Reviewed, UniProtKB/Swiss-Prot Q9VG55 (HUGIN_DROME)

Names and origin

Protein names

Recommended name:
    Protein hugin
Cleaved into the following 3 chains:
    1- Recommended name:
            Hug-gamma
    2- Recommended name:
            Hug-peptide
    3- Recommended name:
            PK-2
        Alternative name(s):
            Drm-PK-2
            Pyrokinin-2
            Myotrophin-2
              Short name=MT-2
              Short name=Drm-MT2

Gene names

Name:	hug
ORF Names:	CG6371

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	191 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Probably has a role in larval molting.
Subcellular location	Secreted.
Tissue specificity	Subgroup of neurosecretory cells in the suboesophageal ganglion from embryonic stage 9 to larval stages.
Developmental stage	During embryogenesis through to adult stages with highest expression at later half of embryogenesis and during larval stages.
Sequence similarities	Belongs to the pyrokinin family.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Neuropeptide
PTM	Amidation Cleavage on pair of basic residues
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	ecdysis, chitin-based cuticle Ref.1 Inferred from mutant phenotype. Source: UniProtKB larval feeding behavior Inferred from mutant phenotype. Source: FlyBase neuropeptide signaling pathway Ref.5 Non-traceable author statement. Source: UniProtKB
Cellular component	extracellular region Ref.5 Non-traceable author statement. Source: UniProtKB
Molecular function	neuropeptide hormone activity Ref.1 Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CG10139	Q9V740	1	EBI-117021,EBI-166770

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 24	24
	Propeptide	25 – 119	95			PRO_0000029908
	Peptide	121 – 137	17	Hug-gamma Potential		PRO_0000029909
	Peptide	140 – ?		Hug-peptide Potential		PRO_0000029910
	Propeptide	? – 171				PRO_0000029911
	Peptide	174 – 181	8	PK-2		PRO_0000029912
	Propeptide	185 – 191	7			PRO_0000029913
Amino acid modifications
	Modified residue	137	1	Leucine amide Potential
	Modified residue	181	1	Leucine amide

Sequences

	Sequence		Length	Mass (Da)
	Q9VG55-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 78F4A9811C57D932	FASTA	191	20,623
	10 20 30 40 50 60 MCGPSYCTLL LIAASCYILV CSHAKSLQGT SKLDLGNHIS AGSARGSLSP ASPALSEARQ 70 80 90 100 110 120 KRAMGDYKEL TDIIDELEEN SLAQKASATM QVAAMPPQGQ EFDLDTMPPL TYYLLLQKLR 130 140 150 160 170 180 QLQSNGEPAY RVRTPRLGRS IDSWRLLDAE GATGMAGGEE AIGGQFMQRM VKKSVPFKPR 190 LGKRAQVCGG D

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Drosophila hugin gene codes for myostimulatory and ecdysis-modifying neuropeptides." Meng X., Wahlstreom G., Immonen T., Kolmer M., Tirronen M., Predel R., Kalkkinen N., Heino T., Sariola H., Roos C. Mech. Dev. 117:5-13(2002) [PubMed: 12204246] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF N-TERMINUS; 140-147 AND 174-180.
[2]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[3]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION.
[4]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Head.
[5]	"Peptidomics of the larval Drosophila melanogaster central nervous system." Baggerman G., Cerstiaens A., De Loof A., Schoofs L. J. Biol. Chem. 277:40368-40374(2002) [PubMed: 12171930] [Abstract] Cited for: PROTEIN SEQUENCE OF 174-181, AMIDATION. Tissue: Larva.
[6]	"Expression of a novel neuropeptide, NVGTLARDFQLPIPNamide, in the larval and adult brain of Drosophila melanogaster." Verleyen P., Baggerman G., Wiehart U., Schoeters E., Van Lommel A., De Loof A., Schoofs L. J. Neurochem. 88:311-319(2004) [PubMed: 14690519] [Abstract] Cited for: PROTEIN SEQUENCE OF 174-181. Tissue: CNS.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ133105 Genomic DNA. Translation: CAB88005.1. AE014297 Genomic DNA. Translation: AAF54833.1. AY047528 mRNA. Translation: AAK77260.1.
RefSeq	NP_524329.1.
UniGene	Dm.2437
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:17451N.
IntAct	Q9VG55. 1 interaction.
Proteomic databases
PRIDE	Q9VG55.
Genome annotation databases
Ensembl	FBgn0028374. Drosophila melanogaster. [Contig view]
GeneID	41547.
KEGG	dme:Dmel_CG6371.
NMPDR	fig|7227.3.peg.12466.
Organism-specific databases
FlyBase	FBgn0028374. hug.
Phylogenomic databases
HOGENOM	Q9VG55.
OMA	Q9VG55. PLTYYLL.
Enzyme and pathway databases
BioCyc	DMEL-XXX-02:DMEL-XXX-02-011300-MON.
Gene expression databases
ArrayExpress	Q9VG55.
GermOnline	CG6371. Drosophila melanogaster.
Family and domain databases
InterPro	IPR001484. Pyrokinin_CS. [Graphical view]
PROSITE	PS00539. PYROKININ. False negative. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	824337.

Entry information

Entry name

HUGIN_DROME

Accession

Primary (citable) accession number: Q9VG55

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2002
Last sequence update:	May 1, 2000
Last modified:	June 16, 2009
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project