HIKES_MOUSE
ID HIKES_MOUSE Reviewed; 197 AA.
AC Q9DD02; D3YUY2; Q30C40; Q9CZT7;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Protein Hikeshi {ECO:0000305};
DE AltName: Full=Lethal gene on chromosome 7 Rinchik 6 protein;
GN Name=Hikeshi {ECO:0000312|MGI:MGI:96738};
GN Synonyms=L7rn6 {ECO:0000303|PubMed:16157679};
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] (ISOFORM 1), POSSIBLE FUNCTION, SUBCELLULAR
RP LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=16157679; DOI=10.1534/genetics.105.048736;
RA Fernandez-Valdivia R., Zhang Y., Pai S., Metzker M.L., Schumacher A.;
RT "L7Rn6 encodes a novel protein required for Clara cell function in mouse
RT lung development.";
RL Genetics 172:389-399(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Kidney;
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].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, 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 [6]
RP TISSUE SPECIFICITY.
RX PubMed=26545878; DOI=10.1136/jmedgenet-2015-103232;
RA Edvardson S., Kose S., Jalas C., Fattal-Valevski A., Watanabe A., Ogawa Y.,
RA Mamada H., Fedick A.M., Ben-Shachar S., Treff N.R., Shaag A., Bale S.,
RA Gaertner J., Imamoto N., Elpeleg O.;
RT "Leukoencephalopathy and early death associated with an Ashkenazi-Jewish
RT founder mutation in the Hikeshi gene.";
RL J. Med. Genet. 53:132-137(2016).
CC -!- FUNCTION: Acts as a specific nuclear import carrier for HSP70 proteins
CC following heat-shock stress: acts by mediating the nucleoporin-
CC dependent translocation of ATP-bound HSP70 proteins into the nucleus.
CC HSP70 proteins import is required to protect cells from heat shock
CC damages. Does not translocate ADP-bound HSP70 proteins into the nucleus
CC (By similarity). May also be indirectly required for organization
CC and/or function of the secretory apparatus in Clara cells in lung.
CC {ECO:0000250}.
CC -!- SUBUNIT: Forms an asymmetric homodimer; required for binding and
CC nuclear import of HSP70 proteins. Interacts with ATP-bound HSP70
CC proteins. Interacts with NUP62 and NUP153 (via F-X-F-G repeats).
CC Interacts with HSPA8. {ECO:0000250|UniProtKB:Q53FT3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16157679}.
CC Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q53FT3}. Nucleus
CC {ECO:0000250|UniProtKB:Q53FT3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9DD02-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9DD02-2; Sequence=VSP_043955;
CC -!- TISSUE SPECIFICITY: Expressed in the central white matter of newborn
CC and adult brain, particularly in regions where oligodendrocytes are
CC generated (PubMed:26545878). {ECO:0000269|PubMed:26545878}.
CC -!- DEVELOPMENTAL STAGE: During late gestation, it is expressed in lung
CC epithelial cells, whereas perinatal expression is restricted to the
CC bronchiolar epithelium. {ECO:0000269|PubMed:16157679}.
CC -!- DISRUPTION PHENOTYPE: Mice display severe emphysematous enlargement of
CC the distal respiratory sacs at birth. Clara cell display enlargement
CC and disorganization of the Golgi complex and formation of aberrant
CC vesicular structures. {ECO:0000269|PubMed:16157679}.
CC -!- SIMILARITY: Belongs to the OPI10 family. {ECO:0000305}.
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DR EMBL; DQ196315; ABA26460.1; -; mRNA.
DR EMBL; DQ196316; ABA26461.1; -; mRNA.
DR EMBL; AK002306; BAB22001.1; -; mRNA.
DR EMBL; AK012166; BAB28072.1; -; mRNA.
DR EMBL; AC161229; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC165077; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003916; AAH03916.1; -; mRNA.
DR CCDS; CCDS21445.1; -. [Q9DD02-1]
DR CCDS; CCDS80748.1; -. [Q9DD02-2]
DR RefSeq; NP_001278215.1; NM_001291286.1.
