HOOK_DROME
ID HOOK_DROME Reviewed; 679 AA.
AC Q24185; Q9VJ15;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 02-FEB-2004, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Protein hook;
DE AltName: Full=dHK;
GN Name=hook {ECO:0000312|FlyBase:FBgn0001202};
GN Synonyms=hk {ECO:0000312|FlyBase:FBgn0001202};
GN ORFNames=CG10653 {ECO:0000312|FlyBase:FBgn0001202};
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], FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND
RP HOMODIMERIZATION.
RX PubMed=8682859; DOI=10.1083/jcb.133.6.1205;
RA Kraemer H., Phistry M.;
RT "Mutations in the Drosophila hook gene inhibit endocytosis of the boss
RT transmembrane ligand into multivesicular bodies.";
RL J. Cell Biol. 133:1205-1215(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=9927460; DOI=10.1093/genetics/151.2.675;
RA Kraemer H., Phistry M.;
RT "Genetic analysis of hook, a gene required for endocytic trafficking in
RT Drosophila.";
RL Genetics 151:675-684(1999).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
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 [6]
RP FUNCTION.
RX PubMed=10198042; DOI=10.1091/mbc.10.4.847;
RA Sunio A., Metcalf A.B., Kraemer H.;
RT "Genetic dissection of endocytic trafficking in Drosophila using a
RT horseradish peroxidase-bride of sevenless chimera: hook is required for
RT normal maturation of multivesicular endosomes.";
RL Mol. Biol. Cell 10:847-859(1999).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11018772;
RX DOI=10.1002/1097-4695(20001105)45:2<105::aid-neu5>3.0.co;2-x;
RA Narayanan R., Kraemer H., Ramaswami M.;
RT "Drosophila endosomal proteins hook and deep orange regulate synapse size
RT but not synaptic vesicle recycling.";
RL J. Neurobiol. 45:105-119(2000).
RN [8]
RP INTERACTION WITH MICROTUBULES.
RX PubMed=11238449; DOI=10.1083/jcb.152.5.923;
RA Walenta J.H., Didier A.J., Liu X., Kraemer H.;
RT "The Golgi-associated hook3 protein is a member of a novel family of
RT microtubule-binding proteins.";
RL J. Cell Biol. 152:923-934(2001).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17435236; DOI=10.1534/genetics.106.065011;
RA Simonsen A., Cumming R.C., Lindmo K., Galaviz V., Cheng S., Rusten T.E.,
RA Finley K.D.;
RT "Genetic modifiers of the Drosophila blue cheese gene link defects in
RT lysosomal transport with decreased life span and altered ubiquitinated-
RT protein profiles.";
RL Genetics 176:1283-1297(2007).
CC -!- FUNCTION: Involved in endocytic trafficking by stabilizing organelles
CC of the endocytic pathway. Probably acts as a cytoskeletal linker
CC protein required to tether endosome vesicles to the cytoskeleton.
CC Involved in modulation of endocytosis at stages required for down-
CC regulation of membrane proteins that control synapse size. Not involved
CC in synaptic vesicle recycling. Required in R7 cells for boss
CC endocytosis into multivesicular bodies (MVBs). Has a role in regulating
CC adult longevity. {ECO:0000269|PubMed:10198042,
CC ECO:0000269|PubMed:11018772, ECO:0000269|PubMed:17435236,
CC ECO:0000269|PubMed:8682859, ECO:0000269|PubMed:9927460}.
CC -!- SUBUNIT: Homodimer. Interacts with microtubules via its N-terminus.
CC {ECO:0000269|PubMed:11238449}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Endosome
CC {ECO:0000269|PubMed:8682859}. Synapse {ECO:0000269|PubMed:11018772}.
CC Note=Enriched at neuromuscular synapses, in both presynaptic and
CC postsynaptic regions. {ECO:0000269|PubMed:11018772}.
CC -!- DOMAIN: The coiled coil domain mediates homodimerization.
CC {ECO:0000269|PubMed:8682859}.
CC -!- DISRUPTION PHENOTYPE: Life span reduction.
CC {ECO:0000269|PubMed:17435236}.
CC -!- SIMILARITY: Belongs to the hook family. {ECO:0000305}.
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DR EMBL; U48362; AAC47261.1; -; mRNA.
DR EMBL; AF044925; AAC09300.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF53742.1; -; Genomic_DNA.
