ID   CUPE_DICDI              Reviewed;         758 AA.
AC   Q7Z200;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Calcium up-regulated protein E;
GN   Name=cupE; ORFNames=DDB_G0294531;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RX   PubMed=14871937; DOI=10.1128/ec.3.1.61-71.2004;
RA   Coukell B., Li Y., Moniakis J., Cameron A.;
RT   "The Ca2+/calcineurin-regulated cup gene family in Dictyostelium discoideum
RT   and its possible involvement in development.";
RL   Eukaryot. Cell 3:61-71(2004).
CC   -!- FUNCTION: May play an important role in stabilizing and/or regulating
CC       the cell membrane during Ca(2+) stress or certain stages of
CC       development. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane {ECO:0000250}; Peripheral
CC       membrane protein {ECO:0000250}.
CC   -!- INDUCTION: Induced by high levels of extracellular Ca(2+).
CC       {ECO:0000269|PubMed:14871937}.
CC   -!- SIMILARITY: Belongs to the cup family. {ECO:0000305}.
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DR   EMBL; AY282571; AAP40293.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7Z200; -.
DR   CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProt.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0043157; P:response to cation stress; IEA:UniProt.
DR   CDD; cd00161; RICIN; 1.
DR   InterPro; IPR035992; Ricin_B-like_lectins.
DR   InterPro; IPR000772; Ricin_B_lectin.
DR   Pfam; PF00652; Ricin_B_lectin; 1.
DR   SUPFAM; SSF50370; SSF50370; 2.
DR   PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Lectin; Membrane; Repeat.
FT   CHAIN           1..758
FT                   /note="Calcium up-regulated protein E"
FT                   /id="PRO_0000327953"
FT   DOMAIN          25..145
FT                   /note="Ricin B-type lectin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   DOMAIN          156..288
FT                   /note="Ricin B-type lectin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   758 AA;  84187 MW;  2235AB4EE769DC78 CRC64;
     MINIEDISKS SNQSEEKQLK STSSKPKYSF AAKSLFKGSN NITPYYLSTS NTFQCVASES
     IQTWLLSDDG HIFTSSGNFV LDVSSGGYFV ELVQLNSNSK TQIWTIDTTN NKIQNQGNGK
     YLDIDNLNIY VAPLNGNATQ QWTTFRRAPI PTGNWGYFQS KQLDSNNNYW GLSVLNNSTS
     YNTSVVMNKV QAKSIKRWSH FITFGGNLVL DIGPSINGSK TYYLNTNVYK ANDLMQQWGI
     NENNQIFNQY YPNLCIGFVG ELGVDSTVNC VLAQPSSACD INFQWIANPT YSLNQIVSEV
     PEQFPAYTSG DLLASYQYLS DDATNGYTDD IRSLYTSINV SLENFYVNVT NATCPSSIHQ
     LKIFQNQIKN ELTYAINVRL VFDNYSGFYS KLFSQGSTNL TNLANLINVD MSSDQVVNGN
     YTDAITSVFY AIISEIPIGG SIIANIGESA EEFGELDAES NDSGPSTYQV TLSKLYDHLN
     ENYENEMANA QRMKNTILQD WGMMSKTFTL CFLPTNNPSS LNMNGFDFQK ISSIASLAYL
     TAMIQMLLPT NYQIYFTPAG YYAPVSSDDY SYTDSTGTYI MAEIDNCNSH PPKALTDKLW
     KNGVSKQEVF TSSYGWNLAT SVTYYNMVGK YGGMFKLSFP TVKNITSVPM QFVMTNGSDR
     VGTFNVKTHF AGLASTYYNS GALGHHYYDI AVTDIDRNKV ANFTVDNNLE ALEGSYVSIK
     TNSLVVQPGY VVGNPTCNQG SFSQGFAASI LIPIYKSN