ID   HIKES_HUMAN             Reviewed;         197 AA.
AC   Q53FT3; Q8WVE8; Q9NVQ2; Q9NZZ1; Q9P022; Q9P0N1;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 2.
DT   11-NOV-2015, entry version 87.
DE   RecName: Full=Protein Hikeshi;
GN   Name=C11orf73; ORFNames=HSPC138, HSPC179, HSPC248;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Umbilical cord blood;
RX   PubMed=11042152; DOI=10.1101/gr.140200;
RA   Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA   Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA   Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT   "Cloning and functional analysis of cDNAs with open reading frames for
RT   300 previously undefined genes expressed in CD34+ hematopoietic
RT   stem/progenitor cells.";
RL   Genome Res. 10:1546-1560(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Teratocarcinoma;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney proximal tubule;
RA   Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA   Tanaka A., Yokoyama S.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-47.
RC   TISSUE=Brain, and Lung;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [6]
RP   FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION,
RP   INTERACTION WITH NUP62; NUP153 AND HSP70 PROTEINS, AND INDUCTION.
RX   PubMed=22541429; DOI=10.1016/j.cell.2012.02.058;
RA   Kose S., Furuta M., Imamoto N.;
RT   "Hikeshi, a nuclear import carrier for hsp70s, protects cells from
RT   heat shock-induced nuclear damage.";
RL   Cell 149:578-589(2012).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA   Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA   Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-
RT   terminal acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- FUNCTION: Acts as a specific nuclear import carrier for HSP70
CC       proteins following heat-shock stress: acts by mediating the
CC       nucleoporin-dependent translocation of ATP-bound HSP70 proteins
CC       into the nucleus. HSP70 proteins import is required to protect
CC       cells from heat shock damages. Does not translocate ADP-bound
CC       HSP70 proteins into the nucleus. {ECO:0000269|PubMed:22541429}.
CC   -!- SUBUNIT: Interacts with ATP-bound HSP70 proteins. Interacts with
CC       NUP62 and NUP153 (via F-X-F-G repeats).
CC       {ECO:0000269|PubMed:22541429}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000269|PubMed:22541429}. Nucleus
CC       {ECO:0000269|PubMed:22541429}.
CC   -!- INDUCTION: Following heat-shock treatment.
CC       {ECO:0000269|PubMed:22541429}.
CC   -!- MISCELLANEOUS: 'Hikeshi' is a traditional Japanese compound word
CC       used for a firefighter, smokejumper, or troubleshooter.
CC       {ECO:0000305|PubMed:22541429}.
CC   -!- SIMILARITY: Belongs to the OPI10 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF29102.1; Type=Frameshift; Positions=62, 68; Evidence={ECO:0000305};
CC       Sequence=AAF29142.1; Type=Frameshift; Positions=9, 57; Evidence={ECO:0000305};
CC       Sequence=AAF36168.1; Type=Frameshift; Positions=67; Evidence={ECO:0000305};
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DR   EMBL; AF151082; AAF36168.1; ALT_FRAME; mRNA.
DR   EMBL; AF161487; AAF29102.1; ALT_FRAME; mRNA.
DR   EMBL; AF161527; AAF29142.1; ALT_FRAME; mRNA.
DR   EMBL; AK001447; BAA91698.1; -; mRNA.
DR   EMBL; AK223198; BAD96918.1; -; mRNA.
DR   EMBL; BC001677; AAH01677.1; -; mRNA.
DR   EMBL; BC006476; AAH06476.1; -; mRNA.
DR   EMBL; BC015991; AAH15991.1; -; mRNA.
DR   EMBL; BC018080; AAH18080.1; -; mRNA.
DR   EMBL; BC021621; AAH21621.1; -; mRNA.
DR   CCDS; CCDS8275.1; -.
DR   RefSeq; NP_057485.2; NM_016401.3.
DR   UniGene; Hs.283322; -.
DR   PDB; 3WVZ; X-ray; 1.88 A; A/B=1-197.
DR   PDB; 3WW0; X-ray; 2.50 A; A/B=1-197.
DR   PDBsum; 3WVZ; -.
DR   PDBsum; 3WW0; -.
DR   ProteinModelPortal; Q53FT3; -.
DR   SMR; Q53FT3; 1-195.
DR   BioGrid; 119574; 8.
DR   IntAct; Q53FT3; 5.
DR   MINT; MINT-3047121; -.
DR   STRING; 9606.ENSP00000278483; -.
DR   BioMuta; C11orf73; -.
DR   DMDM; 110278911; -.
DR   MaxQB; Q53FT3; -.
DR   PaxDb; Q53FT3; -.
DR   PRIDE; Q53FT3; -.
DR   DNASU; 51501; -.
DR   Ensembl; ENST00000278483; ENSP00000278483; ENSG00000149196.
DR   GeneID; 51501; -.
DR   KEGG; hsa:51501; -.
