TMCC2_MOUSE
ID TMCC2_MOUSE Reviewed; 706 AA.
AC Q80W04; Q6A061;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Transmembrane and coiled-coil domains protein 2 {ECO:0000250|UniProtKB:O75069};
GN Name=Tmcc2 {ECO:0000312|MGI:MGI:1916125};
GN Synonyms=Kiaa0481 {ECO:0000303|PubMed:15368895};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 17-706.
RC TISSUE=Fetal brain;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-435; SER-461; SER-467
RP AND SER-500, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Heart, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-163, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: May be involved in the regulation of the proteolytic
CC processing of the amyloid precursor protein (APP) possibly also
CC implicating APOE. {ECO:0000250|UniProtKB:O75069}.
CC -!- SUBUNIT: May form homodimers and heterodimers with TMCC2 or TMCC3 via
CC the coiled-coil domains. Interacts with ribosomal proteins RPL4 and
CC RPS6. Interacts with APOE and proteolytic processed C-terminal fragment
CC C99 of the amyloid precursor protein (APP C99).
CC {ECO:0000250|UniProtKB:O75069}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O75069}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Concentrates in discrete patches along peripheral
CC endoplasmic reticulum tubules. {ECO:0000250|UniProtKB:O75069}.
CC -!- SIMILARITY: Belongs to the TEX28 family. {ECO:0000305}.
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DR EMBL; BC052035; AAH52035.1; -; mRNA.
DR EMBL; AK172957; BAD32235.1; -; mRNA.
DR CCDS; CCDS15284.1; -.
DR RefSeq; NP_001298036.1; NM_001311107.1.
DR RefSeq; NP_001298037.1; NM_001311108.1.
DR RefSeq; NP_849205.1; NM_178874.3.
DR AlphaFoldDB; Q80W04; -.
DR SMR; Q80W04; -.
DR BioGRID; 213094; 7.
DR IntAct; Q80W04; 1.
DR STRING; 10090.ENSMUSP00000038369; -.
DR iPTMnet; Q80W04; -.
DR PhosphoSitePlus; Q80W04; -.
DR jPOST; Q80W04; -.
DR MaxQB; Q80W04; -.
DR PaxDb; Q80W04; -.
DR PeptideAtlas; Q80W04; -.
DR PRIDE; Q80W04; -.
DR ProteomicsDB; 259124; -.
DR Antibodypedia; 2865; 53 antibodies from 18 providers.
DR DNASU; 68875; -.
DR Ensembl; ENSMUST00000045473; ENSMUSP00000038369; ENSMUSG00000042066.
DR GeneID; 68875; -.
DR KEGG; mmu:68875; -.
DR UCSC; uc007cos.1; mouse.
DR CTD; 9911; -.
DR MGI; MGI:1916125; Tmcc2.
DR VEuPathDB; HostDB:ENSMUSG00000042066; -.
DR eggNOG; KOG3850; Eukaryota.
DR GeneTree; ENSGT00940000158314; -.
DR InParanoid; Q80W04; -.
DR OrthoDB; 1175041at2759; -.
DR PhylomeDB; Q80W04; -.
DR TreeFam; TF316292; -.
DR BioGRID-ORCS; 68875; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Tmcc2; mouse.
DR PRO; PR:Q80W04; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q80W04; protein.
DR Bgee; ENSMUSG00000042066; Expressed in fetal liver hematopoietic progenitor cell and 227 other tissues.
DR ExpressionAtlas; Q80W04; baseline and differential.
DR Genevisible; Q80W04; MM.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042982; P:amyloid precursor protein metabolic process; ISO:MGI.
DR InterPro; IPR019394; TEX28/TMCC.
DR PANTHER; PTHR17613; PTHR17613; 1.
DR Pfam; PF10267; Tmemb_cc2; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Endoplasmic reticulum; Membrane; Methylation; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..706
FT /note="Transmembrane and coiled-coil domains protein 2"
FT /id="PRO_0000184598"
FT TRANSMEM 646..666
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 679..699
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 464..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 330..365
FT /evidence="ECO:0000255"
FT COILED 511..630
FT /evidence="ECO:0000255"
FT COMPBIAS 150..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 163
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 435
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 461
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 467
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 500
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 706 AA; 77054 MW; 2BB4604A276C94B2 CRC64;
MKRCKSDELQ QQQGEEDGAG MEDAACLLPG ADLRHGEASS ANSAGGPTSD AGAAVAPNPG
PRSKPPDLKK IQQLSEGSMF GHGLKHLFHS RRRSREREHQ ASQEAQQQQQ QQGLSDQDSP
DEKERSPEMH RVSYAVSLHD LPARPTAFNR VLQQIRSRPS IKRGASLHSS GGSGGRRAKS
SSLEPQRGSP HLLRKAPQDS SLAAILHQHQ GRPRSSSTTD TALLLADGSS AYLLAEEAES
IGDKGDKGDL VALSLPSGPG HGDSDGPISL DVPDGAPDPQ RTKAAIEHLH QKILKITEQI
KIEQEARDDN VAEYLKLANN ADKQQVSRIK QVFEKKNQKS AQTIAQLHKK LEHYRRRLKE
IEQNGPSRQP KDVLRDMQQG LKDVGANMRA GISGFGGGVV EGVKGSLSGL SQATHTAVVS
KPREFASLIR NKFGSADNIA HLKDPMEDGP PEEAARALSG SATLVSSPKY GSDDECSSAS
ASSAGAGSNS GAGPGGALGS PRSNTLYGAP GNLDTLLEEL REIKEGQSHL EDSMEDLKTQ
LQRDYTYMTQ CLQEERYRYE RLEEQLNDLT ELHQNEMTNL KQELASMEEK VAYQSYERAR
DIQEAVESCL TRVTKLELQQ QQQQVVQLEG VENANARALL GKFINVILAL MAVLLVFVST
IANFITPLMK TRLRITSTAL LLLVLFLLWK HWASLTYLLE HVLLPS
