ID A0A2V1AR82_9ASCO Unreviewed; 677 AA.
AC A0A2V1AR82;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=CXQ85_002177 {ECO:0000313|EMBL:PVH20389.1};
OS [Candida] haemuloni.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC Candida/Metschnikowiaceae.
OX NCBI_TaxID=45357 {ECO:0000313|EMBL:PVH20389.1, ECO:0000313|Proteomes:UP000244309};
RN [1] {ECO:0000313|EMBL:PVH20389.1, ECO:0000313|Proteomes:UP000244309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B11899 {ECO:0000313|EMBL:PVH20389.1,
RC ECO:0000313|Proteomes:UP000244309};
RA Chow N.A., Gade L., Batra D., Rowe L.A., Ben-Ami R., Loparev V.N.,
RA Litvintseva A.P.;
RT "Genome Sequence of a Multidrug-Resistant Candida haemulonii Isolate from a
RT Patient with Chronic Leg Ulcers in Israel.";
RL Submitted (DEC-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PVH20389.1}.
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DR EMBL; PKFO01000003; PVH20389.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V1AR82; -.
DR STRING; 45357.A0A2V1AR82; -.
DR EnsemblFungi; CXQ85_002177-t46_1; CXQ85_002177-t46_1-p1; CXQ85_002177.
DR VEuPathDB; FungiDB:CXQ85_002177; -.
DR OrthoDB; 143at2759; -.
DR Proteomes; UP000244309; Unassembled WGS sequence.
DR GO; GO:0099021; C:cortical endoplasmic reticulum lumen; IEA:EnsemblFungi.
DR GO; GO:0034099; C:luminal surveillance complex; IEA:EnsemblFungi.
DR GO; GO:0031965; C:nuclear membrane; IEA:EnsemblFungi.
DR GO; GO:0099020; C:perinuclear endoplasmic reticulum lumen; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:EnsemblFungi.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0015450; F:protein-transporting ATPase activity; IEA:EnsemblFungi.
DR GO; GO:0051082; F:unfolded protein binding; IEA:EnsemblFungi.
DR GO; GO:0070880; P:fungal-type cell wall beta-glucan biosynthetic process; IEA:EnsemblFungi.
DR GO; GO:0036498; P:IRE1-mediated unfolded protein response; IEA:EnsemblFungi.
DR GO; GO:0000742; P:karyogamy involved in conjugation with cellular fusion; IEA:EnsemblFungi.
DR GO; GO:0031204; P:post-translational protein targeting to membrane, translocation; IEA:EnsemblFungi.
DR GO; GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; IEA:EnsemblFungi.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IEA:EnsemblFungi.
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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000244309};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT REGION 652..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 295..322
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 659..677
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 677 AA; 74100 MW; 18C22C4BAF6F5F48 CRC64;
MFKNHSSKFW LSGLTLFYAM LLVVMPFFTS NSGVALAADD DKEESYGTVI GIDLGTTYSC
VGVMKNGKVE ILANDQGNRI TPSYVAFTEE ERLIGDAAKN QAPSNVKNTI FDIKRLIGLK
YKDKVVQKEI KHLPFKIGKK GDMPVVEVSY GGEQKSFSPE EISGMILTKM KSIAEEYLGK
KVTHAVVTVP AYFNDAQRQA TKNAGTIAGL NVLRIVNEPT AAAIAYGLDK TDGEKQIIVY
DLGGGTFDVS LLSIEGGVFE VLATAGDTHL GGEDFDFQVV KHLTKLFEKK HDVSIATNQK
AISKLKREAE KAKRTLSAQM SARIEIDSFV DGIDFSETIS RAKFEELNIA SFKKTLKPVE
SVLKDAGVKK SDVDDIVLVG GSTRIPKIQE LIEKFFDGKK ASKSINPDEA VAYGAAVQAG
VLSGEEGVDD IVLLDVNPLT LGIETTGGVM TTLINRNTAI PTKKSQIFST AADNQPTVMI
SVYEGERAMV KDNNLLGKFE LTGIPPAPRG VPQIEVTFAL DANGILKVDA VDKGTGKKKS
ITITNEKGRL SKEEIDRMVE EAEKYAAQDQ EIKAKIESRN SLENLVHNMK QKLADNDEYV
SKLDDNDKEA LSDAVSEASE FLDENYETAT SEEFEEAKQK LVEITQKISA KLYENPADEE
DAQFGDDSDD DFEHDEL
//
