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Protein Hook homolog 1 (mHK1)

 HOOK1_MOUSE             Reviewed;         728 AA.
Q8BIL5; Q8BIZ2; Q8K0P1; Q8K454; Q9CTN6;
02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
02-FEB-2004, sequence version 2.
12-SEP-2018, entry version 137.
RecName: Full=Protein Hook homolog 1;
Short=mHK1;
Name=Hook1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, AND DISEASE.
TISSUE=Testis;
PubMed=12075009; DOI=10.1093/hmg/11.14.1647;
Mendoza-Lujambio I., Burfeind P., Dixkens C., Meinhardt A.,
Hoyer-Fender S., Engel W., Neesen J.;
"The Hook1 gene is non-functional in the abnormal spermatozoon head
shape (azh) mutant mouse.";
Hum. Mol. Genet. 11:1647-1658(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Brain cortex, Hippocampus, and Retina;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Eye, and Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 530-537, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=OF1; TISSUE=Hippocampus;
Lubec G., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
Burlingame A.L.;
"Comprehensive identification of phosphorylation sites in postsynaptic
density preparations.";
Mol. Cell. Proteomics 5:914-922(2006).
[6]
INTERACTION WITH RIMBP3, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=19091768; DOI=10.1242/dev.030858;
Zhou J., Du Y.R., Qin W.H., Hu Y.G., Huang Y.N., Bao L., Han D.,
Mansouri A., Xu G.L.;
"RIM-BP3 is a manchette-associated protein essential for
spermiogenesis.";
Development 136:373-382(2009).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-727, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[8]
INTERACTION WITH CCDC181.
PubMed=28283191; DOI=10.1016/j.ejcb.2017.02.003;
Schwarz T., Prieler B., Schmid J.A., Grzmil P., Neesen J.;
"Ccdc181 is a microtubule-binding protein that interacts with Hook1 in
haploid male germ cells and localizes to the sperm tail and motile
cilia.";
Eur. J. Cell Biol. 96:276-288(2017).
[9]
INTERACTION WITH LRGUK, AND SUBCELLULAR LOCATION.
PubMed=28003339; DOI=10.1096/fj.201600909R;
Okuda H., DeBoer K., O'Connor A.E., Merriner D.J., Jamsai D.,
O'Bryan M.K.;
"LRGUK1 is part of a multiprotein complex required for manchette
function and male fertility.";
FASEB J. 31:1141-1152(2017).
[10]
STRUCTURE BY NMR OF 10-162.
RIKEN structural genomics initiative (RSGI);
"The solution structure of RSGI RUH-026, conserved domain of Hook1
protein from mouse.";
Submitted (NOV-2004) to the PDB data bank.
-!- FUNCTION: Required for spermatid differentiation. Probably
involved in the positioning of the microtubules of the manchette
and the flagellum in relation to the membrane skeleton
(PubMed:12075009). Component of the FTS/Hook/FHIP complex (FHF
complex). The FHF complex may function to promote vesicle
trafficking and/or fusion via the homotypic vesicular protein
sorting complex (the HOPS complex) (By similarity).
{ECO:0000250|UniProtKB:Q9UJC3, ECO:0000269|PubMed:12075009}.
-!- SUBUNIT: Self-associates (By similarity). Component of the
FTS/Hook/FHIP complex (FHF complex), composed of AKTIP/FTS,
FAM160A2, and one or more members of the Hook family of proteins
HOOK1, HOOK2, and HOOK3 (By similarity). May interact directly
with AKTIP/FTS, HOOK2 and HOOK3 (By similarity). Associates with
several subunits of the homotypic vesicular sorting complex (the
HOPS complex) including VPS16, VPS18, VPS39 and VPS41; these
interactions may be indirect (By similarity). Interacts with
CCDC181 (PubMed:28283191). Interacts (via coiled-coil region) with
RIMBP3 (via C-terminus) (PubMed:19091768). Interacts with LRGUK
(via guanylate kinase-like domain) (PubMed:28003339). Interacts
with microtubules (By similarity). {ECO:0000250|UniProtKB:Q9UJC3,
ECO:0000269|PubMed:19091768, ECO:0000269|PubMed:28003339,
ECO:0000269|PubMed:28283191}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12075009}.
Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12075009,
ECO:0000269|PubMed:28003339}. Note=Localizes to punctate
cytoplasmic foci which do not appear to overlap with early or late
endosomes, the endoplasmic reticulum, multivesicular bodies
(MVBs), lysosomes, or mitochondria (PubMed:12075009). Often found
in close association with microtubules (PubMed:12075009). Does not
associate with the Golgi complex (PubMed:12075009). During
spermiogenesis, it localizes to the manchette in spermatids from
steps 8-10 (PubMed:12075009). It is also present between the
microtubule manchette and the nucleus (PubMed:12075009). During
manchette elongation, it is preferentially localized to the
nuclear ring of the manchette, whereas the strong localization to
the manchette decreases (PubMed:12075009). In more mature
spermatids, while the manchette migrates posteriorly, it localizes
to punctuates spots (PubMed:12075009). At later stages of
spermatid differentiation, the punctuate expression pattern is
found at both the attachment site and the proximal end of the
elongated manchette (PubMed:12075009). In contrast, it is not
present in mature spermatozoa (PubMed:12075009).
{ECO:0000269|PubMed:12075009}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8BIL5-1; Sequence=Displayed;
Name=2; Synonyms=sv;
IsoId=Q8BIL5-2; Sequence=VSP_009340, VSP_009341;
-!- TISSUE SPECIFICITY: Mainly expressed in testis.
{ECO:0000269|PubMed:12075009}.
-!- DISEASE: Note=Defects in Hook1 are the cause of the azh (abnormal
spermatozoon head shape) mutant phenotype, which induces
spermatozoa with highly abnormal head morphology that differs
drastically from the compact and hook-shaped head of the normal
sperm, leading to a strong decrease of fertility.
{ECO:0000269|PubMed:12075009}.
-!- SIMILARITY: Belongs to the hook family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH30877.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AF487912; AAM74055.1; -; mRNA.
EMBL; AK020924; BAB32257.1; -; mRNA.
EMBL; AK043870; BAC31686.1; -; mRNA.
EMBL; AK049897; BAC33977.1; -; mRNA.
EMBL; BC030877; AAH30877.1; ALT_INIT; mRNA.
EMBL; BC061688; AAH61688.1; -; mRNA.
CCDS; CCDS18367.1; -. [Q8BIL5-1]
RefSeq; NP_084290.1; NM_030014.2. [Q8BIL5-1]
UniGene; Mm.49994; -.
PDB; 1WIX; NMR; -; A=12-162.
PDBsum; 1WIX; -.
ProteinModelPortal; Q8BIL5; -.
SMR; Q8BIL5; -.
BioGrid; 219052; 4.
IntAct; Q8BIL5; 2.
STRING; 10090.ENSMUSP00000030306; -.
iPTMnet; Q8BIL5; -.
PhosphoSitePlus; Q8BIL5; -.
EPD; Q8BIL5; -.
PaxDb; Q8BIL5; -.
PeptideAtlas; Q8BIL5; -.
PRIDE; Q8BIL5; -.
Ensembl; ENSMUST00000030306; ENSMUSP00000030306; ENSMUSG00000028572. [Q8BIL5-1]
GeneID; 77963; -.
KEGG; mmu:77963; -.
UCSC; uc008ttb.1; mouse. [Q8BIL5-2]
UCSC; uc008ttc.1; mouse. [Q8BIL5-1]
CTD; 51361; -.
MGI; MGI:1925213; Hook1.
eggNOG; ENOG410IG1M; Eukaryota.
eggNOG; ENOG410XQ3G; LUCA.
GeneTree; ENSGT00690000101702; -.
HOGENOM; HOG000294112; -.
HOVERGEN; HBG051920; -.
InParanoid; Q8BIL5; -.
KO; K16612; -.
OMA; NTMVAKK; -.
OrthoDB; EOG091G06O9; -.
PhylomeDB; Q8BIL5; -.
TreeFam; TF320231; -.
EvolutionaryTrace; Q8BIL5; -.
