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Protein

Trimeric intracellular cation channel type B

Gene

Tmem38b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Potassium channel

Keywords - Biological processi

Ion transport, Potassium transport, Transport

Keywords - Ligandi

Potassium

Protein family/group databases

TCDBi1.A.62.1.2. the homotrimeric cation channel (tric) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Trimeric intracellular cation channel type B
Short name:
TRIC-B
Short name:
TRICB
Alternative name(s):
Mitsugumin-33B
Transmembrane protein 38B
Gene namesi
Name:Tmem38b
Synonyms:D4Ertd89e, Mg33b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1098718. Tmem38b.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4747LumenalSequence analysisAdd
BLAST
Transmembranei48 – 6821HelicalSequence analysisAdd
BLAST
Topological domaini69 – 757CytoplasmicSequence analysis
Transmembranei76 – 9621HelicalSequence analysisAdd
BLAST
Topological domaini97 – 13943CytoplasmicSequence analysisAdd
BLAST
Transmembranei140 – 16021HelicalSequence analysisAdd
BLAST
Topological domaini161 – 20545LumenalSequence analysisAdd
BLAST
Transmembranei206 – 22621HelicalSequence analysisAdd
BLAST
Topological domaini227 – 29266CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Disruption phenotypei

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 E10.5.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 292292Trimeric intracellular cation channel type BPRO_0000291525Add
BLAST

Proteomic databases

MaxQBiQ9DAV9.
PaxDbiQ9DAV9.
PRIDEiQ9DAV9.

PTM databases

PhosphoSiteiQ9DAV9.
SwissPalmiQ9DAV9.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiQ9DAV9.
CleanExiMM_TMEM38B.
ExpressionAtlasiQ9DAV9. baseline and differential.
GenevisibleiQ9DAV9. MM.

Interactioni

Subunit structurei

Homotrimer.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000030127.

Family & Domainsi

Domaini

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).By similarity

Sequence similaritiesi

Belongs to the TMEM38 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3944. Eukaryota.
ENOG410XQ0P. LUCA.
GeneTreeiENSGT00390000018845.
HOGENOMiHOG000037929.
HOVERGENiHBG059853.
InParanoidiQ9DAV9.
OMAiKITMMIT.
OrthoDBiEOG7DJSMZ.
PhylomeDBiQ9DAV9.
TreeFamiTF313483.

Family and domain databases

InterProiIPR007866. TRIC_channel.
[Graphical view]
PANTHERiPTHR12454. PTHR12454. 1 hit.
PfamiPF05197. TRIC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9DAV9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEYPWDDLTL AFSRTSMFPF FDIAHYLVSV MALKQRPGAV AAAWNNPLAS
60 70 80 90 100
WLSAMLHCFG GGILSCMLLA ESPLKFLTNH TNILLASSIW YIVFFCPRDL
110 120 130 140 150
VSQGYSYQPI QFLAAGMKEV TRTWKIVGGV SDANSYYRNA WIVMIVVGWA
160 170 180 190 200
RGAGGAVVTA CEQLLKGDWK PEGDEWLKMS FPCKITLLGS IMFTFQHTRH
210 220 230 240 250
LAISKHDLMF LYTIFLVTIK VTMMMTKDTA VTLTPFEDTL TRMLFGRRQQ
260 270 280 290
QQFSSSEKKT EVKPSSNGSA SSASKRGAEP SGGAKRHAKK ED
Length:292
Mass (Da):32,640
Last modified:June 1, 2001 - v1
Checksum:iDD958501F8CDE083
GO

Sequence cautioni

The sequence CAM21468.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti192 – 1921M → I in BAE22836 (PubMed:16141072).Curated
Sequence conflicti225 – 2251M → I in BAE31700 (PubMed:16141072).Curated
Sequence conflicti291 – 2911E → G in BAE29509 (PubMed:16141072).Curated
Sequence conflicti291 – 2911E → G in BAE29938 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS18193.1.
RefSeqiNP_082329.1. NM_028053.2.
UniGeneiMm.27184.

Genome annotation databases

EnsembliENSMUST00000030127; ENSMUSP00000030127; ENSMUSG00000028420.
GeneIDi52076.
KEGGimmu:52076.
UCSCiuc008sxh.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS18193.1.
RefSeqiNP_082329.1. NM_028053.2.
UniGeneiMm.27184.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000030127.

Protein family/group databases

TCDBi1.A.62.1.2. the homotrimeric cation channel (tric) family.

PTM databases

PhosphoSiteiQ9DAV9.
SwissPalmiQ9DAV9.

Proteomic databases

MaxQBiQ9DAV9.
PaxDbiQ9DAV9.
PRIDEiQ9DAV9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030127; ENSMUSP00000030127; ENSMUSG00000028420.
GeneIDi52076.
KEGGimmu:52076.
UCSCiuc008sxh.2. mouse.

Organism-specific databases

CTDi55151.
MGIiMGI:1098718. Tmem38b.

Phylogenomic databases

eggNOGiKOG3944. Eukaryota.
ENOG410XQ0P. LUCA.
GeneTreeiENSGT00390000018845.
HOGENOMiHOG000037929.
HOVERGENiHBG059853.
InParanoidiQ9DAV9.
OMAiKITMMIT.
OrthoDBiEOG7DJSMZ.
PhylomeDBiQ9DAV9.
TreeFamiTF313483.

Miscellaneous databases

ChiTaRSiTmem38b. mouse.
PROiQ9DAV9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DAV9.
CleanExiMM_TMEM38B.
ExpressionAtlasiQ9DAV9. baseline and differential.
GenevisibleiQ9DAV9. MM.

Family and domain databases

InterProiIPR007866. TRIC_channel.
[Graphical view]
PANTHERiPTHR12454. PTHR12454. 1 hit.
PfamiPF05197. TRIC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Bone marrow, Egg and Placenta.
  3. 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Kidney, Liver, Lung and Testis.

Entry informationi

Entry nameiTM38B_MOUSE
AccessioniPrimary (citable) accession number: Q9DAV9
Secondary accession number(s): A2AQG4
, Q3U6M4, Q3UBM6, Q3UWS8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 107 of the entry and version 1 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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.