STIP1_RAT
ID STIP1_RAT Reviewed; 543 AA.
AC O35814;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 155.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH HSPA8.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=9528774; DOI=10.1128/mcb.18.4.2023;
RA Demand J., Luders J., Hoehfeld J.;
RT "The carboxy-terminal domain of Hsc70 provides binding sites for a distinct
RT set of chaperone cofactors.";
RL Mol. Cell. Biol. 18:2023-2028(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 14-44; 78-87; 124-136; 253-272 AND 316-325, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
CC -!- FUNCTION: Acts as a co-chaperone for HSP90AA1 (By similarity). Mediates
CC the association of the molecular chaperones HSPA8/HSC70 and HSP90
CC (PubMed:9528774). {ECO:0000250|UniProtKB:P31948,
CC ECO:0000269|PubMed:9528774}.
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 (By similarity). Forms a complex with HSPA8/HSC70,
CC HSPCA/HSP-86 and HSPCB/HSP-84. Interacts with PACRG. Interacts with
CC EEF1AKMT3 (By similarity). Interacts with HSP90/HSP90AA1; the
CC interaction dissociates the PPP5C:HSP90AA1 interaction. Interacts with
CC FLCN, FNIP1 and FNIP2 (By similarity). Interacts with HSPA8/HSC70
CC (PubMed:9528774). Interacts with HSP90AB1; upon SMYD2-dependent
CC HSP90AB1 methylation (By similarity). {ECO:0000250|UniProtKB:P31948,
CC ECO:0000250|UniProtKB:Q60864, ECO:0000269|PubMed:9528774}.
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; Y15068; CAA75351.1; -; mRNA.
DR EMBL; BC061529; AAH61529.1; -; mRNA.
DR RefSeq; NP_620266.1; NM_138911.3.
DR AlphaFoldDB; O35814; -.
DR SMR; O35814; -.
DR BioGRID; 251401; 6.
DR IntAct; O35814; 6.
DR MINT; O35814; -.
DR STRING; 10116.ENSRNOP00000028743; -.
DR iPTMnet; O35814; -.
DR PhosphoSitePlus; O35814; -.
DR SwissPalm; O35814; -.
DR World-2DPAGE; 0004:O35814; -.
DR jPOST; O35814; -.
DR PaxDb; O35814; -.
DR PRIDE; O35814; -.
DR Ensembl; ENSRNOT00000116635; ENSRNOP00000091714; ENSRNOG00000021164.
DR GeneID; 192277; -.
DR KEGG; rno:192277; -.
DR UCSC; RGD:621599; rat.
DR CTD; 10963; -.
DR RGD; 621599; Stip1.
DR eggNOG; KOG0548; Eukaryota.
DR GeneTree; ENSGT00940000154911; -.
DR HOGENOM; CLU_000134_46_5_1; -.
DR InParanoid; O35814; -.
DR OMA; HYSKAWE; -.
DR OrthoDB; 933764at2759; -.
DR PhylomeDB; O35814; -.
DR TreeFam; TF300478; -.
DR Reactome; R-RNO-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-RNO-9696273; RND1 GTPase cycle.
DR PRO; PR:O35814; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000021164; Expressed in cerebellum and 20 other tissues.
DR Genevisible; O35814; RN.
DR GO; GO:0101031; C:chaperone complex; ISO:RGD.
DR GO; GO:0120293; C:dynein axonemal particle; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0051087; F:chaperone binding; IPI:RGD.
DR GO; GO:0030544; F:Hsp70 protein binding; IPI:RGD.
DR GO; GO:0051879; F:Hsp90 protein binding; ISO:RGD.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:RGD.
DR GO; GO:0098761; P:cellular response to interleukin-7; ISO:RGD.
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; 1.
DR Pfam; PF13181; TPR_8; 1.
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 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Isopeptide bond;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; TPR repeat;
KW Ubl conjugation.
FT CHAIN 1..543
FT /note="Stress-induced-phosphoprotein 1"
FT /id="PRO_0000106374"
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; 62570 MW; D8313F43BFB7EB73 CRC64;
MEQVNELKEK GNKALSAGNI DDALQCYSEA IKLDPQNHVL YSNRSAAYAK KGDYQKAYED
GCKTVDLKPD WGKGYSRKAA ALEFLNRFEE AKRTYEEGLK HEANNLQLKE GLQNMEARLA
ERKFMNPFNL PNLYQKLEND PRTRTLLSDP TYRELIEQLQ NKPSDLGTKL QDPRVMTTLS
VLLGVDLGSM DEEEEAATPP PPPPPKKEAK PEPMEEDLPE NKKQALKEKE LGNDAYKKKD
FDKALKHYDK AKELDPTNMT YITNQAAVHF EKGDYNKCRE LCEKAIEVGR ENREDYRQIA
KAYARIGNSY FKEERYKDAI HFYNKSLAEH RTPDVLKKCQ QAEKILKEQE RLAYINPDLA
LEEKNKGNEC FQKGDYPQAM KHYTEAIKRN PRDAKLYSNR AACYTKLLEF QLALKDCEEC
IQLEPTFIKG YTRKAAALEA MKDYTKAMDV YQKALDLDSS CKEAADGYQR CMMAQYNRHD
SPEDVKRRAM ADPEVQQIMS DPAMRLILEQ MQKDPQALSE HLKNPVIAQK IQKLMDVGLI
AIR
