ID A0A0S3R2W0_PHAAN Unreviewed; 218 AA.
AC A0A0S3R2W0;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Calcyclin-binding protein {ECO:0000256|ARBA:ARBA00015702};
GN Name=Vigan.01G265900 {ECO:0000313|EMBL:BAT74886.1};
GN ORFNames=VIGAN_01265900 {ECO:0000313|EMBL:BAT74886.1};
OS Vigna angularis var. angularis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=157739 {ECO:0000313|EMBL:BAT74886.1, ECO:0000313|Proteomes:UP000291084};
RN [1] {ECO:0000313|EMBL:BAT74886.1, ECO:0000313|Proteomes:UP000291084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Shumari {ECO:0000313|Proteomes:UP000291084};
RX PubMed=26616024; DOI=10.1038/srep16780;
RA Sakai H., Naito K., Ogiso-Tanaka E., Takahashi Y., Iseki K., Muto C.,
RA Satou K., Teruya K., Shiroma A., Shimoji M., Hirano T., Itoh T., Kaga A.,
RA Tomooka N.;
RT "The power of single molecule real-time sequencing technology in the de
RT novo assembly of a eukaryotic genome.";
RL Sci. Rep. 5:16780-16780(2015).
CC -!- FUNCTION: May be involved in calcium-dependent ubiquitination and
CC subsequent proteasomal degradation of target proteins. Probably serves
CC as a molecular bridge in ubiquitin E3 complexes. Participates in the
CC ubiquitin-mediated degradation of beta-catenin (CTNNB1).
CC {ECO:0000256|ARBA:ARBA00025145}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; AP015034; BAT74886.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S3R2W0; -.
DR Proteomes; UP000291084; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0044548; F:S100 protein binding; IEA:InterPro.
DR GO; GO:0015631; F:tubulin binding; IEA:InterPro.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:InterPro.
DR GO; GO:0006950; P:response to stress; IEA:UniProt.
DR CDD; cd06468; p23_CacyBP; 1.
DR Gene3D; 2.60.40.790; -; 1.
DR InterPro; IPR037201; CacyBP_N.
DR InterPro; IPR037893; CS_CacyBP.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR InterPro; IPR007699; SGS_dom.
DR InterPro; IPR015120; Siah-Interact_N.
DR PANTHER; PTHR47686:SF1; CALCYCLIN-BINDING PROTEIN; 1.
DR PANTHER; PTHR47686; SGS DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF04969; CS; 1.
DR Pfam; PF09032; Siah-Interact_N; 1.
DR SUPFAM; SSF140106; Calcyclin-binding protein-like; 1.
DR SUPFAM; SSF49764; HSP20-like chaperones; 1.
DR PROSITE; PS51203; CS; 1.
DR PROSITE; PS51048; SGS; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000291084};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 69..159
FT /note="CS"
FT /evidence="ECO:0000259|PROSITE:PS51203"
FT DOMAIN 144..218
FT /note="SGS"
FT /evidence="ECO:0000259|PROSITE:PS51048"
SQ SEQUENCE 218 AA; 24569 MW; B2C1D951376E25F0 CRC64;
MAQDLTLDLE ELRHLHSIAK RSRTLSLLSS EIRNLEKISS DANAARAPQI PTPISTGAKV
SPSPALNYST LASFSWDQDV DKVKIYVSME GIDENKIESE FKSISFDVKF HDVQGKNYRC
AISKLHKEIV PEKCKVLVKP KRAIITLVKA SKGNWLDLHF KEDKLKPNLD KEKDPMAGIM
DMMKNMYDEG DDEMKKTIAK AWTDARSGKT ADPLGSYR
//
