ID HOOK1_MOUSE Reviewed; 728 AA.
AC Q8BIL5; Q8BIZ2; Q8K0P1; Q8K454; Q9CTN6;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 02-FEB-2004, sequence version 2.
DT 24-JAN-2024, entry version 164.
DE RecName: Full=Protein Hook homolog 1;
DE Short=mHK1;
GN Name=Hook1;
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 [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DISEASE.
RC TISSUE=Testis;
RX PubMed=12075009; DOI=10.1093/hmg/11.14.1647;
RA Mendoza-Lujambio I., Burfeind P., Dixkens C., Meinhardt A.,
RA Hoyer-Fender S., Engel W., Neesen J.;
RT "The Hook1 gene is non-functional in the abnormal spermatozoon head shape
RT (azh) mutant mouse.";
RL Hum. Mol. Genet. 11:1647-1658(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain cortex, Hippocampus, and Retina;
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 MRNA] (ISOFORM 1).
RC TISSUE=Eye, and Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 530-537, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [6]
RP INTERACTION WITH RIMBP3, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19091768; DOI=10.1242/dev.030858;
RA Zhou J., Du Y.R., Qin W.H., Hu Y.G., Huang Y.N., Bao L., Han D.,
RA Mansouri A., Xu G.L.;
RT "RIM-BP3 is a manchette-associated protein essential for spermiogenesis.";
RL Development 136:373-382(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-727, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, and 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 [8]
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 [9]
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).
RN [10]
RP STRUCTURE BY NMR OF 10-162.
RG RIKEN structural genomics initiative (RSGI);
RT "The solution structure of RSGI RUH-026, conserved domain of Hook1 protein
RT from mouse.";
RL Submitted (NOV-2004) to the PDB data bank.
CC -!- FUNCTION: Component of the FTS/Hook/FHIP complex (FHF complex). The FHF
CC complex may function to promote vesicle trafficking and/or fusion via
CC the homotypic vesicular protein sorting complex (the HOPS complex). FHF
CC complex promotes the distribution of AP-4 complex to the perinuclear
CC area of the cell (By similarity). Required for spermatid
CC differentiation. Probably involved in the positioning of the
CC microtubules of the manchette and the flagellum in relation to the
CC membrane skeleton (PubMed:12075009). {ECO:0000250|UniProtKB:Q9UJC3,
CC ECO:0000269|PubMed:12075009}.
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). Interacts directly with AKTIP/FTS, HOOK2 and
CC HOOK3 (By similarity). Associates with several subunits of the
CC homotypic vesicular sorting complex (the HOPS complex) including VPS16,
CC VPS18, VPS39 and VPS41; these interactions may be indirect (By
CC similarity). Interacts with CCDC181 (PubMed:28283191). Interacts (via
CC coiled-coil region) with RIMBP3 (via C-terminus) (PubMed:19091768).
CC Interacts with LRGUK (via guanylate kinase-like domain)
CC (PubMed:28003339). Interacts with microtubules (By similarity). May
CC interacts with CLN3 (By similarity). Interacts with AP4M1; the
CC interaction is direct, mediates the interaction between FTS-Hook-FHIP
CC (FHF) complex and AP-4 and the perinuclear distribution of AP-4 (By
CC similarity). {ECO:0000250|UniProtKB:Q9UJC3,
CC ECO:0000269|PubMed:19091768, ECO:0000269|PubMed:28003339,
CC ECO:0000269|PubMed:28283191}.
CC -!- INTERACTION:
CC Q8BIL5; P18572: Bsg; NbExp=2; IntAct=EBI-4285715, EBI-772883;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12075009}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12075009,
CC ECO:0000269|PubMed:28003339}. Note=Localizes to punctate cytoplasmic
CC foci which do not appear to overlap with early or late endosomes, the
CC endoplasmic reticulum, multivesicular bodies (MVBs), lysosomes, or
CC mitochondria (PubMed:12075009). Often found in close association with
CC microtubules (PubMed:12075009). Does not associate with the Golgi
CC complex (PubMed:12075009). During spermiogenesis, it localizes to the
CC manchette in spermatids from steps 8-10 (PubMed:12075009). It is also
CC present between the microtubule manchette and the nucleus
CC (PubMed:12075009). During manchette elongation, it is preferentially
CC localized to the nuclear ring of the manchette, whereas the strong
CC localization to the manchette decreases (PubMed:12075009). In more
CC mature spermatids, while the manchette migrates posteriorly, it
CC localizes to punctuates spots (PubMed:12075009). At later stages of
CC spermatid differentiation, the punctuate expression pattern is found at
CC both the attachment site and the proximal end of the elongated
CC manchette (PubMed:12075009). In contrast, it is not present in mature
CC spermatozoa (PubMed:12075009). {ECO:0000269|PubMed:12075009}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BIL5-1; Sequence=Displayed;
CC Name=2; Synonyms=sv;
CC IsoId=Q8BIL5-2; Sequence=VSP_009340, VSP_009341;
CC -!- TISSUE SPECIFICITY: Mainly expressed in testis.
