ID A0A1D5NWN1_CHICK Unreviewed; 380 AA.
AC A0A1D5NWN1; A0A1D5P0W9;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 2.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=E3 ubiquitin-protein ligase KCMF1 {ECO:0000256|ARBA:ARBA00014999};
DE AltName: Full=RING-type E3 ubiquitin transferase KCMF1 {ECO:0000256|ARBA:ARBA00030767};
GN Name=LOC431003 {ECO:0000313|Ensembl:ENSGALP00010017963.1};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031 {ECO:0000313|Ensembl:ENSGALP00010017963.1, ECO:0000313|Proteomes:UP000000539};
RN [1] {ECO:0000313|Ensembl:ENSGALP00010017963.1}
RP IDENTIFICATION.
RC STRAIN=broiler {ECO:0000313|Ensembl:ENSGALP00010017963.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Has intrinsic E3 ubiquitin ligase activity and promotes
CC ubiquitination. {ECO:0000256|ARBA:ARBA00003752}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC -!- SIMILARITY: Belongs to the KCMF1 family.
CC {ECO:0000256|ARBA:ARBA00010938}.
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DR AlphaFoldDB; A0A1D5NWN1; -.
DR SMR; A0A1D5NWN1; -.
DR STRING; 9031.ENSGALP00000044771; -.
DR PaxDb; 9031-ENSGALP00000023277; -.
DR Ensembl; ENSGALT00010030928.1; ENSGALP00010017963.1; ENSGALG00010012888.1.
DR VEuPathDB; HostDB:LOC431003; -.
DR GeneTree; ENSGT00510000047171; -.
DR InParanoid; A0A1D5NWN1; -.
DR OMA; TTRHLTD; -.
DR OrthoDB; 26661at2759; -.
DR Proteomes; UP000000539; Chromosome W.
DR Bgee; ENSGALG00000035780; Expressed in muscle tissue and 8 other cell types or tissues.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0099536; P:synaptic signaling; IBA:GO_Central.
DR CDD; cd02338; ZZ_PCMF_like; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR InterPro; IPR008598; Di19_Zn-bd.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR PANTHER; PTHR12268; E3 UBIQUITIN-PROTEIN LIGASE KCMF1; 1.
DR PANTHER; PTHR12268:SF13; E3 UBIQUITIN-PROTEIN LIGASE KCMF1; 1.
DR Pfam; PF05605; zf-Di19; 1.
DR Pfam; PF00569; ZZ; 1.
DR SMART; SM00355; ZnF_C2H2; 1.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000000539};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
SQ SEQUENCE 380 AA; 41983 MW; 52AD0D725F09262E CRC64;
MSRHEGVSCD ACLKGNFRGR RYKCLICYDY DLCATCYESG ATTTRHTTDH PMQCILTRVD
FDLYYGGEAF SVEQPQSFTC PYCGKMGYTE TSLQEHVASE HAETSTEVIC PICAALPGGD
PNHVTDDFAA HLTLEHRAPR DLDESSGVRH VRRMFHPGRG LGGPRARRSN MHFTSSSTGG
LSSSQSSYST SNRETMDPIA ELLSQLSGVR RSAGQLNSSG PSASQLQQLQ MQLQLERQHA
QAARQQLETA RNATRRTNTS SIPTTLTQSI VATNSSNTEN NQQTTHNSQF LLTRLNDPKM
SEAERQSKES EQADRSLFVQ ELLLSTLMQE ESSSSDEDER GEFADFGAMG CVDIMPLDVA
LENLNLKENN KGNEPLPPPL
//
