ID A0A1S3F201_DIPOR Unreviewed; 414 AA.
AC A0A1S3F201;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=LOW QUALITY PROTEIN: zinc finger protein 396-like {ECO:0000313|RefSeq:XP_012870255.1};
GN Name=LOC105984570 {ECO:0000313|RefSeq:XP_012870255.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012870255.1};
RN [1] {ECO:0000313|RefSeq:XP_012870255.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012870255.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PROSITE-ProRule:PRU00187}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000256|ARBA:ARBA00006991}.
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DR RefSeq; XP_012870255.1; XM_013014801.1.
DR GeneID; 105984570; -.
DR KEGG; dord:105984570; -.
DR InParanoid; A0A1S3F201; -.
DR OrthoDB; 4330481at2759; -.
DR Proteomes; UP000081671; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR CDD; cd07936; SCAN; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 2.
DR Gene3D; 1.10.4020.10; DNA breaking-rejoining enzymes; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR003309; SCAN_dom.
DR InterPro; IPR038269; SCAN_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR45935; PROTEIN ZBED8-RELATED; 1.
DR PANTHER; PTHR45935:SF15; SCAN DOMAIN-CONTAINING PROTEIN 3; 1.
DR Pfam; PF02023; SCAN; 1.
DR Pfam; PF00096; zf-C2H2; 1.
DR SMART; SM00431; SCAN; 1.
DR SMART; SM00355; ZnF_C2H2; 1.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1.
DR SUPFAM; SSF47353; Retrovirus capsid dimerization domain-like; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS50804; SCAN_BOX; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Nucleus {ECO:0000256|PROSITE-ProRule:PRU00187};
KW Reference proteome {ECO:0000313|Proteomes:UP000081671};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 169..251
FT /note="SCAN box"
FT /evidence="ECO:0000259|PROSITE:PS50804"
FT DOMAIN 299..398
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 368..395
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 92..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 414 AA; 46839 MW; A332CE15AAF49913 CRC64;
MVFKSIVSSC KKRVRVVFFG KRGLYRYDNI KDIEMERLLS QIVLKPPGRV LEKAPRVSMA
TASASRPAPG CSLKSGFPGI WLGALGLASS QNHEISPGLS QPRRCRREAR ESQGGKVHWG
PSCPPSPMSS THLPQTPEEP DEVIAVKMEE EEQGSSLHXN SCYSPDTFRQ HFRHFHYQNS
PGPREALSQL GELCCCCWLR PELYSKEHIL ELQVLEQFLA ILPEELQIWV QKHHPENGEE
VVILLEQVER EAHGLAGSFF GLRKAAAVDE LVPWEITPKL PSSQRKPLKQ PQRPSWELPP
LRQHDEDTKT INEKSASRKK TFSGVDLHCD VSSTFPMNAS PSFTSTGTWE QDGRFERRQG
NPSRRKQHKC DECGKIFSQS SSLILHQRIH SGEKPYACDQ WAKAFSQSAI LIQH
//
