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Protein

Integral membrane protein 2C

Gene

Itm2c

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

Functioni

Negative regulator of beta amyloid peptide production. May inhibit the processing of APP by blocking its access to alpha- and beta-secretase. Binding to the beta-secretase-cleaved APP C-terminal fragment is negligible, suggesting that ITM2C is a poor gamma-secretase cleavage inhibitor. May play a role in TNF-induced cell death and neuronal differentiation.1 Publication

GO - Molecular functioni

  • ATP binding Source: MGI
  • beta-amyloid binding Source: MGI

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Integral membrane protein 2C
Alternative name(s):
Transmembrane protein BRI3
Cleaved into the following chain:
Gene namesi
Name:Itm2c
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1927594. Itm2c.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei57 – 7721Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Lysosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 269269Integral membrane protein 2CPRO_0000154827Add
BLAST
Peptidei244 – 26926CT-BRI3PRO_0000232646Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei39 – 391PhosphothreonineBy similarity
Disulfide bondi165 ↔ 224By similarity
Glycosylationi171 – 1711N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

Type I membrane-bound, as well as soluble, furin has a pre-eminent role in ITM2C proteolytic processing. PCSK7 and PCSK5 may also be involved although to a lesser extent. The soluble form of PCSK7 is incapable of processing ITM2C. Fails to undergo shedding by ADAM10 and intramembanaire cleavage by SPPL2B (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei243 – 2442Cleavage; by furinBy similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ91VK4.
MaxQBiQ91VK4.
PaxDbiQ91VK4.
PRIDEiQ91VK4.

PTM databases

iPTMnetiQ91VK4.
PhosphoSiteiQ91VK4.
SwissPalmiQ91VK4.

Expressioni

Gene expression databases

BgeeiQ91VK4.
CleanExiMM_ITM2C.
ExpressionAtlasiQ91VK4. baseline and differential.
GenevisibleiQ91VK4. MM.

Interactioni

Subunit structurei

Interacts with BACE1. Interacts with APP. Interacts with STMN2 (By similarity).By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000027425.

Structurei

3D structure databases

ProteinModelPortaliQ91VK4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini138 – 23295BRICHOSPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the ITM2 family.Curated
Contains 1 BRICHOS domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4681. Eukaryota.
ENOG410XRNN. LUCA.
GeneTreeiENSGT00390000005162.
HOGENOMiHOG000231259.
HOVERGENiHBG059373.
InParanoidiQ91VK4.
KOiK18265.
OMAiNPRMLIE.
OrthoDBiEOG70KGQD.
PhylomeDBiQ91VK4.
TreeFamiTF317770.

Family and domain databases

InterProiIPR007084. BRICHOS_dom.
[Graphical view]
PfamiPF04089. BRICHOS. 1 hit.
[Graphical view]
SMARTiSM01039. BRICHOS. 1 hit.
[Graphical view]
PROSITEiPS50869. BRICHOS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q91VK4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVKISFQPAV AGIKADKADK AAASGPASAS APAAEILLTP AREERPPRHR
60 70 80 90 100
SRKGGSVGGV CYLSMGMVVL LMGLVFASVY IYRYFFLAQL ARDNFFHCGV
110 120 130 140 150
LYEDSLSSQI RTRLELEEDV KIYLEENYER INVPVPQFGG GDPADIIHDF
160 170 180 190 200
QRGLTAYHDI SLDKCYVIEL NTTIVLPPRN FWELLMNVKR GTYLPQTYII
210 220 230 240 250
QEEMVVTEHV RDKEALGSFI YHLCNGKDTY RLRRRSTRRR INKRGGKNCN
260
AIRHFENTFV VETLICGVV
Length:269
Mass (Da):30,482
Last modified:April 26, 2005 - v2
Checksum:iB949E6E05EA65502
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121Missing in BAA92762 (PubMed:10679242).Curated
Sequence conflicti246 – 2461G → A in AAH12952 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB030199 mRNA. Translation: BAA92762.1.
AF272044 mRNA. Translation: AAF89493.1.
AF282981 mRNA. Translation: AAK00277.1.
AK036377 mRNA. Translation: BAC29403.1.
BC012952 mRNA. Translation: AAH12952.1.
CCDSiCCDS35641.1.
RefSeqiNP_071862.2. NM_022417.3.
UniGeneiMm.29870.

