HIG_DROME
ID HIG_DROME Reviewed; 958 AA.
AC Q09101; Q7KQU0; Q8IH50; Q9I7E3; Q9I7E4; Q9V560;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Locomotion-related protein Hikaru genki;
DE Flags: Precursor;
GN Name=hig; ORFNames=CG2040;
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 [MRNA] (ISOFORMS 1; 2; 3 AND 4), FUNCTION, AND
RP DISRUPTION PHENOTYPE.
RC TISSUE=Head;
RX PubMed=8461133; DOI=10.1016/0896-6273(93)90329-p;
RA Hoshino M., Matsuzaki F., Nabeshima Y., Hama C.;
RT "Hikaru genki, a CNS-specific gene identified by abnormal locomotion in
RT Drosophila, encodes a novel type of protein.";
RL Neuron 10:395-407(1993).
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, AND ALTERNATIVE SPLICING.
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] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 429-958 (ISOFORM 1).
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 FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=8625810; DOI=10.1242/dev.122.2.589;
RA Hoshino M., Suzuki E., Nabeshima Y., Hama C.;
RT "Hikaru genki protein is secreted into synaptic clefts from an early stage
RT of synapse formation in Drosophila.";
RL Development 122:589-597(1996).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=9914413; DOI=10.1007/s004270050221;
RA Hoshino M., Suzuki E., Miyake T., Sone M., Komatsu A., Nabeshima Y.,
RA Hama C.;
RT "Neural expression of hikaru genki protein during embryonic and larval
RT development of Drosophila melanogaster.";
RL Dev. Genes Evol. 209:1-9(1999).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-376, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Oregon-R; TISSUE=Head;
RX PubMed=17893096; DOI=10.1093/glycob/cwm097;
RA Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L.,
RA Panin V.;
RT "Identification of N-glycosylated proteins from the central nervous system
RT of Drosophila melanogaster.";
RL Glycobiology 17:1388-1403(2007).
CC -!- FUNCTION: Plays a role in the formation of functional neural circuits
CC from the early stages of synapse formation. Has a role in the
CC development of CNS functions involved in locomotor activity.
CC {ECO:0000269|PubMed:8461133, ECO:0000269|PubMed:8625810,
CC ECO:0000269|PubMed:9914413}.
CC -!- INTERACTION:
CC Q09101; Q0KI85: side-VI; NbExp=2; IntAct=EBI-172012, EBI-6884983;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8625810,
CC ECO:0000269|PubMed:9914413}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=3; Synonyms=A;
CC IsoId=Q09101-1; Sequence=Displayed;
CC Name=1; Synonyms=D;
CC IsoId=Q09101-2; Sequence=VSP_002513;
CC Name=2; Synonyms=C;
CC IsoId=Q09101-3; Sequence=VSP_002512, VSP_002513;
CC Name=4; Synonyms=B;
CC IsoId=Q09101-4; Sequence=VSP_002512;
CC -!- TISSUE SPECIFICITY: Expressed in PCC neurons and neuroblasts in the
CC procephalic neurogenic region in the central nervous system. Expressed
CC in nerves running along the surface of the ventral ganglion and that
CC extend to the peripheral tissues. Also expressed in motor nerves and
CC boutons of certain muscles, in particular of muscle 8 in the A2 and
CC posterior abdominal segments of young adult flies. In the brain,
CC expressed in both the neuropiles and cortical regions except the
CC retinular cells and laminar neuropile. {ECO:0000269|PubMed:8625810,
CC ECO:0000269|PubMed:9914413}.
CC -!- DEVELOPMENTAL STAGE: Most abundant during and/or after neuronal
CC differentiation and during cell specification or axogenesis. Required
CC during pupation for normal motor function development.
CC {ECO:0000269|PubMed:9914413}.
CC -!- DISRUPTION PHENOTYPE: Flies are unable to jump or fly and walk slowly
CC with an unstable gait. Occasionally they exhibit body and wing tremors
CC while standing or walking. {ECO:0000269|PubMed:8461133}.
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DR EMBL; D13884; BAA02984.1; -; mRNA.
DR EMBL; D13885; BAA02985.1; -; mRNA.
