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   27-MAR-2024, entry version 101.
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 (Social amoeba).
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.Q556U6; -.
DR   GlyCosmos; Q556U6; 12 sites, No reported glycans.
DR   PaxDb; 44689-DDB0266529; -.
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; VNQQAHI; -.
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:0000774; F:adenyl-nucleotide exchange factor activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   CDD; cd10230; HYOU1-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; IPR029048; HSP70_C_sf.
DR   InterPro; IPR029047; HSP70_peptide-bd_sf.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   PANTHER; PTHR45639; HSC70CB, ISOFORM G-RELATED; 1.
DR   PANTHER; PTHR45639:SF3; HYPOXIA UP-REGULATED PROTEIN 1; 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   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
//