ID TM245_MOUSE Reviewed; 876 AA.
AC B1AZA5;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 24-JAN-2024, entry version 88.
DE RecName: Full=Transmembrane protein 245;
GN Name=Tmem245;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [3]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-12 AND SER-16, CLEAVAGE OF INITIATOR METHIONINE [LARGE
RP SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Spleen, and Testis;
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).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the autoinducer-2 exporter (AI-2E) (TC 2.A.86)
CC family. {ECO:0000305}.
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DR EMBL; AL929577; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX470220; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS89746.1; -.
DR RefSeq; XP_006537988.1; XM_006537925.3.
DR AlphaFoldDB; B1AZA5; -.
DR STRING; 10090.ENSMUSP00000103234; -.
DR GlyConnect; 2794; 1 N-Linked glycan (1 site).
DR GlyCosmos; B1AZA5; 4 sites, 1 glycan.
DR GlyGen; B1AZA5; 4 sites, 1 N-linked glycan (1 site).
DR iPTMnet; B1AZA5; -.
DR PhosphoSitePlus; B1AZA5; -.
DR jPOST; B1AZA5; -.
DR MaxQB; B1AZA5; -.
DR PaxDb; 10090-ENSMUSP00000103234; -.
DR PeptideAtlas; B1AZA5; -.
DR ProteomicsDB; 259417; -.
DR Pumba; B1AZA5; -.
DR Antibodypedia; 7137; 42 antibodies from 9 providers.
DR Ensembl; ENSMUST00000068792.13; ENSMUSP00000067421.7; ENSMUSG00000055296.15.
DR AGR; MGI:2445107; -.
DR MGI; MGI:2445107; Tmem245.
DR VEuPathDB; HostDB:ENSMUSG00000055296; -.
DR eggNOG; KOG2365; Eukaryota.
DR GeneTree; ENSGT00390000001667; -.
DR HOGENOM; CLU_005960_0_0_1; -.
DR InParanoid; B1AZA5; -.
DR BioGRID-ORCS; 242474; 3 hits in 61 CRISPR screens.
DR ChiTaRS; Tmem245; mouse.
DR PRO; PR:B1AZA5; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; B1AZA5; Protein.
DR Bgee; ENSMUSG00000055296; Expressed in ascending aorta and 237 other cell types or tissues.
DR ExpressionAtlas; B1AZA5; baseline and differential.
DR Genevisible; B1AZA5; MM.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR002549; AI-2E-like.
DR PANTHER; PTHR21716; TRANSMEMBRANE PROTEIN; 1.
DR PANTHER; PTHR21716:SF4; TRANSMEMBRANE PROTEIN 245; 1.
DR Pfam; PF01594; AI-2E_transport; 1.
PE 1: Evidence at protein level;
KW Acetylation; Glycoprotein; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19131326"
FT CHAIN 2..876
FT /note="Transmembrane protein 245"
FT /id="PRO_0000417169"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 457..477
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 623..643
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 647..667
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 728..748
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 749..769
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 773..793
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 812..832
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 32
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H330"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H330"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H330"
FT MOD_RES 327
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3ZXD8"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H330"
FT MOD_RES 331
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H330"
FT MOD_RES 874
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H330"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 497
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 548
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 572
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 876 AA; 97357 MW; 9CDC1AC21F01A7D6 CRC64;
MADRGGPAEA PSPRGSPRPE SRAPRTVGPG ETPRTAALAL RFDKPIKQAF YNTGAVLFVC
LCCGAAVLVY FILEAFLRPL LWAVLCGTFL HPFKSSLTRL GRLWLRRLHR AHTPIVLAAL
LLPLCFADYG VEALGEQALR RRRLLLLLGA GGPLLYGLYC LGSYLGVQVL LAHAGALICR
GLDYFSSLWI WTLVVGYVLM VSFKWNASTQ RYLRAVSIPV WMILLFHIAS LAGSWRIPVF
LVIVFLMSVG TLYEKQNEKE SAGAELPGQV ISMAASTLAN LAISITGYES STEDQPSDPP
TEPTDKGEPP PALSASSSSS SRSSPSSPSP TLGRQRPEMG TFLRKKKTSD IYFVSLVWAI
IAVQLWLNLW IVQLLPVPVA VWIIKKLVIH FGVVGFLEKR CHAWWQVIEC FLKERQEALA
PWPIIGLGKF LLKVDSKLWH WLNKKMIIWL EKMLDKIISI FIIFLLVIGT LLLALLLTAK
VHQESVHMIE VTSSLINETL ANHPEWANWL PEAQVVQRAL NSAANNVYQY GREWITHKLH
KILGDKVNNT AVIEKQVLEL WDRLYHSWFV KNVTHSGRHK GHKMHVSRQN SWLGDILDWQ
DIASFVHENI ETFLSILESL WIVMSRNVSL LFTTVTTLLT ILFYSGTALL NFVLSLIIFL
TTLFYLLSSS DEYYKPVKWV ISLTPLSQPG PSSNIIGQSV EEAIRGVFDA SLKMAGFYGL
YTWLTHTIFG INIVFIPSAL AAILGAVPFL GTYWAAVPAV LDLWLTQGLG CKAILLLVFH
LLPTYFVDTA IYSDISGGGH PYLTGLAVAG GAYYLGLEGA IIGPILLCIL VVASNIYSAM
LVSPTNSMPT PNQTPWPAQT QRTFRDISED LKSSVD
//
