DFI8B_XENLA
ID DFI8B_XENLA Reviewed; 443 AA.
AC Q7T0P6;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Differentially expressed in FDCP 8 homolog B;
DE Short=DEF-8-B;
GN Name=def8-b;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Positively regulates lysosome peripheral distribution and
CC ruffled border formation in osteoclasts. Involved in bone resorption.
CC {ECO:0000250|UniProtKB:Q99J78}.
CC -!- SIMILARITY: Belongs to the DEF8 family. {ECO:0000305}.
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DR EMBL; BC056097; AAH56097.1; -; mRNA.
DR RefSeq; NP_001080885.1; NM_001087416.1.
DR AlphaFoldDB; Q7T0P6; -.
DR SMR; Q7T0P6; -.
DR PRIDE; Q7T0P6; -.
DR DNASU; 380579; -.
DR GeneID; 380579; -.
DR KEGG; xla:380579; -.
DR CTD; 380579; -.
DR Xenbase; XB-GENE-967887; def8.S.
DR OrthoDB; 177737at2759; -.
DR Proteomes; UP000186698; Chromosome 4S.
DR Bgee; 380579; Expressed in oocyte and 19 other tissues.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032418; P:lysosome localization; ISS:UniProtKB.
DR GO; GO:0045780; P:positive regulation of bone resorption; ISS:UniProtKB.
DR GO; GO:1900029; P:positive regulation of ruffle assembly; ISS:UniProtKB.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR036280; Multihaem_cyt_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR025258; Zf-RING_9.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF13901; zf-RING_9; 1.
DR SMART; SM00109; C1; 2.
DR SMART; SM01175; DUF4206; 1.
DR SUPFAM; SSF48695; SSF48695; 1.
DR SUPFAM; SSF57889; SSF57889; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 2: Evidence at transcript level;
KW Metal-binding; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..443
FT /note="Differentially expressed in FDCP 8 homolog B"
FT /id="PRO_0000321917"
FT ZN_FING 134..185
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 364..424
FT /note="Phorbol-ester/DAG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 14..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 443 AA; 51354 MW; 1961E97E6606977F CRC64;
MEYDDKLVRF RQGHLNPFDK KGGAERHPAD SETQPCKDSS TSSPLSVPEY NYPDRVMDLG
VSEDHFSRPV GLFLASDVQQ LRQAIEECKQ EILELPENSD RQKDAVVRLI HLRLKLQELN
DPLEDEPNLR VLLEHRFYKE KSKSVKHLCD KCSTFIWGLI QTWYTCTGCS YSCHSKCLNL
ITKPCVRSKV SHQAEYELSI CPEAGLDSQD YRCAECRTPI SLRAVPSEAR QCDYTGQYYC
ISCHWNDLAV IPARAIHNWD FEPCKVSRYS MRYLALMLGR PVLKLREINP LLFNYVEELV
EIRKLRQDIL LMKPYFITCK EAMEDRLLLQ LQDRQHFVEN DDMYSLQDLL DISSGRLGCS
LTEIHTTFAK HIKLDCERCQ AKGFMCELCK EGDILFPFDS HTSVCQDCAA VFHRDCYYEN
STSCPRCMRL NLRKQVQNPG AEP