ITM2C_RAT
ID ITM2C_RAT Reviewed; 269 AA.
AC Q5PQL7;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Integral membrane protein 2C;
DE Contains:
DE RecName: Full=CT-BRI3;
GN Name=Itm2c;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-39, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Negative regulator of amyloid-beta peptide production. May
CC inhibit the processing of APP by blocking its access to alpha- and
CC beta-secretase. Binding to the beta-secretase-cleaved APP C-terminal
CC fragment is negligible, suggesting that ITM2C is a poor gamma-secretase
CC cleavage inhibitor. May play a role in TNF-induced cell death and
CC neuronal differentiation (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with BACE1. Interacts with APP. Interacts with STMN2
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250}; Single-pass type
CC II membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- PTM: Type I membrane-bound, as well as soluble, furin has a pre-eminent
CC role in ITM2C proteolytic processing. PCSK7 and PCSK5 may also be
CC involved although to a lesser extent. The soluble form of PCSK7 is
CC incapable of processing ITM2C. Fails to undergo shedding by ADAM10 and
CC intramembrane cleavage by SPPL2B (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ITM2 family. {ECO:0000305}.
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DR EMBL; BC087127; AAH87127.1; -; mRNA.
DR RefSeq; NP_001009674.1; NM_001009674.1.
DR AlphaFoldDB; Q5PQL7; -.
DR SMR; Q5PQL7; -.
DR BioGRID; 257010; 1.
DR STRING; 10116.ENSRNOP00000023535; -.
DR GlyGen; Q5PQL7; 1 site.
DR iPTMnet; Q5PQL7; -.
DR PhosphoSitePlus; Q5PQL7; -.
DR SwissPalm; Q5PQL7; -.
DR jPOST; Q5PQL7; -.
DR PaxDb; Q5PQL7; -.
DR PRIDE; Q5PQL7; -.
DR Ensembl; ENSRNOT00000023535; ENSRNOP00000023535; ENSRNOG00000017359.
DR GeneID; 301575; -.
DR KEGG; rno:301575; -.
DR UCSC; RGD:1309503; rat.
DR CTD; 81618; -.
DR RGD; 1309503; Itm2c.
DR eggNOG; KOG4681; Eukaryota.
DR GeneTree; ENSGT00950000183115; -.
DR HOGENOM; CLU_074596_0_0_1; -.
DR InParanoid; Q5PQL7; -.
DR OMA; ARTRMEL; -.
DR OrthoDB; 1322680at2759; -.
DR PhylomeDB; Q5PQL7; -.
DR TreeFam; TF317770; -.
DR PRO; PR:Q5PQL7; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000017359; Expressed in frontal cortex and 20 other tissues.
DR Genevisible; Q5PQL7; RN.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0001540; F:amyloid-beta binding; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; ISO:RGD.
DR GO; GO:0042985; P:negative regulation of amyloid precursor protein biosynthetic process; IBA:GO_Central.
DR GO; GO:0010977; P:negative regulation of neuron projection development; ISO:RGD.
DR GO; GO:0030182; P:neuron differentiation; ISS:UniProtKB.
DR GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; ISO:RGD.
DR InterPro; IPR007084; BRICHOS_dom.
DR InterPro; IPR040145; ITM2.
DR PANTHER; PTHR10962; PTHR10962; 1.
DR Pfam; PF04089; BRICHOS; 1.
DR SMART; SM01039; BRICHOS; 1.
DR PROSITE; PS50869; BRICHOS; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cleavage on pair of basic residues; Disulfide bond;
KW Glycoprotein; Lysosome; Membrane; Phosphoprotein; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..269
FT /note="Integral membrane protein 2C"
FT /id="PRO_0000154829"
FT PEPTIDE 244..269
FT /note="CT-BRI3"
FT /id="PRO_0000232648"
FT TRANSMEM 57..77
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT DOMAIN 138..232
FT /note="BRICHOS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00255"
FT SITE 243..244
FT /note="Cleavage; by furin"
FT /evidence="ECO:0000250"
FT MOD_RES 39
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 165..224
FT /evidence="ECO:0000250"
SQ SEQUENCE 269 AA; 30480 MW; 1DCA247E34951006 CRC64;
MVKISFQPAV AGVKAEKADK AAASGPASAS APAAEILLTP AREERPPRHR SRKGGSVGGV
CYLSMGMVVL LMGLVFASVY IYRYFFLAQL ARDNFFHCGV LYEDSLSSQI RTRLELEEDV
KIYLEENYER INVPVPQFGG GDPADIIHDF QRGLTAYHDI SLDKCYVIEL NTTIVLPPRN
FWELLMNVKR GTYLPQTYII QEEMVVTEHV RDKEALGSFI YHLCNGKDTY RLRRRATRRR
INKRGAKNCN AIRHFENTFV VETLICGVV
