HOOK3_MOUSE
ID HOOK3_MOUSE Reviewed; 718 AA.
AC Q8BUK6; Q540A0; Q8BV48; Q8BW57; Q8BY41;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 02-FEB-2004, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Protein Hook homolog 3;
DE Short=mHK3;
GN Name=Hook3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], INTERACTION WITH IIGP1, AND
RP SUBCELLULAR LOCATION.
RX PubMed=15075236; DOI=10.1242/jcs.01039;
RA Kaiser F., Kaufmann S.H.E., Zerrahn J.;
RT "IIGP, a member of the IFN inducible and microbial defense mediating 47 kDa
RT GTPase family, interacts with the microtubule binding protein hook3.";
RL J. Cell Sci. 117:1747-1756(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Heart, Mammary gland, Ovary, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP TISSUE SPECIFICITY.
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 [5]
RP INTERACTION WITH SPIC (MICROBIAL INFECTION), AND FUNCTION (MICROBIAL
RP INFECTION).
RX PubMed=12950921; DOI=10.1046/j.1365-2958.2003.03668.x;
RA Shotland Y., Kraemer H., Groisman E.A.;
RT "The Salmonella SpiC protein targets the mammalian Hook3 protein function
RT to alter cellular trafficking.";
RL Mol. Microbiol. 49:1565-1576(2003).
RN [6]
RP INTERACTION WITH MSR1.
RX PubMed=17237231; DOI=10.1074/jbc.m611537200;
RA Sano H., Ishino M., Kraemer H., Shimizu T., Mitsuzawa H., Nishitani C.,
RA Kuroki Y.;
RT "The microtubule-binding protein Hook3 interacts with a cytoplasmic domain
RT of scavenger receptor A.";
RL J. Biol. Chem. 282:7973-7981(2007).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=17140400; DOI=10.1111/j.1600-0854.2006.00511.x;
RA Szebenyi G., Hall B., Yu R., Hashim A.I., Kraemer H.;
RT "Hook2 localizes to the centrosome, binds directly to centriolin/CEP110 and
RT contributes to centrosomal function.";
RL Traffic 8:32-46(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP INTERACTION WITH CCDC181.
RX PubMed=28283191; DOI=10.1016/j.ejcb.2017.02.003;
RA Schwarz T., Prieler B., Schmid J.A., Grzmil P., Neesen J.;
RT "Ccdc181 is a microtubule-binding protein that interacts with Hook1 in
RT haploid male germ cells and localizes to the sperm tail and motile cilia.";
RL Eur. J. Cell Biol. 96:276-288(2017).
RN [10]
RP INTERACTION WITH LRGUK, AND SUBCELLULAR LOCATION.
RX PubMed=28003339; DOI=10.1096/fj.201600909r;
RA Okuda H., DeBoer K., O'Connor A.E., Merriner D.J., Jamsai D., O'Bryan M.K.;
RT "LRGUK1 is part of a multiprotein complex required for manchette function
RT and male fertility.";
RL FASEB J. 31:1141-1152(2017).
CC -!- FUNCTION: Probably serves as a target for the spiC protein from
CC Salmonella typhimurium, which inactivates it, leading to a strong
CC alteration in cellular trafficking (By similarity). Component of the
CC FTS/Hook/FHIP complex (FHF complex). The FHF complex may function to
CC promote vesicle trafficking and/or fusion via the homotypic vesicular
CC protein sorting complex (the HOPS complex). May regulate clearance of
CC endocytosed receptors such as MSR1. Participates in defining the
CC architecture and localization of the Golgi complex. Acts as an adapter
CC protein linking the dynein motor complex to various cargos and converts
CC dynein from a non-processive to a highly processive motor in the
CC presence of dynactin. Facilitates the interaction between dynein and
CC dynactin and activates dynein processivity (the ability to move along a
CC microtubule for a long distance without falling off the track) (By
CC similarity). FHF complex promotes the distribution of AP-4 complex to
CC the perinuclear area of the cell (By similarity).
CC {ECO:0000250|UniProtKB:Q86VS8}.
CC -!- FUNCTION: (Microbial infection) Serves as a target for the spiC protein
CC from Salmonella typhimurium, which inactivates it, leading to a strong
CC alteration in cellular trafficking. {ECO:0000269|PubMed:12950921}.