DR EMBL; D13886; BAA02986.1; -; mRNA.
DR EMBL; D13887; BAA02987.1; -; mRNA.
DR EMBL; AE013599; AAF58960.1; -; Genomic_DNA.
DR EMBL; AE013599; AAG22296.1; -; Genomic_DNA.
DR EMBL; AE013599; AAG22297.1; -; Genomic_DNA.
DR EMBL; AE013599; AAS64892.2; -; Genomic_DNA.
DR EMBL; AY069188; AAL39333.1; -; mRNA.
DR EMBL; BT001427; AAN71182.1; -; mRNA.
DR RefSeq; NP_001014514.1; NM_001014514.2. [Q09101-2]
DR RefSeq; NP_525110.2; NM_080371.3. [Q09101-3]
DR RefSeq; NP_724772.1; NM_165666.2. [Q09101-4]
DR RefSeq; NP_724773.1; NM_165667.2. [Q09101-1]
DR AlphaFoldDB; Q09101; -.
DR SMR; Q09101; -.
DR BioGRID; 61786; 6.
DR IntAct; Q09101; 11.
DR STRING; 7227.FBpp0087688; -.
DR GlyGen; Q09101; 6 sites.
DR iPTMnet; Q09101; -.
DR PaxDb; Q09101; -.
DR PRIDE; Q09101; -.
DR DNASU; 35949; -.
DR EnsemblMetazoa; FBtr0088606; FBpp0087687; FBgn0010114. [Q09101-4]
DR EnsemblMetazoa; FBtr0088607; FBpp0087688; FBgn0010114. [Q09101-1]
DR EnsemblMetazoa; FBtr0088608; FBpp0087689; FBgn0010114. [Q09101-3]
DR EnsemblMetazoa; FBtr0100119; FBpp0100157; FBgn0010114. [Q09101-2]
DR GeneID; 35949; -.
DR KEGG; dme:Dmel_CG2040; -.
DR CTD; 35949; -.
DR FlyBase; FBgn0010114; hig.
DR VEuPathDB; VectorBase:FBgn0010114; -.
DR eggNOG; KOG4297; Eukaryota.
DR HOGENOM; CLU_348908_0_0_1; -.
DR InParanoid; Q09101; -.
DR OMA; RHPSENH; -.
DR PhylomeDB; Q09101; -.
DR Reactome; R-DME-114608; Platelet degranulation.
DR Reactome; R-DME-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR Reactome; R-DME-977606; Regulation of Complement cascade.
DR BioGRID-ORCS; 35949; 0 hits in 3 CRISPR screens.
DR ChiTaRS; hig; fly.
DR GenomeRNAi; 35949; -.
DR PRO; PR:Q09101; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0010114; Expressed in brain and 21 other tissues.
DR ExpressionAtlas; Q09101; baseline and differential.
DR Genevisible; Q09101; DM.
DR GO; GO:0043025; C:neuronal cell body; IDA:FlyBase.
DR GO; GO:0043083; C:synaptic cleft; IDA:FlyBase.
DR GO; GO:0008039; P:synaptic target recognition; IMP:FlyBase.
DR CDD; cd00033; CCP; 4.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR Pfam; PF00084; Sushi; 4.
