ID   CUPH_DICDI              Reviewed;         768 AA.
AC   Q54FW5;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Putative calcium up-regulated protein H;
GN   Name=cupH; ORFNames=DDB_G0290563;
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=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: 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   -!- SIMILARITY: Belongs to the cup family. {ECO:0000305}.
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DR   EMBL; AAFI02000164; EAL62142.1; -; Genomic_DNA.
DR   RefSeq; XP_635652.1; XM_630560.1.
DR   AlphaFoldDB; Q54FW5; -.
DR   STRING; 44689.DDB0266360; -.
DR   PaxDb; Q54FW5; -.
DR   EnsemblProtists; EAL62142; EAL62142; DDB_G0290563.
DR   GeneID; 8627724; -.
DR   KEGG; ddi:DDB_G0290563; -.
DR   dictyBase; DDB_G0290563; cupH.
DR   HOGENOM; CLU_020711_0_0_1; -.
DR   PhylomeDB; Q54FW5; -.
DR   PRO; PR:Q54FW5; -.
DR   Proteomes; UP000002195; Chromosome 5.
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; IBA:GO_Central.
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; 2.
PE   3: Inferred from homology;
KW   Cytoplasm; Lectin; Membrane; Reference proteome; Repeat.
FT   CHAIN           1..768
FT                   /note="Putative calcium up-regulated protein H"
FT                   /id="PRO_0000327956"
FT   DOMAIN          25..145
FT                   /note="Ricin B-type lectin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   DOMAIN          116..248
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   768 AA;  85342 MW;  605F5436F473A676 CRC64;
     MINIEDISKS SNQSEEKQLK STSSKPKYSF AAKSLFKGSN NITPYYLSTS NTFQCVASES
     IQTWLLSDDG HIFTSSGNFV LDVSSGGYFV ELVQLNSNSK TQIWTIDTTN NKIQNQGNGN
     YLDIDCFNIC VAPLNGNATQ QWTTFRRAPI PTGNWGYFQS EQLGSNNYWG LSVLNNSTSY
     NTSVVMNKVQ AKSKGQIWQM TSDGHILSRL DGNLVLDIGP SINGSTTNYY LNTNVYKAND
     LMQQWGINEN NQIFNQYYPN LCIGFVGQLG VDSTVNCVLA QPSSACDTCF QWIANPTYSL
     NQIVSEVPEP FPAYTSGDLL ASYQYLSNDA TSNFTDDIRS LYTGINVSLQ SFLSIVTNAT
     CPSSIHSTED FSNVQNQIKT ELIYAIDVRL VFENYSGFYS KLFSQGSSNL TNLANLINVD
     MSSNQMVNAN YTDAITSIFY SLISEIPVGG SIIANIGQSA VEFGELMSQS NYQGASTYQV
     ELSQLYTHLN TNYENEMANA QSMKDTILQD WGMMSKTYAL CFLPTNDPSS LNMNGLDFEK
     ISDVASVAYE IAMIQMLLPT TYQIYFTSAG YWVPYSDGDF AYSDNSGTYI MATIKYSNSY
     PPKELTDKLW NNGVSKQEFF LSAYGWNLAT SLTYYNTTNQ YSNIFKLAFP TIKNFTGVPM
     QFVMTNDGDN LGNFTVKTHF AKFFSTYYSV GDLGHHYFDI AVTDINKNKV ANFTVDIKLK
     ALEGSYVSIK TGSLVVQPGY AVGNPICNQG SYSLMFSASI LIPIYKSE