CC {ECO:0000269|PubMed:12075009}.
CC -!- DISEASE: Note=Defects in Hook1 are the cause of the azh (abnormal
CC spermatozoon head shape) mutant phenotype, which induces spermatozoa
CC with highly abnormal head morphology that differs drastically from the
CC compact and hook-shaped head of the normal sperm, leading to a strong
CC decrease of fertility. {ECO:0000269|PubMed:12075009}.
CC -!- SIMILARITY: Belongs to the hook family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH30877.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF487912; AAM74055.1; -; mRNA.
DR EMBL; AK020924; BAB32257.1; -; mRNA.
DR EMBL; AK043870; BAC31686.1; -; mRNA.
DR EMBL; AK049897; BAC33977.1; -; mRNA.
DR EMBL; BC030877; AAH30877.1; ALT_INIT; mRNA.
DR EMBL; BC061688; AAH61688.1; -; mRNA.
DR CCDS; CCDS18367.1; -. [Q8BIL5-1]
DR RefSeq; NP_084290.1; NM_030014.2. [Q8BIL5-1]
DR PDB; 1WIX; NMR; -; A=12-162.
DR PDBsum; 1WIX; -.
DR AlphaFoldDB; Q8BIL5; -.
DR SMR; Q8BIL5; -.
DR BioGRID; 219052; 5.
DR IntAct; Q8BIL5; 3.
DR STRING; 10090.ENSMUSP00000030306; -.
DR iPTMnet; Q8BIL5; -.
DR PhosphoSitePlus; Q8BIL5; -.
DR SwissPalm; Q8BIL5; -.
DR EPD; Q8BIL5; -.
DR MaxQB; Q8BIL5; -.
DR PaxDb; 10090-ENSMUSP00000030306; -.
DR PeptideAtlas; Q8BIL5; -.
DR ProteomicsDB; 273128; -. [Q8BIL5-1]
DR ProteomicsDB; 273129; -. [Q8BIL5-2]
DR Antibodypedia; 19416; 287 antibodies from 28 providers.
DR DNASU; 77963; -.
DR Ensembl; ENSMUST00000030306.14; ENSMUSP00000030306.8; ENSMUSG00000028572.14. [Q8BIL5-1]
DR GeneID; 77963; -.
DR KEGG; mmu:77963; -.
DR UCSC; uc008ttb.1; mouse. [Q8BIL5-2]
DR UCSC; uc008ttc.1; mouse. [Q8BIL5-1]
DR AGR; MGI:1925213; -.
DR CTD; 51361; -.
DR MGI; MGI:1925213; Hook1.
DR VEuPathDB; HostDB:ENSMUSG00000028572; -.
DR eggNOG; ENOG502QW1T; Eukaryota.
DR GeneTree; ENSGT00940000159251; -.
DR HOGENOM; CLU_011214_1_0_1; -.
DR InParanoid; Q8BIL5; -.
DR OMA; TYKKQVQ; -.
DR OrthoDB; 50921at2759; -.
DR PhylomeDB; Q8BIL5; -.
DR TreeFam; TF320231; -.
DR BioGRID-ORCS; 77963; 4 hits in 77 CRISPR screens.
DR EvolutionaryTrace; Q8BIL5; -.
DR PRO; PR:Q8BIL5; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8BIL5; Protein.
DR Bgee; ENSMUSG00000028572; Expressed in spermatid and 221 other cell types or tissues.
DR ExpressionAtlas; Q8BIL5; baseline and differential.
DR Genevisible; Q8BIL5; MM.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0070695; C:FHF complex; ISS:UniProtKB.
DR GO; GO:0030897; C:HOPS complex; IEA:Ensembl.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
DR GO; GO:0003779; F:actin binding; IDA: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; IDA:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IMP: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:0007030; P:Golgi organization; IMP:MGI.
DR GO; GO:0007040; P:lysosome organization; ISS:UniProtKB.
DR GO; GO:1905198; P:manchette assembly; IMP:MGI.
