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TM245_MOUSE
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   03-AUG-2022, entry version 82.
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   GlyGen; B1AZA5; 4 sites, 1 N-linked glycan (1 site).
DR   iPTMnet; B1AZA5; -.
DR   PhosphoSitePlus; B1AZA5; -.
DR   jPOST; B1AZA5; -.
DR   MaxQB; B1AZA5; -.
DR   PaxDb; B1AZA5; -.
DR   PeptideAtlas; B1AZA5; -.
DR   PRIDE; B1AZA5; -.
DR   ProteomicsDB; 259417; -.
DR   Antibodypedia; 7137; 40 antibodies from 9 providers.
DR   Ensembl; ENSMUST00000068792; ENSMUSP00000067421; ENSMUSG00000055296.
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   OrthoDB; 228524at2759; -.
DR   BioGRID-ORCS; 242474; 3 hits in 58 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 234 other tissues.
DR   ExpressionAtlas; B1AZA5; baseline and differential.
DR   Genevisible; B1AZA5; MM.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR002549; AI-2E-like.
DR   PANTHER; PTHR21716; PTHR21716; 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
 
 
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