CC -!- SUBUNIT: Self-associates (By similarity). Component of the
CC FTS/Hook/FHIP complex (FHF complex), composed of AKTIP/FTS, FHIP1B, and
CC one or more members of the Hook family of proteins HOOK1, HOOK2, and
CC HOOK3 (By similarity). May interact directly with AKTIP/FTS, HOOK1 and
CC HOOK2 (By similarity). Associates with several subunits of the
CC homotypic vesicular sorting complex (the HOPS complex) including VPS16
CC and VPS41; these interactions may be indirect (By similarity).
CC Interacts with IIGP1 (PubMed:15075236). Interacts with MSR1, and this
CC association is stimulated by ligand binding to MSR1 (PubMed:17237231).
CC Interacts with microtubules (By similarity). Interacts with dynein
CC intermediate chain and dynactin (DCTN1) (By similarity). Interacts with
CC CCDC181 (PubMed:28283191). Interacts with LRGUK (PubMed:28003339).
CC {ECO:0000250|UniProtKB:Q86VS8, ECO:0000269|PubMed:15075236,
CC ECO:0000269|PubMed:17237231, ECO:0000269|PubMed:28003339,
CC ECO:0000269|PubMed:28283191}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Salmonella typhimurium
CC spiC. {ECO:0000269|PubMed:12950921}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:15075236, ECO:0000269|PubMed:28003339}. Golgi
CC apparatus {ECO:0000269|PubMed:15075236}. Note=Enriched at the cis-face
CC of the Golgi complex (By similarity). Localizes to microtubule asters
CC in prophase (By similarity). Localizes to the manchette in elongating
CC spermatids (PubMed:28003339). {ECO:0000250|UniProtKB:Q86VS8,
CC ECO:0000269|PubMed:28003339}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, cerebellum, heart, intestine,
CC kidney, liver, lung, skeletal muscle, spleen and stomach (at protein
CC level). {ECO:0000269|PubMed:11238449, ECO:0000269|PubMed:17140400}.
CC -!- SIMILARITY: Belongs to the hook family. {ECO:0000305}.
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DR EMBL; AY223806; AAO43109.1; -; mRNA.
DR EMBL; AK042180; BAC31191.1; -; mRNA.
DR EMBL; AK054263; BAC35709.1; -; mRNA.
DR EMBL; AK080377; BAC37897.1; -; mRNA.
DR EMBL; AK084594; BAC39222.1; -; mRNA.
DR EMBL; AK145149; BAE26261.1; -; mRNA.
DR EMBL; CH466580; EDL32811.1; -; Genomic_DNA.
DR CCDS; CCDS22206.1; -.
DR RefSeq; NP_997542.1; NM_207659.3.
DR AlphaFoldDB; Q8BUK6; -.
DR SMR; Q8BUK6; -.
DR BioGRID; 235828; 5.
DR CORUM; Q8BUK6; -.
DR IntAct; Q8BUK6; 4.
DR STRING; 10090.ENSMUSP00000046788; -.
DR iPTMnet; Q8BUK6; -.
DR PhosphoSitePlus; Q8BUK6; -.
DR EPD; Q8BUK6; -.
DR MaxQB; Q8BUK6; -.
DR PaxDb; Q8BUK6; -.
DR PeptideAtlas; Q8BUK6; -.
DR PRIDE; Q8BUK6; -.
DR ProteomicsDB; 273378; -.
DR Antibodypedia; 11516; 110 antibodies from 27 providers.
DR DNASU; 320191; -.
DR Ensembl; ENSMUST00000037182; ENSMUSP00000046788; ENSMUSG00000037234.
DR GeneID; 320191; -.
DR KEGG; mmu:320191; -.
DR UCSC; uc009lhj.2; mouse.
DR CTD; 84376; -.
DR MGI; MGI:2443554; Hook3.
DR VEuPathDB; HostDB:ENSMUSG00000037234; -.
DR eggNOG; ENOG502QQM8; Eukaryota.
DR GeneTree; ENSGT00940000158075; -.
DR HOGENOM; CLU_011214_1_0_1; -.
DR InParanoid; Q8BUK6; -.
DR OMA; LEFNNHA; -.
DR OrthoDB; 398210at2759; -.
DR PhylomeDB; Q8BUK6; -.
DR TreeFam; TF320231; -.
DR BioGRID-ORCS; 320191; 5 hits in 75 CRISPR screens.
DR ChiTaRS; Hook3; mouse.
DR PRO; PR:Q8BUK6; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8BUK6; protein.
DR Bgee; ENSMUSG00000037234; Expressed in otolith organ and 220 other tissues.
DR ExpressionAtlas; Q8BUK6; baseline and differential.
DR Genevisible; Q8BUK6; MM.
DR GO; GO:0034451; C:centriolar satellite; IDA:MGI.
