STIP1_XENLA
ID STIP1_XENLA Reviewed; 543 AA.
AC Q7ZWU1;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Stress-induced-phosphoprotein 1;
DE Short=STI1;
GN Name=stip1 {ECO:0000312|Xenbase:XB-GENE-958367};
GN ORFNames=XELAEV_18022218mg {ECO:0000312|EMBL:OCT84080.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000312|EMBL:AAH46709.1};
RN [1] {ECO:0000312|EMBL:AAH46709.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000312|EMBL:AAH46709.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|Proteomes:UP000186698}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J {ECO:0000312|Proteomes:UP000186698};
RX PubMed=27762356; DOI=10.1038/nature19840;
RA Session A.M., Uno Y., Kwon T., Chapman J.A., Toyoda A., Takahashi S.,
RA Fukui A., Hikosaka A., Suzuki A., Kondo M., van Heeringen S.J., Quigley I.,
RA Heinz S., Ogino H., Ochi H., Hellsten U., Lyons J.B., Simakov O.,
RA Putnam N., Stites J., Kuroki Y., Tanaka T., Michiue T., Watanabe M.,
RA Bogdanovic O., Lister R., Georgiou G., Paranjpe S.S., van Kruijsbergen I.,
RA Shu S., Carlson J., Kinoshita T., Ohta Y., Mawaribuchi S., Jenkins J.,
RA Grimwood J., Schmutz J., Mitros T., Mozaffari S.V., Suzuki Y., Haramoto Y.,
RA Yamamoto T.S., Takagi C., Heald R., Miller K., Haudenschild C., Kitzman J.,
RA Nakayama T., Izutsu Y., Robert J., Fortriede J., Burns K., Lotay V.,
RA Karimi K., Yasuoka Y., Dichmann D.S., Flajnik M.F., Houston D.W.,
RA Shendure J., DuPasquier L., Vize P.D., Zorn A.M., Ito M., Marcotte E.M.,
RA Wallingford J.B., Ito Y., Asashima M., Ueno N., Matsuda Y., Veenstra G.J.,
RA Fujiyama A., Harland R.M., Taira M., Rokhsar D.S.;
RT "Genome evolution in the allotetraploid frog Xenopus laevis.";
RL Nature 538:336-343(2016).
RN [3] {ECO:0000312|EMBL:OCT84080.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=J {ECO:0000312|EMBL:OCT84080.1};
RC TISSUE=Blood {ECO:0000312|EMBL:OCT84080.1};
RA Session A., Uno Y., Kwon T., Chapman J., Toyoda A., Takahashi S., Fukui A.,
RA Hikosaka A., Putnam N., Stites J., Van Heeringen S., Quigley I., Heinz S.,
RA Hellsten U., Lyons J., Suzuki A., Kondo M., Ogino H., Ochi H.,
RA Bogdanovic O., Lister R., Georgiou G., Paranjpe S., Van Kruijsbergen I.,
RA Mozaffari S., Shu S., Schmutz J., Jenkins J., Grimwood J., Carlson J.,
RA Mitros T., Simakov O., Heald R., Miller K., Haudenschild C., Kuroki Y.,
RA Tanaka T., Michiue T., Watanabe M., Kinoshita T., Ohta Y., Mawaribuchi S.,
RA Suzuki Y., Haramoto Y., Yamamoto T., Takagi C., Kitzman J., Shendure J.,
RA Nakayama T., Izutsu Y., Robert J., Dichmann D., Flajnik M., Houston D.,
RA Marcotte E., Wallingford J., Ito Y., Asashima M., Ueno N., Matsuda Y.,
RA Jan Veenstra G., Fujiyama A., Harland R., Taira M., Rokhsar D.S.;
RT "WGS assembly of Xenopus laevis.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=33263282; DOI=10.7554/elife.58662;
RA Lee C., Cox R.M., Papoulas O., Horani A., Drew K., Devitt C.C., Brody S.L.,
RA Marcotte E.M., Wallingford J.B.;
RT "Functional partitioning of a liquid-like organelle during assembly of
RT axonemal dyneins.";
RL Elife 9:0-0(2020).
