BIP1_DICDI
ID BIP1_DICDI Reviewed; 926 AA.
AC Q556U6; Q86JV8;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Luminal-binding protein 1;
DE Short=BiP 1;
DE AltName: Full=78 kDa glucose-regulated protein homolog;
DE Short=GRP-78;
DE Flags: Precursor;
GN Name=bip1-1; ORFNames=DDB_G0273093;
GN and
GN Name=bip1-2; ORFNames=DDB_G0273813;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Probably plays a role in facilitating the assembly of
CC multimeric protein complexes inside the ER. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
CC -!- CAUTION: The gene for this protein is duplicated in strains AX3 and
CC AX4. These strains contain a duplication of a segment of 750 kb of
CC chromosome 2 compared to the corresponding sequence in strain AX2.
CC {ECO:0000305}.
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DR EMBL; AAFI02000011; EAL70597.1; -; Genomic_DNA.
DR EMBL; AAFI02000009; EAL70764.1; -; Genomic_DNA.
DR RefSeq; XP_644523.1; XM_639431.1.
DR RefSeq; XP_644727.1; XM_639635.1.
DR AlphaFoldDB; Q556U6; -.
DR SMR; Q556U6; -.
DR STRING; 44689.DDB0266529; -.
DR PaxDb; Q556U6; -.
DR EnsemblProtists; EAL70597; EAL70597; DDB_G0273813.
DR EnsemblProtists; EAL70764; EAL70764; DDB_G0273093.
DR GeneID; 8618827; -.
DR GeneID; 8619149; -.
DR KEGG; ddi:DDB_G0273093; -.
DR KEGG; ddi:DDB_G0273813; -.
DR dictyBase; DDB_G0273093; -.
DR dictyBase; DDB_G0273813; -.
DR eggNOG; KOG0103; Eukaryota.
DR eggNOG; KOG0104; Eukaryota.
DR HOGENOM; CLU_005965_5_0_1; -.
DR InParanoid; Q556U6; -.
DR OMA; DHEEPAF; -.
DR PhylomeDB; Q556U6; -.
DR PRO; PR:Q556U6; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0034663; C:endoplasmic reticulum chaperone complex; IBA:GO_Central.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0071456; P:cellular response to hypoxia; IBA:GO_Central.
DR GO; GO:1903298; P:negative regulation of hypoxia-induced intrinsic apoptotic signaling 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; IPR029048; HSP70_C_sf.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR Pfam; PF00012; HSP70; 1.
DR SUPFAM; SSF100934; SSF100934; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS00014; ER_TARGET; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Endoplasmic reticulum; Glycoprotein;
KW Nucleotide-binding; Reference proteome; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..926
FT /note="Luminal-binding protein 1"
FT /id="PRO_0000327977"
FT REGION 458..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 857..926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 923..926
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT COMPBIAS 468..485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..605
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 866..899
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 468
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 544
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 584
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 596
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 649
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 797
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 881
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 926 AA; 104792 MW; EEA198A7B6B5E111 CRC64;
MVKNIKIFLS LFFVVVLGLL ATTANSMVIG IDLGSQTFKV SLIKPGAFET VLNEQSGRKT
ISSVGWFKDE RLFSSDSFSV WARNPKQNYN LIQAFLGIKY KEGLVEEISN GLPLGFKVKN
DTVRNTVSIV YDDDTNYSAE ELTGMLLRRV KDMASSYAGS SIKDCAITIP PYFTQQQRQA
LLDAAQLAGL NVLSLIHDVN AAALSFAMDR TFLEKNESVI FYDMGARHTS VSLVEFESHN
EQIKGVKKNK TVSSASVKGI EWDEKLGGFD FDMVIVNHLK TLLKKQIPSA NVDDIKITIK
LLKEVGKMKE NLSVNQQAQI FIGSLVDDHD FQATISKQQF EELSQSLIER SLLPLKKLIL
STGIKLKDIE YFEVIGGGVR IPFIQQALKD YLKRDTLDKH LNGDEAMSNG AAFYAASLTH
YFKVKEIKLK DILLNSVDVE INNNIINSGG AGETLLEETE DNEDNELNNS GNEQQQQQQP
TINQGGLKDK KIQLFKVNSK LGIKKTVSFS SENGFSLFLN NPTINNPLAT YTVSNVPTPG
EKYNFTGKPK IHCSFRLTTS GIVVLEKAEA EITVSLIKPQ PQQNKTSSST STTKKNTTTI
ETTDGGSEET TDETTTKQQQ QQEKEEEEEV VVVEKVIEYI QKTIRVPLNF TIKYNGCVEP
LSKELSQESN DRINKLDQVD RILRELRQER NNLESFIYET KDKLESNEEY LKCSTQQERD
QLVEELDKTS AWLSDALDND NTETEEYRKQ LKDIKKKADK IVNRVSQYQL VPVALEELED
TVDKVKPMFE IASKDLNVTA EELKETTDKI QSVSDWVQEK KSEFKLADYS KDLQTSSFDI
KFKLYDLERT IKEILKKKKK PVKPSSSKKD KSSKSSKGKS NSTDEKDQKQ KEQKEQQQQQ
KEESQFQNDG AEEQQFEDDH KVHDEL
