MNAR1_MOUSE
ID MNAR1_MOUSE Reviewed; 917 AA.
AC Q8K3V7; Q14CG5; Q69ZS9;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Major intrinsically disordered Notch2-binding receptor 1;
DE AltName: Full=Membrane integral NOTCH2-associated receptor 1;
DE AltName: Full=Protein DD1;
DE AltName: Full=Ubiquitination and mTOR signaling protein;
GN Name=Minar1; Synonyms=Ubtor;
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 [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
RA Mas C., Meda P.;
RT "Full length cloning of DD1, a novel gene expressed in brain and in islets
RT of Langerhans.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
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 2).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-712, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 -!- FUNCTION: Intrinsically disordered protein which may negatively
CC regulate mTOR signaling pathway by stabilizing the mTOR complex
CC component DEPTOR. Negatively regulates angiogenesis. Negatively
CC regulates cell growth (By similarity). Negatively regulates neurite
CC outgrowth in hippocampal neurons (By similarity).
CC {ECO:0000250|UniProtKB:D3ZJ47, ECO:0000250|UniProtKB:Q9UPX6}.
CC -!- SUBUNIT: Interacts with NOTCH2; this interaction increases MINAR1
CC stability. Interacts (via N-terminus) with DEPTOR (via PDZ domain);
CC this interaction may stabilize DEPTOR protein by impairing its
CC ubiquitination. {ECO:0000250|UniProtKB:Q9UPX6}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9UPX6};
CC Single-pass type IV membrane protein {ECO:0000250|UniProtKB:Q9UPX6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8K3V7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8K3V7-2; Sequence=VSP_013706;
CC -!- TISSUE SPECIFICITY: Expressed in brain and in islets of Langerhans.
CC -!- SIMILARITY: Belongs to the MINAR family. {ECO:0000305}.
CC -!- CAUTION: MINAR1 topology is a matter of debate, some authors think the
CC N-terminus is extracellular, while preliminary experimental results
CC suggest a cytosolic location. {ECO:0000250|UniProtKB:Q9UPX6}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32367.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF529169; AAM93262.1; -; mRNA.
DR EMBL; AK035830; BAC29204.1; -; mRNA.
DR EMBL; AK173089; BAD32367.1; ALT_INIT; Transcribed_RNA.
DR EMBL; CH466560; EDL20893.1; -; Genomic_DNA.
DR EMBL; BC113792; AAI13793.1; -; mRNA.
DR CCDS; CCDS23395.1; -. [Q8K3V7-1]
DR RefSeq; NP_705729.1; NM_153509.2. [Q8K3V7-1]
DR RefSeq; XP_006511020.1; XM_006510957.3. [Q8K3V7-1]
DR RefSeq; XP_017168754.1; XM_017313265.1. [Q8K3V7-1]
DR AlphaFoldDB; Q8K3V7; -.
DR SMR; Q8K3V7; -.
DR STRING; 10090.ENSMUSP00000046111; -.
DR iPTMnet; Q8K3V7; -.
DR PhosphoSitePlus; Q8K3V7; -.
DR PaxDb; Q8K3V7; -.
DR PRIDE; Q8K3V7; -.
DR ProteomicsDB; 269041; -. [Q8K3V7-1]
DR ProteomicsDB; 269042; -. [Q8K3V7-2]
DR Antibodypedia; 2612; 31 antibodies from 14 providers.
DR DNASU; 209743; -.
DR Ensembl; ENSMUST00000044491; ENSMUSP00000046111; ENSMUSG00000039313. [Q8K3V7-1]
DR GeneID; 209743; -.
DR KEGG; mmu:209743; -.
DR UCSC; uc009qzn.2; mouse. [Q8K3V7-1]
DR CTD; 23251; -.
DR MGI; MGI:2667167; Minar1.
DR VEuPathDB; HostDB:ENSMUSG00000039313; -.
DR eggNOG; ENOG502QSCS; Eukaryota.
DR GeneTree; ENSGT00530000063851; -.
DR HOGENOM; CLU_016692_0_0_1; -.
DR InParanoid; Q8K3V7; -.
DR OMA; IPDKRRV; -.
DR OrthoDB; 1321736at2759; -.
DR PhylomeDB; Q8K3V7; -.
DR TreeFam; TF350677; -.
DR BioGRID-ORCS; 209743; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Minar1; mouse.
DR PRO; PR:Q8K3V7; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8K3V7; protein.
DR Bgee; ENSMUSG00000039313; Expressed in habenula and 70 other tissues.
DR ExpressionAtlas; Q8K3V7; baseline and differential.
DR Genevisible; Q8K3V7; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0016525; P:negative regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0010977; P:negative regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0032007; P:negative regulation of TOR signaling; ISS:UniProtKB.
DR InterPro; IPR039706; MINAR1-like.
DR InterPro; IPR009626; MINAR1-like_C.
DR PANTHER; PTHR31530; PTHR31530; 1.
DR Pfam; PF06789; MINAR1_C; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Angiogenesis; Cell membrane; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..917
FT /note="Major intrinsically disordered Notch2-binding
FT receptor 1"
FT /id="PRO_0000157134"
FT TOPO_DOM 1..892
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 893..913
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 914..917
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT REGION 337..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 652..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 706..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 746..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..480
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 746..780
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 712
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 373..382
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15368895"
FT /id="VSP_013706"
SQ SEQUENCE 917 AA; 102792 MW; 065DCB22C917E493 CRC64;
MEANQEASLF LVKILEELDS KQNTVSYQDL CKSLCAQFDL SQLAKLRSVL FYTACLDPNF
PATLFKDKMK CSVNNQQSKK IMVAADIVTI FNLIQMNGGT AKEKLPMSCH KVRKKEASFE
SCRSDTEVCS PTVCEPLNCE LSERPFSRGY PTRQSSKCRK MDCKECPQFV PASEPNFLLG
VSKEVKNRAA SLDRLQALSP YSVASPQPCE MQRTYFPMNI ENEPMSDQDS LPISQGIKET
FISSEEPFVV QSCVQKRNIF KEDFHNLMTV SPSLVGTTNK AEEGHGEPQS QKELHKPPFF
NHSFEMPYHN QYLNPVYSPI PDKRRAKHES LDDLQASTYF GPTPVMGTQD TRRCPGRSSK
QTPWPAKSWS LNTEEVPDFE RSFFNRNPSE EKLRYPNSGS QTPNFSGPDR HPVYLVPKDQ
QKVLPAGYAV KPNGLKSKEI SSPVDLEKHE AVKKFKDKSI SCTSGQHSSD TSSVGTQTEQ
HVLDPPKCKD LCTSGQAKYG DRHAMKQSDD DSEIVSDDIS DIFRFLDDMS ISGSTGVIQS
SCYNSTGSLS QLHKSDCDSS PEHHLAKITN GVSSGKGDKC NRPENVHHSE EELKSSVCKL
VLRIGEIERK LESLSGVREE ISQVLGKLNK LDQKIQQPEK VNVQIDLNSL TSEAPSDDSA
SPRVFRAHSG SHGPKLENSP DWCCSDASGS NSESLRVKAL KKSLFTRPSS RSLTEENSAT
ESKIASISNS PRDWRTITYT NRMSLNEEEI KDAGPANNKD WHRKSKEADR QYDIPPQHRL
PKQPKDGFLV EQVFSPHPYP TSLKGHMKSN PLYTDMRLTE LAEVKRGQPS WTIEEYARNS
GDKGKLTALD LQTQESLNPN NLEYWMEDIY TPGYDSLLKR KEAEFRRAKV CKIAALITAA
ACTVILVIVV PICTMKS
