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Hsc70-interacting protein 2 (HIP-replacement)

 F10A2_DROME             Reviewed;         377 AA.
Q86DS1; C0L9I4; C0L9I8; Q86DR2; Q86DR3; Q86DR4; Q86DR5; Q86DR6;
Q86DR7; Q86DR8; Q86DR9; Q86DS0; Q86DS2; Q86DS3; Q8IRT4;
20-APR-2010, integrated into UniProtKB/Swiss-Prot.
20-APR-2010, sequence version 2.
12-SEP-2018, entry version 103.
RecName: Full=Hsc70-interacting protein 2 {ECO:0000250|UniProtKB:P50503, ECO:0000312|EMBL:AAP31294.1};
AltName: Full=HIP-replacement {ECO:0000303|PubMed:19333534};
Name=HIP-R {ECO:0000303|PubMed:19333534}; ORFNames=CG2947;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1] {ECO:0000305, ECO:0000312|EMBL:ACN78890.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ASN-105 AND ALA-290.
STRAIN=XCPA112 {ECO:0000312|EMBL:ACN78895.1},
XCPA126 {ECO:0000312|EMBL:ACN78892.1},
XCPA25 {ECO:0000312|EMBL:ACN78889.1},
XCPA42 {ECO:0000312|EMBL:ACN78890.1},
XCPA53 {ECO:0000312|EMBL:ACN78891.1},
XCPA69 {ECO:0000312|EMBL:ACN78893.1},
XCPA77 {ECO:0000312|EMBL:ACN78894.1}, and
XCPA93 {ECO:0000312|EMBL:ACN78896.1};
PubMed=19333534; DOI=10.1007/s00239-009-9213-x;
Hogan C.C., Bettencourt B.R.;
"Duplicate gene evolution toward multiple fates at the Drosophila
melanogaster HIP/HIP-Replacement locus.";
J. Mol. Evol. 68:337-350(2009).
[2] {ECO:0000312|EMBL:AAN09105.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3] {ECO:0000305, ECO:0000312|EMBL:AAN09105.1}
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4] {ECO:0000312|EMBL:AAK93422.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley {ECO:0000312|EMBL:AAK93422.1};
TISSUE=Embryo {ECO:0000269|PubMed:12537569};
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[5] {ECO:0000305, ECO:0000312|EMBL:AAP31294.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 8-370, AND VARIANTS ASN-105 AND
ALA-290.
STRAIN=Canton-S {ECO:0000312|EMBL:AAP31293.1},
Oregon-R {ECO:0000312|EMBL:AAP31292.1},
XCPA102 {ECO:0000312|EMBL:AAP31300.1},
XCPA105 {ECO:0000312|EMBL:AAP31303.1},
XCPA112 {ECO:0000312|EMBL:AAP31301.1},
XCPA118 {ECO:0000312|EMBL:AAP31299.1},
XCPA122 {ECO:0000312|EMBL:AAP31297.1},
XCPA125 {ECO:0000312|EMBL:AAP31298.1},
XCPA4 {ECO:0000312|EMBL:AAP31296.1},
XCPA51 {ECO:0000312|EMBL:AAP31295.1},
XCPA7 {ECO:0000312|EMBL:AAP31294.1}, and
XCPA77 {ECO:0000312|EMBL:AAP31302.1};
Bettencourt B.R., Lerman D.N., Feder M.E.;
"Escaping gene conversion: Adaptive molecular evolution of Hsp70
trans-regulators.";
Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
[6] {ECO:0000305}
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80, AND IDENTIFICATION
BY MASS SPECTROMETRY.
PubMed=17372656; DOI=10.1039/b617545g;
Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D.,
Juenger M.A., Eng J.K., Aebersold R., Tao W.A.;
"An integrated chemical, mass spectrometric and computational strategy
for (quantitative) phosphoproteomics: application to Drosophila
melanogaster Kc167 cells.";
Mol. Biosyst. 3:275-286(2007).
-!- FUNCTION: One HIP oligomer binds the ATPase domains of at least
two Hsc70 molecules dependent on activation of the Hsc70 ATPase by
Hsp40. Stabilizes the ADP state of Hsc70 that has a high affinity
for substrate protein. Through its own chaperone activity, it may
contribute to the interaction of Hsc70 with various target
proteins (By similarity). {ECO:0000250|UniProtKB:P50503}.
-!- SUBUNIT: Homotetramer. Interacts with Hsc70 as well as DNAJ
homologs and Hsp90 (By similarity).
{ECO:0000250|UniProtKB:P50503}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P50503}.
-!- SIMILARITY: Belongs to the FAM10 family. {ECO:0000255}.
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EMBL; FJ686062; ACN78889.1; -; Genomic_DNA.
EMBL; FJ686063; ACN78890.1; -; Genomic_DNA.
EMBL; FJ686064; ACN78891.1; -; Genomic_DNA.
EMBL; FJ686065; ACN78892.1; -; Genomic_DNA.
EMBL; FJ686066; ACN78893.1; -; Genomic_DNA.
EMBL; FJ686067; ACN78894.1; -; Genomic_DNA.
EMBL; FJ686068; ACN78895.1; -; Genomic_DNA.
