HUGIN_DROME
ID HUGIN_DROME Reviewed; 191 AA.
AC Q9VG55;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Protein hugin;
DE Contains:
DE RecName: Full=Hug-gamma;
DE Contains:
DE RecName: Full=Hug-peptide;
DE Contains:
DE RecName: Full=PK-2;
DE AltName: Full=Drm-PK-2;
DE AltName: Full=Myotrophin-2;
DE Short=Drm-MT2;
DE Short=MT-2;
DE AltName: Full=Pyrokinin-2;
DE Flags: Precursor;
GN Name=Hug; ORFNames=CG6371;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF N-TERMINUS, PROTEIN
RP SEQUENCE OF 140-147 AND 174-180, PROBABLE FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=12204246; DOI=10.1016/s0925-4773(02)00175-2;
RA Meng X., Wahlstreom G., Immonen T., Kolmer M., Tirronen M., Predel R.,
RA Kalkkinen N., Heino T., Sariola H., Roos C.;
RT "The Drosophila hugin gene codes for myostimulatory and ecdysis-modifying
RT neuropeptides.";
RL Mech. Dev. 117:5-13(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
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]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
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]
RP PROTEIN SEQUENCE OF 174-181, AND AMIDATION AT LEU-181.
RC TISSUE=Larva;
RX PubMed=12171930; DOI=10.1074/jbc.m206257200;
RA Baggerman G., Cerstiaens A., De Loof A., Schoofs L.;
RT "Peptidomics of the larval Drosophila melanogaster central nervous
RT system.";
RL J. Biol. Chem. 277:40368-40374(2002).
RN [6]
RP PROTEIN SEQUENCE OF 174-181.
RC TISSUE=CNS;
RX PubMed=14690519; DOI=10.1046/j.1471-4159.2003.02161.x;
RA Verleyen P., Baggerman G., Wiehart U., Schoeters E., Van Lommel A.,
RA De Loof A., Schoofs L.;
RT "Expression of a novel neuropeptide, NVGTLARDFQLPIPNamide, in the larval
RT and adult brain of Drosophila melanogaster.";
RL J. Neurochem. 88:311-319(2004).
CC -!- FUNCTION: Probably has a role in larval molting.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12204246}.
CC -!- TISSUE SPECIFICITY: Expressed in a subgroup of neurosecretory cells in
CC the subesophageal ganglion from embryonic stage 9 to larval stages.
CC {ECO:0000269|PubMed:12204246}.
CC -!- DEVELOPMENTAL STAGE: Expressed during embryogenesis through to adult
CC stages with highest expression at later half of embryogenesis and
CC during larval stages. {ECO:0000269|PubMed:12204246}.
CC -!- SIMILARITY: Belongs to the pyrokinin family. {ECO:0000305}.
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DR EMBL; AJ133105; CAB88005.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF54833.1; -; Genomic_DNA.
DR EMBL; AY047528; AAK77260.1; -; mRNA.
DR RefSeq; NP_524329.1; NM_079605.2.
DR AlphaFoldDB; Q9VG55; -.
DR BioGRID; 66642; 4.
DR DIP; DIP-17451N; -.
DR IntAct; Q9VG55; 1.
DR STRING; 7227.FBpp0082108; -.
DR PaxDb; Q9VG55; -.
DR PRIDE; Q9VG55; -.
DR DNASU; 41547; -.
DR EnsemblMetazoa; FBtr0082639; FBpp0082108; FBgn0028374.
DR GeneID; 41547; -.
DR KEGG; dme:Dmel_CG6371; -.
DR CTD; 15573; -.
DR FlyBase; FBgn0028374; Hug.
DR VEuPathDB; VectorBase:FBgn0028374; -.
DR eggNOG; ENOG502TAND; Eukaryota.
DR HOGENOM; CLU_1422905_0_0_1; -.
DR InParanoid; Q9VG55; -.
DR OMA; RMMKKSV; -.
DR OrthoDB; 1455199at2759; -.
DR PhylomeDB; Q9VG55; -.
DR BioGRID-ORCS; 41547; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 41547; -.
DR PRO; PR:Q9VG55; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0028374; Expressed in brain and 13 other tissues.
DR Genevisible; Q9VG55; DM.
DR GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:FlyBase.
DR GO; GO:0008255; F:ecdysis-triggering hormone activity; ISS:FlyBase.
DR GO; GO:0005179; F:hormone activity; NAS:FlyBase.
DR GO; GO:0016084; F:myostimulatory hormone activity; IDA:FlyBase.
DR GO; GO:0071855; F:neuropeptide receptor binding; IPI:FlyBase.
DR GO; GO:0005102; F:signaling receptor binding; ISS:FlyBase.
DR GO; GO:0018990; P:ecdysis, chitin-based cuticle; IMP:UniProtKB.
DR GO; GO:0030536; P:larval feeding behavior; IMP:FlyBase.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IDA:FlyBase.
PE 1: Evidence at protein level;
KW Amidation; Cleavage on pair of basic residues; Direct protein sequencing;
KW Neuropeptide; Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:12204246"
FT PROPEP 25..119
FT /evidence="ECO:0000269|PubMed:12204246"
FT /id="PRO_0000029908"
FT PEPTIDE 121..137
FT /note="Hug-gamma"
FT /evidence="ECO:0000255"
FT /id="PRO_0000029909"
FT PEPTIDE 140..?
FT /note="Hug-peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000029910"
FT PROPEP ?..171
FT /evidence="ECO:0000269|PubMed:12204246"
FT /id="PRO_0000029911"
FT PEPTIDE 174..181
FT /note="PK-2"
FT /evidence="ECO:0000269|PubMed:12204246"
FT /id="PRO_0000029912"
FT PROPEP 185..191
FT /evidence="ECO:0000269|PubMed:12204246"
FT /id="PRO_0000029913"
FT MOD_RES 137
FT /note="Leucine amide"
FT /evidence="ECO:0000255"
FT MOD_RES 181
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:12171930"
SQ SEQUENCE 191 AA; 20623 MW; 78F4A9811C57D932 CRC64;
MCGPSYCTLL LIAASCYILV CSHAKSLQGT SKLDLGNHIS AGSARGSLSP ASPALSEARQ
KRAMGDYKEL TDIIDELEEN SLAQKASATM QVAAMPPQGQ EFDLDTMPPL TYYLLLQKLR
QLQSNGEPAY RVRTPRLGRS IDSWRLLDAE GATGMAGGEE AIGGQFMQRM VKKSVPFKPR
LGKRAQVCGG D
