ID G1SXL3_RABIT Unreviewed; 369 AA.
AC G1SXL3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=STI1 domain-containing protein {ECO:0000259|SMART:SM00727};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000008303.2, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000008303.2, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke {ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000008303.2}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000008303.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: One HIP oligomer binds the ATPase domains of at least two
CC HSC70 molecules dependent on activation of the HSC70 ATPase by HSP40.
CC Stabilizes the ADP state of HSC70 that has a high affinity for
CC substrate protein. Through its own chaperone activity, it may
CC contribute to the interaction of HSC70 with various target proteins.
CC {ECO:0000256|ARBA:ARBA00037033}.
CC -!- SIMILARITY: Belongs to the FAM10 family.
CC {ECO:0000256|ARBA:ARBA00009015}.
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DR RefSeq; XP_002721443.1; XM_002721397.3.
DR AlphaFoldDB; G1SXL3; -.
DR SMR; G1SXL3; -.
DR STRING; 9986.ENSOCUP00000008303; -.
DR PaxDb; 9986-ENSOCUP00000008303; -.
DR Ensembl; ENSOCUT00000009635.3; ENSOCUP00000008303.2; ENSOCUG00000009636.3.
DR GeneID; 100354640; -.
DR KEGG; ocu:100354640; -.
DR CTD; 6767; -.
DR eggNOG; KOG1308; Eukaryota.
DR GeneTree; ENSGT00390000001347; -.
DR HOGENOM; CLU_026202_0_1_1; -.
DR InParanoid; G1SXL3; -.
DR OMA; NATIREC; -.
DR OrthoDB; 257381at2759; -.
DR TreeFam; TF313244; -.
DR Proteomes; UP000001811; Unplaced.
DR Bgee; ENSOCUG00000009636; Expressed in autopod skin and 18 other cell types or tissues.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR CDD; cd14438; Hip_N; 1.
DR Gene3D; 1.10.260.100; -; 1.
DR Gene3D; 6.10.250.3420; -; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR034649; Hip_N.
DR InterPro; IPR041243; STI1/HOP_DP.
DR InterPro; IPR006636; STI1_HS-bd.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR45883; HSC70-INTERACTING PROTEIN; 1.
DR PANTHER; PTHR45883:SF2; HSC70-INTERACTING PROTEIN; 1.
DR Pfam; PF18253; HipN; 1.
DR Pfam; PF17830; STI1-HOP_DP; 1.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00727; STI1; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50005; TPR; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001811};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW ProRule:PRU00339}.
FT REPEAT 148..181
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 319..358
FT /note="STI1"
FT /evidence="ECO:0000259|SMART:SM00727"
FT REGION 39..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 369 AA; 41309 MW; EBCF15247257764A CRC64;
MDPRKVNELR AFVKLCKQDP SVLHTEEMRF LREWVESMGG KVPPATHKAK PEENIKEEKT
DSKKAEETIQ TDEPSSEESD LEIDNEGVIE PDTDAPQEMG DENVEITEEM MDQANEKKGA
AIEALNDGEL QKAIDLFTDA IKLNPRLAIL YAKRASVFVK LQKPNAAIRD CDRAIDINPD
SAQPYKWRGK AHRLLGHWEE AAHDLALACK LDYDEDASAV LKEVQPRAQK IAEHRRKYER
KREEREIKER MERVKKAREE HERAQREEEA RRQSGAQYGS FPGGFPGGMP GNFPGGMPGM
GGAMPGMAGM PGLNEILSDP EVLAAMQDPE VMVAFQDVAQ NPANMSKYQS NPKVMNLISK
LSAKFGGQA
//
