HOOK_AEDAE
ID HOOK_AEDAE Reviewed; 685 AA.
AC Q17AF4;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Protein hook;
GN Name=hook {ECO:0000250|UniProtKB:Q24185};
GN Synonyms=hk {ECO:0000250|UniProtKB:Q24185}; ORFNames=AAEL005341;
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LVPib12;
RX PubMed=17510324; DOI=10.1126/science.1138878;
RA Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL Science 316:1718-1723(2007).
CC -!- FUNCTION: Involved in endocytic trafficking. Probably acts as a
CC cytoskeletal linker protein that tethers endosome vesicles to the
CC cytoskeleton. {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}.
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; CH477336; EAT43206.1; -; Genomic_DNA.
DR RefSeq; XP_001650717.1; XM_001650667.1.
DR AlphaFoldDB; Q17AF4; -.
DR SMR; Q17AF4; -.
DR STRING; 7159.AAEL005341-PA; -.
DR PRIDE; Q17AF4; -.
DR GeneID; 5566328; -.
DR KEGG; aag:5566328; -.
DR VEuPathDB; VectorBase:AAEL005341; -.
DR eggNOG; ENOG502QQM8; Eukaryota.
DR HOGENOM; CLU_011214_1_0_1; -.
DR InParanoid; Q17AF4; -.
DR OMA; LEFNNHA; -.
DR OrthoDB; 398210at2759; -.
DR PhylomeDB; Q17AF4; -.
DR Proteomes; UP000008820; Chromosome 2.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
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 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 InterPro; IPR038077; Troponin_sf.
DR Pfam; PF05622; HOOK; 1.
DR Pfam; PF19047; HOOK_N; 1.
DR SUPFAM; SSF90250; SSF90250; 1.
DR PROSITE; PS50021; CH; 1.
PE 3: Inferred from homology;
KW Coiled coil; Cytoplasm; Cytoskeleton; Endocytosis; Endosome; Microtubule;
KW Reference proteome.
FT CHAIN 1..685
FT /note="Protein hook"
FT /id="PRO_0000379059"
FT DOMAIN 6..122
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REGION 430..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 661..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 134..570
FT /evidence="ECO:0000255"
FT COMPBIAS 598..625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 685 AA; 77356 MW; D257A159FB7992EB CRC64;
MESDKMEIYE SLIRWLGVLQ LSAPHENIQQ LSDGVALAQA LNLIAPEMFS EGWLAKIKVD
VGHNWRLKVS NLKKIIEGVY VYYQDILSLN LSEKLRPDAM KIAEKCDGYE LGRLLQLILG
CAVNCLEKQK YITQIMELEE SLQRNIMAAL QDIEYVWQGV SPSRNSINAT SLDVKTLQED
RDSLAQKCHE TNKKMLILIE EKSVLQQEIT KLQALIARYE NPNLIGDDGT SLGPVQLGST
RYNDLRKVVD SLKDELLQAE TARDDLKMKS AMQEKEIADL QVKIDELHTA TAEIAQLKDE
IDILKEANDK LKMCETQLLT YKKKLEDYND LKKQIKMLEE CSAEYLKQNL QHEEEAKKYS
GLKGQVELYK KEIQDLHAKL DSEMSKTVKT EFEYNQLQAK LSAVQREKEN LLSERDVLRE
TCDELKCGQA AEDSESGNTM SKELHSSDVR DRIERLEREN KVLREGQGGQ TALSQLLDDA
NQRNEKLRDQ LKAANQRVLL LSQHHNEDIS SKSDMDIQLK QALELNEQRS SQIDEAQSQM
TQLHTKIANL EAALAAKDQE LLAADSRYKK CVEKAKEVIK TLDPRAINEA LLLEKPSQDG
EASSSSATGS GGDASTLTST GSGRVPMGVQ EEQLIATAFY RLGMTCQREA VDSRLALLSG
PGQSFLSRQR QPAPRKPMNM PFAKK
