ID G5ARS2_HETGA Unreviewed; 278 AA.
AC G5ARS2;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Calcyclin-binding protein {ECO:0000256|ARBA:ARBA00015702};
GN ORFNames=GW7_21560 {ECO:0000313|EMBL:EHA99732.1};
OS Heterocephalus glaber (Naked mole rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Heterocephalus.
OX NCBI_TaxID=10181 {ECO:0000313|EMBL:EHA99732.1, ECO:0000313|Proteomes:UP000006813};
RN [1] {ECO:0000313|EMBL:EHA99732.1, ECO:0000313|Proteomes:UP000006813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993625; DOI=10.1038/nature10533;
RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT "Genome sequencing reveals insights into physiology and longevity of the
RT naked mole rat.";
RL Nature 479:223-227(2011).
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}.
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DR EMBL; JH166641; EHA99732.1; -; Genomic_DNA.
DR AlphaFoldDB; G5ARS2; -.
DR STRING; 10181.G5ARS2; -.
DR eggNOG; KOG3260; Eukaryota.
DR InParanoid; G5ARS2; -.
DR Proteomes; UP000006813; 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; 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:UP000006813};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 123..217
FT /note="CS"
FT /evidence="ECO:0000259|PROSITE:PS51203"
FT DOMAIN 201..278
FT /note="SGS"
FT /evidence="ECO:0000259|PROSITE:PS51048"
SQ SEQUENCE 278 AA; 31368 MW; AAFDA329BF76150D CRC64;
MASALEEVRG SAPARGQEAC VPLRSRGPFL SRRAAANRKL PKGWTGAEAE RVPCELQNDL
EEVKVLLEKA TRKRVRDALT AEKSKIETEI KNKVQQKSQK KPEFLDNEKP AALVAPTTTG
YTVKISNYGW DQSDKFVKIY ITLTGVHQAP AENVQVHFTE RSFDLLVKNL NGKSYSMTVN
NLLKPISVEG SSKKIKTDTV LILCRKKAEN TRWEYLTQVE KECKEKEKPS YDAETDPSEG
LMNVLKTIYE DGDDDMKQTI NKAWVESREK QAKGDAEF
//
