ID A0A6J1U5W5_9SAUR Unreviewed; 791 AA.
AC A0A6J1U5W5;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 1.
DT 28-JAN-2026, entry version 23.
DE SubName: Full=RING finger protein unkempt homolog isoform X3 {ECO:0000313|RefSeq:XP_026523264.1};
GN Name=UNK {ECO:0000313|RefSeq:XP_026523264.1};
OS Notechis scutatus (mainland tiger snake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Hydrophiinae; Notechis.
OX NCBI_TaxID=8663 {ECO:0000313|Proteomes:UP000504612, ECO:0000313|RefSeq:XP_026523264.1};
RN [1] {ECO:0000313|RefSeq:XP_026523264.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the unkempt family.
CC {ECO:0000256|ARBA:ARBA00008808}.
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DR RefSeq; XP_026523264.1; XM_026667479.1.
DR AlphaFoldDB; A0A6J1U5W5; -.
DR GeneID; 113412077; -.
DR CTD; 85451; -.
DR Proteomes; UP000504612; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:1990715; F:mRNA CDS binding; IEA:TreeGrafter.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048667; P:cell morphogenesis involved in neuron differentiation; IEA:TreeGrafter.
DR CDD; cd16771; RING-HC_UNK; 1.
DR Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 2.
DR InterPro; IPR040594; UNK_Znf_1.
DR InterPro; IPR057295; UNK_Znf_4.
DR InterPro; IPR057296; UNK_Znf_5.
DR InterPro; IPR045234; Unkempt-like.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR InterPro; IPR001841; Znf_RING.
DR PANTHER; PTHR14493:SF36; RING FINGER PROTEIN UNKEMPT HOMOLOG; 1.
DR PANTHER; PTHR14493; UNKEMPT FAMILY MEMBER; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR Pfam; PF23261; zf-CCCH_11; 1.
DR Pfam; PF25427; zf-CCCH_UNK; 1.
DR Pfam; PF23035; zf-CCCH_UNK-like_4th; 1.
DR Pfam; PF18384; zf_CCCH_5; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00356; ZnF_C3H1; 5.
DR SUPFAM; SSF90229; CCCH zinc finger; 1.
DR PROSITE; PS50103; ZF_C3H1; 4.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; Reference proteome {ECO:0000313|Proteomes:UP000504612};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00723}.
FT DOMAIN 82..111
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 122..152
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 249..283
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 291..319
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 82..111
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 122..152
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 249..283
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 291..319
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 237..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 628..704
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 239..251
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..363
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 791 AA; 86910 MW; 69D55509CC1961A3 CRC64;
MSKGPVGTGP PATGPVVAAS ALQAQPEKPQ HYTYLKEFRT EQCPLFVQHK CTQHRPYTCF
HWHFVNQRRR RSIRRRDGTF NYSPDIYCTK YDETTGICPE GDECPFLHRT TGDTERRYHL
RYYKTGICIH ETDSKGNCTK NGLHCAFAHG PHDLRSPVYD IRELQAMEAL QNGQTTSESG
IEGQSAVAAS HAMIEKILSE EPRWQDTTYV LGNYKTEQCK KPPRLCRQGY ACPYYHNSKD
RRRSPRKHKY RSSPCPSVKH GDEWGDPSKC DNGDACQYCH TRTEQQFHPE IYKSTKCNDM
QQSGSCPRGP FCAFAHVEQP PLSEDLQPTS AVSSPTQAGP VMYMPSAAGD SVPVSPSSPQ
APDLSNVWNK PGTLPTSPTS ATILCRNSSL GSPSNLCGSP PGAIGKPHSL ESIGFPTDSV
TSASSYKKAP GFEREDLVGA EYLKNFKCQQ AKIKSHSMEH RTQEQPLLQP KQDILGILPV
GSPLTSSISS SITSSLAATP PSPAGTSSVP GMNANALPFY PTSDTVESVI GGSLLQSSAP
VNIPGSLGSS ASFHSASPSP PVSLSSHFLH QSQGHLSQSE NTFLGTSASH GSLGLNGMNS
SIWEHFASGS FSPSTSPAFL SGPGAAELAR LRQELDEANS TIKQWEDSWK QAKQACDAWK
KEAEEANDRA STATLECELA REQRETLELQ VKKLQEEIER IHTGQDPQFL RSFSDLENLS
LSTLYNLQKQ LRANLERVDK AVFQLQSVKC LKCQEENRVV LPCQHTVLCE TCAEEGECPI
CHPNRPHALQ S
//
