DFI8A_XENLA
ID DFI8A_XENLA Reviewed; 443 AA.
AC Q6DDJ3;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Differentially expressed in FDCP 8 homolog A;
DE Short=DEF-8-A;
GN Name=def8-a;
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=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) 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; BC077567; AAH77567.1; -; mRNA.
DR RefSeq; NP_001086859.1; NM_001093390.1.
DR AlphaFoldDB; Q6DDJ3; -.
DR SMR; Q6DDJ3; -.
DR DNASU; 446694; -.
DR GeneID; 446694; -.
DR KEGG; xla:446694; -.
DR CTD; 446694; -.
DR Xenbase; XB-GENE-17345812; def8.L.
DR OMA; IEPRLCD; -.
DR OrthoDB; 177737at2759; -.
DR Proteomes; UP000186698; Chromosome 4L.
DR Bgee; 446694; Expressed in spleen 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 A"
FT /id="PRO_0000321916"
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 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 443 AA; 51323 MW; 7486DA5142EC474A CRC64;
MEYDDKLVRF RQGHLNPFDK QGGAERHPAD SEAQPPKDSS TISPHSIPEY HCPDRVMDLG
VSEDHFSRPV GLFLASDIQQ LRQAIEECKQ EILELPENSD RQKDAVVRLI HLRLKLQELN
DPLEDEPNLR ILLEHRFYKE KSKSVKHVCD KCSTFIWGLI QTWYTCTGCS YSCHSKCLNL
ITKPCVRSKV SHQAEYELSI CPEAGLDSQD YRCAECRTPI SLRAVPSEAR QCDYTGQYYC
ISCHWNDLAV IPARAIHNWD FEPRKVSRCS MRYLALMLGR PVLKLREINP LLFNYVEELV
EIRKLRQDIL LMKPYFITCK EAMEARLLLQ LQDRQHFVEN DDMYSLQDLL DISSGRLGCT
LTEIHTTFAK HIKLDCERCQ AKGFVCELCK EGDILFPFDS HTSVCQDCAA VFHRDCYYDN
STSCPRCMRL SLRKQTQNPE AEP