DR   UCSC; uc001pbu.3; human.
DR   CTD; 51501; -.
DR   GeneCards; C11orf73; -.
DR   HGNC; HGNC:26938; C11orf73.
DR   HPA; HPA035063; -.
DR   HPA; HPA035064; -.
DR   MIM; 614908; gene.
DR   neXtProt; NX_Q53FT3; -.
DR   PharmGKB; PA144596492; -.
DR   eggNOG; KOG4067; Eukaryota.
DR   eggNOG; ENOG4111H6N; LUCA.
DR   GeneTree; ENSGT00390000004056; -.
DR   HOGENOM; HOG000175561; -.
DR   HOVERGEN; HBG081226; -.
DR   InParanoid; Q53FT3; -.
DR   OMA; QFGQRML; -.
DR   PhylomeDB; Q53FT3; -.
DR   TreeFam; TF313222; -.
DR   Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
DR   ChiTaRS; C11orf73; human.
DR   GeneWiki; C11orf73; -.
DR   GenomeRNAi; 51501; -.
DR   NextBio; 55179; -.
DR   PRO; PR:Q53FT3; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   Bgee; Q53FT3; -.
DR   CleanEx; HS_C11orf73; -.
DR   ExpressionAtlas; Q53FT3; baseline and differential.
DR   Genevisible; Q53FT3; HS.
DR   GO; GO:0030054; C:cell junction; IDA:HPA.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR   GO; GO:0005622; C:intracellular; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0030544; F:Hsp70 protein binding; IDA:UniProtKB.
DR   GO; GO:0008565; F:protein transporter activity; IDA:UniProtKB.
DR   GO; GO:0034605; P:cellular response to heat; IDA:UniProtKB.
DR   GO; GO:0007030; P:Golgi organization; IEA:Ensembl.
DR   GO; GO:0030324; P:lung development; IEA:Ensembl.
DR   GO; GO:0006606; P:protein import into nucleus; IDA:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IDA:UniProtKB.
DR   GO; GO:1900034; P:regulation of cellular response to heat; TAS:Reactome.
DR   InterPro; IPR008493; DUF775.
DR   InterPro; IPR031318; OPI10.
DR   PANTHER; PTHR12925:SF0; PTHR12925:SF0; 1.
DR   Pfam; PF05603; DUF775; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Cytoplasm; Nucleus; Polymorphism;
KW   Protein transport; Reference proteome; Transport.
FT   CHAIN         1    197       Protein Hikeshi.
FT                                /FTId=PRO_0000245262.
FT   VARIANT      47     47       P -> A (in dbSNP:rs11539213).
FT                                {ECO:0000269|PubMed:15489334}.
FT                                /FTId=VAR_026968.
FT   CONFLICT     82     82       F -> L (in Ref. 1; AAF29102 and 3;
FT                                BAD96918). {ECO:0000305}.
FT   STRAND        2      6       {ECO:0000244|PDB:3WVZ}.
FT   STRAND       16     19       {ECO:0000244|PDB:3WVZ}.
FT   STRAND       22     29       {ECO:0000244|PDB:3WVZ}.
FT   HELIX        30     32       {ECO:0000244|PDB:3WVZ}.
FT   STRAND       34     40       {ECO:0000244|PDB:3WVZ}.
FT   STRAND       42     44       {ECO:0000244|PDB:3WVZ}.
FT   STRAND       50     57       {ECO:0000244|PDB:3WVZ}.
FT   STRAND       68     73       {ECO:0000244|PDB:3WVZ}.
FT   STRAND       75     77       {ECO:0000244|PDB:3WVZ}.
FT   STRAND       79     83       {ECO:0000244|PDB:3WVZ}.
FT   STRAND      108    117       {ECO:0000244|PDB:3WVZ}.
FT   HELIX       118    121       {ECO:0000244|PDB:3WVZ}.
FT   HELIX       137    154       {ECO:0000244|PDB:3WVZ}.
FT   HELIX       160    162       {ECO:0000244|PDB:3WVZ}.
FT   STRAND      171    173       {ECO:0000244|PDB:3WVZ}.
FT   HELIX       174    188       {ECO:0000244|PDB:3WVZ}.
FT   TURN        192    195       {ECO:0000244|PDB:3WW0}.
SQ   SEQUENCE   197 AA;  21628 MW;  4FA524439B630511 CRC64;
     MFGCLVAGRL VQTAAQQVAE DKFVFDLPDY ESINHVVVFM LGTIPFPEGM GGSVYFSYPD
     SNGMPVWQLL GFVTNGKPSA IFKISGLKSG EGSQHPFGAM NIVRTPSVAQ IGISVELLDS
     MAQQTPVGNA AVSSVDSFTQ FTQKMLDNFY NFASSFAVSQ AQMTPSPSEM FIPANVVLKW
     YENFQRRLAQ NPLFWKT
//