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 GO; GO:0007286; P:spermatid development; IMP:MGI.
DR CDD; cd22225; HkD_Hook1; 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:SF36; PROTEIN HOOK HOMOLOG 1; 1.
DR Pfam; PF05622; HOOK; 1.
DR Pfam; PF19047; HOOK_N; 1.
DR SUPFAM; SSF116907; Hook domain; 1.
DR PROSITE; PS50021; CH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Coiled coil; Cytoplasm;
KW Cytoskeleton; Developmental protein; Differentiation;
KW Direct protein sequencing; Microtubule; Phosphoprotein; Protein transport;
KW Reference proteome; Spermatogenesis; Transport.
FT CHAIN 1..728
FT /note="Protein Hook homolog 1"
FT /id="PRO_0000219193"
FT DOMAIN 12..128
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REGION 1..555
FT /note="Sufficient for interaction with microtubules"
FT /evidence="ECO:0000250"
FT REGION 481..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 657..728
FT /note="Sufficient for interaction with AKTIP and VPS18"
FT /evidence="ECO:0000250"
FT COILED 168..443
FT /evidence="ECO:0000255"
FT COILED 477..658
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJC3"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJC3"
FT MOD_RES 719
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJC3"
FT MOD_RES 727
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 543..549
FT /note="SSKLKQK -> VSNRVHN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12075009,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_009340"
FT VAR_SEQ 550..728
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12075009,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_009341"
FT CONFLICT 185
FT /note="E -> Q (in Ref. 2; BAC31686)"
FT /evidence="ECO:0000305"
FT CONFLICT 334
FT /note="N -> T (in Ref. 2; BAC33977)"
FT /evidence="ECO:0000305"
FT HELIX 13..22
FT /evidence="ECO:0007829|PDB:1WIX"
FT HELIX 34..37
FT /evidence="ECO:0007829|PDB:1WIX"
FT HELIX 41..50
FT /evidence="ECO:0007829|PDB:1WIX"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:1WIX"
FT HELIX 57..60
FT /evidence="ECO:0007829|PDB:1WIX"
FT HELIX 66..69
FT /evidence="ECO:0007829|PDB:1WIX"
FT HELIX 72..90
FT /evidence="ECO:0007829|PDB:1WIX"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:1WIX"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:1WIX"
FT HELIX 105..109
FT /evidence="ECO:0007829|PDB:1WIX"
FT HELIX 114..127
FT /evidence="ECO:0007829|PDB:1WIX"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:1WIX"
FT HELIX 134..143
FT /evidence="ECO:0007829|PDB:1WIX"
FT HELIX 146..162
FT /evidence="ECO:0007829|PDB:1WIX"
SQ SEQUENCE 728 AA; 84439 MW; 5AC9A80D5D61581C CRC64;
MEDPQPLPQS ELPLCDSLII WLQTFKTASP CQDVKQLTNG VTMAQVLHQI DVAWFSESWL
SRIKDDVGDN WRIKASNLKK VLHGITSYYH EFLGQQISEE LIPDLNQITE CADPVELGRL
LQLILGCAVN CEKKQEHIKN IMTLEESVQH VVMTAIQELM SKEIVISPAS DTVGELEQQL
KRALEELQEA IAEKEELKQR CQELDMQVTT LQDEKNSLVS ENEMMNEKLD QLDGSFDDPN
TMVAKKYFHV QLQLEQLQEE NYRLEAAKDD YRVHCEELEK QLIEFQHRND ELTSLAEETR
ALKDEIDVLR ATSDKANKLE STVEVYRQKL QDLNDLRKQV KSLQETNMMY MHNTVSLEEE
LKKANAARAQ LETYKRQVQD LHTKLSSESK RADTLAFEMK RLEEKHETLL KEKERLIEQR
DTLKETNEEL RCSKAQQDHL NQADASATKS YENLAAEIMP VEYREVFIRL QHENKMLRLQ
QEGTENERIE QLQEQLEQKH RKMNELETEQ RLSKERIGEL QQQIEDLQKS LQEQGSKSEG
ESSSKLKQKL EAHMEKLTEV HEELQKKQEL IEDLQPDISQ NAQKISELEA ALQKKDEDMK
AMEERYKMYL EKARNVIKTL DPKLNPASAE IMLLRKQLAE KERRIEILES ECKVAKLRDY
EEKLIVSAWY NKSLAFQKLG MESRLVSGAS ACKDSVAAAP ARSFLAQQRH ITNTRRNLSV
KVPAAASD
//
