MAN1_MOUSE
ID MAN1_MOUSE Reviewed; 921 AA.
AC Q9WU40; Q0VGU6; Q3USB5;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 25-MAY-2022, entry version 142.
DE RecName: Full=Inner nuclear membrane protein Man1;
DE AltName: Full=LEM domain-containing protein 3;
GN Name=Lemd3; Synonyms=Man1;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 1-331.
RX PubMed=10671519; DOI=10.1074/jbc.275.7.4840;
RA Lin F., Blake D.L., Callebaut I., Skerjanc I.S., Holmer L., McBurney M.W.,
RA Paulin-Levasseur M., Worman H.J.;
RT "MAN1, an inner nuclear membrane protein that shares the LEM domain with
RT lamina-associated polypeptide 2 and emerin.";
RL J. Biol. Chem. 275:4840-4847(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 437-921 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 509-921.
RC STRAIN=C57BL/6J; TISSUE=Bone;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140 AND SER-263, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, 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 -!- FUNCTION: Can function as a specific repressor of TGF-beta, activin,
CC and BMP signaling through its interaction with the R-SMAD proteins.
CC Antagonizes TGF-beta-induced cell proliferation arrest (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with SMAD1, SMAD2, SMAD3 and SMAD5. Binds to both
CC phosphorylated and unphosphorylated R-SMADS (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus inner membrane; Multi-pass membrane
CC protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9WU40-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9WU40-2; Sequence=VSP_026782;
CC -!- SEQUENCE CAUTION:
CC Sequence=BC082610; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC140381; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF112300; AAD31594.1; -; mRNA.
DR EMBL; BC082610; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK140538; BAE24418.1; -; mRNA.
DR RefSeq; NP_001074662.2; NM_001081193.2.
DR AlphaFoldDB; Q9WU40; -.
DR SMR; Q9WU40; -.
DR BioGRID; 237587; 7.
DR IntAct; Q9WU40; 1.
DR MINT; Q9WU40; -.
DR STRING; 10090.ENSMUSP00000113103; -.
DR iPTMnet; Q9WU40; -.
DR PhosphoSitePlus; Q9WU40; -.
DR EPD; Q9WU40; -.
DR jPOST; Q9WU40; -.
DR MaxQB; Q9WU40; -.
DR PaxDb; Q9WU40; -.
DR PRIDE; Q9WU40; -.
DR ProteomicsDB; 287305; -. [Q9WU40-1]
DR ProteomicsDB; 287306; -. [Q9WU40-2]
DR GeneID; 380664; -.
DR KEGG; mmu:380664; -.
DR CTD; 23592; -.
DR MGI; MGI:3580376; Lemd3.
DR eggNOG; KOG0147; Eukaryota.
DR InParanoid; Q9WU40; -.
DR OrthoDB; 873705at2759; -.
DR Reactome; R-MMU-4419969; Depolymerisation of the Nuclear Lamina.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013404; RAC2 GTPase cycle.
DR Reactome; R-MMU-9013405; RHOD GTPase cycle.
DR Reactome; R-MMU-9013408; RHOG GTPase cycle.
DR Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR Reactome; R-MMU-9696264; RND3 GTPase cycle.
DR Reactome; R-MMU-9696270; RND2 GTPase cycle.
DR Reactome; R-MMU-9696273; RND1 GTPase cycle.
DR BioGRID-ORCS; 380664; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Lemd3; mouse.
DR PRO; PR:Q9WU40; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9WU40; protein.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0005639; C:integral component of nuclear inner membrane; IBA:GO_Central.
DR GO; GO:0005635; C:nuclear envelope; IDA:MGI.
DR GO; GO:0005637; C:nuclear inner membrane; ISO:MGI.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; IMP:MGI.
DR GO; GO:0002044; P:blood vessel endothelial cell migration involved in intussusceptive angiogenesis; IMP:MGI.
DR GO; GO:0032926; P:negative regulation of activin receptor signaling pathway; ISO:MGI.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; ISO:MGI.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; ISO:MGI.
DR GO; GO:0006998; P:nuclear envelope organization; IBA:GO_Central.
DR GO; GO:0006997; P:nucleus organization; IMP:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:MGI.
DR GO; GO:1903053; P:regulation of extracellular matrix organization; IMP:MGI.
