype. Source: MGI heart development Inferred from mutant phenotype. Source: MGI in utero embryonic development Inferred from mutant phenotype. Source: MGI mesoderm formation Inferred from mutant phenotype. Source: MGI neural crest cell migration Inferred from mutant phenotype. Source: MGI patterning of blood vessels Inferred from mutant phenotype. Source: MGI pharyngeal system development Inferred from mutant phenotype. Source: MGI smooth muscle cell differentiation Inferred from mutant phenotype. Source: MGI transforming growth factor beta receptor signaling pathway Inferred from direct assay. Source: MGI
Cellular component	apical part of cell Inferred from direct assay. Source: MGI integral to plasma membrane Inferred from direct assay. Source: MGI
Molecular function	activin binding Inferred from physical interaction. Source: MGI activin receptor activity, type I Inferred from direct assay. Source: MGI transforming growth factor beta binding Inferred from direct assay. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Signal peptide	1 – 20	20	By similarity
	Chain	21 – 509	489	Activin receptor type-1
Regions
	Topological domain	21 – 123	103	Extracellular Potential
	Transmembrane	124 – 146	23	Potential
	Topological domain	147 – 509	363	Cytoplasmic Potential
	Domain	178 – 207	30	GS
	Domain	208 – 502	295	Protein kinase
	Nucleotide binding	214 – 222	9	ATP By similarity
Sites
	Active site	336	1	Proton acceptor By similarity
	Binding site	235	1	ATP By similarity
Amino acid modifications
	Modified residue	501	1	Phosphoserine By similarity
	Glycosylation	102	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	27	1	K → E in BAE29239 and BAE29286. Ref.3
	Sequence conflict	60	1	N → Y in AAA40495. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P37172-1 [UniParc]. Last modified October 17, 2006. Version 2. Checksum: 05BCFC22C5740028	FASTA	509	57,226
	10 20 30 40 50 60 MVDGVMILPV LMMMAFPSPS VEDEKPKVNQ KLYMCVCEGL SCGNEDHCEG QQCFSSLSIN 70 80 90 100 110 120 DGFHVYQKGC FQVYEQGKMT CKTPPSPGQA VECCQGDWCN RNITAQLPTK GKSFPGTQNF 130 140 150 160 170 180 HLEVGLIILS VVFAVCLLAC ILGVALRKFK RRNQERLNPR DVEYGTIEGL ITTNVGDSTL 190 200 210 220 230 240 AELLDHSCTS GSGSGLPFLV QRTVARQITL LECVGKGRYG EVWRGSWQGE NVAVKIFSSR 250 260 270 280 290 300 DEKSWFRETE LYNTVMLRHE NILGFIASDM TSRHSSTQLW LITHYHEMGS LYDYLQLTTL 310 320 330 340 350 360 DTVSCLRIVL SIASGLAHLH IEIFGTQGKS AIAHRDLKSK NILVKKNGQC CIADLGLAVM 370 380 390 400 410 420 HSQSTNQLDV GNNPRVGTKR YMAPEVLDET IQVDCFDSYK RVDIWAFGLV LWEVARRMVS 430 440 450 460 470 480 NGIVEDYKPP FYDVVPNDPS FEDMRKVVCV DQQRPNIPNR WFSDPTLTSL AKLMKECWYQ 490 500 NPSARLTALR IKKTLTKIDN SLDKLKTDC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of a type I TGF-beta receptor and its effect on TGF-beta binding to the type II receptor." Ebner R., Chen H., Shum L., Lawler S., Lee A.L., Zioncheck T.F., Lopez A.R., Derynck R. Science 260:1344-1348(1993) [PubMed: 8388127] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Mammary gland.
[2]	"High-throughput sequence identification of gene coding variants within alcohol-related QTLs." Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J., Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M. Mamm. Genome 12:657-663(2001) [PubMed: 11471062] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: ILS and ISS.
[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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Bone marrow.
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6. Tissue: Brain.
[5]	"BMP signaling through ACVRI is required for left-right patterning in the early mouse embryo." Kishigami S., Yoshikawa S., Castranio T., Okazaki K., Furuta Y., Mishina Y. Dev. Biol. 276:185-193(2004) [PubMed: 15531373] [Abstract] Cited for: DEVELOPMENTAL STAGE, FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L15436 mRNA. Translation: AAA40495.1. AF332087 mRNA. Translation: AAK56115.1. AF332088 mRNA. Translation: AAK56116.1. AK150014 mRNA. Translation: BAE29239.1. AK150075 mRNA. Translation: BAE29286.1. BC058718 mRNA. Translation: AAH58718.1.
PIR	I59576. A37489.
RefSeq	NP_001103674.1. NP_001103675.1. NP_031420.2.
UniGene	Mm.689
3D structure databases
HSSP	HSSP built from PDB template 1IAS based on UniProtKB P36897.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:5798N.
PTM databases
PhosphoSite	P37172.
Genome annotation databases
Ensembl	ENSMUSG00000026836. Mus musculus. [Contig view]
GeneID	11477.
KEGG	mmu:11477.
Organism-specific databases
MGI	MGI:87911. Acvr1.
Phylogenomic databases
HOGENOM	P37172.
HOVERGEN	P37172.
Gene expression databases
ArrayExpress	P37172.
CleanEx	MM_ACVR1. MM_TGFB1.
GermOnline	ENSMUSG00000026836. Mus musculus.
Family and domain databases
InterPro	IPR000333. Activin_II_recpt. IPR000472. Activin_rcpt. IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_bd_CS. IPR017442. Se/Thr_pkinase-rel. IPR008271. Ser_thr_pkin_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]
PRINTS	PR00653. ACTIVIN2R.
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00467. GS. 1 hit. [Graphical view]
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]
BLOCKS	Search...
Other Resources
SOURCE	Search...
ProtoNet	Search...

Entry information

Entry name

ACVR1_MOUSE

Accession

Primary (citable) accession number: P37172
Secondary accession number(s): Q3UDH5, Q91VF1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 17, 2006
Last modified:	July 22, 2008
This is version 82 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)