STIP1_CAEEL
ID STIP1_CAEEL Reviewed; 320 AA.
AC O16259;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Stress-induced-phosphoprotein 1 {ECO:0000303|PubMed:19467242, ECO:0000312|EMBL:CCD63252.1};
DE Short=CeSTI1 {ECO:0000303|PubMed:19467242};
DE Short=STI1 {ECO:0000303|PubMed:19467242};
DE AltName: Full=Hsc70/Hsp90-organizing protein {ECO:0000303|PubMed:19559711};
DE Short=CeHop {ECO:0000303|PubMed:19559711};
DE Short=Hop {ECO:0000303|PubMed:19559711};
GN Name=sti-1 {ECO:0000312|EMBL:CCD63252.1, ECO:0000312|WormBase:R09E12.3};
GN ORFNames=R09E12.3;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000312|EMBL:CCD63252.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CCD63252.1};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH HSP-1 AND
RP DAF-21, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19467242; DOI=10.1016/j.jmb.2009.05.035;
RA Song H.O., Lee W., An K., Lee H.S., Cho J.H., Park Z.Y., Ahnn J.;
RT "C. elegans STI-1, the homolog of Sti1/Hop, is involved in aging and stress
RT response.";
RL J. Mol. Biol. 390:604-617(2009).
RN [3] {ECO:0000305}
RP FUNCTION, INTERACTION WITH HSP-1 AND DAF-21, TISSUE SPECIFICITY, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=19559711; DOI=10.1016/j.jmb.2009.06.051;
RA Gaiser A.M., Brandt F., Richter K.;
RT "The non-canonical Hop protein from Caenorhabditis elegans exerts essential
RT functions and forms binary complexes with either Hsc70 or Hsp90.";
RL J. Mol. Biol. 391:621-634(2009).
RN [4] {ECO:0000312|PDB:4GCN}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 1-124 AND 131-253.
RG Midwest center for structural genomics (MCSG);
RL Submitted (JUL-2012) to the PDB data bank.
CC -!- FUNCTION: Plays a role in gonad development. Up-regulates longevity and
CC thermotolerance. Binds daf-21/hsp90 and inhibits its ATPase activity.
CC {ECO:0000269|PubMed:19467242, ECO:0000269|PubMed:19559711}.
CC -!- SUBUNIT: Forms a complex with hsp-1/hsp70 and daf-21/hsp90. Interacts
CC with daf-21/hsp90 (via the C-terminal MEEVD pentapeptide).
CC {ECO:0000269|PubMed:19467242, ECO:0000269|PubMed:19559711}.
CC -!- INTERACTION:
CC O16259; Q18688: daf-21; NbExp=3; IntAct=EBI-6514174, EBI-313329;
CC O16259; P09446: hsp-1; NbExp=3; IntAct=EBI-6514174, EBI-322448;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19467242}.
CC Note=Detected in cytoplasm in early-stage embryos.
CC {ECO:0000269|PubMed:19467242}.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously in the whole body. Detected
CC predominantly in the pharyngeal muscles, vulva epithelial cells,
CC striated body-wall muscles, spermathecae and intestinal cell ring. Also
CC observed in the tail regions of hermaphrodite and in the sensory rays
CC and spicules of males. {ECO:0000269|PubMed:19467242,
CC ECO:0000269|PubMed:19559711}.
CC -!- DEVELOPMENTAL STAGE: Expressed at all developmental stages.
CC {ECO:0000269|PubMed:19467242}.
CC -!- INDUCTION: Up-regulated by heat stress (at protein level).
CC {ECO:0000269|PubMed:19467242}.
CC -!- DISRUPTION PHENOTYPE: Reduced brood size and decreased fertility under
CC heat stress. Decreased thermotolerance and shortening of life span by
CC 68% and 77% at 20 degrees Celsius and 25 degrees Celsius respectively.
CC Growth of gonads is hampered resulting in shortened arms of the gonads,
CC abnormally shaped spermathecae, lower sperm number and endomitotic
CC oocyte development. {ECO:0000269|PubMed:19467242,
CC ECO:0000269|PubMed:19559711}.
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DR EMBL; FO080369; CCD63252.1; -; Genomic_DNA.
DR PIR; T03899; T03899.
DR RefSeq; NP_503322.1; NM_070921.6.
DR PDB; 4GCN; X-ray; 1.85 A; A/B=1-124.
DR PDB; 4GCO; X-ray; 1.60 A; A=131-253.
DR PDBsum; 4GCN; -.
DR PDBsum; 4GCO; -.
DR AlphaFoldDB; O16259; -.
DR SMR; O16259; -.
DR BioGRID; 43661; 22.
DR ComplexPortal; CPX-4003; Hsp90-sti-1 chaperone complex.
DR IntAct; O16259; 22.
DR STRING; 6239.R09E12.3; -.
DR EPD; O16259; -.
DR PaxDb; O16259; -.