DR GO; GO:1902531; P:regulation of intracellular signal transduction; IEA:InterPro.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IMP:MGI.
DR CDD; cd12286; RRM_Man1; 1.
DR Gene3D; 1.10.10.1180; -; 1.
DR Gene3D; 1.10.720.40; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR011015; LEM/LEM-like_dom_sf.
DR InterPro; IPR003887; LEM_dom.
DR InterPro; IPR034997; Man1.
DR InterPro; IPR034394; Man1_RRM.
DR InterPro; IPR041885; MAN1_winged_helix_dom.
DR InterPro; IPR018996; MSC.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR PANTHER; PTHR13428:SF10; PTHR13428:SF10; 1.
DR Pfam; PF03020; LEM; 1.
DR Pfam; PF09402; MSC; 1.
DR SMART; SM00540; LEM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR SUPFAM; SSF63451; SSF63451; 1.
DR PROSITE; PS50954; LEM; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..921
FT /note="Inner nuclear membrane protein Man1"
FT /id="PRO_0000206150"
FT TRANSMEM 486..506
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 637..657
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 7..51
FT /note="LEM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00313"
FT DNA_BIND 717..736
FT /evidence="ECO:0000250"
FT REGION 47..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 709..921
FT /note="Interaction with SMAD1, SMAD2, SMAD3 and SMAD5"
FT /evidence="ECO:0000250"
FT COMPBIAS 53..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..234
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2U8"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2U8"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2U8"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2U8"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 287
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2U8"
FT MOD_RES 412
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2U8"
FT MOD_RES 787
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2U8"
FT MOD_RES 893
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2U8"
FT MOD_RES 921
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2U8"
FT VAR_SEQ 575
FT /note="K -> KVHLVFKITAENLCFKTLSDASN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026782"
FT CONFLICT 804
FT /note="P -> Q (in Ref. 4; BAE24418)"
FT /evidence="ECO:0000305"
FT CONFLICT 861
FT /note="L -> F (in Ref. 4; BAE24418)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 921 AA; 100307 MW; EBFA12FE19D79F3D CRC64;
MAAATAAAAP QQLSDEELFS QLRRYGLSPG PVTESTRPVY LKKLKKLREE EQQQQQQQQQ
QQHRAGGRGN KTRNSNNNNT ATAMGGRPGS GDLAYLRSPA GLGRLSASAA ESPVAGGSGG
AAAVPAAGSK VLLGFSSDES DVEASPREQA GGGGGGGARR DRAALQYRGL RAPPAPPAAG
EVTGGHPGER RKPHSWWGAR RPAGPEPQPP AAGSDGAAED ADEELADGED RDPEAEEPLW
ASRAVNGSRL LPYSSCREHY SDSEEEEEEG EEDGDVAPAR QVLKDDSLAR HRPRRSHSKP
FSALTAKSGG SRQETSVQGG GALAMNDRAA AAGSLDRSRN LEEAAAEPGG GGGGGCGCDP
VDSIPRYRAG AKKLAPLLSP PSPDGDSTLE SPTGPLLKTN NHIGGGAFGV DSPGLYANSL
PPGATAAAAP GTLRINHANH TGSNHTYLKT AYGKPKLCEP EEELLQQFKR EEVSPTGSFS
AHYLSMFLLT AACLFFLILG LTYLGMRGTG VPEDGGLIKN PFDETFGKIQ ESEKNLLMST
LYKLHDRLAQ IAGDHECGSS SQRMLSVQEA AAYLKNLGPE YEDVFNTSLL WIFKNGKDVG
IRCVGYGPEE DLTNITDVQF LQSTRPQMPF WCRFRRAFIT VTHRLLLLCL GVVLVCVALR
YMRYRWTKEE EETRQMYDMV VKIIDVLRSH NEACQETKDL QPYMPLPHVR DSLIQPQDRK
KMKKVWDRAV DFLAANESRV RTETRRVGGA DFLVWRWIQP SASCDKTLVI PSKVWQGQAF
HLDRRNSPPN SLTPCLKIRN MFDPVMEIGD HWHLAIQEAI LEKCSDNDGI VHIAVDRNSR
EGCVYVKCLS PEYAGKAFKA LHGSWFDGKL VTVKYLRLDR YHHRFPQALT CNTPLKPANK
HMNSLSHLRL RTGLANSQGS S