DR GO; GO:0005813; C:centrosome; IDA:BHF-UCL.
DR GO; GO:0005801; C:cis-Golgi network; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0070695; C:FHF complex; ISS:UniProtKB.
DR GO; GO:0030897; C:HOPS complex; ISO:MGI.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0000242; C:pericentriolar material; IDA:BHF-UCL.
DR GO; GO:0034452; F:dynactin binding; ISS:UniProtKB.
DR GO; GO:0045505; F:dynein intermediate chain binding; ISS:UniProtKB.
DR GO; GO:0045503; F:dynein light chain binding; ISO:MGI.
DR GO; GO:0051959; F:dynein light intermediate chain binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; ISO:MGI.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; ISO:MGI.
DR GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; IBA:GO_Central.
DR GO; GO:0045022; P:early endosome to late endosome transport; ISS:UniProtKB.
DR GO; GO:0007032; P:endosome organization; ISS:UniProtKB.
DR GO; GO:0008333; P:endosome to lysosome transport; ISS:UniProtKB.
DR GO; GO:0051645; P:Golgi localization; ISO:MGI.
DR GO; GO:0022027; P:interkinetic nuclear migration; IMP:BHF-UCL.
DR GO; GO:0007040; P:lysosome organization; ISS:UniProtKB.
DR GO; GO:0034454; P:microtubule anchoring at centrosome; IMP:MGI.
DR GO; GO:0050768; P:negative regulation of neurogenesis; IMP:BHF-UCL.
DR GO; GO:0097150; P:neuronal stem cell population maintenance; IMP:MGI.
DR GO; GO:0071539; P:protein localization to centrosome; IMP:BHF-UCL.
DR GO; GO:1905719; P:protein localization to perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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 Acetylation; Coiled coil; Cytoplasm; Cytoskeleton; Golgi apparatus;
KW Microtubule; Phosphoprotein; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..718
FT /note="Protein Hook homolog 3"
FT /id="PRO_0000219198"
FT DOMAIN 10..126
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REGION 1..164
FT /note="Sufficient for interaction with microtubules"
FT /evidence="ECO:0000250"
FT REGION 450..671
FT /note="Sufficient for interaction with IIGP1"
FT /evidence="ECO:0000269|PubMed:15075236"
FT REGION 553..718
FT /note="Required for association with Golgi"
FT /evidence="ECO:0000250"
FT REGION 682..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 168..433
FT /evidence="ECO:0000255"
FT COILED 462..663
FT /evidence="ECO:0000255"
FT COMPBIAS 686..710
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q86VS8"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86VS8"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 693
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86VS8"
FT MOD_RES 707
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86VS8"
FT CONFLICT 94
FT /note="Q -> H (in Ref. 2; BAC37897)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 718 AA; 83218 MW; 72577D065F118172 CRC64;
MFNVESVERV ELCESLLTWI QTFNVDAPCQ TAEDLTNGVV MSQVLQKIDP VYFDDNWLNR
IKTEVGDNWR LKISNLKKIL KGILDYNHEI LGQQINDFTL PDVNLIGEHS DAAELGRMLQ
LILGCAVNCE QKQEYIQAIM MMEESVQHVV MTAIQELMSK ESPVSAGHDA YVDLDRQLKK
TTEELNEALS AKEEIAQRCH ELDMQVAALQ EEKSSLLAEN QILMERLNQS DSIEDPNSPA
GRRHLQLQTQ LEQLQEETFR LEAAKDDYRI RCEELEKEIS ELRQQNDELT TLADEAQSLK
DEIDVLRHSS DKVSKLEGQV ESYKKKLEDL GDLRRQVKLL EEKNTMYMQN TVSLEEELRK
ANAARGQLET YKRQVVELQN RLSDESKKAD KLDFEYKRLK EKVDGLQKEK DRLRTERDSL
KETIEELRCV QAQEGQLTTQ GLMPLGSQES SDSLAAEIVT PEIREKLIRL QHENKMLKLN
QEDSDNEKIA LLQSLLDDAN LRKNELETEN RLVNQRLLEV QSQVEELQKS LQDQGSKAED
SVLLKKKLEE HLEKLHEANN ELQKKRAIIE DLEPRFNNSS LRIEELQEAL RKKEEEMKQM
EERYKKYLEK AKSVIRTLDP KQNQGAAPEI QALKNQLQER DRLFHSLEKE YEKTKSQRDM
EEKYIVSAWY NMGMTLHKKA AEDRLASTGS GQSFLARQRQ ATSTRRSYPG HVQPATAR
