ID B2ART7_PODAN Unreviewed; 663 AA.
AC B2ART7;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=Endoplasmic reticulum chaperone BiP {ECO:0000256|ARBA:ARBA00019933};
DE EC=3.6.4.10 {ECO:0000256|ARBA:ARBA00012554};
DE AltName: Full=Immunoglobulin heavy chain-binding protein homolog {ECO:0000256|ARBA:ARBA00031728};
GN ORFNames=PODANS_4_6420 {ECO:0000313|EMBL:CAP66865.1};
OS Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS (Pleurage anserina).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC Podospora anserina.
OX NCBI_TaxID=515849 {ECO:0000313|EMBL:CAP66865.1};
RN [1] {ECO:0000313|EMBL:CAP66865.1, ECO:0000313|Proteomes:UP000001197}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC {ECO:0000313|Proteomes:UP000001197}, and S mat+
RC {ECO:0000313|EMBL:CAP66865.1};
RX PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL Genome Biol. 9:R77.1-R77.22(2008).
RN [2] {ECO:0000313|EMBL:CAP66865.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S mat+ {ECO:0000313|EMBL:CAP66865.1};
RA Genoscope - CEA;
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000001197}
RP GENOME REANNOTATION.
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC {ECO:0000313|Proteomes:UP000001197};
RX PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Genetics 197:421-432(2014).
RN [4] {ECO:0000313|EMBL:CDP28607.1}
RP NUCLEOTIDE SEQUENCE.
RA Grognet P., Bidard F., Kuchly C., Chan Ho Tong L., Coppin E.,
RA Ait Benkhali J., Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probably plays a role in facilitating the assembly of
CC multimeric protein complexes inside the ER. Is required for secretory
CC polypeptide translocation. May physically associate with SEC63 protein
CC in the endoplasmic reticulum and this interaction may be regulated by
CC ATP hydrolysis. {ECO:0000256|ARBA:ARBA00002226}.
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:0000256|ARBA:ARBA00001629};
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|RuleBase:RU003322}.
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DR EMBL; CU633895; CAP66865.1; -; Genomic_DNA.
DR EMBL; FO904939; CDP28607.1; -; Genomic_DNA.
DR RefSeq; XP_001906199.1; XM_001906164.1.
DR AlphaFoldDB; B2ART7; -.
DR STRING; 515849.B2ART7; -.
DR GeneID; 6190110; -.
DR KEGG; pan:PODANSg3227; -.
DR VEuPathDB; FungiDB:PODANS_4_6420; -.
DR eggNOG; KOG0100; Eukaryota.
DR HOGENOM; CLU_005965_7_0_1; -.
DR OrthoDB; 143at2759; -.
DR Proteomes; UP000001197; Chromosome 4.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR CDD; cd10241; HSPA5-like_NBD; 1.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 3.30.30.30; -; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR042050; BIP_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:SF144; ENDOPLASMIC RETICULUM CHAPERONE BIP; 1.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
DR SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003322};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003322};
KW Reference proteome {ECO:0000313|Proteomes:UP000001197};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..663
FT /note="Endoplasmic reticulum chaperone BiP"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007638797"
SQ SEQUENCE 663 AA; 72334 MW; E88DF23EFCD458B9 CRC64;
MERRSRSWAL GLSIIGFFAL LFSAGFVQQV KADDVSEYGT VIGIDLGTTY SCVGVMQKGK
VEILVNDQGN RITPSYVAFT DEERLVGDAA KNQAPANPYN TIYDIKRLIG RKFSEKELQT
DIKHFPFKVV SKNDKPAVTV KVNGEDKTFT PEEISAMVLG KMKETAESYL GKKVTHAVVT
VPAYFNDNQR QATKDAGMIA GLNVLRIVNE PTAAAIAYGL DKTDGERQII VYDLGGGTFD
VSLLSIDQGV FEVLATAGDT HLGGEDFDQR VINHFAKTFN KKHGVDVTTD AKAMGKLKRE
AEKAKRTLSS QMSTRIEIES LFGGKDFSET LTRAKFEELN NDLFRKTLEP VKQVLKDAKV
AKGEVDDIVL VGGSTRIPKV QALIEEFFGG KKASKGINPD EAVAFGAAVQ AGVLSGEEGT
EEIVLMDVNP LTLGIETTGG VMTKLITRNT PIPTRKSQIF STAADNQPVV LIQVYEGERS
MTKDNNLLGK FELTGIPPAP RGVPQIEVSF ELDANGILKV SAHDKGTGKA ESITITNDKG
RLTQEEIDRM VAEAEKYAEE DKATRERIEA RNGLENYAFS LKNQVNDEEG MGKKISEEDK
ETILDAVKET QDWLEENAAT ASTEDFEEQK EKLSGVAYPI TSKLYSAGGA GGEDDEPAGH
DEL
//
