HOOK_DICDI
ID HOOK_DICDI Reviewed; 734 AA.
AC Q54IK9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Protein hook homolog;
DE AltName: Full=DdHk3;
GN Name=hook; Synonyms=hk3; ORFNames=DDB_G0288691;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Cytoskeletal linker protein involved in tethering membrane
CC bound organelles to the cytoskeleton. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Interacts with microtubules (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- DOMAIN: The large coiled coil domain may mediate homodimerization.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the hook family. {ECO:0000305}.
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DR EMBL; AAFI02000120; EAL63077.1; -; Genomic_DNA.
DR RefSeq; XP_636577.1; XM_631485.1.
DR AlphaFoldDB; Q54IK9; -.
DR SMR; Q54IK9; -.
DR STRING; 44689.DDB0219928; -.
DR PaxDb; Q54IK9; -.
DR EnsemblProtists; EAL63077; EAL63077; DDB_G0288691.
DR GeneID; 8626750; -.
DR KEGG; ddi:DDB_G0288691; -.
DR dictyBase; DDB_G0288691; hook.
DR eggNOG; ENOG502RSPB; Eukaryota.
DR HOGENOM; CLU_377875_0_0_1; -.
DR InParanoid; Q54IK9; -.
DR OMA; LEFNNHA; -.
DR PhylomeDB; Q54IK9; -.
DR PRO; PR:Q54IK9; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0051959; F:dynein light intermediate chain binding; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; ISS:dictyBase.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; ISS:dictyBase.
DR GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; IBA:GO_Central.
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; Microtubule; Reference proteome.
FT CHAIN 1..734
FT /note="Protein hook homolog"
FT /id="PRO_0000333270"
FT DOMAIN 1..113
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REGION 146..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 200..245
FT /evidence="ECO:0000255"
FT COILED 291..700
FT /evidence="ECO:0000255"
SQ SEQUENCE 734 AA; 84236 MW; 26E3C44E174648BB CRC64;
MIETSFIKWI NSFKDLSNSI EDLKELSNGT IFNEICCQIA PKYFDIDSLR KDGLDNWIFR
EENIKNIVER VDEFYIEEMG LNDQISSINC EEIANENIDE IILLIEAILG MAMESENNEA
VIENILSLDQ DTQNDLMVVV AKIQQSHQPN TVDNSKSFDK DGSILSQSPS QSNNSISNNN
NNNNIDSSNI SKSNISSNNN NNNSSNNNKE EILNLQNEIE KLKREKQEIQ NDLDESNIQL
SNVTMDRDRI TIDKQKTEEV CSSLHESIIG LQKQLDETMA QTTTMNALND ETYKTEINDL
HMQVESKEKQ LSELKKKVDE ANRLANENRS LRDEIDILRE KAANAEATEE KLKKHQKKIE
EIGDLKKKIK ELEDQNDSYI QQTLDLEEQL SKNNTYRTQA DSGKQQISSL KIELAKLELS
LKSIKEDRDK LSESLNTVEL ERDSLQSQVT NLRNTIDNQQ QEYETKFVDL QSSISLNSGG
SGGLGDEVID GSTKERIARL ERDNKRLKEV AEKASELENQ LEDANQSKEL LTIQIKQLEE
QKQQSNNTNN NNNNNNMVDS SEIESLKQQL KEKEKEISTL KRKLEESNLS LDENRKQLVE
LSQRPTTQSP GDIEKLENYE NLLKENDGLE GRLRAARNII KDLREKHKSY SNQETQLATK
DEVITKLEGL VKKKTDINED LRKQLEEGRE ESQREINLML SAFLKIGLEM EQVKIQNISS
SKEPRSFLNK KRAD