ID A0A3M0KA71_HIRRU Unreviewed; 221 AA.
AC A0A3M0KA71;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 22-FEB-2023, entry version 11.
DE RecName: Full=Calcyclin-binding protein {ECO:0000256|ARBA:ARBA00015702};
GN ORFNames=DUI87_14445 {ECO:0000313|EMBL:RMC08204.1};
OS Hirundo rustica rustica.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Sylvioidea; Hirundinidae;
OC Hirundo.
OX NCBI_TaxID=333673 {ECO:0000313|EMBL:RMC08204.1, ECO:0000313|Proteomes:UP000269221};
RN [1] {ECO:0000313|EMBL:RMC08204.1, ECO:0000313|Proteomes:UP000269221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Chelidonia {ECO:0000313|EMBL:RMC08204.1};
RC TISSUE=Blood {ECO:0000313|EMBL:RMC08204.1};
RA Formenti G., Chiara M., Poveda L., Francoijs K.-J., Bonisoli-Alquati A.,
RA Canova L., Gianfranceschi L., Horner D.S., Saino N.;
RT "A high quality draft genome assembly of the barn swallow (H. rustica
RT rustica).";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RMC08204.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QRBI01000117; RMC08204.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M0KA71; -.
DR STRING; 333673.A0A3M0KA71; -.
DR Proteomes; UP000269221; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; 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 CDD; cd06468; p23_CacyBP; 1.
DR Gene3D; 2.60.40.790; -; 1.
DR Gene3D; 4.10.860.10; UVR domain; 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; PTHR13164:SF3; CALCYCLIN-BINDING PROTEIN; 1.
DR PANTHER; PTHR13164; CALICYLIN BINDING PROTEIN; 1.
DR Pfam; PF04969; CS; 1.
DR Pfam; PF05002; SGS; 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 Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000269221};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 66..159
FT /note="CS"
FT /evidence="ECO:0000259|PROSITE:PS51203"
FT DOMAIN 144..221
FT /note="SGS"
FT /evidence="ECO:0000259|PROSITE:PS51048"
SQ SEQUENCE 221 AA; 25572 MW; 523152980F71EDA7 CRC64;
MAVAREELQK DLEEVKELLT KATRKRVRDV LLAEKQKLEL EIKNQPAPKP KDVAEEEKSS
LGGYTVKINN YGWDQSDKFV KIYISLNGVQ KLPAENVQVN FTERSFDLLV KNLNGKNYTM
TFNNLLKPIS VEGSSRKIKT DMVLVMCKKK REEKWDCLTQ VEKESKEKEK AAYDTTDPSE
GLMNILKKMY AEGDDEMKRT INKAWVESRE KQYKGDIPMD I
//