ID A0A016U564_9BILA Unreviewed; 285 AA.
AC A0A016U564;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Calcyclin-binding protein {ECO:0000256|ARBA:ARBA00015702};
GN Name=Acey_s0057.g2735 {ECO:0000313|EMBL:EYC10041.1};
GN ORFNames=Y032_0057g2735 {ECO:0000313|EMBL:EYC10041.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC10041.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(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}.
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:EYC10041.1}.
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DR EMBL; JARK01001393; EYC10041.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016U564; -.
DR Proteomes; UP000024635; 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 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:UP000024635};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 121..215
FT /note="CS"
FT /evidence="ECO:0000259|PROSITE:PS51203"
FT DOMAIN 199..285
FT /note="SGS"
FT /evidence="ECO:0000259|PROSITE:PS51048"
FT REGION 87..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 285 AA; 32528 MW; 81D4C8FC36B547A8 CRC64;
MAKLLEKYVG LRATHVVKQH DGMYSLSETT NPPKRFTSSD LFAIPAMDAK ELALDLEDLR
LLLTSSKRPA VQQWIKSKIE EIEKKIASQK EKQPAPVPHS NDSSPAPDAN KSATPSSLPT
VKVTNYGWDE SDKFVKVYIT LQGVHNANPS TIQHTFSNFG YDILISDFSG KNYVMTMKGL
RDEIVPESSQ IKQKQDMLLV MMKKKTEGKK WEQLTKLEYD EKQKRKPKFD DKAMGDDPQA
SLMNMMKQMY EEGDDELKRT IRKAWHEGQN KRNTADMPLP SLDDM
//