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MEAK7_MOUSE
ID   MEAK7_MOUSE             Reviewed;         455 AA.
AC   Q8K0P3; Q69ZF1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=MTOR-associated protein MEAK7 {ECO:0000305};
DE            Short=MEAK7 {ECO:0000305};
DE   AltName: Full=TBC/LysM-associated domain-containing protein 1;
DE   AltName: Full=TLD domain-containing protein 1;
GN   Name=Meak7; Synonyms=Kiaa1609, Tldc1 {ECO:0000312|MGI:MGI:1921597};
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] (ISOFORM 2).
RC   TISSUE=Pancreatic islet;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Urinary bladder;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Colon;
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).
CC   -!- FUNCTION: Activates an alternative mTOR signaling through RPS6KB2
CC       activation and EIF4EBP1 repression to regulate cell proliferation and
CC       migration. Recruits MTOR at the lysosome, essential for MTOR signaling
CC       at the lysosome. {ECO:0000250|UniProtKB:Q6P9B6}.
CC   -!- SUBUNIT: Interacts (via C-terminal domain) with MTOR and MLST8; the
CC       interaction with MTOR increases upon nutrient stimulation.
CC       {ECO:0000250|UniProtKB:Q6P9B6}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q6P9B6}.
CC       Cytoplasm {ECO:0000250|UniProtKB:Q6P9B6}. Lysosome
CC       {ECO:0000250|UniProtKB:Q6P9B6}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8K0P3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8K0P3-2; Sequence=VSP_030079, VSP_030080;
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32493.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAD32493.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AK173215; BAD32493.1; ALT_SEQ; mRNA.
DR   EMBL; AK079186; BAC37572.1; -; mRNA.
DR   EMBL; BC030874; AAH30874.1; -; mRNA.
DR   CCDS; CCDS40494.1; -. [Q8K0P3-1]
DR   RefSeq; NP_083159.1; NM_028883.2. [Q8K0P3-1]
DR   AlphaFoldDB; Q8K0P3; -.
DR   SMR; Q8K0P3; -.
DR   STRING; 10090.ENSMUSP00000044430; -.
DR   iPTMnet; Q8K0P3; -.
DR   PhosphoSitePlus; Q8K0P3; -.
DR   EPD; Q8K0P3; -.
DR   jPOST; Q8K0P3; -.
DR   MaxQB; Q8K0P3; -.
DR   PaxDb; Q8K0P3; -.
DR   PeptideAtlas; Q8K0P3; -.
DR   PRIDE; Q8K0P3; -.
DR   ProteomicsDB; 259457; -. [Q8K0P3-1]
DR   Antibodypedia; 48850; 224 antibodies from 18 providers.
DR   Ensembl; ENSMUST00000049156; ENSMUSP00000044430; ENSMUSG00000034105. [Q8K0P3-1]
DR   GeneID; 74347; -.
DR   KEGG; mmu:74347; -.
DR   UCSC; uc009nqh.1; mouse. [Q8K0P3-1]
DR   CTD; 57707; -.
DR   MGI; MGI:1921597; Meak7.
DR   VEuPathDB; HostDB:ENSMUSG00000034105; -.
DR   eggNOG; KOG2557; Eukaryota.
DR   GeneTree; ENSGT00940000158087; -.
DR   HOGENOM; CLU_036763_2_0_1; -.
DR   InParanoid; Q8K0P3; -.
DR   OMA; VIEDWVF; -.
DR   OrthoDB; 585082at2759; -.
DR   PhylomeDB; Q8K0P3; -.
DR   TreeFam; TF316541; -.
DR   BioGRID-ORCS; 74347; 1 hit in 71 CRISPR screens.
DR   ChiTaRS; Tldc1; mouse.
DR   PRO; PR:Q8K0P3; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q8K0P3; protein.
DR   Bgee; ENSMUSG00000034105; Expressed in retinal neural layer and 166 other tissues.
DR   ExpressionAtlas; Q8K0P3; baseline and differential.
DR   Genevisible; Q8K0P3; MM.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:1903204; P:negative regulation of oxidative stress-induced neuron death; IDA:MGI.
DR   GO; GO:0150032; P:positive regulation of protein localization to lysosome; ISS:UniProtKB.
DR   GO; GO:0030334; P:regulation of cell migration; ISS:UniProtKB.
DR   GO; GO:0042127; P:regulation of cell population proliferation; ISS:UniProtKB.
DR   GO; GO:0043200; P:response to amino acid; ISS:UniProtKB.
DR   GO; GO:0032868; P:response to insulin; ISS:UniProtKB.
DR   GO; GO:0031667; P:response to nutrient levels; ISS:UniProtKB.
DR   GO; GO:0031929; P:TOR signaling; ISS:UniProtKB.
DR   InterPro; IPR006571; TLDc_dom.
DR   Pfam; PF07534; TLD; 1.
DR   SMART; SM00584; TLDc; 1.
DR   PROSITE; PS51886; TLDC; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cytoplasm; Lipoprotein; Lysosome; Membrane;
KW   Myristate; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..455
FT                   /note="MTOR-associated protein MEAK7"
FT                   /id="PRO_0000313641"
FT   DOMAIN          242..410
FT                   /note="TLDc"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01234"
FT   REGION          435..455
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        436..455
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P9B6"
FT   VAR_SEQ         21..72
FT                   /note="QAEVDKLFDVLSSSEGGVATGTFSLEAMKSHVKEALPPAMVTRLYNGMQRVK
FT                   -> HPGCAVRHLPQLPPGPGASATLAPAVLHAAPRAELLPALQPHHQPGAQPACP (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15368895"
FT                   /id="VSP_030079"
FT   VAR_SEQ         73..455
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15368895"
FT                   /id="VSP_030080"
SQ   SEQUENCE   455 AA;  50845 MW;  470FAB93926646C0 CRC64;
     MGNAKSLSGQ KMASRFLPEE QAEVDKLFDV LSSSEGGVAT GTFSLEAMKS HVKEALPPAM
     VTRLYNGMQR VKPTDRTLGS CRSVSREQFT AFLSQLLRGS CEEKGLMVMN MISDAEGPTK
     TRDVQKFTED LVASVAHVLT HRHELRGWTC RKSEVPPDSM QAMVAQLLSE MKFQDGYKFQ
     GPQCLDQVCD QAMIEEWVFH VPHVGMFLSV VVHRGLCLLG SSFDPSTLVP ECLADQGGRF
     ESILDVLSVI YLSSHLAPEH RQRWRLLFST QLHGQSFSQL CSHITSQGPS LLVLEDRDGY
     VFGGFASCSW EVKPQFQGDN RCFLFSIAPR MATHLHTGYN NHFMYLNYGQ QTMPNGLGMG
     GQHHYFGLWV AADFGKGHSK AKPACTTYNS PQLSAQEDFL FDKMEVWGLG NLLEEYEGKN
     KKSVLDSNPE ARSLLEISGR ARHSEGLREV PRDED
 
 
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