Q9DAV9 (TM38B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Trimeric intracellular cation channel type B
Short name=TRIC-B
Short name=TRICB

Alternative name(s):
Mitsugumin-33B
Transmembrane protein 38B

Gene names

Name:	Tmem38b
Synonyms:	D4Ertd89e, Mg33b

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 › Mus

Protein attributes

Sequence length	292 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Monovalent cation channel required for maintenance of rapid intracellular calcium release. May act as a potassium counter-ion channel that functions in synchronization with calcium release from intracellular stores. Ref.1
Subunit structure	Homotrimer By similarity.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.1.
Tissue specificity	Widely expressed. Ref.1
Domain	The second transmembrane domain has been proposed to cross only half of the lipid bilayer and to loop back into the cytosol, so that the domains on each side of this domain are both found on the cytosolic face of the membrane. The cytosolic loop may form an ion-conducting pore By similarity.
Disruption phenotype	Mice are neonatal lethal. Mice lacking Tmem38a and Tmem38b show a weak heartbeat at E9.5 followed by loss of cardiomyocyte viability and embryonic lethality around E10.5. Ref.1
Sequence similarities	Belongs to the TMEM38 family.
Sequence caution	The sequence CAM21468.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Ion transport Potassium transport Transport
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane Transmembrane helix
Ligand	Potassium
Molecular function	Ionic channel Potassium channel
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	potassium channel activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 292	292	Trimeric intracellular cation channel type B		PRO_0000291525
Regions
	Topological domain	1 – 47	47	Lumenal Potential
	Transmembrane	48 – 68	21	Helical; Potential
	Topological domain	69 – 75	7	Cytoplasmic Potential
	Transmembrane	76 – 96	21	Helical; Potential
	Topological domain	97 – 139	43	Cytoplasmic Potential
	Transmembrane	140 – 160	21	Helical; Potential
	Topological domain	161 – 205	45	Lumenal Potential
	Transmembrane	206 – 226	21	Helical; Potential
	Topological domain	227 – 292	66	Cytoplasmic Potential
Amino acid modifications
	Modified residue	266	1	Phosphoserine By similarity
	Modified residue	281	1	Phosphoserine By similarity
Experimental info
	Sequence conflict	192	1	M → I in BAE22836. Ref.2
	Sequence conflict	225	1	M → I in BAE31700. Ref.2
	Sequence conflict	291	1	E → G in BAE29509. Ref.2
	Sequence conflict	291	1	E → G in BAE29938. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9DAV9 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: DD958501F8CDE083	FASTA	292	32,640
	10 20 30 40 50 60 MEYPWDDLTL AFSRTSMFPF FDIAHYLVSV MALKQRPGAV AAAWNNPLAS WLSAMLHCFG 70 80 90 100 110 120 GGILSCMLLA ESPLKFLTNH TNILLASSIW YIVFFCPRDL VSQGYSYQPI QFLAAGMKEV 130 140 150 160 170 180 TRTWKIVGGV SDANSYYRNA WIVMIVVGWA RGAGGAVVTA CEQLLKGDWK PEGDEWLKMS 190 200 210 220 230 240 FPCKITLLGS IMFTFQHTRH LAISKHDLMF LYTIFLVTIK VTMMMTKDTA VTLTPFEDTL 250 260 270 280 290 TRMLFGRRQQ QQFSSSEKKT EVKPSSNGSA SSASKRGAEP SGGAKRHAKK ED

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"TRIC channels are essential for Ca2+ handling in intracellular stores." Yazawa M., Ferrante C., Feng J., Mio K., Ogura T., Zhang M., Lin P.-H., Pan Z., Komazaki S., Kato K., Nishi M., Zhao X., Weisleder N., Sato C., Ma J., Takeshima H. Nature 448:78-82(2007) [PubMed: 17611541] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
[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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Bone marrow, Egg and Placenta.
[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: 19468303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[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: FVB/N. Tissue: Mammary tumor.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB261159 mRNA. Translation: BAF62542.1. AK005479 mRNA. Translation: BAB24068.1. AK136131 mRNA. Translation: BAE22836.1. AK150377 mRNA. Translation: BAE29509.1. AK150892 mRNA. Translation: BAE29938.1. AK153075 mRNA. Translation: BAE31700.1. AL844585 Genomic DNA. Translation: CAM21467.1. AL844585 Genomic DNA. Translation: CAM21468.1. Sequence problems. BC011072 mRNA. Translation: AAH11072.1.
IPI	IPI00119084.
RefSeq	NP_082329.1. NM_028053.2.
UniGene	Mm.27184.
3D structure databases
ModBase	Search...
Protein family/group databases
TCDB	1.A.62.1.2. homotrimeric cation channel (TRIC) family.
PTM databases
PhosphoSite	Q9DAV9.
Proteomic databases
PRIDE	Q9DAV9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000030127; ENSMUSP00000030127; ENSMUSG00000028420. ENSMUST00000144167; ENSMUSP00000120304; ENSMUSG00000028420.
GeneID	52076.
KEGG	mmu:52076.
UCSC	uc008sxh.2. mouse.
Organism-specific databases
CTD	55151.
MGI	MGI:1098718. Tmem38b.
Phylogenomic databases
eggNOG	roNOG13137.
GeneTree	ENSGT00390000018845.
HOGENOM	HBG315839.
HOVERGEN	HBG059853.
InParanoid	Q9DAV9.
OMA	NGWIVMI.
OrthoDB	EOG4DJJXB.
PhylomeDB	Q9DAV9.
Gene expression databases
ArrayExpress	Q9DAV9.
Bgee	Q9DAV9.
CleanEx	MM_TMEM38B.
Genevestigator	Q9DAV9.
Family and domain databases
InterPro	IPR007866. TRIC_channel. [Graphical view]
PANTHER	PTHR12454. DUF714. 1 hit.
Pfam	PF05197. TRIC. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	308474.
SOURCE	Search...

Entry information

Entry name

TM38B_MOUSE

Accession

Primary (citable) accession number: Q9DAV9
Secondary accession number(s): A2AQG4 , Q3U6M4, Q3UBM6, Q3UWS8

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 26, 2007
Last sequence update:	June 1, 2001
Last modified:	November 16, 2011
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program