DR SMART; SM00032; CCP; 5.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF57535; SSF57535; 4.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS50923; SUSHI; 5.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; Differentiation;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Neurogenesis;
KW Reference proteome; Repeat; Secreted; Signal; Sushi.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..958
FT /note="Locomotion-related protein Hikaru genki"
FT /id="PRO_0000014774"
FT DOMAIN 527..599
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 612..708
FT /note="Ig-like C2-type"
FT DOMAIN 712..770
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 771..829
FT /note="Sushi 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 830..892
FT /note="Sushi 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 892..954
FT /note="Sushi 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT REGION 129..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 929..958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 318..320
FT /note="Cell attachment site"
FT COMPBIAS 266..344
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17893096"
FT CARBOHYD 525
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 605
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 620
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 752
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 789
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 569..597
FT /evidence="ECO:0000250"
FT DISULFID 643..695
FT /evidence="ECO:0000250"
FT DISULFID 714..755
FT /evidence="ECO:0000250"
FT DISULFID 741..768
FT /evidence="ECO:0000250"
FT DISULFID 773..814
FT /evidence="ECO:0000250"
FT DISULFID 800..827
FT /evidence="ECO:0000250"
FT DISULFID 832..877
FT /evidence="ECO:0000250"
FT DISULFID 863..890
FT /evidence="ECO:0000250"
FT DISULFID 894..939
FT /evidence="ECO:0000250"
FT DISULFID 922..952
FT /evidence="ECO:0000250"
FT VAR_SEQ 529..553
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:8461133"
FT /id="VSP_002512"
FT VAR_SEQ 892..958
FT /note="Missing (in isoform 1 and isoform 2)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:8461133"
FT /id="VSP_002513"
FT CONFLICT 81
FT /note="E -> D (in Ref. 1; BAA02984/BAA02985/BAA02986/
FT BAA02987)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="P -> L (in Ref. 1; BAA02984/BAA02985/BAA02986/
FT BAA02987)"
FT /evidence="ECO:0000305"
FT CONFLICT 367
FT /note="D -> N (in Ref. 1; BAA02984/BAA02985/BAA02986/
FT BAA02987)"
FT /evidence="ECO:0000305"
FT CONFLICT 396
FT /note="K -> R (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 398
FT /note="T -> A (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 716
FT /note="Q -> R (in Ref. 1; BAA02984/BAA02985/BAA02986/
FT BAA02987)"
FT /evidence="ECO:0000305"
FT CONFLICT 760
FT /note="N -> S (in Ref. 1; BAA02984/BAA02985/BAA02986/
FT BAA02987)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 958 AA; 107028 MW; 7B2A08477672E674 CRC64;
MWSRQRMRHK PLWALISLTV LLLVLDKSNA NTEPVETSTT SEPDASPGCR APDVRFTIVK
PEATTEQPLA KFETTQIYLP EDFTTADVEF VDSVPRHPNE NHAAVINPYS LDLGDDHLHV
GDAAASLVGD DDLGDEDEDH HGDPEDKRLN ANRKQGKRRR AGSGRRRRIE NENGQTGRGR
GSRYKRHAIL HDTEASPETD RWAGSKLAAE GDVYYVHIAD ILKSREPNRE LKSKLHKLKM
KARLNKCLAE GGKEKCTRLL KKKPKKKVVE KEQTLKKEKK FPKEEQSKEK VPENGQTPKE
DELELDHPET AAAHHRRRGD SHAAELDQRD RSPRWRRRRS TEFKGDLGQL PPESGIGPEP
EPLADQDLKD LQQYGNQSSS ARVALLWQRV KRKSGKTTGA LSRPKGGGDS SSKTTSRKDK
GIYDEEAGYT PIHPDDPEFD EEEEEDEEVD ILQQFTEVSE IRFPGEIGPM GDRRLCKIRC
VKGKWVGPLC ATNEEDDNGN VKFQPLYKSC HVNRIPSHLL LSYRNISVTP IPPNRGWRKT
RLSKSTLLSN TEINVGWDLP HGHSLQARCQ ELGIYKLLGE SRVLCSNGLW APRMPSCVPT
TVLTNYSEDS APSIRIKIFN GSHSFEPSGV MAVPPHSTVL MDCMYPRVRG TPEWSWTSWY
MQYSTGWSPA QEEKAVRYRL SIKNIENNDS GTFTCTSPRG LTNSIAVVVA TSTCPQLTEP
LAPLKLRLEG NKLGQRAHYE CPEGFRLDGA WNATCLASGN WSSPTPTCHA IQCPRLELDD
PHLSLIELNT SAWGRAVFKC QWGFKLTGPA QLDCEPSGVW SGPVPRCKVI QCVMPVAPLN
GRIGGTSLSQ RRLTVGALVT FSCNDGHSLV GESSIICTEN GQWSHSPPFC KSQCPYPGDP
PNGLIAPLKF NYDAGDYLSV QCRPGFVQSY EGPPERPKCQ PDGRWSGPMP KCKSYEEV