F10A1_DROME
ID F10A1_DROME Reviewed; 377 AA.
AC C4NYP8; C0L9I4; C0L9I8; C9QP24; Q8IRT4;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 2.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Hsc70-interacting protein 1 {ECO:0000303|PubMed:19333534};
GN Name=HIP {ECO:0000303|PubMed:19333534}; ORFNames=CG32789;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ACQ66626.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ASN-105; ASP-227 AND
RP ALA-290.
RC STRAIN=XCPA112 {ECO:0000312|EMBL:ACQ66628.1},
RC XCPA126 {ECO:0000312|EMBL:ACQ66630.1},
RC XCPA25 {ECO:0000312|EMBL:ACQ66626.1}, XCPA77 {ECO:0000312|EMBL:ACQ66629.1},
RC and XCPA93 {ECO:0000312|EMBL:ACQ66627.1};
RX PubMed=19333534; DOI=10.1007/s00239-009-9213-x;
RA Hogan C.C., Bettencourt B.R.;
RT "Duplicate gene evolution toward multiple fates at the Drosophila
RT melanogaster HIP/HIP-Replacement locus.";
RL J. Mol. Evol. 68:337-350(2009).
RN [2] {ECO:0000312|EMBL:AAN09108.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAN09108.2}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4] {ECO:0000312|EMBL:ACX32977.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:ACX32977.1}; TISSUE=Embryo;
RA Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
CC -!- FUNCTION: One HIP oligomer binds the ATPase domains of at least two
CC Hsc70 molecules dependent on activation of the Hsc70 ATPase by Hsp40.
CC Stabilizes the ADP state of Hsc70 that has a high affinity for
CC substrate protein. Through its own chaperone activity, it may
CC contribute to the interaction of Hsc70 with various target proteins (By
CC similarity). {ECO:0000250|UniProtKB:P50503}.
CC -!- SUBUNIT: Homotetramer. Interacts with Hsc70 as well as DNAJ homologs
CC and Hsp90 (By similarity). {ECO:0000250|UniProtKB:P50503}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P50503}.
CC -!- SIMILARITY: Belongs to the FAM10 family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ACX32977.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; FJ686088; ACQ66626.1; -; Genomic_DNA.
DR EMBL; FJ686092; ACQ66627.1; -; Genomic_DNA.
DR EMBL; FJ686093; ACQ66628.1; -; Genomic_DNA.
DR EMBL; FJ686094; ACQ66629.1; -; Genomic_DNA.
DR EMBL; FJ686095; ACQ66630.1; -; Genomic_DNA.
DR EMBL; AE014298; AAN09108.2; -; Genomic_DNA.
DR EMBL; BT099906; ACX32977.1; ALT_INIT; mRNA.
DR RefSeq; NP_001014719.2; NM_001014719.2.
DR RefSeq; NP_570074.3; NM_130718.5.
DR RefSeq; NP_726885.1; NM_166988.4.
DR RefSeq; NP_726886.1; NM_166989.5.
DR AlphaFoldDB; C4NYP8; -.
DR SMR; C4NYP8; -.
DR BioGRID; 57855; 50.
DR BioGRID; 76808; 1.
DR STRING; 7227.FBpp0070573; -.
DR iPTMnet; C4NYP8; -.
DR PaxDb; C4NYP8; -.
DR PRIDE; C4NYP8; -.
DR DNASU; 31335; -.
DR DNASU; 318211; -.
DR EnsemblMetazoa; FBtr0070597; FBpp0070572; FBgn0029676.
DR EnsemblMetazoa; FBtr0070598; FBpp0070573; FBgn0029676.
DR EnsemblMetazoa; FBtr0070600; FBpp0070575; FBgn0260484.
DR EnsemblMetazoa; FBtr0333764; FBpp0305905; FBgn0029676.
DR GeneID; 31335; -.
DR GeneID; 318211; -.
DR KEGG; dme:Dmel_CG2947; -.
DR KEGG; dme:Dmel_CG32789; -.
DR CTD; 31335; -.
DR CTD; 318211; -.
DR FlyBase; FBgn0260484; HIP.
DR VEuPathDB; VectorBase:FBgn0029676; -.
DR VEuPathDB; VectorBase:FBgn0260484; -.
DR eggNOG; KOG1308; Eukaryota.
DR HOGENOM; CLU_026202_0_1_1; -.
DR InParanoid; C4NYP8; -.
DR OMA; HPRKYER; -.
DR OrthoDB; 1282821at2759; -.
DR PhylomeDB; C4NYP8; -.
DR Reactome; R-DME-3371453; Regulation of HSF1-mediated heat shock response.
DR PRO; PR:C4NYP8; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0029676; Expressed in imaginal disc and 11 other tissues.
DR ExpressionAtlas; C4NYP8; baseline and differential.
DR Genevisible; C4NYP8; DM.
DR GO; GO:0005737; C:cytoplasm; HDA:FlyBase.
DR GO; GO:0005829; C:cytosol; ISS:FlyBase.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0051087; F:chaperone binding; ISS:FlyBase.
DR GO; GO:0031072; F:heat shock protein binding; ISS:FlyBase.
DR GO; GO:0030544; F:Hsp70 protein binding; ISS:UniProtKB.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; ISS:UniProtKB.
DR CDD; cd14438; Hip_N; 1.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR034649; Hip_N.
DR InterPro; IPR006636; STI1_HS-bd.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF18253; HipN; 1.
DR SMART; SM00727; STI1; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 2.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Phosphoprotein; Reference proteome; Repeat;
KW TPR repeat.
FT CHAIN 1..377
FT /note="Hsc70-interacting protein 1"
FT /id="PRO_0000393584"
FT REPEAT 126..159
FT /note="TPR 1"
FT /evidence="ECO:0000255"
FT REPEAT 161..193
FT /note="TPR 2"
FT /evidence="ECO:0000255"
FT REPEAT 195..227
FT /note="TPR 3"
FT /evidence="ECO:0000255"
FT DOMAIN 294..336
FT /note="STI1"
FT /evidence="ECO:0000255"
FT REGION 68..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 239..276
FT /evidence="ECO:0000255"
FT COMPBIAS 83..101
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..377
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT VARIANT 105
FT /note="S -> N (in strain: XCPA112)"
FT /evidence="ECO:0000269|PubMed:19333534"
FT VARIANT 227
FT /note="E -> D (in strain: XCPA25)"
FT /evidence="ECO:0000269|PubMed:19333534"
FT VARIANT 290
FT /note="G -> A (in strain: XCPA77, XCPA93 and XCPA126)"
FT /evidence="ECO:0000269|PubMed:19333534"
SQ SEQUENCE 377 AA; 41037 MW; D62D41198348A786 CRC64;
MAFTMQTGDL KKLKYFIDFA LENPTFLNMP QLQFVKDFVE KFGGTVPPGQ FNGGSAGGKC
PFGGVAGAKA NEPANAPEDS EDEKSLSDPE SDVELDMEGV IEADSDPAQP MGNYSKKATE
EEVEQASELR AQAASAYGQQ KFDEAIALYT KAIELSPGNA LFHAKRGQAF LKLKKPNACI
RDCDVALELN SDLAAGYKFR GRARRLLGDF ELAAHDLRQA CKLDFDEETD EWLKEVTPNA
KKIEQHRLKQ ERRQAERKIK ERQRDQRRAR KEQEKHNASS GGSSGEFSGG NPGNGNMSDI
LGAMSDPEVS AAIQDILSNP GNITKYASNP KIYNLIKKIV PGGDVGAAFG QAGEKAGKPS
EPKPKKDSAD FVDDGLD
