ID   HOOK_DROVI              Reviewed;         678 AA.
AC   O61493; B4LS91;
DT   02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   24-JAN-2024, entry version 96.
DE   RecName: Full=Protein hook;
GN   Name=hook {ECO:0000250|UniProtKB:Q24185};
GN   Synonyms=hk {ECO:0000250|UniProtKB:Q24185}; ORFNames=GJ11581;
OS   Drosophila virilis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7244;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15010-1051.87;
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(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:0000250|UniProtKB:Q24185}.
CC   -!- SUBUNIT: Homodimer. Interacts with microtubules via its N-terminus.
CC       {ECO:0000250|UniProtKB:Q24185}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:Q24185}. Endosome
CC       {ECO:0000250|UniProtKB:Q24185}. Synapse {ECO:0000250|UniProtKB:Q24185}.
CC       Note=Enriched at neuromuscular synapses, in both presynaptic and
CC       postsynaptic regions. {ECO:0000250|UniProtKB:Q24185}.
CC   -!- DOMAIN: The coiled coil domain mediates homodimerization.
CC       {ECO:0000250|UniProtKB:Q24185}.
CC   -!- SIMILARITY: Belongs to the hook family. {ECO:0000305}.
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DR   EMBL; AF044926; AAC09301.1; -; Genomic_DNA.
DR   EMBL; CH940649; EDW63699.1; -; Genomic_DNA.
DR   RefSeq; XP_002051544.1; XM_002051508.2.
DR   AlphaFoldDB; O61493; -.
DR   SMR; O61493; -.
DR   STRING; 7244.O61493; -.
DR   GeneID; 6628469; -.
DR   KEGG; dvi:6628469; -.
DR   eggNOG; ENOG502QQM8; Eukaryota.
DR   InParanoid; O61493; -.
DR   OrthoDB; 50921at2759; -.
DR   Proteomes; UP000008792; Unassembled WGS sequence.
DR   GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR   GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR   GO; GO:0031122; P:cytoplasmic microtubule organization; IEA:InterPro.
DR   GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; ISS:UniProtKB.
DR   GO; GO:0006897; P:endocytosis; ISS:UniProtKB.
DR   CDD; cd22222; HkD_Hook; 1.
DR   Gene3D; 1.10.418.10; Calponin-like domain; 1.
DR   InterPro; IPR001715; CH_dom.
DR   InterPro; IPR036872; CH_dom_sf.
DR   InterPro; IPR008636; Hook_C.
DR   InterPro; IPR043936; HOOK_N.
DR   PANTHER; PTHR18947; HOOK PROTEINS; 1.
DR   PANTHER; PTHR18947:SF39; PROTEIN HOOK; 1.
DR   Pfam; PF05622; HOOK; 1.
DR   Pfam; PF19047; HOOK_N; 1.
DR   SUPFAM; SSF116907; Hook domain; 1.
DR   PROSITE; PS50021; CH; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Developmental protein; Endocytosis;
KW   Endosome; Microtubule; Reference proteome; Synapse.
FT   CHAIN           1..678
FT                   /note="Protein hook"
FT                   /id="PRO_0000219200"
FT   DOMAIN          5..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..435
FT                   /evidence="ECO:0000255"
FT   COILED          479..589
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   678 AA;  77199 MW;  1B8535E80F06C673 CRC64;
     MSTQNGMYYS LLEWFKTLNL NAPHANAEEL ADGVALAQAL NQFAPESFTN SWLSKIKSSA
     VGGNWRLRMS NLKKVVEGVY EYYSDVLNYT LQHDFVKPDV QAIAEKCDLS ELERLLQLVL
     GCAVNCAKKQ SYICEIMCLE EELQANIMRA LQELESSTRQ TTEGGVVSSL SRNSLSGMLD
     GNAKALEERD AMAQKCFETE KKMLLLIDEK TNLQQELHKL QLEFARLEHN TIGDDGVSLG
     PIQAGSVRYN ELRRQLELVK EELLQSEGAR EDLKIKAQQQ ETDLLHMQQR IDELMKSTAE
     LTALKDEVDV LRESTDKLKV CEAQLETYKK KLEEYNDLKK HVKMLEERSA DYVQQNAQFE
     EDAKRYANTK GQVELFKKEI QDLHAQLDNE SSKNVKLEFD NKNLESKTLA LQREKDNLLK
     ERDNLREAFD ELKCGQLSTN SGSLTGTTMS RELQPPAMMD KMQRLEAENK ALREGQGGQT
     ALAQLLDDAN KRCEHLREQL KTANERILSL SHASQSDDPI LKENEFSKQI KQLMELNEQK
     TLQIEESATQ NSTMQCKITQ LESTLATREQ ELMAYEVKYR KCIERAKEVI KNIDPRIASV
     MEANNLEKSV DVIEEESKTK MSGMEEQLMA SAFYRLGVNA QRDAVDSKLA LLMGSGQTFL
     ARQRQSAPRK PLTTMKSK
//