DR PeptideAtlas; O16259; -.
DR EnsemblMetazoa; R09E12.3.1; R09E12.3.1; WBGene00019983.
DR UCSC; R09E12.3; c. elegans.
DR WormBase; R09E12.3; CE12646; WBGene00019983; sti-1.
DR eggNOG; KOG0548; Eukaryota.
DR GeneTree; ENSGT00940000170181; -.
DR HOGENOM; CLU_000134_46_1_1; -.
DR InParanoid; O16259; -.
DR OMA; KRWECLP; -.
DR OrthoDB; 933764at2759; -.
DR PhylomeDB; O16259; -.
DR PRO; PR:O16259; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00019983; Expressed in pharyngeal muscle cell (C elegans) and 5 other tissues.
DR GO; GO:0101031; C:chaperone complex; IPI:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0042030; F:ATPase inhibitor activity; IDA:WormBase.
DR GO; GO:0030544; F:Hsp70 protein binding; IPI:WormBase.
DR GO; GO:0051879; F:Hsp90 protein binding; IPI:WormBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:WormBase.
DR GO; GO:0032780; P:negative regulation of ATP-dependent activity; IDA:WormBase.
DR GO; GO:0022417; P:protein maturation by protein folding; IC:ComplexPortal.
DR GO; GO:0000003; P:reproduction; IMP:WormBase.
DR GO; GO:0009408; P:response to heat; IMP:WormBase.
DR Gene3D; 1.25.40.10; -; 2.
DR InterPro; IPR041243; STI1.
DR InterPro; IPR045248; Sti1-like.
DR InterPro; IPR006636; STI1_HS-bd.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR22904; PTHR22904; 1.
DR Pfam; PF17830; STI1; 1.
DR SMART; SM00727; STI1; 1.
DR SMART; SM00028; TPR; 6.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50005; TPR; 6.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Developmental protein; Reference proteome; Repeat;
KW Stress response; TPR repeat.
FT CHAIN 1..320
FT /note="Stress-induced-phosphoprotein 1"
FT /id="PRO_0000422047"
FT REPEAT 5..38
FT /note="TPR 1"
FT /evidence="ECO:0000255"
FT REPEAT 40..72
FT /note="TPR 2"
FT /evidence="ECO:0000255"
FT REPEAT 80..113
FT /note="TPR 3"
FT /evidence="ECO:0000255"
FT REPEAT 140..173
FT /note="TPR 4"
FT /evidence="ECO:0000255"
FT REPEAT 175..207
FT /note="TPR 5"
FT /evidence="ECO:0000255"
FT REPEAT 208..241
FT /note="TPR 6"
FT /evidence="ECO:0000255"
FT DOMAIN 269..308
FT /note="STI1"
FT /evidence="ECO:0000255"
FT REGION 241..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 1..17
FT /evidence="ECO:0007829|PDB:4GCN"
FT HELIX 21..34
FT /evidence="ECO:0007829|PDB:4GCN"
FT HELIX 39..51
FT /evidence="ECO:0007829|PDB:4GCN"
FT HELIX 55..71
FT /evidence="ECO:0007829|PDB:4GCN"
FT HELIX 76..92
FT /evidence="ECO:0007829|PDB:4GCN"
FT HELIX 96..109
FT /evidence="ECO:0007829|PDB:4GCN"
FT HELIX 113..123
FT /evidence="ECO:0007829|PDB:4GCN"
FT HELIX 137..152
FT /evidence="ECO:0007829|PDB:4GCO"
FT HELIX 156..169
FT /evidence="ECO:0007829|PDB:4GCO"
FT HELIX 174..186
FT /evidence="ECO:0007829|PDB:4GCO"
FT HELIX 190..203
FT /evidence="ECO:0007829|PDB:4GCO"
FT HELIX 208..220
FT /evidence="ECO:0007829|PDB:4GCO"
FT HELIX 224..237
FT /evidence="ECO:0007829|PDB:4GCO"
FT HELIX 242..251
FT /evidence="ECO:0007829|PDB:4GCO"
SQ SEQUENCE 320 AA; 36962 MW; 9D21907275A09780 CRC64;
MTDAAIAEKD LGNAAYKQKD FEKAHVHYDK AIELDPSNIT FYNNKAAVYF EEKKFAECVQ
FCEKAVEVGR ETRADYKLIA KAMSRAGNAF QKQNDLSLAV QWFHRSLSEF RDPELVKKVK
ELEKQLKAAE RLAYINPELA QEEKNKGNEY FKKGDYPTAM RHYNEAVKRD PENAILYSNR
AACLTKLMEF QRALDDCDTC IRLDSKFIKG YIRKAACLVA MREWSKAQRA YEDALQVDPS
NEEAREGVRN CLRSNDEDPE KAKERSLADP EVQEILRDPG MRMILEQMSN DPGAVREHLK
NPEIFQKLMK LRDAGVIQMR