Genome annotation databases

EnsembliENSMUST00000027425; ENSMUSP00000027425; ENSMUSG00000026223.
GeneIDi64294.
KEGGimmu:64294.
UCSCiuc011wof.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB030199 mRNA. Translation: BAA92762.1.
AF272044 mRNA. Translation: AAF89493.1.
AF282981 mRNA. Translation: AAK00277.1.
AK036377 mRNA. Translation: BAC29403.1.
BC012952 mRNA. Translation: AAH12952.1.
CCDSiCCDS35641.1.
RefSeqiNP_071862.2. NM_022417.3.
UniGeneiMm.29870.

3D structure databases

ProteinModelPortaliQ91VK4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000027425.

PTM databases

iPTMnetiQ91VK4.
PhosphoSiteiQ91VK4.
SwissPalmiQ91VK4.

Proteomic databases

EPDiQ91VK4.
MaxQBiQ91VK4.
PaxDbiQ91VK4.
PRIDEiQ91VK4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000027425; ENSMUSP00000027425; ENSMUSG00000026223.
GeneIDi64294.
KEGGimmu:64294.
UCSCiuc011wof.1. mouse.

Organism-specific databases

CTDi81618.
MGIiMGI:1927594. Itm2c.

Phylogenomic databases

eggNOGiKOG4681. Eukaryota.
ENOG410XRNN. LUCA.
GeneTreeiENSGT00390000005162.
HOGENOMiHOG000231259.
HOVERGENiHBG059373.
InParanoidiQ91VK4.
KOiK18265.
OMAiNPRMLIE.
OrthoDBiEOG70KGQD.
PhylomeDBiQ91VK4.
TreeFamiTF317770.

Miscellaneous databases

ChiTaRSiItm2c. mouse.
PROiQ91VK4.
SOURCEiSearch...

Gene expression databases

BgeeiQ91VK4.
CleanExiMM_ITM2C.
ExpressionAtlasiQ91VK4. baseline and differential.
GenevisibleiQ91VK4. MM.

Family and domain databases

InterProiIPR007084. BRICHOS_dom.
[Graphical view]
PfamiPF04089. BRICHOS. 1 hit.
[Graphical view]
SMARTiSM01039. BRICHOS. 1 hit.
[Graphical view]
PROSITEiPS50869. BRICHOS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Growth suppression of Escherichia coli by induction of expression of mammalian genes with transmembrane or ATPase domains."
    Inoue S., Sano H., Ohta M.
    Biochem. Biophys. Res. Commun. 268:553-561(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Embryo.
  2. "Sequence, genomic structure and tissue expression of human BRI3, a member of the BRI gene family."
    Vidal R., Calero M., Revesz T., Plant G., Ghiso J., Frangione B.
    Gene 266:95-102(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Cloning and characterization of a type II integral transmembrane protein gene, Itm2c, that is highly expressed in the mouse brain."
    Choi S.C., Kim J., Kim T.H., Cho S.Y., Park S.S., Kim K.D., Lee S.H.
    Mol. Cells 12:391-397(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: ICR.
  4. "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.
  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].
    Strain: 129.
    Tissue: Mammary tumor.
  6. "bri3, a novel gene, participates in tumor necrosis factor-alpha-induced cell death."
    Wu H., Liu G., Li C., Zhao S.
    Biochem. Biophys. Res. Commun. 311:518-524(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  7. "Beta-amyloid protein converting enzyme 1 and brain-specific type II membrane protein BRI3: binding partners processed by furin."
    Wickham L., Benjannet S., Marcinkiewicz E., Chretien M., Seidah N.G.
    J. Neurochem. 92:93-102(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.

Entry informationi

Entry nameiITM2C_MOUSE
AccessioniPrimary (citable) accession number: Q91VK4
Secondary accession number(s): Q9JI06, Q9JME8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: April 26, 2005
Last modified: June 8, 2016
This is version 102 of the entry and version 2 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.