APMAP_DROME
ID APMAP_DROME Reviewed; 579 AA.
AC Q9VB46; D2NUG9; Q24160; Q8MT56;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Adipocyte plasma membrane-associated protein Hemomucin {ECO:0000305|PubMed:8662683};
DE AltName: Full=Protein Hemomucin {ECO:0000303|PubMed:8662683};
GN Name=Hmu {ECO:0000312|FlyBase:FBgn0015737};
GN Synonyms=Rbp5 {ECO:0000312|EMBL:AAF56697.1},
GN rrm5 {ECO:0000312|EMBL:AAF56697.1}, SPH210 {ECO:0000312|EMBL:AAF56697.1};
GN ORFNames=CG3373 {ECO:0000312|FlyBase:FBgn0015737};
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|Proteomes:UP000000803};
RN [1] {ECO:0000312|EMBL:AAC47118.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-42; 49-60; 77-91;
RP 103-115; 151-163; 171-205; 216-229; 261-283; 317-324; 340-356 AND 363-377,
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND PHOSPHORYLATION.
RC STRAIN=Canton-S {ECO:0000312|EMBL:AAC47118.1};
RC TISSUE=Hemocyte {ECO:0000312|EMBL:AAC47118.1};
RX PubMed=8662683; DOI=10.1074/jbc.271.22.12708;
RA Theopold U., Samakovlis C., Erdjument-Bromage H., Dillon N., Axelsson B.,
RA Schmidt O., Tempst P., Hultmark D.;
RT "Helix pomatia lectin, an inducer of Drosophila immune response, binds to
RT hemomucin, a novel surface mucin.";
RL J. Biol. Chem. 271:12708-12715(1996).
RN [2] {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 [3] {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 [4] {ECO:0000312|EMBL:AAM48401.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAM48401.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAM48401.1};
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 [5] {ECO:0000312|EMBL:ADB25328.1, ECO:0000312|EMBL:AFA28426.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000305}
RP FUNCTION.
RX PubMed=12769978; DOI=10.1016/s0022-1910(97)00013-9;
RA Schmidt O., Theopold U.;
RT "Helix pomatia lectin and annexin V, two molecular probes for insect
RT microparticles: possible involvement in hemolymph coagulation.";
RL J. Insect Physiol. 43:667-674(1997).
RN [7] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION BY ECDYSONE,
RP AND GLYCOSYLATION.
RX PubMed=11164341; DOI=10.1016/s0965-1748(00)00117-x;
RA Theopold U., Dorian C., Schmidt O.;
RT "Changes in glycosylation during Drosophila development. The influence of
RT ecdysone on hemomucin isoforms.";
RL Insect Biochem. Mol. Biol. 31:189-197(2001).
RN [8] {ECO:0000305}
RP INTERACTION WITH STURKOPF.
RX PubMed=30917324; DOI=10.1016/j.celrep.2019.02.110;
RA Werthebach M., Stewart F.A., Gahlen A., Mettler-Altmann T., Akhtar I.,
RA Maas-Enriquez K., Droste A., Eichmann T.O., Poschmann G., Stuehler K.,
RA Beller M.;
RT "Control of Drosophila Growth and Survival by the Lipid Droplet-Associated
RT Protein CG9186/Sturkopf.";
RL Cell Rep. 26:3726-3740(2019).
CC -!- FUNCTION: Transmembrane mucin that may be involved in cellular adhesion
CC and the innate immune response (PubMed:8662683, PubMed:12769978).
CC Membrane-tethered mucins are involved in many cell surface functions
CC and form a physical barrier around cells to regulate cell-cell and/or
CC cell-substrate interactions, and protect against pathogens or harmful
CC extracellular conditions (PubMed:8662683, PubMed:12769978,
CC PubMed:11164341). This mucin likely acts in hemocyte adhesion as it is
CC released from hemocytes during coagulation and is also able to bind
CC lipophorin particles which form part of the hemocyte coagulogen
CC (PubMed:12769978). Able to induce expression of the antibacterial
CC proteins in the presence of GalNAc-specific lectins and so probably
CC also functions in the innate immune response (PubMed:8662683).
CC {ECO:0000269|PubMed:11164341, ECO:0000269|PubMed:12769978,
CC ECO:0000269|PubMed:8662683}.
CC -!- SUBUNIT: Interacts with sturkopf. {ECO:0000269|PubMed:30917324}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8662683};
CC Single-pass membrane protein {ECO:0000255}. Note=Detected on membrane
CC of hemocytes. {ECO:0000269|PubMed:8662683}.
CC -!- TISSUE SPECIFICITY: Detected in ovaries (at protein level)
CC (PubMed:11164341). In larvae, detected in the fat body, salivary
CC glands, imaginal disks and gut (at protein level) (PubMed:11164341). In
CC adults, expressed in the cardia, and in regions of the ventriculus
CC including the area posterior to the cardia (PubMed:8662683). In females
CC also expressed in follicle cells (PubMed:8662683).
CC {ECO:0000269|PubMed:11164341, ECO:0000269|PubMed:8662683}.
CC -!- DEVELOPMENTAL STAGE: Detected throughout development and in adults (at
CC protein level) (PubMed:11164341). Expressed in embryos, larvae and
CC adults (PubMed:8662683). {ECO:0000269|PubMed:11164341,
CC ECO:0000269|PubMed:8662683}.
