ID H3AC88_LATCH Unreviewed; 303 AA.
AC H3AC88;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN Name=RNF144A {ECO:0000313|Ensembl:ENSLACP00000007259.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000007259.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000007259.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC EC=2.3.2.31; Evidence={ECO:0000256|ARBA:ARBA00001798};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the RBR family. RNF144 subfamily.
CC {ECO:0000256|ARBA:ARBA00038342}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AFYH01097251; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01097252; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01097253; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01097254; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01097255; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01097256; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01097257; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01097258; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01097259; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01097260; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005998973.1; XM_005998911.2.
DR AlphaFoldDB; H3AC88; -.
DR STRING; 7897.ENSLACP00000007259; -.
DR Ensembl; ENSLACT00000007319.1; ENSLACP00000007259.1; ENSLACG00000006438.1.
DR GeneID; 102351857; -.
DR CTD; 570968; -.
DR eggNOG; KOG1815; Eukaryota.
DR GeneTree; ENSGT00940000157701; -.
DR HOGENOM; CLU_053598_1_0_1; -.
DR InParanoid; H3AC88; -.
DR OMA; SSVYKME; -.
DR OrthoDB; 2943236at2759; -.
DR TreeFam; TF324777; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000006438; Expressed in post-anal tail muscle and 4 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR CDD; cd20366; BRcat_RBR_RNF144A; 1.
DR CDD; cd16777; mRING-HC-C4C4_RBR_RNF144A; 1.
DR CDD; cd20352; Rcat_RBR_RNF144; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR11685:SF99; E3 UBIQUITIN-PROTEIN LIGASE RNF144A; 1.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF01485; IBR; 2.
DR SMART; SM00647; IBR; 2.
DR SMART; SM00184; RING; 2.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008672};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT TRANSMEM 261..287
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 26..247
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 30..76
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 303 AA; 34261 MW; C3522AC8573E42E9 CRC64;
MEISCYNCAT MTTARYRPTW DLALDPLVSC KLCLGEYPVE QMTTLAQCQC LFCTLCLKQY
VELLIKEGLE TAISCPDAAC PKGGHLQENE IECMVAAEIM QRYRKLQFER EVLLDPCKTW
CPSSTCQSVC QLQEVEPRNP QLVQCKTCRL EFCSVCKSNW HPGQGCQESL TITSFLPGET
SSFFKNEDDD APIKRCPKCK VYIERDEGCA QMMCKNCKHA FCWYCLESLD DDFLLIHYDK
GPCRNKLGHS RASVIWHRTQ VVGIFAGFGL LLLVASPFLL LATPFVLCCK CKCNKGDDDP
LPT
//