EMBL; FJ686069; ACN78896.1; -; Genomic_DNA.
EMBL; AE014298; AAN09105.1; -; Genomic_DNA.
EMBL; AY051998; AAK93422.1; -; mRNA.
EMBL; AY274369; AAP31292.1; -; Genomic_DNA.
EMBL; AY274370; AAP31293.1; -; Genomic_DNA.
EMBL; AY274371; AAP31294.1; -; Genomic_DNA.
EMBL; AY274372; AAP31295.1; -; Genomic_DNA.
EMBL; AY274373; AAP31296.1; -; Genomic_DNA.
EMBL; AY274374; AAP31297.1; -; Genomic_DNA.
EMBL; AY274375; AAP31298.1; -; Genomic_DNA.
EMBL; AY274376; AAP31299.1; -; Genomic_DNA.
EMBL; AY274377; AAP31300.1; -; Genomic_DNA.
EMBL; AY274378; AAP31301.1; -; Genomic_DNA.
EMBL; AY274379; AAP31302.1; -; Genomic_DNA.
EMBL; AY274380; AAP31303.1; -; Genomic_DNA.
RefSeq; NP_001014719.2; NM_001014719.2.
RefSeq; NP_570074.3; NM_130718.5.
RefSeq; NP_726885.1; NM_166988.4.
RefSeq; NP_726886.1; NM_166989.5.
UniGene; Dm.33464; -.
ProteinModelPortal; Q86DS1; -.
SMR; Q86DS1; -.
BioGrid; 57855; 50.
BioGrid; 76808; 1.
IntAct; Q86DS1; 2.
iPTMnet; Q86DS1; -.
PRIDE; Q86DS1; -.
EnsemblMetazoa; FBtr0070597; FBpp0070572; FBgn0029676.
EnsemblMetazoa; FBtr0070598; FBpp0070573; FBgn0029676.
EnsemblMetazoa; FBtr0070600; FBpp0070575; FBgn0260484.
EnsemblMetazoa; FBtr0333764; FBpp0305905; FBgn0029676.
GeneID; 31335; -.
GeneID; 318211; -.
KEGG; dme:Dmel_CG2947; -.
KEGG; dme:Dmel_CG32789; -.
UCSC; CG2947-RA; d. melanogaster.
CTD; 31335; -.
CTD; 318211; -.
FlyBase; FBgn0029676; HIP-R.
eggNOG; ENOG410IN5Q; Eukaryota.
eggNOG; COG0457; LUCA.
GeneTree; ENSGT00390000001347; -.
InParanoid; Q86DS1; -.
KO; K09560; -.
OrthoDB; EOG091G0KXF; -.
PhylomeDB; Q86DS1; -.
Reactome; R-DME-3371453; Regulation of HSF1-mediated heat shock response.
PRO; PR:Q86DS1; -.
Proteomes; UP000000803; Chromosome X.
Bgee; FBgn0029676; Expressed in 4 organ(s), highest expression level in larva.
ExpressionAtlas; Q86DS1; baseline and differential.
Genevisible; Q86DS1; DM.
GO; GO:0005829; C:cytosol; ISS:FlyBase.
GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
GO; GO:0051087; F:chaperone binding; ISS:FlyBase.
GO; GO:0031072; F:heat shock protein binding; ISS:FlyBase.
GO; GO:0030544; F:Hsp70 protein binding; ISS:UniProtKB.
GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; ISS:UniProtKB.
CDD; cd14438; Hip_N; 1.
Gene3D; 1.25.40.10; -; 1.
InterPro; IPR034649; Hip_N.
InterPro; IPR006636; STI1_HS-bd.
InterPro; IPR013026; TPR-contain_dom.
InterPro; IPR011990; TPR-like_helical_dom_sf.
InterPro; IPR019734; TPR_repeat.
SMART; SM00727; STI1; 1.
SMART; SM00028; TPR; 3.
SUPFAM; SSF48452; SSF48452; 1.
PROSITE; PS50005; TPR; 2.
PROSITE; PS50293; TPR_REGION; 1.
1: Evidence at protein level;
Coiled coil; Complete proteome; Cytoplasm; Phosphoprotein;
Reference proteome; Repeat; TPR repeat.
CHAIN 1 377 Hsc70-interacting protein 2.
/FTId=PRO_0000393585.
REPEAT 126 159 TPR 1. {ECO:0000255}.
REPEAT 161 193 TPR 2. {ECO:0000255}.
REPEAT 195 227 TPR 3. {ECO:0000255}.
DOMAIN 294 336 STI1. {ECO:0000255}.
COILED 239 276 {ECO:0000255}.
MOD_RES 80 80 Phosphoserine.
{ECO:0000269|PubMed:17372656}.
VARIANT 105 105 S -> N (in strain: XCPA69 and XCPA112).
{ECO:0000269|PubMed:19333534,
ECO:0000269|Ref.5}.
VARIANT 290 290 G -> A (in strain: XCPA4, XCPA7, XCPA25,
XCPA51, XCPA77, XCPA93, XCPA102, XCPA105,
XCPA122 and XCPA125).
{ECO:0000269|PubMed:19333534,
ECO:0000269|Ref.5}.
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


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