CC -!- INDUCTION: By ecdysone; in embryonic cell lines.
CC {ECO:0000269|PubMed:11164341}.
CC -!- PTM: O-glycosylated. Glycosylated in the ovary of 4 day old females.
CC {ECO:0000269|PubMed:11164341}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:8662683}.
CC -!- SIMILARITY: Belongs to the strictosidine synthase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ADB25328.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U42014; AAC47118.1; -; mRNA.
DR EMBL; AE014297; AAF56697.1; -; Genomic_DNA.
DR EMBL; AY118372; AAM48401.1; -; mRNA.
DR EMBL; BT120112; ADB25328.1; ALT_FRAME; mRNA.
DR EMBL; BT133185; AFA28426.1; -; mRNA.
DR RefSeq; NP_477159.1; NM_057811.4.
DR AlphaFoldDB; Q9VB46; -.
DR SMR; Q9VB46; -.
DR STRING; 7227.FBpp0084534; -.
DR PaxDb; Q9VB46; -.
DR PRIDE; Q9VB46; -.
DR DNASU; 43294; -.
DR EnsemblMetazoa; FBtr0085164; FBpp0084534; FBgn0015737.
DR GeneID; 43294; -.
DR KEGG; dme:Dmel_CG3373; -.
DR UCSC; CG3373-RA; d. melanogaster.
DR CTD; 50823; -.
DR FlyBase; FBgn0015737; Hmu.
DR VEuPathDB; VectorBase:FBgn0015737; -.
DR eggNOG; KOG1520; Eukaryota.
DR GeneTree; ENSGT00440000039984; -.
DR HOGENOM; CLU_023267_1_0_1; -.
DR InParanoid; Q9VB46; -.
DR OMA; IYEESRC; -.
DR OrthoDB; 757814at2759; -.
DR PhylomeDB; Q9VB46; -.
DR BioGRID-ORCS; 43294; 0 hits in 1 CRISPR screen.
DR ChiTaRS; Hmu; fly.
DR GenomeRNAi; 43294; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0015737; Expressed in crop (Drosophila) and 47 other tissues.
DR ExpressionAtlas; Q9VB46; baseline and differential.
DR GO; GO:0009986; C:cell surface; IDA:FlyBase.
DR GO; GO:0012505; C:endomembrane system; HDA:FlyBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004064; F:arylesterase activity; ISS:FlyBase.
DR GO; GO:0016844; F:strictosidine synthase activity; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR Gene3D; 2.120.10.30; -; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR018119; Strictosidine_synth_cons-reg.
DR Pfam; PF03088; Str_synth; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Glycoprotein; Lyase; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..579
FT /note="Adipocyte plasma membrane-associated protein
FT Hemomucin"
FT /id="PRO_0000454230"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 7..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..579
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT REGION 427..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..525
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..571
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 207
FT /note="G -> A (in Ref. 5; ADB25328)"
FT /evidence="ECO:0000305"
FT CONFLICT 255
FT /note="H -> Q (in Ref. 4; AAM48401)"
FT /evidence="ECO:0000305"
FT CONFLICT 341
FT /note="V -> I (in Ref. 1; AAC47118)"
FT /evidence="ECO:0000305"
FT CONFLICT 383
FT /note="V -> I (in Ref. 1; AAC47118)"
FT /evidence="ECO:0000305"
FT CONFLICT 387
FT /note="L -> Q (in Ref. 5; ADB25328)"
FT /evidence="ECO:0000305"
FT CONFLICT 516
FT /note="T -> P (in Ref. 1; AAC47118)"
FT /evidence="ECO:0000305"
FT CONFLICT 532
FT /note="T -> TTPT (in Ref. 1; AAC47118)"
FT /evidence="ECO:0000305"
FT CONFLICT 554
FT /note="D -> E (in Ref. 1; AAC47118)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 579 AA; 63416 MW; 7584B7C08D31490B CRC64;
MGLLYALRVR IMNFMIFFLL IILMPGLPPR TTFPFKDYIV TPPKDLKGAL ESNFHLEGAE
RLLEGRVYGP ECLIARNNEI YTGIHGGEVI KLTSNHVTHV TKIGQPCEDI YEESRCGRPL
GLAFDTQGNN LIIADAYYGL WQVDLGTNKK TLLVSPAQEL AGKSINRPAK IFNGVTVSKE
GDVYWTDSSS DFTIEDLVFA SFANPSGRLF KYNRSKNVSE VLLDELAFAN GLALSPNEDF
IVVAETGAMR LTKYHLKGAK AGQSEVFVDG LPGLPDNLTP DAEGIWVPLV QSADSEHPNG
FTLFTRFPSV RLFLARMLAL FELPFRYLNS VYPNKFSQRF VHFVGHMESI TVLAPKRTTV
VRVDWNGNIV GSLHGFDKSA ATVSHVLEFQ DFLFLGSPTN QYLARVKSPK AKQPTLKVRN
VRVEGEGLEA SIGVPPSKAT PKPKAAPSTT TPKPTTTTTT TTPKPTTKTT TTTTTPKPTT
TTTTKKPTTT TTTTTTTPKP TTTKPPTAKP STTTTTTTTP KPTTTTTPTT PTPEPSKPKV
KRTVPEKPAP VEEDIPSDTQ PPKKEKLKVI NKQGVNVEL