PRO; PR:Q8BIL5; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000028572; Expressed in 232 organ(s), highest expression level in testis.
CleanEx; MM_HOOK1; -.
ExpressionAtlas; Q8BIL5; baseline and differential.
Genevisible; Q8BIL5; MM.
GO; GO:0005813; C:centrosome; IBA:GO_Central.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IEA:GOC.
GO; GO:0070695; C:FHF complex; ISS:UniProtKB.
GO; GO:0030897; C:HOPS complex; IEA:Ensembl.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
GO; GO:0003779; F:actin binding; IDA:MGI.
GO; GO:0051959; F:dynein light intermediate chain binding; IBA:GO_Central.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0008017; F:microtubule binding; IDA:MGI.
GO; GO:0031122; P:cytoplasmic microtubule organization; IMP:MGI.
GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; IBA:GO_Central.
GO; GO:0045022; P:early endosome to late endosome transport; ISS:UniProtKB.
GO; GO:0007032; P:endosome organization; ISS:UniProtKB.
GO; GO:0008333; P:endosome to lysosome transport; ISS:UniProtKB.
GO; GO:0007030; P:Golgi organization; IMP:MGI.
GO; GO:0007040; P:lysosome organization; ISS:UniProtKB.
GO; GO:1905198; P:manchette assembly; IMP:MGI.
GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0007286; P:spermatid development; IMP:MGI.
Gene3D; 1.10.418.10; -; 1.
InterPro; IPR001715; CH-domain.
InterPro; IPR036872; CH_dom_sf.
InterPro; IPR008636; Hook-like_fam.
Pfam; PF05622; HOOK; 1.
PROSITE; PS50021; CH; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Coiled coil;
Complete proteome; Cytoplasm; Cytoskeleton; Developmental protein;
Differentiation; Direct protein sequencing; Microtubule;
Phosphoprotein; Protein transport; Reference proteome;
Spermatogenesis; Transport.
CHAIN 1 728 Protein Hook homolog 1.
/FTId=PRO_0000219193.
DOMAIN 12 128 Calponin-homology (CH).
{ECO:0000255|PROSITE-ProRule:PRU00044}.
REGION 1 555 Sufficient for interaction with
microtubules. {ECO:0000250}.
REGION 657 728 Sufficient for interaction with AKTIP and
VPS18. {ECO:0000250}.
COILED 168 443 {ECO:0000255}.
COILED 477 658 {ECO:0000255}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:Q9UJC3}.
MOD_RES 235 235 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UJC3}.
MOD_RES 719 719 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UJC3}.
MOD_RES 727 727 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
VAR_SEQ 543 549 SSKLKQK -> VSNRVHN (in isoform 2).
{ECO:0000303|PubMed:12075009,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_009340.
VAR_SEQ 550 728 Missing (in isoform 2).
{ECO:0000303|PubMed:12075009,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_009341.
CONFLICT 185 185 E -> Q (in Ref. 2; BAC31686).
{ECO:0000305}.
CONFLICT 334 334 N -> T (in Ref. 2; BAC33977).
{ECO:0000305}.
HELIX 13 22 {ECO:0000244|PDB:1WIX}.
HELIX 34 37 {ECO:0000244|PDB:1WIX}.
HELIX 41 50 {ECO:0000244|PDB:1WIX}.
TURN 52 54 {ECO:0000244|PDB:1WIX}.
HELIX 57 60 {ECO:0000244|PDB:1WIX}.
HELIX 66 69 {ECO:0000244|PDB:1WIX}.
HELIX 72 90 {ECO:0000244|PDB:1WIX}.
TURN 91 93 {ECO:0000244|PDB:1WIX}.
TURN 99 101 {ECO:0000244|PDB:1WIX}.
HELIX 105 109 {ECO:0000244|PDB:1WIX}.
HELIX 114 127 {ECO:0000244|PDB:1WIX}.
STRAND 130 132 {ECO:0000244|PDB:1WIX}.
HELIX 134 143 {ECO:0000244|PDB:1WIX}.
HELIX 146 162 {ECO:0000244|PDB:1WIX}.
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


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