STIP1_CRIGR
ID STIP1_CRIGR Reviewed; 543 AA.
AC O54981;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Stress-induced-phosphoprotein 1;
DE Short=STI1;
DE AltName: Full=Hsc70/Hsp90-organizing protein;
DE Short=Hop;
GN Name=STIP1; Synonyms=HOP;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary;
RX PubMed=10409656; DOI=10.1074/jbc.274.30.21049;
RA Heine H., Delude R.L., Monks B.G., Espevik T., Golenbock D.T.;
RT "Bacterial lipopolysaccharide induces expression of the stress response
RT genes hop and H411.";
RL J. Biol. Chem. 274:21049-21055(1999).
CC -!- FUNCTION: Acts as a co-chaperone for HSP90AA1. Mediates the association
CC of the molecular chaperones HSPA8/HSC70 and HSP90.
CC {ECO:0000250|UniProtKB:O35814, ECO:0000250|UniProtKB:P31948}.
CC -!- SUBUNIT: Probably forms a complex composed of chaperones HSP90 and
CC HSP70, co-chaperones STIP1/HOP, CDC37, PPP5C, PTGES3/p23, TSC1 and
CC client protein TSC2. Forms a complex with HSPA8/HSC70, HSPCA/HSP-86 and
CC HSPCB/HSP-84. Interacts with PACRG. Interacts with EEF1AKMT3 (By
CC similarity). Interacts with HSP90/HSP90AA1; the interaction dissociates
CC the PPP5C:HSP90AA1 interaction. Interacts with FLCN, FNIP1 and FNIP2.
CC Interacts with HSPA8/HSC70. Interacts with HSP90AB1; upon SMYD2-
CC dependent HSP90AB1 methylation. {ECO:0000250|UniProtKB:O35814,
CC ECO:0000250|UniProtKB:P31948, ECO:0000250|UniProtKB:Q60864}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q60864}. Nucleus
CC {ECO:0000250|UniProtKB:Q60864}. Dynein axonemal particle
CC {ECO:0000250|UniProtKB:Q7ZWU1}.
CC -!- DOMAIN: The TPR 1 repeat interacts with the C-terminal of HSC70. The
CC TPR 4, 5 and 6 repeats (also called TPR2A domain) and TPR 7, 8 and 9
CC repeats (also called TPR2B domain) interact with HSP90 (By similarity).
CC {ECO:0000250}.
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DR EMBL; AF039202; AAB94760.1; -; mRNA.
DR RefSeq; NP_001233607.1; NM_001246678.1.
DR AlphaFoldDB; O54981; -.
DR SMR; O54981; -.
DR STRING; 10029.NP_001233607.1; -.
DR GeneID; 100689413; -.
DR KEGG; cge:100689413; -.
DR CTD; 10963; -.
DR eggNOG; KOG0548; Eukaryota.
DR OrthoDB; 933764at2759; -.
DR GO; GO:0120293; C:dynein axonemal particle; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0030544; F:Hsp70 protein binding; IEA:InterPro.
DR GO; GO:0051879; F:Hsp90 protein binding; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR Gene3D; 1.25.40.10; -; 3.
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; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR22904; PTHR22904; 1.
DR Pfam; PF17830; STI1; 2.
DR Pfam; PF00515; TPR_1; 2.
DR SMART; SM00727; STI1; 2.
DR SMART; SM00028; TPR; 9.
DR SUPFAM; SSF48452; SSF48452; 3.
DR PROSITE; PS50005; TPR; 9.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Isopeptide bond; Nucleus; Phosphoprotein; Repeat;
KW TPR repeat; Ubl conjugation.
FT CHAIN 1..543
FT /note="Stress-induced-phosphoprotein 1"
FT /id="PRO_0000106371"
FT REPEAT 4..37
FT /note="TPR 1"
FT REPEAT 39..71
FT /note="TPR 2"
FT REPEAT 73..105
FT /note="TPR 3"
FT DOMAIN 130..169
FT /note="STI1 1"
FT REPEAT 225..258
FT /note="TPR 4"
FT REPEAT 260..292
FT /note="TPR 5"
FT REPEAT 300..333
FT /note="TPR 6"
FT REPEAT 360..393
FT /note="TPR 7"
FT REPEAT 395..427
FT /note="TPR 8"
FT REPEAT 428..461
FT /note="TPR 9"
FT DOMAIN 492..531
FT /note="STI1 2"
FT REGION 191..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 222..239
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 208..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P31948"
FT MOD_RES 8
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P31948"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31948"
FT MOD_RES 198
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P31948"
FT MOD_RES 301
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P31948"
FT MOD_RES 312
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P31948"
FT MOD_RES 325
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P31948"
FT MOD_RES 332
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P31948"
FT MOD_RES 344
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P31948"
FT MOD_RES 354
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P31948"
FT MOD_RES 446
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P31948"
FT MOD_RES 481
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31948"
FT CROSSLNK 123
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P31948"
FT CROSSLNK 123
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P31948"
FT CROSSLNK 210
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P31948"
FT CROSSLNK 210
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P31948"
SQ SEQUENCE 543 AA; 62651 MW; 4E6A9C17EEFBF287 CRC64;
MEQVNELKEK GNKALSAGNI DDALQCYSEA IKLDPQNHVL YSNRSAAYAK KGDYQKAYED
GCKTVDLKPD WGKGYSRKAA ALEFLNRFEE AKRTYEEGLK HEANNLQLKE GLQNMEARLA
ERKFMNPFNL PNLYQKLEND PRTRTLLSDP TYRELIEQLR NKPSDLGTKI QDPRIMTTLS
VLLGVDLGSM DEEEEAATPP PPPPSKKEAK PEPMEEDLPE NKKQALKEKE MGNEAYKKKD
FDMALKHYDR AKELDPTNMT YITNQAAVHF EKGDYNKCRE LCEKAIEVGR ENREDYRQIA
KAYARIGNSY FKEERYKDAI HFYNKSLAEH RTPDVLKKCQ QAEKILKEQE RLAYINPDLA
LEEKNKGNEC FQKGDYPQAM KHYTEAIKRN PKDAKLYSNR AACYTKLLEF QLALKDCEEC
IQLEPTFIKG YTRKAAALEA MKDYTKAMDV YQKALELDSS CKEAADGYQR CMMAQYNRHD
SPEDVKRRAM ADPEVQQIMS DPAMRLILEQ MQKDPQALSE HLKNPVIAQK IQKLMDVGLI
AIR