DR RefSeq; NP_001278216.1; NM_001291287.1. [Q9DD02-2]
DR RefSeq; NP_080580.1; NM_026304.3. [Q9DD02-1]
DR RefSeq; XP_006508195.1; XM_006508132.3. [Q9DD02-2]
DR AlphaFoldDB; Q9DD02; -.
DR SMR; Q9DD02; -.
DR BioGRID; 212353; 6.
DR STRING; 10090.ENSMUSP00000119806; -.
DR iPTMnet; Q9DD02; -.
DR PhosphoSitePlus; Q9DD02; -.
DR EPD; Q9DD02; -.
DR MaxQB; Q9DD02; -.
DR PaxDb; Q9DD02; -.
DR PeptideAtlas; Q9DD02; -.
DR PRIDE; Q9DD02; -.
DR ProteomicsDB; 273109; -. [Q9DD02-1]
DR ProteomicsDB; 273110; -. [Q9DD02-2]
DR Antibodypedia; 31443; 175 antibodies from 25 providers.
DR Ensembl; ENSMUST00000075010; ENSMUSP00000102856; ENSMUSG00000062797. [Q9DD02-2]
DR Ensembl; ENSMUST00000153470; ENSMUSP00000119806; ENSMUSG00000062797. [Q9DD02-1]
DR GeneID; 67669; -.
DR KEGG; mmu:67669; -.
DR UCSC; uc009igh.2; mouse. [Q9DD02-1]
DR CTD; 51501; -.
DR MGI; MGI:96738; Hikeshi.
DR VEuPathDB; HostDB:ENSMUSG00000062797; -.
DR eggNOG; KOG4067; Eukaryota.
DR GeneTree; ENSGT00390000004056; -.
DR HOGENOM; CLU_084839_2_0_1; -.
DR InParanoid; Q9DD02; -.
DR OMA; RMEQNPN; -.
DR OrthoDB; 1223488at2759; -.
DR PhylomeDB; Q9DD02; -.
DR TreeFam; TF313222; -.
DR Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
DR BioGRID-ORCS; 67669; 8 hits in 73 CRISPR screens.
DR PRO; PR:Q9DD02; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9DD02; protein.
DR Bgee; ENSMUSG00000062797; Expressed in medial ganglionic eminence and 261 other tissues.
DR ExpressionAtlas; Q9DD02; baseline and differential.
DR Genevisible; Q9DD02; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0030544; F:Hsp70 protein binding; ISS:UniProtKB.
DR GO; GO:0061608; F:nuclear import signal receptor activity; ISO:MGI.
DR GO; GO:0034605; P:cellular response to heat; ISS:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; IMP:MGI.
DR GO; GO:0030324; P:lung development; IMP:MGI.
DR GO; GO:0006606; P:protein import into nucleus; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; ISS:UniProtKB.
DR InterPro; IPR008493; DUF775.
DR InterPro; IPR031318; OPI10.
DR PANTHER; PTHR12925; PTHR12925; 1.
DR Pfam; PF05603; DUF775; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Nucleus; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..197
FT /note="Protein Hikeshi"
FT /id="PRO_0000245263"
FT REGION 18..55
FT /note="Required for F-X-F-G repeats-nucleoporins
FT recognition and nuclear import"
FT /evidence="ECO:0000250|UniProtKB:Q53FT3"
FT REGION 124..134
FT /note="Flexible linker region involved in nuclear import of
FT HSP70 proteins"
FT /evidence="ECO:0000250|UniProtKB:Q53FT3"
FT VAR_SEQ 1..39
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_043955"
FT CONFLICT 125
FT /note="T -> A (in Ref. 2; BAB28072)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 197 AA; 21619 MW; 69C2CF45B6EC8A2B CRC64;
MFGCLVAGRL VQTAAQQVAE DKFVFDLPDY ENINHVVVFM LGTIPFPEGM GGSVYFSYPD
SNGVPVWQLL GFVTNGKPSA IFKISGLKSG EGSQHPFGAM NIVRTPSVAQ IGISVELLDS
LAQQTPVGSA AVSSVDSFTQ FTQKMLDNFY NFASSFALSQ AQMTPNPSEM FIPANVVLKW
YENFQRRLAQ NPLFWKT