CC -!- FUNCTION: Acts as a co-chaperone for HSP90AA1 (By similarity). Mediates
CC the association of the molecular chaperones HSPA8/HSC70 and HSP90 (By
CC similarity). {ECO:0000250|UniProtKB:O35814,
CC ECO:0000250|UniProtKB:P31948}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q60864}. Nucleus
CC {ECO:0000250|UniProtKB:Q60864}. Dynein axonemal particle
CC {ECO:0000269|PubMed:33263282}.
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DR EMBL; BC046709; AAH46709.1; -; mRNA.
DR EMBL; CM004472; OCT84080.1; -; Genomic_DNA.
DR RefSeq; NP_001080263.1; NM_001086794.2.
DR AlphaFoldDB; Q7ZWU1; -.
DR SMR; Q7ZWU1; -.
DR STRING; 8355.Q7ZWU1; -.
DR DNASU; 379955; -.
DR GeneID; 379955; -.
DR KEGG; xla:379955; -.
DR CTD; 379955; -.
DR Xenbase; XB-GENE-958367; stip1.L.
DR OMA; TCNDAID; -.
DR OrthoDB; 933764at2759; -.
DR Proteomes; UP000186698; Chromosome 4L.
DR Bgee; 379955; Expressed in zone of skin and 19 other tissues.
DR GO; GO:0120293; C:dynein axonemal particle; IDA: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; 1.
DR Pfam; PF13181; TPR_8; 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 Cytoplasm; Nucleus; Reference proteome; Repeat; TPR repeat.
FT CHAIN 1..543
FT /note="Stress-induced-phosphoprotein 1"
FT /id="PRO_0000452442"
FT REPEAT 4..37
FT /note="TPR 1"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00339"
FT REPEAT 38..71
FT /note="TPR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT REPEAT 39..71
FT /note="TPR 11"
FT /evidence="ECO:0000255"
FT REPEAT 72..105
FT /note="TPR 3"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00339"
FT DOMAIN 130..169
FT /note="STI1 1"
FT /evidence="ECO:0000255"
FT REPEAT 225..258
FT /note="TPR 4"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00339"
FT REPEAT 259..292
FT /note="TPR 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT REPEAT 260..292
FT /note="TPR 14"
FT /evidence="ECO:0000255"
FT REPEAT 300..333
FT /note="TPR 6"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00339"
FT REPEAT 360..393
FT /note="TPR 7"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00339"
FT REPEAT 394..427
FT /note="TPR 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT REPEAT 395..427
FT /note="TPR 17"
FT /evidence="ECO:0000255"
FT REPEAT 428..461
FT /note="TPR 9"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00339"
FT DOMAIN 492..531
FT /note="STI1 2"
FT /evidence="ECO:0000255"
FT REGION 189..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 543 AA; 62107 MW; A72D65AB2008C395 CRC64;
MEAANALKEK GNKALSAGNL DEAVKCYTEA IKLDPKNHVL YSNRSAAYAK KKEFTKALED
GSKTVELKAD WGKGYSRKAA ALEFLNRFEE AKKTYEEGLR HEPTNAQLKE GLQNMEARLA
EKKFMNPFNS PNLFQKLESD PRTRALLSDP SYKELIEQLR NKPSDLGTKL QDPRVMTTLS
VLLGVELGNV DEEEEDTPPP PPPQPKKETK PEPMEEDLPE NKKQAQKEKE LGNEAYKKKD
FETALKHYGQ ARELDPANMT YITNQAAVYF EMGDYSKCRE LCEKAIEVGR ENREDYRLIA
KAYARIGNSY FKEEKNKEAI QFFNKSLAEH RTPEVLKKCQ QAEKILKEQE RVAYINPDLA
LEAKNKGNES FQKGDYPQAM KHYSEAIKRN PNDAKLYSNR AACYTKLLEF LLAVKDCEEC
IRLEPSFIKG YTRKAAALEA MKDFTKAMDA YQKAMELDST SKEATDGYQR CMMSQYNRND
NPEDVKRRAM ADPEVQQIMS DPAMRLILEQ MQKDPQALSD HLKNPVIAQK IQKLMDVGLI
AIR
