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Database: UniProt
Entry: A0A016U564_9BILA
LinkDB: A0A016U564_9BILA
Original site: A0A016U564_9BILA 
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
//
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