Q8K348 (ACV1C_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Activin receptor type-1C
EC=2.7.11.30

Alternative name(s):
Activin receptor type IC
Short name=ACTR-IC
Activin receptor-like kinase 7
Short name=ALK-7

Gene names

Name:	Acvr1c
Synonyms:	Alk7

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	493 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	Serine/threonine protein kinase which forms a receptor complex on ligand binding. The receptor complex consisting of 2 type II and 2 type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators, SMAD2 and SMAD3. Receptor for activin AB, activin B and NODAL. Plays a role in cell differentiation, growth arrest and apoptosis.
Catalytic activity	ATP + [receptor-protein] = ADP + [receptor-protein] phosphate.
Cofactor	Magnesium or manganese.
Subunit structure	Binds the type 2 receptor protein ACVR2A By similarity.
Subcellular location	Membrane; Single-pass type I membrane protein By similarity.
Tissue specificity	Expressed in interdigital regions in developing limb buds. Ref.1
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.
Sequence caution	The sequence AK142396 differs from that shown. Reason: Frameshift at position 236.

Ontologies

Keywords
Biological process	Apoptosis
Cellular component	Membrane
Domain	Signal Transmembrane Transmembrane helix
Ligand	ATP-binding Magnesium Manganese Metal-binding Nucleotide-binding
Molecular function	Kinase Receptor Serine/threonine-protein kinase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell differentiation Inferred from sequence or structural similarity. Source: UniProtKB lipid storage Inferred from mutant phenotype PubMed 18480258. Source: MGI negative regulation of chorionic trophoblast cell proliferation Inferred from electronic annotation. Source: Compara negative regulation of insulin secretion Inferred from mutant phenotype PubMed 18480258. Source: MGI negative regulation of trophoblast cell migration Inferred from electronic annotation. Source: Compara nodal signaling pathway Inferred from electronic annotation. Source: Compara positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Inferred from electronic annotation. Source: Compara regulation of apoptotic process Inferred from sequence or structural similarity. Source: UniProtKB response to dietary excess Inferred from mutant phenotype PubMed 18480259. Source: MGI response to glucose stimulus Inferred from mutant phenotype PubMed 18480258. Source: MGI response to insulin stimulus Inferred from mutant phenotype PubMed 18480259. Source: MGI
Cellular_component	activin receptor complex Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW activin receptor activity, type I Inferred from sequence or structural similarity. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW transforming growth factor beta-activated receptor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 25	25	Potential
	Chain	26 – 493	468	Activin receptor type-1C		PRO_0000042629
Regions
	Topological domain	27 – 113	87	Extracellular Potential
	Transmembrane	114 – 134	21	Helical; Potential
	Topological domain	135 – 493	359	Cytoplasmic Potential
	Domain	165 – 194	30	GS
	Domain	195 – 485	291	Protein kinase
	Nucleotide binding	201 – 209	9	ATP By similarity UniProtKB Q04771
Sites
	Active site	323	1	Proton acceptor By similarity UniProtKB Q04771
	Binding site	222	1	ATP By similarity UniProtKB Q04771

Sequences

	Sequence		Length	Mass (Da)
	Q8K348 [UniParc]. Last modified July 27, 2011. Version 3. Checksum: CB9BE5E368CA2D2F	FASTA	493	54,700
	10 20 30 40 50 60 MTPARGSALS LALLLVALAA DLAAGLKCVC LLCDSSNFTC QTEGACWASV MLTNGKEQVI 70 80 90 100 110 120 KSCVSLPELN AQVFCHSSNN VTKTECCFTD FCNNITLHLP TASPNAPRLG PTELTVVITV 130 140 150 160 170 180 PVCLLSIAAM LTIWACQDRQ CTYRKTKRHN VEEALAEYSL VNAGKTLKDL IYDATASGSG 190 200 210 220 230 240 SGLPLLVQRT IARTIVLQEI VGKGRFGEVW HGRWCGEDVA VKIFSSRDER SWFREAEIYQ 250 260 270 280 290 300 TVMLRHENIL GFIAADNKDN GTWTQLWLVS EYHEQGSLYD YLNRNIVTVA GMVKLALSIA 310 320 330 340 350 360 SGLAHLHMEI VGTQGKPAIA HRDIKSKNIL VKKCDTCAIA DLGLAVKHDS IMNTIDIPQN 370 380 390 400 410 420 PKVGTKRYMA PEMLDDTMNL SIFESFKRAD IYSVGLVYWE IARRCSVGGV VEEYQLPYYD 430 440 450 460 470 480 MVPSDPSIEE MRKVVCDQKL RPNLPNQWQS CEALRVMGRI MRECWYANGA ARLTALRVKK 490 TISQLCVKED CKA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"ALK7, a receptor for nodal, is dispensable for embryogenesis and left-right patterning in the mouse." Joernvall H., Reissmann E., Andersson O., Mehrkash M., Ibanez C.F. Mol. Cell. Biol. 24:9383-9389(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[2]	"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]. Tissue: Fetal lung.
[3]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[4]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-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] OF 173-363. Strain: C57BL/6J. Tissue: Mammary gland.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK142396 mRNA. No translation available. AL772179 Genomic DNA. Translation: CAM13260.1. CH466519 Genomic DNA. Translation: EDL26940.1. BC028780 mRNA. Translation: AAH28780.1.
IPI	IPI00720121.
RefSeq	NP_001104500.1. NM_001111030.1.
UniGene	Mm.77751.
3D structure databases
ProteinModelPortal	Q8K348.
SMR	Q8K348. Positions 25-97, 145-485.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-2842395.
STRING	10090.ENSMUSP00000028178.
PTM databases
PhosphoSite	Q8K348.
Proteomic databases
PRIDE	Q8K348.
Protocols and materials databases
DNASU	269275.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000028178; ENSMUSP00000028178; ENSMUSG00000026834.
GeneID	269275.
KEGG	mmu:269275.
Organism-specific databases
CTD	130399.
MGI	MGI:2661081. Acvr1c.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00560000076615.
HOGENOM	HOG000230587.
HOVERGEN	HBG054502.
InParanoid	A2AJR4.
KO	K13568.
OMA	YRKKKRP.
OrthoDB	EOG4PVNZN.
Enzyme and pathway databases
Reactome	REACT_115202. Signal Transduction. REACT_127416. Developmental Biology.
Gene expression databases
ArrayExpress	Q8K348.
Bgee	Q8K348.
CleanEx	MM_ACVR1C.
Genevestigator	Q8K348.
GermOnline	ENSMUSG00000026834. Mus musculus.
Family and domain databases
InterPro	IPR000472. Activin_rcpt. IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR008271. Ser/Thr_kinase_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]
SMART	SM00467. GS. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
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]
ProtoNet	Search...
Other
NextBio	392768.
SOURCE	Search...

Entry information

Entry name

ACV1C_MOUSE

Accession

Primary (citable) accession number: Q8K348
Secondary accession number(s): A2AJR4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 25, 2005
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 101 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program