BIP1_USTMA
ID BIP1_USTMA Reviewed; 660 AA.
AC A0A0D1CD96;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2015, sequence version 1.
DT 03-AUG-2022, entry version 27.
DE RecName: Full=Endoplasmic reticulum chaperone BIP1 {ECO:0000303|PubMed:26487566};
DE EC=3.6.4.10 {ECO:0000250|UniProtKB:P11021};
GN Name=BIP1 {ECO:0000303|PubMed:26487566}; ORFNames=UMAG_15034;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SUBCELLULAR LOCATION, INDUCTION, AND INTERACTION WITH DNJ1.
RX PubMed=26487566; DOI=10.1111/nph.13703;
RA Lo Presti L., Lopez Diaz C., Turra D., Di Pietro A., Hampel M., Heimel K.,
RA Kahmann R.;
RT "A conserved co-chaperone is required for virulence in fungal plant
RT pathogens.";
RL New Phytol. 209:1135-1148(2016).
CC -!- FUNCTION: Probably plays a role in facilitating the assembly of
CC multimeric protein complexes inside the ER (By similarity). Is required
CC for secretory polypeptide translocation (By similarity).
CC {ECO:0000250|UniProtKB:P16474}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.10;
CC Evidence={ECO:0000250|UniProtKB:P11021};
CC -!- SUBUNIT: Interacts with the ER co-chaperonne DNJ1.
CC {ECO:0000269|PubMed:26487566}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000269|PubMed:26487566}.
CC -!- INDUCTION: Expression is increased in the absence of DNJ1.
CC {ECO:0000269|PubMed:26487566}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM003141; KIS71057.1; -; Genomic_DNA.
DR RefSeq; XP_011387505.1; XM_011389203.1.
DR STRING; 237631.A0A0D1CD96; -.
DR EnsemblFungi; KIS71057; KIS71057; UMAG_15034.
DR GeneID; 23568125; -.
DR KEGG; uma:UMAG_15034; -.
DR VEuPathDB; FungiDB:UMAG_15034; -.
DR OrthoDB; 288077at2759; -.
DR Proteomes; UP000000561; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0034663; C:endoplasmic reticulum chaperone complex; IBA:GO_Central.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
DR GO; GO:0051787; F:misfolded protein binding; IBA:GO_Central.
DR GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0034620; P:cellular response to unfolded protein; IBA:GO_Central.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029048; HSP70_C_sf.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR PANTHER; PTHR19375; PTHR19375; 2.
DR Pfam; PF00012; HSP70; 2.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF100934; SSF100934; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chaperone; Endoplasmic reticulum; Hydrolase;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..660
FT /note="Endoplasmic reticulum chaperone BIP1"
FT /id="PRO_0000454651"
FT REGION 131..285
FT /note="Nucleotide-binding (NBD)"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT REGION 404..504
FT /note="Substrate-binding (SBD)"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT MOTIF 657..660
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT BINDING 74..77
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT BINDING 232..234
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT BINDING 298..305
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT BINDING 369..372
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
SQ SEQUENCE 660 AA; 71100 MW; 4C76318A96769B88 CRC64;
MVLASRTTAL AQRRKAARAT GMSRPAFMTI IMAILALLTL SAFMSPASSA GGMGVAAAAD
KRSEYGTVIG IDLGTTYSCV GAQVNGRVEI ITNDQGNRIT PSYVAFTPWG ESDLKKDAKH
LPFKLVEKNG KPAIQVTVNG EKKVFTPEEV SAMVLQKMKE TAEAYLGHKV THAVVTVPAY
FNDAQRQATK DAGTIAGLNV LRIVNEPTAA AIAYGLDKKD GESQIIVYDL GGGTFDVSLL
SIDSGVFEVL ATAGDTHLGG EDFDNRVSEY ILKQFKKKTG LDASSNKRSV GKLKREVERA
KRTLSSQMST KIEIDGFFEG NDLDETLTRA KFEELNMDLF RKTMKPVEQV LKDAGVKKDE
IDDVVLVGGS TRIPKVQAML KEYFGREPSK GINPDEAVAW GAAVQGGVLA GDESLGDVVL
IDVNPLTLGI ETNGGVMTKL IPRNTVVPTK KSQIFSTAAD NQNTVLIQVF EGERSMTKDN
NLLGKFELTG IPPAPRGTPQ IEVTFELDAN GIMKVSAADK GTGKSESITI SNDKGRLTPE
EIERMVAEAE EFAEQDEAVR KRIEALNNLQ NFIASLRSQL SDKEGLGGKL DKEDKETIKQ
SLKDAEAWLD ENSQTAEGSD IEEQLSELQA AVAPITAKIY QGGAAAGGDD EPLNYGHDEL
