MAN1_DROME
ID MAN1_DROME Reviewed; 650 AA.
AC Q7JRE4; Q961B2;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Inner nuclear membrane protein Man1 {ECO:0000305};
DE AltName: Full=LEM domain-containing protein Man1 {ECO:0000303|PubMed:16439308};
GN Name=MAN1 {ECO:0000312|FlyBase:FBgn0034962};
GN ORFNames=CG3167 {ECO:0000312|FlyBase:FBgn0034962};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|EMBL:AAN71453.1};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000312|EMBL:AAK93140.1, ECO:0000312|EMBL:AAN71453.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAK93140.1, ECO:0000312|EMBL:AAN71453.1};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4] {ECO:0000305}
RP FUNCTION, INTERACTION WITH LAM AND LAMC, SUBCELLULAR LOCATION, TOPOLOGY,
RP AND DEVELOPMENTAL STAGE.
RX PubMed=16439308; DOI=10.1016/j.ejcb.2005.10.002;
RA Wagner N., Kagermeier B., Loserth S., Krohne G.;
RT "The Drosophila melanogaster LEM-domain protein MAN1.";
RL Eur. J. Cell Biol. 85:91-105(2006).
RN [5] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18723885; DOI=10.1534/genetics.108.091371;
RA Pinto B.S., Wilmington S.R., Hornick E.E., Wallrath L.L., Geyer P.K.;
RT "Tissue-specific defects are caused by loss of the Drosophila MAN1 LEM
RT domain protein.";
RL Genetics 180:133-145(2008).
RN [6] {ECO:0000305}
RP FUNCTION, INTERACTION WITH MAD AND BAF, AND DEVELOPMENTAL STAGE.
RX PubMed=20036230; DOI=10.1016/j.ydbio.2009.11.036;
RA Wagner N., Weyhersmueller A., Blauth A., Schuhmann T., Heckmann M.,
RA Krohne G., Samakovlis C.;
RT "The Drosophila LEM-domain protein MAN1 antagonizes BMP signaling at the
RT neuromuscular junction and the wing crossveins.";
RL Dev. Biol. 339:1-13(2010).
RN [7] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24700158; DOI=10.1534/genetics.114.162941;
RA Barton L.J., Wilmington S.R., Martin M.J., Skopec H.M., Lovander K.E.,
RA Pinto B.S., Geyer P.K.;
RT "Unique and shared functions of nuclear lamina LEM domain proteins in
RT Drosophila.";
RL Genetics 197:653-665(2014).
CC -!- FUNCTION: Inner nuclear membrane protein (PubMed:16439308). Acts as a
CC negative regulator of the BMP (Dpp) signaling cascade during crossvein
CC development in pupal wings and possibly during synaptic transmission at
CC the neuromuscular junction (NMJ) (PubMed:18723885, PubMed:20036230).
CC Appears to be required for pupal development and consequently
CC transition to the adult stage (PubMed:18723885, PubMed:20036230).
CC During pupal development, plays essential and redundant functions with
CC the other LEM domain proteins; bocks and Ote (PubMed:24700158).
CC {ECO:0000269|PubMed:16439308, ECO:0000269|PubMed:18723885,
CC ECO:0000269|PubMed:20036230, ECO:0000269|PubMed:24700158}.
CC -!- SUBUNIT: Interacts with Lam and LamC (PubMed:16439308). Interacts with
CC Mad (PubMed:20036230). Interacts (via N-terminus) with baf
CC (PubMed:20036230). {ECO:0000269|PubMed:16439308,
CC ECO:0000269|PubMed:20036230}.
CC -!- SUBCELLULAR LOCATION: Nucleus inner membrane
CC {ECO:0000269|PubMed:16439308}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16439308}. Cytoplasm {ECO:0000269|PubMed:16439308}.
CC Nucleus, nucleoplasm {ECO:0000269|PubMed:16439308}. Cytoplasm,
CC cytoskeleton, spindle pole {ECO:0000269|PubMed:16439308}. Note=During
CC anaphase and metaphase, detected in the nuclear envelope and spindle
CC poles. {ECO:0000269|PubMed:16439308}.
CC -!- DEVELOPMENTAL STAGE: High levels of expression in eggs and first instar
CC larvae (at protein level) (PubMed:16439308). Levels decline between the
CC second and third instar stages, and then increase during the pupal to
CC adult stages (at protein level) (PubMed:16439308). Expressed in the
CC pupal and larval wing (PubMed:20036230). In pupal wings, expression
CC appears to be enhanced in the presumptive longitudinal veins
CC (PubMed:20036230). {ECO:0000269|PubMed:16439308,
CC ECO:0000269|PubMed:20036230}.
CC -!- DISRUPTION PHENOTYPE: Loss of maternal and zygotic activity results in
CC a reduction in survival at each developmental stage, with mutants
CC rarely surviving to the adult stage (PubMed:18723885). Adult escapers
CC display held out wings and exhibit wing patterning defects with
CC thickened longitudinal veins, a varied number of anterior crossveins,
CC branched posterior crossvein and folded wing blades (PubMed:18723885).
CC In adults, climbing is impaired and their climbing ability further
CC decreases with age (PubMed:18723885). Males are sterile and females
CC display reduced fecundity (PubMed:18723885). No significant decrease in
CC adult survival, however double mutants with either Ote or bocks do not
CC survive to the adult stage (PubMed:24700158). No effect on nuclear
CC envelope formation (PubMed:18723885). Larval brain size and imaginal
CC disks are normal in double mutants with either Ote or bocks
CC (PubMed:24700158). {ECO:0000269|PubMed:18723885,
CC ECO:0000269|PubMed:24700158}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK93140.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE013599; AAF47143.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM68294.1; -; Genomic_DNA.