DR EMBL; AY069337; AAL39482.1; -; mRNA.
DR RefSeq; NP_476573.1; NM_057225.4.
DR AlphaFoldDB; Q24185; -.
DR SMR; Q24185; -.
DR BioGRID; 61158; 25.
DR IntAct; Q24185; 4.
DR STRING; 7227.FBpp0080722; -.
DR PaxDb; Q24185; -.
DR PRIDE; Q24185; -.
DR EnsemblMetazoa; FBtr0081180; FBpp0080722; FBgn0001202.
DR GeneID; 35169; -.
DR KEGG; dme:Dmel_CG10653; -.
DR UCSC; CG10653-RA; d. melanogaster.
DR CTD; 35169; -.
DR FlyBase; FBgn0001202; hook.
DR VEuPathDB; VectorBase:FBgn0001202; -.
DR eggNOG; ENOG502QQM8; Eukaryota.
DR GeneTree; ENSGT00940000167690; -.
DR HOGENOM; CLU_011214_1_0_1; -.
DR InParanoid; Q24185; -.
DR OMA; LEFNNHA; -.
DR OrthoDB; 398210at2759; -.
DR PhylomeDB; Q24185; -.
DR SignaLink; Q24185; -.
DR BioGRID-ORCS; 35169; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 35169; -.
DR PRO; PR:Q24185; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0001202; Expressed in embryonic/larval hemocyte (Drosophila) and 26 other tissues.
DR Genevisible; Q24185; DM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0045202; C:synapse; IMP:FlyBase.
DR GO; GO:0051959; F:dynein light intermediate chain binding; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IPI:FlyBase.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; IDA:UniProtKB.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase.
DR GO; GO:0006897; P:endocytosis; IMP:FlyBase.
DR Gene3D; 1.10.418.10; -; 1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR008636; Hook_C.
DR InterPro; IPR043936; HOOK_N.
DR Pfam; PF05622; HOOK; 1.
DR Pfam; PF19047; HOOK_N; 1.
DR PROSITE; PS50021; CH; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Cytoskeleton; Developmental protein; Endocytosis;
KW Endosome; Microtubule; Reference proteome; Synapse.
FT CHAIN 1..679
FT /note="Protein hook"
FT /id="PRO_0000219199"
FT DOMAIN 6..123
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REGION 1..155
FT /note="Interaction with microtubules"
FT /evidence="ECO:0000250"
FT COILED 135..437
FT /evidence="ECO:0000255"
FT COILED 480..574
FT /evidence="ECO:0000255"
FT CONFLICT 273
FT /note="E -> K (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 679 AA; 76665 MW; C0AB51E0AAD285AC CRC64;
MSAPKNEMYY SLLEWFKTLN LNAPHADAES LADGVALAQA LNQFAPESFT DAWLSKIKAS
AVGSNWRLRM SNLKKVTQSV YDYYSDVLNY SLSDFSKPDL QRIAEKCDLG ELERLLQLVL
GCAVNCAEKQ SYITEIMCLE EELQANIMRA LQELEATRQA STPEGGVASS LSRGSRTGLL
DSKAVQEDRD ALAQKCFETE KKMLLLIDEK TNLQQELHKL QQEFARLEQH STVIGDDGVS
LGPVQTGSVR YNELRRQLDL LKEELLQSEG AREDLKIKAQ QQDTDLLHMQ MRIEELMKSS
AEVTTLKDEV DVLRESNDKL KICEAQLDTY KKKLEDYNDL KKQVKILEER SADYVQQNAQ
FEEDAKRYAN TKGQVELFKK EIQDLHAKLD AESSKNVKLE FDNKNLESKN LALQRAKDSL
LKERDNLREA VDELKCGQLS SNTALTGTTV SRELQPSATV EKLQRLEAEN KALREGQGGQ
TALAQLLDDA NKRCENLREQ LKTANERILS LSHASQSDDP ILKESEFGKQ IKQLMELNEQ
KTLQLEEAVT QSTSLQCKVT QLETNLSARE QEILVYDAKY RKCVEKAKEV IKSIDPRIAS
ALDASVLEKS ADLVEEEPKP KMSVMEEQLM TSAFYRLGVN AQRDAIDSKL AILMGSGQTF
LARQRQSAPR KSLSAMKSK
