ID   HOOK_DROPE              Reviewed;         677 AA.
AC   B4G831;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 2.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Protein hook;
GN   Name=hook {ECO:0000250|UniProtKB:Q24185};
GN   Synonyms=hk {ECO:0000250|UniProtKB:Q24185}; ORFNames=GL19224;
OS   Drosophila persimilis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7234;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSH-3 / Tucson 14011-0111.49;
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EDW28511.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=EDW28511.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; CH479180; EDW28511.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_002014515.1; XM_002014479.1.
DR   AlphaFoldDB; B4G831; -.
DR   SMR; B4G831; -.
DR   STRING; 7234.FBpp0183331; -.
DR   eggNOG; ENOG502QQM8; Eukaryota.
DR   Proteomes; UP000008744; Unassembled WGS sequence.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR   GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR   GO; GO:0031267; F:small GTPase binding; IEA:EnsemblMetazoa.
DR   GO; GO:0031122; P:cytoplasmic microtubule organization; IEA:InterPro.
DR   GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; ISS:UniProtKB.
DR   GO; GO:0008340; P:determination of adult lifespan; ISS:UniProtKB.
DR   GO; GO:0006897; P:endocytosis; ISS:UniProtKB.
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   3: Inferred from homology;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Developmental protein; Endocytosis;
KW   Endosome; Microtubule; Reference proteome; Synapse.
FT   CHAIN           1..677
FT                   /note="Protein hook"
FT                   /id="PRO_0000379066"
FT   DOMAIN          6..123
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT   COILED          135..436
FT                   /evidence="ECO:0000255"
FT   COILED          478..588
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   677 AA;  76821 MW;  AE45AADAFA97AFCA CRC64;
     MSAAKNEMYY SLLEWFKTLN LNAPHADAES LADGVAVAQA LNQFAPESFT DSWLAKIKAS
     AVGINWRLRM SNLKKVTQSL YDYYSEVLNY TLSDFVKPDV QRIAEKCDLV ELERLLQLVL
     GCAVNCAKKQ SYITEIMCLE EELQANIMRA LQELESSRNA AEGGIVTSLS RSSISGMLDG
     KVLQEERDAM AQKCFETEKK MLLLIDEKTN LQQELQRVQK EFARLEHSST VIGDDGVSLG
     PVQTGSVRYN ELRRQLDLLK EELLQSEGAR EDLKLKAQQQ ETDLWHMQMR IDELLKSTAE
     VTTLKDEVDV LRESNDKLKI CEGQLDTYKK KLEDYNDLKK QVKILEERSA DYVQQNAQFE
     EDAKRYANTK GQIELFKKEI QDLHTKLDSE SSKNVKLEFD NKNLEGKNLA LQRAKDSLLK
     ERDNLRETVD ELKCGHLSSN SGLTGTTVSR ELQPPATVEK MQRLEAENKA LREGQGGQTA
     LAQLLDDANK RCENLREQLK TANERILSLS HASQSDDPIL KESEFGKQIK QLMELNEQKT
     LQLEESVTQS SSLQCKVTQL ETNLTAREQE VMAYDAKYRK CLEKAKEVIK SFDPRIASAI
     DASALEKYFD VVEEEPKPKM SVMEEQLMTS AFYRLGVNAQ RDAVDSKLAI LMGSGQTFLA
     RQRQSAPRKS LSAMKSK