DR EMBL; AE013599; AHN56607.1; -; Genomic_DNA.
DR EMBL; AY051716; AAK93140.1; ALT_INIT; mRNA.
DR EMBL; BT001698; AAN71453.1; -; mRNA.
DR RefSeq; NP_001286812.1; NM_001299883.1.
DR RefSeq; NP_611873.1; NM_138029.3.
DR RefSeq; NP_726404.1; NM_166651.2.
DR AlphaFoldDB; Q7JRE4; -.
DR SMR; Q7JRE4; -.
DR IntAct; Q7JRE4; 1.
DR STRING; 7227.FBpp0072075; -.
DR PaxDb; Q7JRE4; -.
DR PRIDE; Q7JRE4; -.
DR DNASU; 37838; -.
DR EnsemblMetazoa; FBtr0072166; FBpp0072075; FBgn0034962.
DR EnsemblMetazoa; FBtr0072167; FBpp0072076; FBgn0034962.
DR EnsemblMetazoa; FBtr0345949; FBpp0311863; FBgn0034962.
DR GeneID; 37838; -.
DR KEGG; dme:Dmel_CG3167; -.
DR UCSC; CG3167-RA; d. melanogaster.
DR UCSC; CG3167-RB; d. melanogaster.
DR CTD; 37838; -.
DR FlyBase; FBgn0034962; MAN1.
DR VEuPathDB; VectorBase:FBgn0034962; -.
DR eggNOG; KOG0147; Eukaryota.
DR GeneTree; ENSGT00940000171142; -.
DR HOGENOM; CLU_011086_0_0_1; -.
DR InParanoid; Q7JRE4; -.
DR OMA; RTIAWNR; -.
DR OrthoDB; 873705at2759; -.
DR PhylomeDB; Q7JRE4; -.
DR Reactome; R-DME-9013405; RHOD GTPase cycle.
DR Reactome; R-DME-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III.
DR SignaLink; Q7JRE4; -.
DR BioGRID-ORCS; 37838; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 37838; -.
DR PRO; PR:Q7JRE4; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0034962; Expressed in egg cell and 26 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0012505; C:endomembrane system; HDA:FlyBase.
DR GO; GO:0005639; C:integral component of nuclear inner membrane; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IDA:FlyBase.
DR GO; GO:0006998; P:nuclear envelope organization; IBA:GO_Central.
DR GO; GO:1902531; P:regulation of intracellular signal transduction; IEA:InterPro.
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; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR PANTHER; PTHR13428:SF12; PTHR13428:SF12; 1.
DR Pfam; PF03020; LEM; 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 Cytoplasm; Cytoskeleton; Developmental protein; Membrane; Nucleus;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..650
FT /note="Inner nuclear membrane protein Man1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000436843"
FT TOPO_DOM 1..230
FT /note="Nuclear"
FT /evidence="ECO:0000269|PubMed:16439308"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 252..400
FT /note="Perinuclear space"
FT /evidence="ECO:0000269|PubMed:16439308"
FT TRANSMEM 401..421
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 422..650
FT /note="Nuclear"
FT /evidence="ECO:0000269|PubMed:16439308"
FT DOMAIN 3..47
FT /note="LEM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00313"
FT REGION 1..214
FT /note="Involved in inner nuclear membrane localization"
FT /evidence="ECO:0000269|PubMed:16439308"
FT REGION 61..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..650
FT /note="May be required for its role in BMP signaling"
FT /evidence="ECO:0000269|PubMed:20036230"
SQ SEQUENCE 650 AA; 73879 MW; C8AAB20DB798C9D5 CRC64;
MSTESLNSLS DKELHRKLIQ SGFPSTPVTE TTRAVLIEKL RKHTRADKLK KRSNKYVLYS
KEQQESPPFP QYHQYHAPQP PQNYANGLDN NNDLDQTGGS SAYNRSLDES DSSPLQLSAS
KMYAPPPVVA SNYDGDCSPH SLGLNGKYLQ PCSMPYAIDT SNNYGKPSGK AKLSDGGVVN
RLLSFRDTTI QRKFNYPTGQ ASRIPLRKER LTRFALSDLK SFIRNPDIRP YVIPRVLISL
FLIFLTIITV LYVGKRFEQS PIDKAALKYT LCNPNDMQMI SEKVNCIEKD SLRGALDMSE
ELFRHLNERA RLHHCKDANL SPALEIGEFV REMVSNPKTH RGNLHSNLMA AKYLITENPQ
WSIQVVDSTK HLGQTSHFEL SEPNLPLKCI VLKKVTRFFT VIGALLLIVA GFLIVYVAVV
IYRVKQKEAL LAVDQFQKDI INELIYLSSQ SESPEVVINQ LQEKFLPAKK RSKLLSSWNK
ALKQLEKNDS RVLFGMVNRD GKAMRTIAWN RNVDKKDVGL VKKWQSPAFD NSNKIANPPT
PCLKIRHMFD SSEVDQANLK QSIVESIIEK VGTRCKICDV QLDVQSCCVY IRCASEEDAG
TIHKEINGWW FDKRLISIKF LRLERYLSRF PKPSAEPLYF HTNEAANTHS
